Endoplasmic reticulum dysfunction in neurological disease
Endoplasmic reticulum (ER) dysfunction might have an important part to play in a range of neurological disorders, including cerebral ischaemia, sleep apnoea, Alzheimer's disease, multiple sclerosis, amyotrophic lateral sclerosis, the prion diseases, and familial encephalopathy with neuroserpin...
Uložené v:
| Vydané v: | Lancet neurology Ročník 12; číslo 1; s. 105 - 118 |
|---|---|
| Hlavní autori: | , , , , , |
| Médium: | Journal Article |
| Jazyk: | English |
| Vydavateľské údaje: |
England
Elsevier Ltd
01.01.2013
Elsevier Limited Elsevier |
| Predmet: | |
| ISSN: | 1474-4422, 1474-4465, 1474-4465 |
| On-line prístup: | Získať plný text |
| Tagy: |
Pridať tag
Žiadne tagy, Buďte prvý, kto otaguje tento záznam!
|
| Abstract | Endoplasmic reticulum (ER) dysfunction might have an important part to play in a range of neurological disorders, including cerebral ischaemia, sleep apnoea, Alzheimer's disease, multiple sclerosis, amyotrophic lateral sclerosis, the prion diseases, and familial encephalopathy with neuroserpin inclusion bodies. Protein misfolding in the ER initiates the well studied unfolded protein response in energy-starved neurons during stroke, which is relevant to the toxic effects of reperfusion. The toxic peptide amyloid β induces ER stress in Alzheimer's disease, which leads to activation of similar pathways, whereas the accumulation of polymeric neuroserpin in the neuronal ER triggers a poorly understood ER-overload response. In other neurological disorders, such as Parkinson's and Huntington's diseases, ER dysfunction is well recognised but the mechanisms by which it contributes to pathogenesis remain unclear. By targeting components of these signalling responses, amelioration of their toxic effects and so the treatment of a range of neurodegenerative disorders might become possible. |
|---|---|
| AbstractList | Endoplasmic reticulum (ER) dysfunction might have an important part to play in a range of neurological disorders, including cerebral ischaemia, sleep apnoea, Alzheimer's disease, multiple sclerosis, amyotrophic lateral sclerosis, the prion diseases, and familial encephalopathy with neuroserpin inclusion bodies. Protein misfolding in the ER initiates the well studied unfolded protein response in energy-starved neurons during stroke, which is relevant to the toxic effects of reperfusion. The toxic peptide amyloid β induces ER stress in Alzheimer's disease, which leads to activation of similar pathways, whereas the accumulation of polymeric neuroserpin in the neuronal ER triggers a poorly understood ER-overload response. In other neurological disorders, such as Parkinson's and Huntington's diseases, ER dysfunction is well recognised but the mechanisms by which it contributes to pathogenesis remain unclear. By targeting components of these signalling responses, amelioration of their toxic effects and so the treatment of a range of neurodegenerative disorders might become possible. Endoplasmic reticulum (ER) dysfunction might have an important part to play in a range of neurological disorders, including cerebral ischaemia, sleep apnoea, Alzheimer's disease, multiple sclerosis, amyotrophic lateral sclerosis, the prion diseases, and familial encephalopathy with neuroserpin inclusion bodies. Protein misfolding in the ER initiates the well studied unfolded protein response in energy-starved neurons during stroke, which is relevant to the toxic effects of reperfusion. The toxic peptide amyloid β induces ER stress in Alzheimer's disease, which leads to activation of similar pathways, whereas the accumulation of polymeric neuroserpin in the neuronal ER triggers a poorly understood ER-overload response. In other neurological disorders, such as Parkinson's and Huntington's diseases, ER dysfunction is well recognised but the mechanisms by which it contributes to pathogenesis remain unclear. By targeting components of these signalling responses, amelioration of their toxic effects and so the treatment of a range of neurodegenerative disorders might become possible.Endoplasmic reticulum (ER) dysfunction might have an important part to play in a range of neurological disorders, including cerebral ischaemia, sleep apnoea, Alzheimer's disease, multiple sclerosis, amyotrophic lateral sclerosis, the prion diseases, and familial encephalopathy with neuroserpin inclusion bodies. Protein misfolding in the ER initiates the well studied unfolded protein response in energy-starved neurons during stroke, which is relevant to the toxic effects of reperfusion. The toxic peptide amyloid β induces ER stress in Alzheimer's disease, which leads to activation of similar pathways, whereas the accumulation of polymeric neuroserpin in the neuronal ER triggers a poorly understood ER-overload response. In other neurological disorders, such as Parkinson's and Huntington's diseases, ER dysfunction is well recognised but the mechanisms by which it contributes to pathogenesis remain unclear. By targeting components of these signalling responses, amelioration of their toxic effects and so the treatment of a range of neurodegenerative disorders might become possible. Endoplasmic reticulum (ER) dysfunction might have an important part to play in a range of neurological disorders, including cerebral ischaemia, sleep apnoea, Alzheimer's disease, multiple sclerosis, amyotrophic lateral sclerosis, the prion diseases, and familial encephalopathy with neuroserpin inclusion bodies. Protein misfolding in the ER initiates the well studied unfolded protein response in energy-starved neurons during stroke, which is relevant to the toxic effects of reperfusion. The toxic peptide amyloid [beta] induces ER stress in Alzheimer's disease, which leads to activation of similar pathways, whereas the accumulation of polymeric neuroserpin in the neuronal ER triggers a poorly understood ER-overload response. In other neurological disorders, such as Parkinson's and Huntington's diseases, ER dysfunction is well recognised but the mechanisms by which it contributes to pathogenesis remain unclear. By targeting components of these signalling responses, amelioration of their toxic effects and so the treatment of a range of neurodegenerative disorders might become possible. Summary Endoplasmic reticulum (ER) dysfunction might have an important part to play in a range of neurological disorders, including cerebral ischaemia, sleep apnoea, Alzheimer's disease, multiple sclerosis, amyotrophic lateral sclerosis, the prion diseases, and familial encephalopathy with neuroserpin inclusion bodies. Protein misfolding in the ER initiates the well studied unfolded protein response in energy-starved neurons during stroke, which is relevant to the toxic effects of reperfusion. The toxic peptide amyloid β induces ER stress in Alzheimer's disease, which leads to activation of similar pathways, whereas the accumulation of polymeric neuroserpin in the neuronal ER triggers a poorly understood ER-overload response. In other neurological disorders, such as Parkinson's and Huntington's diseases, ER dysfunction is well recognised but the mechanisms by which it contributes to pathogenesis remain unclear. By targeting components of these signalling responses, amelioration of their toxic effects and so the treatment of a range of neurodegenerative disorders might become possible. Endoplasmic reticulum (ER) dysfunction is important in the pathogenesis of many neurological diseases. In this review, we examine the evidence for ER dysfunction in a range of neurological conditions including cerebral ischaemia, sleep apnoea, Alzheimer's disease, multiple sclerosis, amyotrophic lateral sclerosis, the prion diseases and Familial Encephalopathy with Neuroserpin Inclusion Bodies (FENIB). Protein misfolding in the endoplasmic reticulum initiates a well-studied 'Unfolded Protein Response' in energy-starved neurones during stroke that is relevant to the toxicity of reperfusion. The toxic peptide Aβ induces 'ER stress' in Alzheimer's disease leading to activation of similar pathways, while the accumulation of polymeric neuroserpin in the neuronal ER triggers a poorly understood 'ER overload response'. In other neurological disorders such as Parkinson's and Huntington's diseases ER dysfunction is well recognised but the mechanisms for this are less clear. By targeting components of these signalling responses, it may prove possible to ameliorate their toxic effects and treat a range of neurodegenerative conditions. |
| Author | Crowther, Damian C Lomas, David A Miranda, Elena Roussel, Benoit D Kruppa, Antonina J Marciniak, Stefan J |
| Author_xml | – sequence: 1 givenname: Benoit D surname: Roussel fullname: Roussel, Benoit D organization: Department of Medicine, Cambridge Institute for Medical Research, University of Cambridge, Cambridge, UK – sequence: 2 givenname: Antonina J surname: Kruppa fullname: Kruppa, Antonina J organization: Department of Medicine, Cambridge Institute for Medical Research, University of Cambridge, Cambridge, UK – sequence: 3 givenname: Elena surname: Miranda fullname: Miranda, Elena organization: Charles Darwin Department of Biology and Biotechnology and Institut Pasteur–Cenci Bolognetti Foundation, Sapienza University of Rome, Rome, Italy – sequence: 4 givenname: Damian C surname: Crowther fullname: Crowther, Damian C organization: Department of Genetics, University of Cambridge, Cambridge, UK – sequence: 5 givenname: David A surname: Lomas fullname: Lomas, David A organization: Department of Medicine, Cambridge Institute for Medical Research, University of Cambridge, Cambridge, UK – sequence: 6 givenname: Stefan J surname: Marciniak fullname: Marciniak, Stefan J email: sjm20@cam.ac.uk organization: Department of Medicine, Cambridge Institute for Medical Research, University of Cambridge, Cambridge, UK |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/23237905$$D View this record in MEDLINE/PubMed https://inserm.hal.science/inserm-01296824$$DView record in HAL |
| BookMark | eNqNkm9r1TAUh4NM3B_9CErBNxOs5qRp0yAqY0wnXPCF-jrkJqeamSbXpB3cb2-73k24INurhPCcJyfnl2NyEGJAQp4DfQMUmrffgAtecs7YKbBXgrKqLcUjcrQ7buqDuz1jh-Q45ytKGfAWnpBDVrFKSFofEXkRbNx4nXtnioSDM6Mf-8JuczcGM7gYCheKgGOKPv50RvvCuow641PyuNM-47PdekJ-fLr4fn5Zrr5-_nJ-tipNA3IoWY0VmArWHOuarqWsmta0rcVaSEY7Cx0XmgI3tkFEAxy1tAI6jZ3tKGB1Ql4v3l_aq01yvU5bFbVTl2cr5ULG1CsKTDYt49cw4acLvknxz4h5UL3LBr3XAeOYFTDBRMVEwx-AVpI2AGK2vtxDr-KYwvTumRIgKG3lRL3YUeO6R3vX7e24J-DdApgUc07YKeMGPU95SNp5BVTN4aqbcNWc3KRXN-EqMVXXe9W3F9xX93Gpwymma4dJZeMwGLQuoRmUje5ew4c9g_EuzL_hN24x_5uFykzRRTI7pmHPhlnw_v-CBzTwF35s4W0 |
| CODEN | LANCAO |
| CitedBy_id | crossref_primary_10_3389_fncel_2017_00377 crossref_primary_10_1016_j_chembiol_2016_09_001 crossref_primary_10_1371_journal_pone_0185664 crossref_primary_10_1016_j_freeradbiomed_2025_05_002 crossref_primary_10_1016_j_brainres_2016_03_044 crossref_primary_10_1093_toxsci_kfz132 crossref_primary_10_1007_s12192_016_0741_1 crossref_primary_10_1016_j_neurobiolaging_2014_12_021 crossref_primary_10_1016_j_bbadis_2014_05_003 crossref_primary_10_3892_ijmm_2018_3858 crossref_primary_10_1007_s12035_014_8672_2 crossref_primary_10_1016_j_ejphar_2017_06_006 crossref_primary_10_1097_NEN_0000000000000196 crossref_primary_10_1016_j_brainres_2023_148742 crossref_primary_10_1007_s12035_014_8695_8 crossref_primary_10_1021_acsnano_5c02952 crossref_primary_10_1007_s00418_016_1527_3 crossref_primary_10_1016_j_ijdevneu_2018_11_001 crossref_primary_10_1002_anie_202101468 crossref_primary_10_1517_14728222_2013_791284 crossref_primary_10_1371_journal_pone_0112837 crossref_primary_10_3389_fnmol_2017_00187 crossref_primary_10_1016_j_mcn_2023_103822 crossref_primary_10_1016_j_neuron_2017_01_010 crossref_primary_10_3233_JAD_150678 crossref_primary_10_1016_j_phymed_2022_153985 crossref_primary_10_1016_j_febslet_2014_11_029 crossref_primary_10_1038_s41598_023_29852_x crossref_primary_10_3390_v12010017 crossref_primary_10_1038_ncomms4620 crossref_primary_10_3892_ijmm_2018_3724 crossref_primary_10_1016_j_toxlet_2013_08_001 crossref_primary_10_1016_j_trac_2023_117128 crossref_primary_10_3892_ijmm_2018_3607 crossref_primary_10_1007_s12038_013_9391_y crossref_primary_10_1016_j_yexcr_2018_06_033 crossref_primary_10_12677_PI_2021_101006 crossref_primary_10_1038_ncomms11020 crossref_primary_10_1080_10715762_2018_1546852 crossref_primary_10_1186_s12974_017_0878_6 crossref_primary_10_1038_nrdp_2016_51 crossref_primary_10_1016_j_nbd_2018_08_026 crossref_primary_10_1016_j_brainres_2016_03_029 crossref_primary_10_1371_journal_pone_0299898 crossref_primary_10_1523_JNEUROSCI_4002_14_2015 crossref_primary_10_1007_s11011_016_9830_1 crossref_primary_10_3390_nu16152430 crossref_primary_10_1111_neup_12080 crossref_primary_10_1007_s12640_019_00084_0 crossref_primary_10_1007_s12975_014_0359_5 crossref_primary_10_1016_j_neuron_2015_05_041 crossref_primary_10_1021_acs_analchem_4c03559 crossref_primary_10_3389_fnins_2024_1348151 crossref_primary_10_1093_toxres_tfac028 crossref_primary_10_1016_j_etap_2024_104585 crossref_primary_10_1016_j_apsb_2025_07_026 crossref_primary_10_3389_fnins_2018_00111 crossref_primary_10_1038_s41573_021_00320_3 crossref_primary_10_1042_BJ20150274 crossref_primary_10_1016_j_brainres_2014_02_020 crossref_primary_10_1007_s13365_020_00906_4 crossref_primary_10_1016_j_nbd_2021_105400 crossref_primary_10_1186_s40064_014_0777_6 crossref_primary_10_3390_cells8111326 crossref_primary_10_1016_j_jhazmat_2022_128527 crossref_primary_10_1016_j_phrs_2016_09_004 crossref_primary_10_1016_j_biopha_2020_110601 crossref_primary_10_1186_s12974_016_0788_z crossref_primary_10_3390_ijms18061168 crossref_primary_10_1038_ncomms3753 crossref_primary_10_1111_jcmm_13285 crossref_primary_10_1007_s12035_016_9790_9 crossref_primary_10_3390_neuroglia6010012 crossref_primary_10_1038_s41598_021_88090_1 crossref_primary_10_1111_cns_12373 crossref_primary_10_1016_j_yexmp_2019_04_016 crossref_primary_10_1126_scitranslmed_3007641 crossref_primary_10_3390_ijms23010345 crossref_primary_10_1007_s12017_017_8467_5 crossref_primary_10_1002_ange_202213336 crossref_primary_10_1186_s13195_022_00996_8 crossref_primary_10_1016_j_bbadis_2017_06_003 crossref_primary_10_3390_ijms21238948 crossref_primary_10_1016_j_psyneuen_2018_05_029 crossref_primary_10_1093_hmg_ddt310 crossref_primary_10_1021_jacs_2c07225 crossref_primary_10_3390_ijms232113537 crossref_primary_10_1016_j_bbamcr_2018_08_012 crossref_primary_10_1002_jat_4083 crossref_primary_10_1007_s10072_024_07766_4 crossref_primary_10_1523_JNEUROSCI_2961_13_2013 crossref_primary_10_1016_j_trsl_2024_06_005 crossref_primary_10_1016_j_gene_2015_04_035 crossref_primary_10_1093_nsr_nwad233 crossref_primary_10_3390_ijms140918670 crossref_primary_10_3390_biom5021099 crossref_primary_10_1186_s13024_016_0129_9 crossref_primary_10_1093_brain_aww101 crossref_primary_10_1007_s12264_015_1544_6 crossref_primary_10_1186_s13059_023_03007_7 crossref_primary_10_1016_j_biomaterials_2018_08_046 crossref_primary_10_1186_s40478_016_0383_7 crossref_primary_10_1016_j_pharmthera_2013_07_010 crossref_primary_10_1159_000363387 crossref_primary_10_1007_s00401_015_1462_8 crossref_primary_10_1002_jemt_22790 crossref_primary_10_1038_nrd3976 crossref_primary_10_1002_da_22549 crossref_primary_10_1007_s11064_018_2581_0 crossref_primary_10_3390_ijms21186792 crossref_primary_10_1074_jbc_M117_780957 crossref_primary_10_3389_fnins_2018_00638 crossref_primary_10_1080_15548627_2017_1375633 crossref_primary_10_1007_s12035_020_01929_y crossref_primary_10_1111_febs_14422 crossref_primary_10_1007_s12035_021_02486_8 crossref_primary_10_1016_j_nbd_2014_11_005 crossref_primary_10_1016_j_arr_2020_101114 crossref_primary_10_1016_j_neubiorev_2014_10_019 crossref_primary_10_4103_1673_5374_280321 crossref_primary_10_1111_boc_201800023 crossref_primary_10_1016_j_biomaterials_2015_04_045 crossref_primary_10_1007_s13258_016_0495_2 crossref_primary_10_1007_s12017_015_8346_x crossref_primary_10_1002_jcb_28361 crossref_primary_10_3389_fphar_2019_00967 crossref_primary_10_1016_j_brainres_2019_146334 crossref_primary_10_1371_journal_pone_0234147 crossref_primary_10_3390_antiox10060983 crossref_primary_10_1111_cns_12205 crossref_primary_10_1155_2018_4670210 crossref_primary_10_1016_j_clim_2016_09_014 crossref_primary_10_1177_1535370214553772 crossref_primary_10_1186_alzrt260 crossref_primary_10_1111_acel_12801 crossref_primary_10_3390_molecules22101692 crossref_primary_10_1016_j_gene_2016_05_018 crossref_primary_10_1016_j_neulet_2014_01_058 crossref_primary_10_1002_advs_202411720 crossref_primary_10_1038_s41419_021_04045_4 crossref_primary_10_1042_AN20120095 crossref_primary_10_1093_jnen_nlw009 crossref_primary_10_3171_2016_2_FOCUS15637 crossref_primary_10_1007_s12035_020_02202_y crossref_primary_10_1371_journal_pone_0178867 crossref_primary_10_1038_srep18929 crossref_primary_10_1371_journal_pgen_1008704 crossref_primary_10_1007_s00210_025_04480_6 crossref_primary_10_1080_10590501_2014_881648 crossref_primary_10_1038_s41419_022_05153_5 crossref_primary_10_3389_fphar_2025_1570125 crossref_primary_10_1016_j_pharmthera_2014_11_015 crossref_primary_10_1186_s13024_023_00665_w crossref_primary_10_1016_j_chembiol_2019_10_005 crossref_primary_10_1073_pnas_1321845111 crossref_primary_10_1111_nan_12260 crossref_primary_10_1016_j_mod_2015_04_001 crossref_primary_10_1007_s12035_015_9309_9 crossref_primary_10_1016_j_freeradbiomed_2013_10_013 crossref_primary_10_1016_j_yjmcc_2014_03_016 crossref_primary_10_1007_s12035_016_9777_6 crossref_primary_10_3389_fnins_2018_00669 crossref_primary_10_1016_j_neuroscience_2018_07_023 crossref_primary_10_3233_JAD_161266 crossref_primary_10_2147_JIR_S319023 crossref_primary_10_1002_ange_202101468 crossref_primary_10_1038_s41598_017_16570_4 crossref_primary_10_1097_j_pain_0000000000001161 crossref_primary_10_1016_j_expneurol_2023_114629 crossref_primary_10_1016_j_freeradbiomed_2016_04_006 crossref_primary_10_3390_ijms24032381 crossref_primary_10_3389_fncel_2017_00410 crossref_primary_10_1371_journal_pgen_1003998 crossref_primary_10_3390_life15060945 crossref_primary_10_3389_fmolb_2023_1169658 crossref_primary_10_3389_fphys_2021_729925 crossref_primary_10_1016_j_bbrc_2013_06_057 crossref_primary_10_1016_j_bbadis_2014_07_009 crossref_primary_10_1186_s12974_016_0527_5 crossref_primary_10_1016_j_brainresbull_2016_11_006 crossref_primary_10_1111_bph_13095 crossref_primary_10_1111_nep_13145 crossref_primary_10_1002_anie_202213336 crossref_primary_10_1016_j_nbd_2019_104520 crossref_primary_10_1111_jnc_13991 crossref_primary_10_1002_ajmg_a_61184 crossref_primary_10_3390_ijms141122067 crossref_primary_10_1016_j_nano_2016_11_001 crossref_primary_10_3390_cells7060056 crossref_primary_10_3390_ijms20194666 crossref_primary_10_1016_j_nbd_2014_02_011 crossref_primary_10_1177_0271678X16650218 crossref_primary_10_3390_cells7060054 crossref_primary_10_1038_nrn3689 crossref_primary_10_1002_cm_21294 crossref_primary_10_1038_cdd_2017_35 crossref_primary_10_3389_fninf_2018_00026 crossref_primary_10_1016_j_neulet_2016_10_031 crossref_primary_10_1016_j_intimp_2024_113205 crossref_primary_10_1016_j_mehy_2016_01_022 crossref_primary_10_1111_jphp_12267 crossref_primary_10_1007_s00018_021_03907_6 crossref_primary_10_1016_j_phrs_2020_104702 crossref_primary_10_4103_1673_5374_257529 crossref_primary_10_3389_fneur_2020_588548 crossref_primary_10_1007_s00281_013_0373_9 crossref_primary_10_1038_ncomms10332 crossref_primary_10_1016_j_freeradbiomed_2021_04_025 crossref_primary_10_1155_2013_256404 crossref_primary_10_1016_j_ceca_2014_02_005 crossref_primary_10_1007_s12035_014_9029_6 crossref_primary_10_1515_hsz_2020_0167 crossref_primary_10_1016_j_brainresbull_2017_08_007 crossref_primary_10_1016_j_biopha_2016_05_001 crossref_primary_10_1074_jbc_RA120_012614 crossref_primary_10_1177_09603271241251447 crossref_primary_10_1016_j_exger_2019_02_011 crossref_primary_10_1002_mds_25744 crossref_primary_10_1038_s41598_017_06012_6 crossref_primary_10_1007_s41061_023_00446_5 crossref_primary_10_3390_molecules201219865 crossref_primary_10_1371_journal_pone_0093258 crossref_primary_10_1007_s12031_015_0685_4 crossref_primary_10_3109_00207454_2015_1059836 crossref_primary_10_3389_fneur_2019_00297 crossref_primary_10_1016_j_neuint_2021_105104 crossref_primary_10_1080_17435390_2016_1214761 crossref_primary_10_1002_glia_23802 crossref_primary_10_1089_ars_2016_6759 crossref_primary_10_3389_fnins_2021_660714 crossref_primary_10_1002_ana_24170 crossref_primary_10_1002_biof_1171 crossref_primary_10_1016_j_bbr_2024_114969 crossref_primary_10_1371_journal_ppat_1004946 crossref_primary_10_1111_bph_13651 crossref_primary_10_1093_toxres_tfae158 crossref_primary_10_1007_s12035_013_8527_2 crossref_primary_10_1016_j_arr_2022_101774 crossref_primary_10_1038_srep13666 crossref_primary_10_1016_j_neurobiolaging_2014_11_021 crossref_primary_10_1007_s11726_023_1402_4 crossref_primary_10_1016_j_neuint_2013_09_020 crossref_primary_10_1002_jat_4367 crossref_primary_10_1016_j_tox_2019_152245 crossref_primary_10_1007_s12035_014_8813_7 crossref_primary_10_1039_c5mt00049a crossref_primary_10_1042_BSR20221443 crossref_primary_10_1016_j_bbi_2016_05_010 crossref_primary_10_3390_ijms18040854 crossref_primary_10_1016_j_exer_2013_09_019 crossref_primary_10_1038_s41598_024_61844_3 crossref_primary_10_1016_j_freeradbiomed_2013_05_014 crossref_primary_10_1016_j_pharmthera_2021_107848 crossref_primary_10_1038_cddis_2014_354 crossref_primary_10_1371_journal_pone_0090803 crossref_primary_10_1128_MCB_00980_14 crossref_primary_10_1038_s41398_022_01862_9 crossref_primary_10_1093_ijnp_pyx030 crossref_primary_10_1038_aps_2016_75 crossref_primary_10_1039_c3mt20264j crossref_primary_10_4161_auto_32136 crossref_primary_10_1007_s12640_016_9671_z crossref_primary_10_1146_annurev_pathol_012513_104649 crossref_primary_10_1007_s12035_015_9682_4 crossref_primary_10_1016_j_fct_2016_04_021 crossref_primary_10_1111_jcmm_14479 crossref_primary_10_1016_j_nlm_2018_05_004 crossref_primary_10_1093_jb_mvx047 crossref_primary_10_1016_j_arr_2019_02_001 crossref_primary_10_1111_tra_12647 crossref_primary_10_1007_s12264_019_00411_7 crossref_primary_10_1007_s40263_025_01217_0 crossref_primary_10_1134_S0006297921070063 crossref_primary_10_3389_fnmol_2018_00086 crossref_primary_10_1177_1744806919876150 crossref_primary_10_1038_nrn3494 crossref_primary_10_1016_j_biopha_2022_113936 crossref_primary_10_1007_s10495_015_1142_0 crossref_primary_10_1371_journal_pone_0117412 crossref_primary_10_3390_jfb13040260 crossref_primary_10_1038_srep21145 crossref_primary_10_1155_2013_674751 crossref_primary_10_15252_embj_201592224 crossref_primary_10_3390_ijms21114121 crossref_primary_10_1016_j_transproceed_2014_04_016 crossref_primary_10_3390_ijms140612411 crossref_primary_10_1016_j_jep_2024_119016 crossref_primary_10_1016_j_lfs_2025_123875 crossref_primary_10_1513_AnnalsATS_201506_358KV crossref_primary_10_3390_biomedicines10082009 crossref_primary_10_3390_cells9122581 crossref_primary_10_1016_S1674_6384_16_60006_0 crossref_primary_10_4103_NRR_NRR_D_24_00044 crossref_primary_10_1016_j_bpj_2014_06_032 crossref_primary_10_1074_jbc_RA119_008263 crossref_primary_10_1038_srep15015 crossref_primary_10_1038_nchembio_1664 crossref_primary_10_1016_j_nano_2016_02_009 crossref_primary_10_1007_s00294_020_01090_y crossref_primary_10_1016_j_toxlet_2015_02_004 crossref_primary_10_1089_ars_2014_6122 crossref_primary_10_1089_neu_2015_4348 crossref_primary_10_1016_j_freeradbiomed_2017_08_003 crossref_primary_10_1186_2051_5960_1_24 crossref_primary_10_1371_journal_pone_0136620 crossref_primary_10_1016_j_toxlet_2020_01_019 crossref_primary_10_1016_j_tins_2016_01_008 crossref_primary_10_1155_2014_527518 crossref_primary_10_1186_s12974_019_1620_3 crossref_primary_10_3390_ijms20215421 crossref_primary_10_3390_ijms23020584 crossref_primary_10_3389_fnagi_2020_00274 crossref_primary_10_1038_tp_2015_123 crossref_primary_10_1038_s42003_021_02873_w crossref_primary_10_1371_journal_pone_0232111 crossref_primary_10_1007_s11064_016_2076_9 crossref_primary_10_1016_j_freeradbiomed_2014_08_028 crossref_primary_10_1039_D1FO01963E crossref_primary_10_1016_j_neuroscience_2014_03_047 |
| Cites_doi | 10.1074/jbc.M109.027102 10.1093/brain/awp267 10.1093/hmg/ddp464 10.1146/annurev.cellbio.18.011402.160624 10.1074/jbc.M109.020891 10.1016/j.bbrc.2007.01.043 10.1371/journal.pbio.0050290 10.1038/cdd.2010.142 10.1016/j.brainres.2005.04.058 10.1523/JNEUROSCI.18-02-00731.1998 10.1038/43894 10.1016/j.yexcr.2007.12.025 10.1152/physrev.00015.2006 10.1038/ng764 10.1038/cdd.2010.82 10.1111/j.1471-4159.2005.03428.x 10.1016/j.bbrc.2006.03.173 10.1111/j.1471-4159.2010.07143.x 10.1038/ncb0805-766 10.1007/s00401-005-1038-0 10.1038/nn1603 10.1083/jcb.200711066 10.1083/jcb.200809125 10.1097/00004647-200304000-00010 10.1111/j.1471-4159.2006.03838.x 10.1124/jpet.104.069088 10.1371/journal.pone.0010489 10.1074/jbc.M110.156430 10.1016/j.neulet.2005.12.038 10.1073/pnas.0509227103 10.1179/016164107X229803 10.1172/JCI29571 10.1186/1750-1326-6-81 10.1523/JNEUROSCI.2422-09.2010 10.1016/j.neuint.2009.12.005 10.1016/S1534-5807(03)00022-4 10.1038/nature11058 10.1128/MCB.24.6.2352-2363.2004 10.1002/glia.20242 10.1016/j.neuint.2009.01.010 10.1016/j.neuron.2007.12.021 10.1093/hmg/ddi396 10.1101/gad.1250704 10.1038/sj.jcbfm.9600005 10.1038/70265 10.1016/j.brainres.2010.06.016 10.1271/bbb.100622 10.1016/j.exger.2006.01.013 10.1093/hmg/ddq266 10.1016/j.tins.2008.06.005 10.1083/jcb.200310015 10.1385/JMN:28:2:111 10.1016/j.neuint.2010.10.006 10.1038/85463 10.1016/j.neuint.2010.12.010 10.1002/jnr.21648 10.1126/science.1060627 10.1523/JNEUROSCI.5367-11.2012 10.1016/j.expneurol.2007.04.009 10.1016/B978-0-12-396456-4.00003-1 10.1523/JNEUROSCI.5232-07.2008 10.1101/gad.1830709 10.1016/j.neuron.2008.09.008 10.3233/JAD-2010-1360 10.1172/JCI39678 10.1016/S0306-4522(02)00910-7 10.1083/jcb.200508099 10.1016/j.neuint.2010.03.017 10.1101/gad.1640108 10.1111/j.1471-4159.2009.06188.x 10.1016/j.brainresbull.2010.10.004 10.1007/s00439-005-0024-x 10.1007/s12640-009-9110-5 10.1093/brain/awl044 10.1126/science.1104882 10.1016/j.brainres.2004.12.051 10.1016/S0968-0004(96)10073-6 10.1046/j.1471-4159.2001.00462.x 10.1038/nature06022 10.1371/journal.pone.0019339 10.1124/pr.110.003814 10.1016/j.ceca.2010.01.003 10.1126/science.1101902 10.1523/JNEUROSCI.4289-06.2007 10.1074/jbc.M109.010744 10.1111/j.1471-4159.2008.05392.x 10.1016/S0169-328X(01)00256-X 10.1016/S0006-8993(01)03229-2 10.2353/ajpath.2009.080814 10.1016/S0896-6273(02)01045-0 10.1038/ncb1213 10.1111/j.1471-4159.2004.02555.x 10.1111/j.1471-4159.2006.04440.x 10.1186/1750-1326-5-56 10.1016/j.molcel.2004.08.025 10.1038/16729 10.1097/NEN.0b013e3181d44992 10.1074/jbc.M109.018325 10.1111/j.1471-4159.2005.03276.x 10.1086/503116 10.1038/77060 10.1046/j.1471-4159.2002.01165.x 10.1016/S1097-2765(03)00105-9 10.1038/sj.cdd.4401365 10.1016/j.brainres.2008.11.104 10.1093/hmg/ddr100 10.1016/j.cmet.2005.03.004 10.1242/jcs.087510 10.1021/cb100321m 10.1016/j.brainres.2006.02.095 10.1016/j.neuroscience.2007.04.017 10.1038/ng0298-106 10.1093/hmg/ddq546 10.1016/j.brainres.2004.11.058 10.1016/j.neuron.2008.10.047 10.1126/science.1201396 10.1073/pnas.1115623109 10.1126/science.1190354 10.1074/jbc.M111.272617 10.1016/j.neuroscience.2011.01.012 10.1093/hmg/ddn041 10.1038/415092a 10.3858/emm.2010.42.5.040 10.1016/j.devcel.2008.06.015 10.1016/j.neuron.2010.11.010 10.1016/j.neulet.2010.10.071 10.1006/exnr.1998.7002 10.1073/pnas.0707906105 10.1016/j.mito.2010.10.007 10.1038/33416 10.1097/01.jnen.0000218445.30535.6f 10.1038/sj.cdd.4402276 10.1038/ng1620 10.1101/gad.1673408 10.1016/j.neuroscience.2007.10.047 10.1038/nn.2297 |
| ContentType | Journal Article |
| Copyright | 2013 Elsevier Ltd Elsevier Ltd Copyright © 2013 Elsevier Ltd. All rights reserved. Attribution |
| Copyright_xml | – notice: 2013 Elsevier Ltd – notice: Elsevier Ltd – notice: Copyright © 2013 Elsevier Ltd. All rights reserved. – notice: Attribution |
| DBID | AAYXX CITATION CGR CUY CVF ECM EIF NPM 3V. 7RV 7TK 7X7 7XB 88E 88G 8AO 8C2 8FI 8FJ 8FK ABUWG AFKRA AZQEC BENPR CCPQU DWQXO FYUFA GHDGH GNUQQ K9. KB0 M0S M1P M2M NAPCQ PHGZM PHGZT PJZUB PKEHL PPXIY PQEST PQQKQ PQUKI PRINS PSYQQ Q9U 7X8 1XC VOOES |
| DOI | 10.1016/S1474-4422(12)70238-7 |
| DatabaseName | CrossRef Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed ProQuest Central (Corporate) Nursing & Allied Health Database Neurosciences Abstracts Health & Medical Collection ProQuest Central (purchase pre-March 2016) Medical Database (Alumni Edition) Psychology Database (Alumni) ProQuest Pharma Collection Lancet Titles Hospital Premium Collection Hospital Premium Collection (Alumni Edition) ProQuest Central (Alumni) (purchase pre-March 2016) ProQuest Central (Alumni Edition) ProQuest Central UK/Ireland ProQuest Central Essentials ProQuest Central ProQuest One Community College ProQuest Central Korea Health Research Premium Collection Health Research Premium Collection (Alumni) ProQuest Central Student ProQuest Health & Medical Complete (Alumni) Nursing & Allied Health Database (Alumni Edition) Health & Medical Collection (Alumni Edition) Medical Database Psychology Database Nursing & Allied Health Premium ProQuest Central Premium ProQuest One Academic (New) ProQuest Health & Medical Research Collection ProQuest One Academic Middle East (New) ProQuest One Health & Nursing ProQuest One Academic Eastern Edition (DO NOT USE) ProQuest One Academic (retired) ProQuest One Academic UKI Edition ProQuest Central China ProQuest One Psychology ProQuest Central Basic MEDLINE - Academic Hyper Article en Ligne (HAL) Hyper Article en Ligne (HAL) (Open Access) |
| DatabaseTitle | CrossRef MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) ProQuest One Psychology ProQuest Central Student ProQuest One Academic Middle East (New) ProQuest Central Essentials Lancet Titles ProQuest Health & Medical Complete (Alumni) ProQuest Central (Alumni Edition) ProQuest One Community College ProQuest One Health & Nursing ProQuest Pharma Collection ProQuest Central China ProQuest Central ProQuest Health & Medical Research Collection Health Research Premium Collection Health and Medicine Complete (Alumni Edition) ProQuest Central Korea Health & Medical Research Collection ProQuest Central (New) ProQuest Medical Library (Alumni) ProQuest Central Basic ProQuest One Academic Eastern Edition ProQuest Nursing & Allied Health Source ProQuest Hospital Collection Health Research Premium Collection (Alumni) ProQuest Psychology Journals (Alumni) Neurosciences Abstracts ProQuest Hospital Collection (Alumni) Nursing & Allied Health Premium ProQuest Health & Medical Complete ProQuest Medical Library ProQuest Psychology Journals ProQuest One Academic UKI Edition ProQuest Nursing & Allied Health Source (Alumni) ProQuest One Academic ProQuest One Academic (New) ProQuest Central (Alumni) MEDLINE - Academic |
| DatabaseTitleList | MEDLINE - Academic Neurosciences Abstracts MEDLINE ProQuest One Psychology |
| Database_xml | – sequence: 1 dbid: NPM name: PubMed url: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: 7RV name: Nursing & allied health premium. url: https://search.proquest.com/nahs sourceTypes: Aggregation Database |
| DeliveryMethod | fulltext_linktorsrc |
| Discipline | Medicine |
| EISSN | 1474-4465 |
| EndPage | 118 |
| ExternalDocumentID | oai:HAL:inserm-01296824v1 2839238881 23237905 10_1016_S1474_4422_12_70238_7 S1474442212702387 1_s2_0_S1474442212702387 |
| Genre | Research Support, Non-U.S. Gov't Journal Article Review |
| GrantInformation_xml | – fundername: Telethon grantid: GGP11057 – fundername: Medical Research Council grantid: G0601840 – fundername: Wellcome Trust grantid: 100140 – fundername: Medical Research Council grantid: G0700990 – fundername: Wellcome Trust grantid: 089703 – fundername: Medical Research Council grantid: G1002610 – fundername: Medical Research Council grantid: G0901786 – fundername: Wellcome Trust grantid: G1002610 |
| GroupedDBID | --- --K --M -RU .1- .FO 0R~ 123 1B1 1P~ 1~5 29L 4.4 457 4G. 53G 5VS 7-5 71M 7RV 7X7 88E 8AO 8C2 8FI 8FJ AAEDT AAEDW AAIKJ AAKOC AALRI AAMRU AAQFI AAQQT AATTM AAXKI AAXLA AAXUO AAYWO ABBQC ABCQJ ABIVO ABJNI ABMAC ABMZM ABOCM ABTEW ABUWG ABWVN ACGFS ACIEU ACLOT ACPRK ACRLP ACRPL ACVFH ADBBV ADCNI ADMUD ADNMO AEIPS AEKER AENEX AEUPX AEVXI AFKRA AFPUW AFRHN AFTJW AFXIZ AGHFR AGWIK AHMBA AIGII AIIUN AITUG AJRQY AJUYK AKBMS AKRWK AKYEP ALMA_UNASSIGNED_HOLDINGS AMRAJ ANZVX APXCP AXJTR AZQEC BENPR BKEYQ BKOJK BNPGV BPHCQ BVXVI CCPQU CS3 DU5 DWQXO EBS EFJIC EFKBS EJD EO8 EO9 EP2 EP3 EX3 F5P FDB FEDTE FIRID FNPLU FYGXN FYUFA G-Q GBLVA GNUQQ HF~ HMCUK HVGLF HZ~ IHE J1W JCF KOM M1P M2M M41 MO0 N9A NAPCQ O-L O9- OP~ OZT P-8 P-9 P2P PC. PHGZM PHGZT PJZUB PPXIY PQQKQ PROAC PSQYO PSYQQ ROL RPZ SDG SEL SES SPCBC SSH SSN SSZ T5K TLN UHS UKHRP UV1 WOW XBR Z5R ~HD 3V. AACTN AFCTW AFKWA AJOXV ALIPV AMFUW RIG SDF AADPK ABLVK ABYKQ AJBFU ZA5 9DU AAYXX AFFHD CITATION AGCQF AGRNS CGR CUY CVF ECM EIF NPM 7TK 7XB 8FK K9. PKEHL PQEST PQUKI PRINS Q9U 7X8 PUEGO 1XC VOOES |
| ID | FETCH-LOGICAL-c619t-25e31c31b4e550b99368c88de57920fd1f47a014cd6eeec14ea9d71faefdf01e3 |
| IEDL.DBID | BENPR |
| ISICitedReferencesCount | 383 |
| ISICitedReferencesURI | http://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=Summon&SrcAuth=ProQuest&DestLinkType=CitingArticles&DestApp=WOS_CPL&KeyUT=000312429400025&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D |
| ISSN | 1474-4422 1474-4465 |
| IngestDate | Tue Oct 14 20:30:10 EDT 2025 Wed Oct 01 10:38:32 EDT 2025 Sun Sep 28 02:19:31 EDT 2025 Mon Oct 06 16:55:47 EDT 2025 Mon Jul 21 05:29:34 EDT 2025 Sat Nov 29 03:40:56 EST 2025 Tue Nov 18 21:19:04 EST 2025 Fri Feb 23 02:28:59 EST 2024 Sun Feb 23 10:18:51 EST 2025 Tue Oct 14 19:33:17 EDT 2025 |
| IsDoiOpenAccess | true |
| IsOpenAccess | true |
| IsPeerReviewed | true |
| IsScholarly | true |
| Issue | 1 |
| Language | English |
| License | https://www.elsevier.com/tdm/userlicense/1.0 Copyright © 2013 Elsevier Ltd. All rights reserved. Attribution: http://creativecommons.org/licenses/by |
| LinkModel | DirectLink |
| MergedId | FETCHMERGED-LOGICAL-c619t-25e31c31b4e550b99368c88de57920fd1f47a014cd6eeec14ea9d71faefdf01e3 |
| Notes | SourceType-Scholarly Journals-1 content type line 14 ObjectType-Feature-4 ObjectType-Undefined-1 ObjectType-Review-2 ObjectType-Article-3 ObjectType-Article-1 ObjectType-Feature-2 ObjectType-Review-3 content type line 23 ObjectType-Article-2 ObjectType-Feature-1 |
| ORCID | 0000-0003-0575-8112 |
| OpenAccessLink | https://inserm.hal.science/inserm-01296824 |
| PMID | 23237905 |
| PQID | 1237170089 |
| PQPubID | 26255 |
| PageCount | 14 |
| ParticipantIDs | hal_primary_oai_HAL_inserm_01296824v1 proquest_miscellaneous_1272732764 proquest_miscellaneous_1239061171 proquest_journals_1237170089 pubmed_primary_23237905 crossref_citationtrail_10_1016_S1474_4422_12_70238_7 crossref_primary_10_1016_S1474_4422_12_70238_7 elsevier_sciencedirect_doi_10_1016_S1474_4422_12_70238_7 elsevier_clinicalkeyesjournals_1_s2_0_S1474442212702387 elsevier_clinicalkey_doi_10_1016_S1474_4422_12_70238_7 |
| PublicationCentury | 2000 |
| PublicationDate | January 2013 2013 2013-01-00 2013-Jan 20130101 2013-01 |
| PublicationDateYYYYMMDD | 2013-01-01 |
| PublicationDate_xml | – month: 01 year: 2013 text: January 2013 |
| PublicationDecade | 2010 |
| PublicationPlace | England |
| PublicationPlace_xml | – name: England – name: London |
| PublicationTitle | Lancet neurology |
| PublicationTitleAlternate | Lancet Neurol |
| PublicationYear | 2013 |
| Publisher | Elsevier Ltd Elsevier Limited Elsevier |
| Publisher_xml | – name: Elsevier Ltd – name: Elsevier Limited – name: Elsevier |
| References | Hayashi, Hamakawa, Nagotani (bib82) 2005; 1037 Hetz, Thielen, Matus (bib127) 2009; 23 Lin, Bailey, Ho (bib16) 2007; 117 Resende, Ferreiro, Pereira, Oliveira (bib21) 2008; 86 Wang, Agnello, Sotolongo, Segatori (bib53) 2011; 6 Kruger, Kuhn, Muller (bib123) 1998; 18 Inden, Kitamura, Takeuchi (bib33) 2007; 101 Sokka, Putkonen, Mudo (bib99) 2007; 27 Bezprozvanny, Mattson (bib112) 2008; 31 Nunziante, Ackermann, Dietrich (bib7) 2011; 286 Harding, Calfon, Urano, Novoa, Ron (bib71) 2002; 18 Mori, Yamashita, Uchino (bib128) 2011; 58 Kondo, Murakami, Tatsumi (bib74) 2005; 7 Zhao, Longo-Guess, Harris, Lee, Ackerman (bib18) 2005; 37 Stutzmann, Mattson (bib25) 2011; 63 Qi, Okuma, Hosoi, Nomura (bib88) 2004; 311 Song, Lee, Kam (bib23) 2008; 182 Shimura, Schlossmacher, Hattori (bib122) 2001; 293 Moreno, Radford, Peretti (bib9) 2012; 485 Calfon, Zeng, Urano (bib75) 2002; 415 Harding, Zhang, Zeng (bib68) 2003; 11 Tajiri, Oyadomari, Yano (bib94) 2004; 11 Sasaki (bib39) 2010; 69 Katayama, Imaizumi, Sato (bib103) 1999; 1 Quaglio, Restelli, Garofoli (bib5) 2011; 6 Morimoto, Oida, Shimazawa (bib81) 2007; 147 Kudo, Okumura, Imaizumi (bib113) 2006; 344 Kumar, Krause, Yoshida, Mori, DeGracia (bib92) 2003; 23 Wang, Popko, Roos (bib45) 2011; 20 Jiang, Gan, Ebrahim, Lin, Melrose, Yen (bib135) 2010; 5 Duennwald, Lindquist (bib35) 2008; 22 Narendra, Tanaka, Suen, Youle (bib121) 2008; 183 Zhu, Fenik, Zhan, Sanfillipo-Cohn, Naidoo, Veasey (bib59) 2008; 28 Meusser, Hirsch, Jarosch, Sommer (bib77) 2005; 7 D'Urso, Prior, Greiner-Petter, Gabreels-Festen, Muller (bib14) 1998; 18 Bouman, Schlierf, Lutz (bib30) 2011; 18 Li, Hayashi, Jin (bib134) 2005; 1048 Reijonen, Putkonen, Norremolle, Lindholm, Korhonen (bib136) 2008; 314 Southwood, Garbern, Jiang, Gow (bib13) 2002; 36 Maurin, Jousse, Averous (bib70) 2005; 1 Owen, Kumar, Zhang, McGrath, Cavener, Krause (bib64) 2005; 94 Kieran, Woods, Villunger, Strasser, Prehn (bib41) 2007; 104 Shimura, Hattori, Kubo (bib120) 2000; 25 Marciniak, Ron (bib61) 2006; 86 Hoozemans, van Haastert, Eikelenboom, de Vos, Rozemuller, Scheper (bib118) 2007; 354 Silva, Ries, Oo (bib28) 2005; 95 Colla, Coune, Liu (bib32) 2012; 32 Dalton, Healey, Irving, Marciniak (bib67) 2012; 106 Saxena, Cabuy, Caroni (bib44) 2009; 12 Hoozemans, van Haastert, Nijholt, Rozemuller, Eikelenboom, Scheper (bib20) 2009; 174 Szydlowska, Tymianski (bib83) 2010; 47 Pennuto, Tinelli, Malaguti (bib15) 2008; 57 Cross, Bond, Sadowski (bib138) 2012; 109 Hao, Sharp, Ross-Inta (bib69) 2005; 307 Saltini, Dominici, Lovati (bib114) 2006; 398 Oida, Shimazawa, Imaizumi, Hara (bib55) 2008; 151 Hitomi, Katayama, Eguchi (bib91) 2004; 165 Carnemolla, Fossale, Agostoni (bib125) 2009; 284 Coe, Michalak (bib84) 2009; 28 Hayashi, Saito, Okuno, Ferrand-Drake, Dodd, Chan (bib95) 2005; 25 Miranda, MacLeod, Davies (bib130) 2008; 17 Pahl, Baeuerle (bib131) 1997; 22 Boyce, Bryant, Jousse (bib72) 2005; 307 Luheshi, Tartaglia, Brorsson (bib102) 2007; 5 Harding, Zhang, Zeng (bib66) 2003; 11 Hara, Kamiya, Adachi (bib34) 2011; 58 Egawa, Yamamoto, Inoue (bib116) 2011; 286 Yamamoto, Tashiro, Imoto (bib137) 2011; 75 Yoshida, Matsui, Hosokawa, Kaufman, Nagata, Mori (bib79) 2003; 4 Kitada, Asakawa, Hattori (bib119) 1998; 392 Walker, Farg, Bye, McLean, Horne, Atkin (bib42) 2010; 133 Honjo, Ito, Horibe, Takahashi, Kawakami (bib4) 2010; 1349 Marciniak, Garcia-Bonilla, Hu, Harding, Ron (bib65) 2006; 172 Lee, Won, Suh (bib3) 2010; 42 Dossena, Imeri, Mangieri (bib6) 2008; 60 Zhao, Rosales, Seburn, Ron, Ackerman (bib19) 2010; 19 Lin, Kemper, Dupree, Harding, Ron, Popko (bib17) 2006; 129 Jin, Sanjo, Uchihara (bib24) 2010; 20 Hidvegi, Ewing, Hale (bib132) 2010; 329 Althausen, Mengesdorf, Mies (bib87) 2001; 78 Bauereis, Haskins, Lebaron, Renthal (bib115) 2011; 488 Urushitani, Sik, Sakurai, Nukina, Takahashi, Julien (bib126) 2006; 9 Lee, Lee, Lee (bib22) 2010; 5 Sado, Yamasaki, Iwanaga (bib27) 2009; 1257 Chigurupati, Wei, Belal (bib117) 2009; 284 Tsaytler, Harding, Ron, Bertolotti (bib73) 2011; 332 Paschen, Hayashi, Saito, Chan (bib97) 2004; 90 Nagata, Ilieva, Murakami (bib43) 2007; 29 Marciniak, Yun, Oyadomari (bib62) 2004; 18 Davis, Shrimpton, Holohan (bib129) 1999; 401 Ouyang, Xu, Emery, Lee, Giffard (bib57) 2011; 11 Kantor, Harding, Ron (bib10) 2005; 118 Chen, Burdette, Porter (bib52) 2010; 19 Bellucci, Navarria, Zaltieri (bib31) 2011; 116 Nishitoh, Kadowaki, Nagai (bib46) 2008; 22 Shibata, Hattori, Sasaki, Gotoh, Hamada, Fukuuchi (bib89) 2003; 118 Kang, Lu, Guan (bib49) 2011; 18 Penas, Verdu, Asensio-Pinilla (bib60) 2011; 178 Bennett, Shaler, Woodman (bib37) 2007; 448 Haynes, Titus, Cooper (bib78) 2004; 15 Osada, Kosuge, Ishige, Ito (bib56) 2010; 57 Rane, Kang, Chakrabarti, Feigenbaum, Hegde (bib8) 2008; 15 Ghribi, Herman, DeWitt, Forbes, Savory (bib108) 2001; 96 Hoozemans, Stieler, van Haastert (bib105) 2006; 41 Chihara, Saito, Murakami (bib93) 2009; 110 McCaig, Imai, Gallagher (bib98) 2005; 1034 Kikuchi, Almer, Yamashita (bib40) 2006; 103 Osada, Kosuge, Kihara, Ishige, Ito (bib54) 2009; 54 Unterberger, Hoftberger, Gelpi, Flicker, Budka, Voigtlander (bib106) 2006; 65 Benavides, Pastor, Santos, Tranque, Calvo (bib96) 2005; 52 Milhavet, Martindale, Camandola (bib111) 2002; 83 Tamatani, Matsuyama, Yamaguchi (bib101) 2001; 7 Casas-Tinto, Zhang, Sanchez-Garcia, Gomez-Velazquez, Rincon-Limas, Fernandez-Funez (bib110) 2011; 20 Fonseca, Ishigaki, Oslowski (bib51) 2010; 120 Smith, Jiang, Pei (bib124) 2005; 14 Harding, Zhang, Ron (bib63) 1999; 397 Hosoi, Ogawa, Ozawa (bib76) 2010; 56 O'Connor, Sadleir, Maus (bib26) 2008; 60 Chen, Wu, Lvovskaya, Herndon, Supnet, Bezprozvanny (bib133) 2011; 6 Liu, Guo, Guo, Zhao, Gong, Zhao (bib50) 2011; 84 Hoozemans, Veerhuis, Van Haastert (bib104) 2005; 110 Xue, Daly, Yngvadottir (bib90) 2006; 78 Dukes, Van Laar, Cascio, Hastings (bib29) 2008; 106 Seyb, Ansar, Bean, Michaelis (bib107) 2006; 28 Yu, Luo, Fu, Mattson (bib100) 1999; 155 Kroeger, Miranda, MacLeod (bib48) 2009; 284 Zhang, Liu, Hu (bib86) 2006; 98 Higo, Hamada, Hisatsune (bib38) 2010; 68 Schapansky, Olson, Van Der Ploeg, Glazner (bib109) 2007; 208 Kaneko, Koike, Saito, Kitamura, Okuma, Nomura (bib2) 2010; 30 Nakka, Gusain, Raghubir (bib1) 2010; 17 Richardson, Mohammad, Pavitt (bib12) 2004; 24 Lajoie, Snapp (bib36) 2011; 124 Leegwater, Vermeulen, Konst (bib11) 2001; 29 Davies, Miranda, Roussel, Kaufman, Marciniak, Lomas (bib47) 2009; 284 Nguyen, Wang, Perry (bib85) 2002; 924 Kudo, Kanemoto, Hara (bib58) 2008; 15 Rissanen, Sivenius, Jolkkonen (bib80) 2006; 1087 Rane (10.1016/S1474-4422(12)70238-7_bib8) 2008; 15 Marciniak (10.1016/S1474-4422(12)70238-7_bib65) 2006; 172 Song (10.1016/S1474-4422(12)70238-7_bib23) 2008; 182 Nishitoh (10.1016/S1474-4422(12)70238-7_bib46) 2008; 22 Pahl (10.1016/S1474-4422(12)70238-7_bib131) 1997; 22 Benavides (10.1016/S1474-4422(12)70238-7_bib96) 2005; 52 Carnemolla (10.1016/S1474-4422(12)70238-7_bib125) 2009; 284 Kitada (10.1016/S1474-4422(12)70238-7_bib119) 1998; 392 Richardson (10.1016/S1474-4422(12)70238-7_bib12) 2004; 24 Bauereis (10.1016/S1474-4422(12)70238-7_bib115) 2011; 488 Dalton (10.1016/S1474-4422(12)70238-7_bib67) 2012; 106 Bellucci (10.1016/S1474-4422(12)70238-7_bib31) 2011; 116 Haynes (10.1016/S1474-4422(12)70238-7_bib78) 2004; 15 Reijonen (10.1016/S1474-4422(12)70238-7_bib136) 2008; 314 Lajoie (10.1016/S1474-4422(12)70238-7_bib36) 2011; 124 Unterberger (10.1016/S1474-4422(12)70238-7_bib106) 2006; 65 Dossena (10.1016/S1474-4422(12)70238-7_bib6) 2008; 60 Ouyang (10.1016/S1474-4422(12)70238-7_bib57) 2011; 11 Mori (10.1016/S1474-4422(12)70238-7_bib128) 2011; 58 Sado (10.1016/S1474-4422(12)70238-7_bib27) 2009; 1257 Boyce (10.1016/S1474-4422(12)70238-7_bib72) 2005; 307 Egawa (10.1016/S1474-4422(12)70238-7_bib116) 2011; 286 Hoozemans (10.1016/S1474-4422(12)70238-7_bib20) 2009; 174 Saltini (10.1016/S1474-4422(12)70238-7_bib114) 2006; 398 Tsaytler (10.1016/S1474-4422(12)70238-7_bib73) 2011; 332 Hayashi (10.1016/S1474-4422(12)70238-7_bib82) 2005; 1037 Smith (10.1016/S1474-4422(12)70238-7_bib124) 2005; 14 Bezprozvanny (10.1016/S1474-4422(12)70238-7_bib112) 2008; 31 Marciniak (10.1016/S1474-4422(12)70238-7_bib62) 2004; 18 Harding (10.1016/S1474-4422(12)70238-7_bib68) 2003; 11 Kruger (10.1016/S1474-4422(12)70238-7_bib123) 1998; 18 Southwood (10.1016/S1474-4422(12)70238-7_bib13) 2002; 36 Davis (10.1016/S1474-4422(12)70238-7_bib129) 1999; 401 Tamatani (10.1016/S1474-4422(12)70238-7_bib101) 2001; 7 D'Urso (10.1016/S1474-4422(12)70238-7_bib14) 1998; 18 Saxena (10.1016/S1474-4422(12)70238-7_bib44) 2009; 12 Chihara (10.1016/S1474-4422(12)70238-7_bib93) 2009; 110 Hayashi (10.1016/S1474-4422(12)70238-7_bib95) 2005; 25 Chen (10.1016/S1474-4422(12)70238-7_bib133) 2011; 6 Lin (10.1016/S1474-4422(12)70238-7_bib16) 2007; 117 Walker (10.1016/S1474-4422(12)70238-7_bib42) 2010; 133 Hao (10.1016/S1474-4422(12)70238-7_bib69) 2005; 307 Ghribi (10.1016/S1474-4422(12)70238-7_bib108) 2001; 96 Kudo (10.1016/S1474-4422(12)70238-7_bib58) 2008; 15 Lee (10.1016/S1474-4422(12)70238-7_bib22) 2010; 5 Li (10.1016/S1474-4422(12)70238-7_bib134) 2005; 1048 Zhao (10.1016/S1474-4422(12)70238-7_bib18) 2005; 37 Nakka (10.1016/S1474-4422(12)70238-7_bib1) 2010; 17 Kaneko (10.1016/S1474-4422(12)70238-7_bib2) 2010; 30 Inden (10.1016/S1474-4422(12)70238-7_bib33) 2007; 101 Hara (10.1016/S1474-4422(12)70238-7_bib34) 2011; 58 Milhavet (10.1016/S1474-4422(12)70238-7_bib111) 2002; 83 Nunziante (10.1016/S1474-4422(12)70238-7_bib7) 2011; 286 Sasaki (10.1016/S1474-4422(12)70238-7_bib39) 2010; 69 Hosoi (10.1016/S1474-4422(12)70238-7_bib76) 2010; 56 Sokka (10.1016/S1474-4422(12)70238-7_bib99) 2007; 27 Zhao (10.1016/S1474-4422(12)70238-7_bib19) 2010; 19 Luheshi (10.1016/S1474-4422(12)70238-7_bib102) 2007; 5 Katayama (10.1016/S1474-4422(12)70238-7_bib103) 1999; 1 Miranda (10.1016/S1474-4422(12)70238-7_bib130) 2008; 17 Leegwater (10.1016/S1474-4422(12)70238-7_bib11) 2001; 29 Casas-Tinto (10.1016/S1474-4422(12)70238-7_bib110) 2011; 20 Narendra (10.1016/S1474-4422(12)70238-7_bib121) 2008; 183 Shibata (10.1016/S1474-4422(12)70238-7_bib89) 2003; 118 Harding (10.1016/S1474-4422(12)70238-7_bib71) 2002; 18 Kudo (10.1016/S1474-4422(12)70238-7_bib113) 2006; 344 Cross (10.1016/S1474-4422(12)70238-7_bib138) 2012; 109 Meusser (10.1016/S1474-4422(12)70238-7_bib77) 2005; 7 Kieran (10.1016/S1474-4422(12)70238-7_bib41) 2007; 104 Kondo (10.1016/S1474-4422(12)70238-7_bib74) 2005; 7 Duennwald (10.1016/S1474-4422(12)70238-7_bib35) 2008; 22 Liu (10.1016/S1474-4422(12)70238-7_bib50) 2011; 84 Hetz (10.1016/S1474-4422(12)70238-7_bib127) 2009; 23 Kumar (10.1016/S1474-4422(12)70238-7_bib92) 2003; 23 Chen (10.1016/S1474-4422(12)70238-7_bib52) 2010; 19 Rissanen (10.1016/S1474-4422(12)70238-7_bib80) 2006; 1087 Wang (10.1016/S1474-4422(12)70238-7_bib53) 2011; 6 Moreno (10.1016/S1474-4422(12)70238-7_bib9) 2012; 485 Maurin (10.1016/S1474-4422(12)70238-7_bib70) 2005; 1 Jin (10.1016/S1474-4422(12)70238-7_bib24) 2010; 20 McCaig (10.1016/S1474-4422(12)70238-7_bib98) 2005; 1034 Davies (10.1016/S1474-4422(12)70238-7_bib47) 2009; 284 Yamamoto (10.1016/S1474-4422(12)70238-7_bib137) 2011; 75 O'Connor (10.1016/S1474-4422(12)70238-7_bib26) 2008; 60 Higo (10.1016/S1474-4422(12)70238-7_bib38) 2010; 68 Hitomi (10.1016/S1474-4422(12)70238-7_bib91) 2004; 165 Kantor (10.1016/S1474-4422(12)70238-7_bib10) 2005; 118 Coe (10.1016/S1474-4422(12)70238-7_bib84) 2009; 28 Yoshida (10.1016/S1474-4422(12)70238-7_bib79) 2003; 4 Osada (10.1016/S1474-4422(12)70238-7_bib56) 2010; 57 Silva (10.1016/S1474-4422(12)70238-7_bib28) 2005; 95 Chigurupati (10.1016/S1474-4422(12)70238-7_bib117) 2009; 284 Lin (10.1016/S1474-4422(12)70238-7_bib17) 2006; 129 Fonseca (10.1016/S1474-4422(12)70238-7_bib51) 2010; 120 Bouman (10.1016/S1474-4422(12)70238-7_bib30) 2011; 18 Oida (10.1016/S1474-4422(12)70238-7_bib55) 2008; 151 Hoozemans (10.1016/S1474-4422(12)70238-7_bib118) 2007; 354 Shimura (10.1016/S1474-4422(12)70238-7_bib120) 2000; 25 Nagata (10.1016/S1474-4422(12)70238-7_bib43) 2007; 29 Jiang (10.1016/S1474-4422(12)70238-7_bib135) 2010; 5 Calfon (10.1016/S1474-4422(12)70238-7_bib75) 2002; 415 Zhang (10.1016/S1474-4422(12)70238-7_bib86) 2006; 98 Zhu (10.1016/S1474-4422(12)70238-7_bib59) 2008; 28 Hoozemans (10.1016/S1474-4422(12)70238-7_bib105) 2006; 41 Pennuto (10.1016/S1474-4422(12)70238-7_bib15) 2008; 57 Hoozemans (10.1016/S1474-4422(12)70238-7_bib104) 2005; 110 Quaglio (10.1016/S1474-4422(12)70238-7_bib5) 2011; 6 Lee (10.1016/S1474-4422(12)70238-7_bib3) 2010; 42 Dukes (10.1016/S1474-4422(12)70238-7_bib29) 2008; 106 Xue (10.1016/S1474-4422(12)70238-7_bib90) 2006; 78 Penas (10.1016/S1474-4422(12)70238-7_bib60) 2011; 178 Schapansky (10.1016/S1474-4422(12)70238-7_bib109) 2007; 208 Osada (10.1016/S1474-4422(12)70238-7_bib54) 2009; 54 Paschen (10.1016/S1474-4422(12)70238-7_bib97) 2004; 90 Seyb (10.1016/S1474-4422(12)70238-7_bib107) 2006; 28 Morimoto (10.1016/S1474-4422(12)70238-7_bib81) 2007; 147 Stutzmann (10.1016/S1474-4422(12)70238-7_bib25) 2011; 63 Wang (10.1016/S1474-4422(12)70238-7_bib45) 2011; 20 Tajiri (10.1016/S1474-4422(12)70238-7_bib94) 2004; 11 Resende (10.1016/S1474-4422(12)70238-7_bib21) 2008; 86 Hidvegi (10.1016/S1474-4422(12)70238-7_bib132) 2010; 329 Nguyen (10.1016/S1474-4422(12)70238-7_bib85) 2002; 924 Yu (10.1016/S1474-4422(12)70238-7_bib100) 1999; 155 Honjo (10.1016/S1474-4422(12)70238-7_bib4) 2010; 1349 Kang (10.1016/S1474-4422(12)70238-7_bib49) 2011; 18 Urushitani (10.1016/S1474-4422(12)70238-7_bib126) 2006; 9 Shimura (10.1016/S1474-4422(12)70238-7_bib122) 2001; 293 Colla (10.1016/S1474-4422(12)70238-7_bib32) 2012; 32 Harding (10.1016/S1474-4422(12)70238-7_bib66) 2003; 11 Harding (10.1016/S1474-4422(12)70238-7_bib63) 1999; 397 Kroeger (10.1016/S1474-4422(12)70238-7_bib48) 2009; 284 Marciniak (10.1016/S1474-4422(12)70238-7_bib61) 2006; 86 Bennett (10.1016/S1474-4422(12)70238-7_bib37) 2007; 448 Szydlowska (10.1016/S1474-4422(12)70238-7_bib83) 2010; 47 Kikuchi (10.1016/S1474-4422(12)70238-7_bib40) 2006; 103 Owen (10.1016/S1474-4422(12)70238-7_bib64) 2005; 94 Althausen (10.1016/S1474-4422(12)70238-7_bib87) 2001; 78 Qi (10.1016/S1474-4422(12)70238-7_bib88) 2004; 311 |
| References_xml | – volume: 117 start-page: 448 year: 2007 end-page: 456 ident: bib16 article-title: The integrated stress response prevents demyelination by protecting oligodendrocytes against immune-mediated damage publication-title: J Clin Invest – volume: 24 start-page: 2352 year: 2004 end-page: 2363 ident: bib12 article-title: Mutations causing childhood ataxia with central nervous system hypomyelination reduce eukaryotic initiation factor 2B complex formation and activity publication-title: Mol Cell Biol – volume: 90 start-page: 694 year: 2004 end-page: 701 ident: bib97 article-title: GADD34 protein levels increase after transient ischemia in the cortex but not in the CA1 subfield: implications for post-ischemic recovery of protein synthesis in ischemia-resistant cells publication-title: J Neurochem – volume: 397 start-page: 271 year: 1999 end-page: 274 ident: bib63 article-title: Translation and protein folding are coupled by an endoplasmic reticulum resident kinase publication-title: Nature – volume: 109 start-page: E869 year: 2012 end-page: E878 ident: bib138 article-title: The molecular basis for selective inhibition of unconventional mRNA splicing by an IRE1-binding small molecule publication-title: Proc Natl Acad Sci USA – volume: 96 start-page: 30 year: 2001 end-page: 38 ident: bib108 article-title: Aβ(1-42) and aluminum induce stress in the endoplasmic reticulum in rabbit hippocampus, involving nuclear translocation of gadd 153 and NF-κB publication-title: Brain Res Mol Brain Res – volume: 98 start-page: 102 year: 2006 end-page: 112 ident: bib86 article-title: Irreversible aggregation of protein synthesis machinery after focal brain ischemia publication-title: J Neurochem – volume: 54 start-page: 403 year: 2009 end-page: 409 ident: bib54 article-title: Apolipoprotein E-deficient mice are more vulnerable to ER stress after transient forebrain ischemia publication-title: Neurochem Int – volume: 293 start-page: 263 year: 2001 end-page: 269 ident: bib122 article-title: Ubiquitination of a new form of α-synuclein by parkin from human brain: implications for Parkinson's disease publication-title: Science – volume: 314 start-page: 950 year: 2008 end-page: 960 ident: bib136 article-title: Inhibition of endoplasmic reticulum stress counteracts neuronal cell death and protein aggregation caused by N-terminal mutant huntingtin proteins publication-title: Exp Cell Res – volume: 104 start-page: 20606 year: 2007 end-page: 20611 ident: bib41 article-title: Deletion of the BH3-only protein puma protects motoneurons from ER stress-induced apoptosis and delays motoneuron loss in ALS mice publication-title: Proc Natl Acad Sci USA – volume: 284 start-page: 18202 year: 2009 end-page: 18209 ident: bib47 article-title: Neuroserpin polymers activate NF-κB by a calcium signalling pathway that is independent of the unfolded protein response publication-title: J Biol Chem – volume: 329 start-page: 229 year: 2010 end-page: 232 ident: bib132 article-title: An autophagy-enhancing drug promotes degradation of mutant α publication-title: Science – volume: 15 start-page: 359 year: 2008 end-page: 370 ident: bib8 article-title: Reduced translocation of nascent prion protein during ER stress contributes to neurodegeneration publication-title: Dev Cell – volume: 1 start-page: 273 year: 2005 end-page: 277 ident: bib70 article-title: The GCN2 kinase biases feeding behavior to maintain amino acid homeostasis in omnivores publication-title: Cell Metab – volume: 332 start-page: 91 year: 2011 end-page: 94 ident: bib73 article-title: Selective inhibition of a regulatory subunit of protein phosphatase 1 restores proteostasis publication-title: Science – volume: 415 start-page: 92 year: 2002 end-page: 96 ident: bib75 article-title: IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA publication-title: Nature – volume: 11 start-page: 403 year: 2004 end-page: 415 ident: bib94 article-title: Ischemia-induced neuronal cell death is mediated by the endoplasmic reticulum stress pathway involving CHOP publication-title: Cell Death Differ – volume: 23 start-page: 462 year: 2003 end-page: 471 ident: bib92 article-title: Dysfunction of the unfolded protein response during global brain ischemia and reperfusion publication-title: J Cereb Blood Flow Metab – volume: 485 start-page: 507 year: 2012 end-page: 511 ident: bib9 article-title: Sustained translational repression by eIF2α-P mediates prion neurodegeneration publication-title: Nature – volume: 29 start-page: 767 year: 2007 end-page: 771 ident: bib43 article-title: Increased ER stress during motor neuron degeneration in a transgenic mouse model of amyotrophic lateral sclerosis publication-title: Neurol Res – volume: 95 start-page: 974 year: 2005 end-page: 986 ident: bib28 article-title: CHOP/GADD153 is a mediator of apoptotic death in substantia nigra dopamine neurons in an in vivo neurotoxin model of parkinsonism publication-title: J Neurochem – volume: 124 start-page: 3332 year: 2011 end-page: 3343 ident: bib36 article-title: Changes in BiP availability reveal hypersensitivity to acute endoplasmic reticulum stress in cells expressing mutant huntingtin publication-title: J Cell Sci – volume: 15 start-page: 767 year: 2004 end-page: 776 ident: bib78 article-title: Degradation of misfolded proteins prevents ER-derived oxidative stress and cell death publication-title: Mol Cell – volume: 18 start-page: 731 year: 1998 end-page: 740 ident: bib14 article-title: Overloaded endoplasmic reticulum-Golgi compartments, a possible pathomechanism of peripheral neuropathies caused by mutations of the peripheral myelin protein PMP22 publication-title: J Neurosci – volume: 344 start-page: 525 year: 2006 end-page: 530 ident: bib113 article-title: Altered localization of amyloid precursor protein under endoplasmic reticulum stress publication-title: Biochem Biophys Res Commun – volume: 9 start-page: 108 year: 2006 end-page: 118 ident: bib126 article-title: Chromogranin-mediated secretion of mutant superoxide dismutase proteins linked to amyotrophic lateral sclerosis publication-title: Nat Neurosci – volume: 18 start-page: 3066 year: 2004 end-page: 3077 ident: bib62 article-title: CHOP induces death by promoting protein synthesis and oxidation in the stressed endoplasmic reticulum publication-title: Genes Dev – volume: 7 start-page: 186 year: 2005 end-page: 194 ident: bib74 article-title: OASIS, a CREB/ATF-family member, modulates UPR signalling in astrocytes publication-title: Nat Cell Biol – volume: 448 start-page: 704 year: 2007 end-page: 708 ident: bib37 article-title: Global changes to the ubiquitin system in Huntington's disease publication-title: Nature – volume: 286 start-page: 7947 year: 2011 end-page: 7957 ident: bib116 article-title: The endoplasmic reticulum stress sensor, ATF6α, protects against neurotoxin-induced dopaminergic neuronal death publication-title: J Biol Chem – volume: 37 start-page: 974 year: 2005 end-page: 979 ident: bib18 article-title: Protein accumulation and neurodegeneration in the woozy mutant mouse is caused by disruption of SIL1, a cochaperone of BiP publication-title: Nat Genet – volume: 147 start-page: 957 year: 2007 end-page: 967 ident: bib81 article-title: Involvement of endoplasmic reticulum stress after middle cerebral artery occlusion in mice publication-title: Neuroscience – volume: 6 start-page: 81 year: 2011 ident: bib133 article-title: Dantrolene is neuroprotective in Huntington's disease transgenic mouse model publication-title: Mol Neurodegener – volume: 56 start-page: 216 year: 2010 end-page: 220 ident: bib76 article-title: Homocysteine induces X-box-binding protein 1 splicing in the mice brain publication-title: Neurochem Int – volume: 6 start-page: 158 year: 2011 end-page: 168 ident: bib53 article-title: Ca2+ homeostasis modulation enhances the amenability of L444P glucosylcerebrosidase to proteostasis regulation in patient-derived fibroblasts publication-title: ACS Chem Biol – volume: 11 start-page: 279 year: 2011 end-page: 286 ident: bib57 article-title: Overexpressing GRP78 influences Ca2+ handling and function of mitochondria in astrocytes after ischemia-like stress publication-title: Mitochondrion – volume: 20 start-page: 261 year: 2010 end-page: 273 ident: bib24 article-title: Presenilin-1 holoprotein is an interacting partner of sarco endoplasmic reticulum calcium-ATPase and confers resistance to endoplasmic reticulum stress publication-title: J Alzheimers Dis – volume: 118 start-page: 491 year: 2003 end-page: 499 ident: bib89 article-title: Activation of caspase-12 by endoplasmic reticulum stress induced by transient middle cerebral artery occlusion in mice publication-title: Neuroscience – volume: 86 start-page: 2091 year: 2008 end-page: 2099 ident: bib21 article-title: ER stress is involved in Aβ-induced GSK-3β activation and tau phosphorylation publication-title: J Neurosci Res – volume: 20 start-page: 2144 year: 2011 end-page: 2160 ident: bib110 article-title: The ER stress factor XBP1s prevents amyloid-β neurotoxicity publication-title: Hum Mol Genet – volume: 42 start-page: 386 year: 2010 end-page: 394 ident: bib3 article-title: Induction of the unfolded protein response and cell death pathway in Alzheimer's disease, but not in aged Tg2576 mice publication-title: Exp Mol Med – volume: 28 start-page: F96 year: 2009 end-page: 103 ident: bib84 article-title: Calcium binding chaperones of the endoplasmic reticulum publication-title: Gen Physiol Biophys – volume: 488 start-page: 11 year: 2011 end-page: 16 ident: bib115 article-title: Proteomic insights into the protective mechanisms of an in vitro oxidative stress model of early stage Parkinson's disease publication-title: Neurosci Lett – volume: 57 start-page: 393 year: 2008 end-page: 405 ident: bib15 article-title: Ablation of the UPR-mediator CHOP restores motor function and reduces demyelination in Charcot-Marie-Tooth 1B mice publication-title: Neuron – volume: 58 start-page: 35 year: 2011 end-page: 43 ident: bib34 article-title: Endoplasmic reticulum stress inducers provide protection against 6-hydroxydopamine-induced cytotoxicity publication-title: Neurochem Int – volume: 11 start-page: 619 year: 2003 end-page: 633 ident: bib68 article-title: An integrated stress response regulates amino acid metabolism and resistance to oxidative stress publication-title: Mol Cell – volume: 83 start-page: 673 year: 2002 end-page: 681 ident: bib111 article-title: Involvement of Gadd153 in the pathogenic action of presenilin-1 mutations publication-title: J Neurochem – volume: 106 start-page: 333 year: 2008 end-page: 346 ident: bib29 article-title: Changes in endoplasmic reticulum stress proteins and aldolase A in cells exposed to dopamine publication-title: J Neurochem – volume: 57 start-page: 1 year: 2010 end-page: 7 ident: bib56 article-title: Characterization of neuronal and astroglial responses to ER stress in the hippocampal CA1 area in mice following transient forebrain ischemia publication-title: Neurochem Int – volume: 118 start-page: 99 year: 2005 end-page: 106 ident: bib10 article-title: Heightened stress response in primary fibroblasts expressing mutant eIF2B genes from CACH/VWM leukodystrophy patients publication-title: Hum Genet – volume: 174 start-page: 1241 year: 2009 end-page: 1251 ident: bib20 article-title: The unfolded protein response is activated in pretangle neurons in Alzheimer's disease hippocampus publication-title: Am J Pathol – volume: 1034 start-page: 51 year: 2005 end-page: 61 ident: bib98 article-title: Evolution of GADD34 expression after focal cerebral ischaemia publication-title: Brain Res – volume: 84 start-page: 94 year: 2011 end-page: 102 ident: bib50 article-title: Involvement of IRE1α signaling in the hippocampus in patients with mesial temporal lobe epilepsy publication-title: Brain Res Bull – volume: 11 start-page: 619 year: 2003 end-page: 633 ident: bib66 article-title: An integrated stress response regulates amino acid metabolism and resistance to oxidative stress publication-title: Mol Cell – volume: 31 start-page: 454 year: 2008 end-page: 463 ident: bib112 article-title: Neuronal calcium mishandling and the pathogenesis of Alzheimer's disease publication-title: Trends Neurosci – volume: 18 start-page: 769 year: 2011 end-page: 782 ident: bib30 article-title: Parkin is transcriptionally regulated by ATF4: evidence for an interconnection between mitochondrial stress and ER stress publication-title: Cell Death Differ – volume: 398 start-page: 53 year: 2006 end-page: 58 ident: bib114 article-title: A novel polymorphism in SEL1L confers susceptibility to Alzheimer's disease publication-title: Neurosci Lett – volume: 60 start-page: 598 year: 2008 end-page: 609 ident: bib6 article-title: Mutant prion protein expression causes motor and memory deficits and abnormal sleep patterns in a transgenic mouse model publication-title: Neuron – volume: 284 start-page: 18167 year: 2009 end-page: 18173 ident: bib125 article-title: Rrs1 is involved in endoplasmic reticulum stress response in Huntington disease publication-title: J Biol Chem – volume: 307 start-page: 1776 year: 2005 end-page: 1778 ident: bib69 article-title: Uncharged tRNA and sensing of amino acid deficiency in mammalian piriform cortex publication-title: Science – volume: 110 start-page: 956 year: 2009 end-page: 965 ident: bib93 article-title: Increased vulnerability of hippocampal pyramidal neurons to the toxicity of kainic acid in OASIS-deficient mice publication-title: J Neurochem – volume: 19 start-page: 3502 year: 2010 end-page: 3515 ident: bib52 article-title: The early-onset torsion dystonia-associated protein, torsinA, is a homeostatic regulator of endoplasmic reticulum stress response publication-title: Hum Mol Genet – volume: 165 start-page: 347 year: 2004 end-page: 356 ident: bib91 article-title: Involvement of caspase-4 in endoplasmic reticulum stress-induced apoptosis and Aβ-induced cell death publication-title: J Cell Biol – volume: 354 start-page: 707 year: 2007 end-page: 711 ident: bib118 article-title: Activation of the unfolded protein response in Parkinson's disease publication-title: Biochem Biophys Res Commun – volume: 17 start-page: 189 year: 2010 end-page: 202 ident: bib1 article-title: Endoplasmic reticulum stress plays critical role in brain damage after cerebral ischemia/reperfusion in rats publication-title: Neurotox Res – volume: 22 start-page: 1451 year: 2008 end-page: 1464 ident: bib46 article-title: ALS-linked mutant SOD1 induces ER stress- and ASK1-dependent motor neuron death by targeting Derlin-1 publication-title: Genes Dev – volume: 110 start-page: 165 year: 2005 end-page: 172 ident: bib104 article-title: The unfolded protein response is activated in Alzheimer's disease publication-title: Acta Neuropathol – volume: 25 start-page: 302 year: 2000 end-page: 305 ident: bib120 article-title: Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase publication-title: Nat Genet – volume: 106 start-page: 189 year: 2012 end-page: 221 ident: bib67 article-title: Phosphoproteins in stress-induced disease publication-title: Prog Mol Biol Transl Sci – volume: 151 start-page: 109 year: 2008 end-page: 111 ident: bib55 article-title: Involvement of endoplasmic reticulum stress in the neuronal death induced by transient forebrain ischemia in gerbil publication-title: Neuroscience – volume: 172 start-page: 201 year: 2006 end-page: 209 ident: bib65 article-title: Activation-dependent substrate recruitment by the eukaryotic translation initiation factor 2 kinase PERK publication-title: J Cell Biol – volume: 129 start-page: 1306 year: 2006 end-page: 1318 ident: bib17 article-title: Interferon-γ inhibits central nervous system remyelination through a process modulated by endoplasmic reticulum stress publication-title: Brain – volume: 20 start-page: 1008 year: 2011 end-page: 1015 ident: bib45 article-title: The unfolded protein response in familial amyotrophic lateral sclerosis publication-title: Hum Mol Genet – volume: 63 start-page: 700 year: 2011 end-page: 727 ident: bib25 article-title: Endoplasmic reticulum Ca publication-title: Pharmacol Rev – volume: 101 start-page: 1491 year: 2007 end-page: 1504 ident: bib33 article-title: Neurodegeneration of mouse nigrostriatal dopaminergic system induced by repeated oral administration of rotenone is prevented by 4-phenylbutyrate, a chemical chaperone publication-title: J Neurochem – volume: 75 start-page: 284 year: 2011 end-page: 288 ident: bib137 article-title: Quinotrierixin inhibited ER stress-induced XBP1 mRNA splicing through inhibition of protein synthesis publication-title: Biosci Biotechnol Biochem – volume: 7 start-page: 317 year: 2001 end-page: 323 ident: bib101 article-title: ORP150 protects against hypoxia/ischemia-induced neuronal death publication-title: Nat Med – volume: 25 start-page: 41 year: 2005 end-page: 53 ident: bib95 article-title: Damage to the endoplasmic reticulum and activation of apoptotic machinery by oxidative stress in ischemic neurons publication-title: J Cereb Blood Flow Metab – volume: 28 start-page: 2168 year: 2008 end-page: 2178 ident: bib59 article-title: Eif-2a protects brainstem motoneurons in a murine model of sleep apnea publication-title: J Neurosci – volume: 401 start-page: 376 year: 1999 end-page: 379 ident: bib129 article-title: Familial dementia caused by polymerization of mutant neuroserpin publication-title: Nature – volume: 284 start-page: 18323 year: 2009 end-page: 18333 ident: bib117 article-title: The homocysteine-inducible endoplasmic reticulum stress protein counteracts calcium store depletion and induction of CCAAT enhancer-binding protein homologous protein in a neurotoxin model of Parkinson disease publication-title: J Biol Chem – volume: 47 start-page: 122 year: 2010 end-page: 129 ident: bib83 article-title: Calcium, ischemia and excitotoxicity publication-title: Cell Calcium – volume: 27 start-page: 901 year: 2007 end-page: 908 ident: bib99 article-title: Endoplasmic reticulum stress inhibition protects against excitotoxic neuronal injury in the rat brain publication-title: J Neurosci – volume: 178 start-page: 33 year: 2011 end-page: 44 ident: bib60 article-title: Valproate reduces CHOP levels and preserves oligodendrocytes and axons after spinal cord injury publication-title: Neuroscience – volume: 15 start-page: 364 year: 2008 end-page: 375 ident: bib58 article-title: A molecular chaperone inducer protects neurons from ER stress publication-title: Cell Death Differ – volume: 103 start-page: 6025 year: 2006 end-page: 6030 ident: bib40 article-title: Spinal cord endoplasmic reticulum stress associated with a microsomal accumulation of mutant superoxide dismutase-1 in an ALS model publication-title: Proc Natl Acad Sci USA – volume: 14 start-page: 3801 year: 2005 end-page: 3811 ident: bib124 article-title: Endoplasmic reticulum stress and mitochondrial cell death pathways mediate A53T mutant alpha-synuclein-induced toxicity publication-title: Hum Mol Genet – volume: 155 start-page: 302 year: 1999 end-page: 314 ident: bib100 article-title: The endoplasmic reticulum stress-responsive protein GRP78 protects neurons against excitotoxicity and apoptosis: suppression of oxidative stress and stabilization of calcium homeostasis publication-title: Exp Neurol – volume: 23 start-page: 2294 year: 2009 end-page: 2306 ident: bib127 article-title: XBP-1 deficiency in the nervous system protects against amyotrophic lateral sclerosis by increasing autophagy publication-title: Genes Dev – volume: 4 start-page: 265 year: 2003 end-page: 271 ident: bib79 article-title: A time-dependent phase shift in the Mammalian unfolded protein response publication-title: Dev Cell – volume: 78 start-page: 779 year: 2001 end-page: 787 ident: bib87 article-title: Changes in the phosphorylation of initiation factor eIF-2α, elongation factor eEF-2 and p70 S6 kinase after transient focal cerebral ischaemia in mice publication-title: J Neurochem – volume: 1257 start-page: 16 year: 2009 end-page: 24 ident: bib27 article-title: Protective effect against Parkinson's disease-related insults through the activation of XBP1 publication-title: Brain Res – volume: 5 start-page: 56 year: 2010 ident: bib135 article-title: ER stress response plays an important role in aggregation of α-synuclein publication-title: Mol Neurodegener – volume: 392 start-page: 605 year: 1998 end-page: 608 ident: bib119 article-title: Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism publication-title: Nature – volume: 307 start-page: 935 year: 2005 end-page: 939 ident: bib72 article-title: A selective inhibitor of eIF2α dephosphorylation protects cells from ER stress publication-title: Science – volume: 1087 start-page: 60 year: 2006 end-page: 66 ident: bib80 article-title: Prolonged bihemispheric alterations in unfolded protein response related gene expression after experimental stroke publication-title: Brain Res – volume: 28 start-page: 111 year: 2006 end-page: 123 ident: bib107 article-title: β-amyloid and endoplasmic reticulum stress responses in primary neurons: effects of drugs that interact with the cytoskeleton publication-title: J Mol Neurosci – volume: 1037 start-page: 52 year: 2005 end-page: 58 ident: bib82 article-title: HMG CoA reductase inhibitors reduce ischemic brain injury of Wistar rats through decreasing oxidative stress on neurons publication-title: Brain Res – volume: 22 start-page: 3308 year: 2008 end-page: 3319 ident: bib35 article-title: Impaired ERAD and ER stress are early and specific events in polyglutamine toxicity publication-title: Genes Dev – volume: 69 start-page: 346 year: 2010 end-page: 355 ident: bib39 article-title: Endoplasmic reticulum stress in motor neurons of the spinal cord in sporadic amyotrophic lateral sclerosis publication-title: J Neuropathol Exp Neurol – volume: 1048 start-page: 59 year: 2005 end-page: 68 ident: bib134 article-title: The protective effect of dantrolene on ischemic neuronal cell death is associated with reduced expression of endoplasmic reticulum stress markers publication-title: Brain Res – volume: 120 start-page: 744 year: 2010 end-page: 755 ident: bib51 article-title: Wolfram syndrome 1 gene negatively regulates ER stress signaling in rodent and human cells publication-title: J Clin Invest – volume: 5 start-page: e10489 year: 2010 ident: bib22 article-title: Activation of PERK signaling attenuates Aβ-mediated ER stress publication-title: PLoS One – volume: 7 start-page: 766 year: 2005 end-page: 772 ident: bib77 article-title: ERAD: the long road to destruction publication-title: Nat Cell Biol – volume: 183 start-page: 795 year: 2008 end-page: 803 ident: bib121 article-title: Parkin is recruited selectively to impaired mitochondria and promotes their autophagy publication-title: J Cell Biol – volume: 22 start-page: 63 year: 1997 end-page: 67 ident: bib131 article-title: The ER-overload response: activation of NF-κB publication-title: Trends Biochem Sci – volume: 12 start-page: 627 year: 2009 end-page: 636 ident: bib44 article-title: A role for motoneuron subtype-selective ER stress in disease manifestations of FALS mice publication-title: Nat Neurosci – volume: 1349 start-page: 90 year: 2010 end-page: 96 ident: bib4 article-title: Protein disulfide isomerase-immunopositive inclusions in patients with Alzheimer disease publication-title: Brain Res – volume: 36 start-page: 585 year: 2002 end-page: 596 ident: bib13 article-title: The unfolded protein response modulates disease severity in Pelizaeus-Mezbacher disease publication-title: Neuron – volume: 18 start-page: 575 year: 2002 end-page: 599 ident: bib71 article-title: Transcriptional and translational control in the mammalian unfolded protein response publication-title: Annu Rev Cell Dev Biol – volume: 60 start-page: 988 year: 2008 end-page: 1009 ident: bib26 article-title: Phosphorylation of the translation initiation factor eIF2α increases BACE1 levels and promotes amyloidogenesis publication-title: Neuron – volume: 65 start-page: 348 year: 2006 end-page: 357 ident: bib106 article-title: Endoplasmic reticulum stress features are prominent in Alzheimer disease but not in prion diseases in vivo publication-title: J Neuropathol Exp Neurol – volume: 284 start-page: 22793 year: 2009 end-page: 22802 ident: bib48 article-title: Endoplasmic reticulum-associated degradation (ERAD) and autophagy cooperate to degrade polymerogenic mutant serpins publication-title: J Biol Chem – volume: 311 start-page: 388 year: 2004 end-page: 393 ident: bib88 article-title: Edaravone protects against hypoxia/ischemia-induced endoplasmic reticulum dysfunction publication-title: J Pharmacol Exp Ther – volume: 86 start-page: 1133 year: 2006 end-page: 1149 ident: bib61 article-title: Endoplasmic reticulum stress signaling in disease publication-title: Physiol Rev – volume: 5 start-page: e290 year: 2007 ident: bib102 article-title: Systematic in vivo analysis of the intrinsic determinants of amyloid β pathogenicity publication-title: PLoS Biol – volume: 6 start-page: e19339 year: 2011 ident: bib5 article-title: Expression of mutant or cytosolic PrP in transgenic mice and cells is not associated with endoplasmic reticulum stress or proteasome dysfunction publication-title: PLoS One – volume: 286 start-page: 33942 year: 2011 end-page: 33953 ident: bib7 article-title: Proteasomal dysfunction and endoplasmic reticulum stress enhance trafficking of prion protein aggregates through the secretory pathway and increase accumulation of pathologic prion protein publication-title: J Biol Chem – volume: 19 start-page: 25 year: 2010 end-page: 35 ident: bib19 article-title: Alteration of the unfolded protein response modifies neurodegeneration in a mouse model of Marinesco-Sjögren syndrome publication-title: Hum Mol Genet – volume: 32 start-page: 3306 year: 2012 end-page: 3320 ident: bib32 article-title: Endoplasmic reticulum stress is important for the manifestations of α-synucleinopathy in vivo publication-title: J Neurosci – volume: 182 start-page: 675 year: 2008 end-page: 684 ident: bib23 article-title: E2-25K/Hip-2 regulates caspase-12 in ER stress-mediated Aβ neurotoxicity publication-title: J Cell Biol – volume: 17 start-page: 1527 year: 2008 end-page: 1539 ident: bib130 article-title: The intracellular accumulation of polymeric neuroserpin explains the severity of the dementia FENIB publication-title: Hum Mol Genet – volume: 924 start-page: 159 year: 2002 end-page: 166 ident: bib85 article-title: Depletion of intracellular calcium stores is toxic to SH-SY5Y neuronal cells publication-title: Brain Res – volume: 1 start-page: 479 year: 1999 end-page: 485 ident: bib103 article-title: Presenilin-1 mutations downregulate the signalling pathway of the unfolded-protein response publication-title: Nat Cell Biol – volume: 29 start-page: 383 year: 2001 end-page: 388 ident: bib11 article-title: Subunits of the translation initiation factor eIF2B are mutant in leukoencephalopathy with vanishing white matter publication-title: Nat Genet – volume: 41 start-page: 380 year: 2006 end-page: 386 ident: bib105 article-title: The unfolded protein response affects neuronal cell cycle protein expression: implications for Alzheimer's disease pathogenesis publication-title: Exp Gerontol – volume: 52 start-page: 261 year: 2005 end-page: 275 ident: bib96 article-title: CHOP plays a pivotal role in the astrocyte death induced by oxygen and glucose deprivation publication-title: Glia – volume: 18 start-page: 133 year: 2011 end-page: 144 ident: bib49 article-title: The TSC1 and TSC2 tumor suppressors are required for proper ER stress response and protect cells from ER stress-induced apoptosis publication-title: Cell Death Differ – volume: 58 start-page: 344 year: 2011 end-page: 353 ident: bib128 article-title: Derlin-1 overexpression ameliorates mutant SOD1-induced endoplasmic reticulum stress by reducing mutant SOD1 accumulation publication-title: Neurochem Int – volume: 68 start-page: 865 year: 2010 end-page: 878 ident: bib38 article-title: Mechanism of ER stress-induced brain damage by IP publication-title: Neuron – volume: 18 start-page: 106 year: 1998 end-page: 108 ident: bib123 article-title: Ala30Pro mutation in the gene encoding α-synuclein in Parkinson's disease publication-title: Nat Genet – volume: 116 start-page: 588 year: 2011 end-page: 605 ident: bib31 article-title: Induction of the unfolded protein response by α-synuclein in experimental models of Parkinson's disease publication-title: J Neurochem – volume: 30 start-page: 3924 year: 2010 end-page: 3932 ident: bib2 article-title: Loss of HRD1-mediated protein degradation causes amyloid precursor protein accumulation and amyloid-β generation publication-title: J Neurosci – volume: 78 start-page: 659 year: 2006 end-page: 670 ident: bib90 article-title: Spread of an inactive form of caspase-12 in humans is due to recent positive selection publication-title: Am J Hum Genet – volume: 133 start-page: 105 year: 2010 end-page: 116 ident: bib42 article-title: Protein disulphide isomerase protects against protein aggregation and is S-nitrosylated in amyotrophic lateral sclerosis publication-title: Brain – volume: 94 start-page: 1235 year: 2005 end-page: 1242 ident: bib64 article-title: PERK is responsible for the increased phosphorylation of eIF2α and the severe inhibition of protein synthesis after transient global brain ischemia publication-title: J Neurochem – volume: 208 start-page: 169 year: 2007 end-page: 176 ident: bib109 article-title: NF-κB activated by ER calcium release inhibits Aβ-mediated expression of CHOP protein: enhancement by AD-linked mutant presenilin 1 publication-title: Exp Neurol – volume: 284 start-page: 22793 year: 2009 ident: 10.1016/S1474-4422(12)70238-7_bib48 article-title: Endoplasmic reticulum-associated degradation (ERAD) and autophagy cooperate to degrade polymerogenic mutant serpins publication-title: J Biol Chem doi: 10.1074/jbc.M109.027102 – volume: 133 start-page: 105 year: 2010 ident: 10.1016/S1474-4422(12)70238-7_bib42 article-title: Protein disulphide isomerase protects against protein aggregation and is S-nitrosylated in amyotrophic lateral sclerosis publication-title: Brain doi: 10.1093/brain/awp267 – volume: 19 start-page: 25 year: 2010 ident: 10.1016/S1474-4422(12)70238-7_bib19 article-title: Alteration of the unfolded protein response modifies neurodegeneration in a mouse model of Marinesco-Sjögren syndrome publication-title: Hum Mol Genet doi: 10.1093/hmg/ddp464 – volume: 18 start-page: 575 year: 2002 ident: 10.1016/S1474-4422(12)70238-7_bib71 article-title: Transcriptional and translational control in the mammalian unfolded protein response publication-title: Annu Rev Cell Dev Biol doi: 10.1146/annurev.cellbio.18.011402.160624 – volume: 284 start-page: 18323 year: 2009 ident: 10.1016/S1474-4422(12)70238-7_bib117 article-title: The homocysteine-inducible endoplasmic reticulum stress protein counteracts calcium store depletion and induction of CCAAT enhancer-binding protein homologous protein in a neurotoxin model of Parkinson disease publication-title: J Biol Chem doi: 10.1074/jbc.M109.020891 – volume: 354 start-page: 707 year: 2007 ident: 10.1016/S1474-4422(12)70238-7_bib118 article-title: Activation of the unfolded protein response in Parkinson's disease publication-title: Biochem Biophys Res Commun doi: 10.1016/j.bbrc.2007.01.043 – volume: 5 start-page: e290 year: 2007 ident: 10.1016/S1474-4422(12)70238-7_bib102 article-title: Systematic in vivo analysis of the intrinsic determinants of amyloid β pathogenicity publication-title: PLoS Biol doi: 10.1371/journal.pbio.0050290 – volume: 18 start-page: 769 year: 2011 ident: 10.1016/S1474-4422(12)70238-7_bib30 article-title: Parkin is transcriptionally regulated by ATF4: evidence for an interconnection between mitochondrial stress and ER stress publication-title: Cell Death Differ doi: 10.1038/cdd.2010.142 – volume: 1048 start-page: 59 year: 2005 ident: 10.1016/S1474-4422(12)70238-7_bib134 article-title: The protective effect of dantrolene on ischemic neuronal cell death is associated with reduced expression of endoplasmic reticulum stress markers publication-title: Brain Res doi: 10.1016/j.brainres.2005.04.058 – volume: 18 start-page: 731 year: 1998 ident: 10.1016/S1474-4422(12)70238-7_bib14 article-title: Overloaded endoplasmic reticulum-Golgi compartments, a possible pathomechanism of peripheral neuropathies caused by mutations of the peripheral myelin protein PMP22 publication-title: J Neurosci doi: 10.1523/JNEUROSCI.18-02-00731.1998 – volume: 401 start-page: 376 year: 1999 ident: 10.1016/S1474-4422(12)70238-7_bib129 article-title: Familial dementia caused by polymerization of mutant neuroserpin publication-title: Nature doi: 10.1038/43894 – volume: 314 start-page: 950 year: 2008 ident: 10.1016/S1474-4422(12)70238-7_bib136 article-title: Inhibition of endoplasmic reticulum stress counteracts neuronal cell death and protein aggregation caused by N-terminal mutant huntingtin proteins publication-title: Exp Cell Res doi: 10.1016/j.yexcr.2007.12.025 – volume: 86 start-page: 1133 year: 2006 ident: 10.1016/S1474-4422(12)70238-7_bib61 article-title: Endoplasmic reticulum stress signaling in disease publication-title: Physiol Rev doi: 10.1152/physrev.00015.2006 – volume: 29 start-page: 383 year: 2001 ident: 10.1016/S1474-4422(12)70238-7_bib11 article-title: Subunits of the translation initiation factor eIF2B are mutant in leukoencephalopathy with vanishing white matter publication-title: Nat Genet doi: 10.1038/ng764 – volume: 18 start-page: 133 year: 2011 ident: 10.1016/S1474-4422(12)70238-7_bib49 article-title: The TSC1 and TSC2 tumor suppressors are required for proper ER stress response and protect cells from ER stress-induced apoptosis publication-title: Cell Death Differ doi: 10.1038/cdd.2010.82 – volume: 95 start-page: 974 year: 2005 ident: 10.1016/S1474-4422(12)70238-7_bib28 article-title: CHOP/GADD153 is a mediator of apoptotic death in substantia nigra dopamine neurons in an in vivo neurotoxin model of parkinsonism publication-title: J Neurochem doi: 10.1111/j.1471-4159.2005.03428.x – volume: 344 start-page: 525 year: 2006 ident: 10.1016/S1474-4422(12)70238-7_bib113 article-title: Altered localization of amyloid precursor protein under endoplasmic reticulum stress publication-title: Biochem Biophys Res Commun doi: 10.1016/j.bbrc.2006.03.173 – volume: 116 start-page: 588 year: 2011 ident: 10.1016/S1474-4422(12)70238-7_bib31 article-title: Induction of the unfolded protein response by α-synuclein in experimental models of Parkinson's disease publication-title: J Neurochem doi: 10.1111/j.1471-4159.2010.07143.x – volume: 7 start-page: 766 year: 2005 ident: 10.1016/S1474-4422(12)70238-7_bib77 article-title: ERAD: the long road to destruction publication-title: Nat Cell Biol doi: 10.1038/ncb0805-766 – volume: 110 start-page: 165 year: 2005 ident: 10.1016/S1474-4422(12)70238-7_bib104 article-title: The unfolded protein response is activated in Alzheimer's disease publication-title: Acta Neuropathol doi: 10.1007/s00401-005-1038-0 – volume: 9 start-page: 108 year: 2006 ident: 10.1016/S1474-4422(12)70238-7_bib126 article-title: Chromogranin-mediated secretion of mutant superoxide dismutase proteins linked to amyotrophic lateral sclerosis publication-title: Nat Neurosci doi: 10.1038/nn1603 – volume: 182 start-page: 675 year: 2008 ident: 10.1016/S1474-4422(12)70238-7_bib23 article-title: E2-25K/Hip-2 regulates caspase-12 in ER stress-mediated Aβ neurotoxicity publication-title: J Cell Biol doi: 10.1083/jcb.200711066 – volume: 183 start-page: 795 year: 2008 ident: 10.1016/S1474-4422(12)70238-7_bib121 article-title: Parkin is recruited selectively to impaired mitochondria and promotes their autophagy publication-title: J Cell Biol doi: 10.1083/jcb.200809125 – volume: 23 start-page: 462 year: 2003 ident: 10.1016/S1474-4422(12)70238-7_bib92 article-title: Dysfunction of the unfolded protein response during global brain ischemia and reperfusion publication-title: J Cereb Blood Flow Metab doi: 10.1097/00004647-200304000-00010 – volume: 98 start-page: 102 year: 2006 ident: 10.1016/S1474-4422(12)70238-7_bib86 article-title: Irreversible aggregation of protein synthesis machinery after focal brain ischemia publication-title: J Neurochem doi: 10.1111/j.1471-4159.2006.03838.x – volume: 311 start-page: 388 year: 2004 ident: 10.1016/S1474-4422(12)70238-7_bib88 article-title: Edaravone protects against hypoxia/ischemia-induced endoplasmic reticulum dysfunction publication-title: J Pharmacol Exp Ther doi: 10.1124/jpet.104.069088 – volume: 5 start-page: e10489 year: 2010 ident: 10.1016/S1474-4422(12)70238-7_bib22 article-title: Activation of PERK signaling attenuates Aβ-mediated ER stress publication-title: PLoS One doi: 10.1371/journal.pone.0010489 – volume: 286 start-page: 7947 year: 2011 ident: 10.1016/S1474-4422(12)70238-7_bib116 article-title: The endoplasmic reticulum stress sensor, ATF6α, protects against neurotoxin-induced dopaminergic neuronal death publication-title: J Biol Chem doi: 10.1074/jbc.M110.156430 – volume: 398 start-page: 53 year: 2006 ident: 10.1016/S1474-4422(12)70238-7_bib114 article-title: A novel polymorphism in SEL1L confers susceptibility to Alzheimer's disease publication-title: Neurosci Lett doi: 10.1016/j.neulet.2005.12.038 – volume: 103 start-page: 6025 year: 2006 ident: 10.1016/S1474-4422(12)70238-7_bib40 article-title: Spinal cord endoplasmic reticulum stress associated with a microsomal accumulation of mutant superoxide dismutase-1 in an ALS model publication-title: Proc Natl Acad Sci USA doi: 10.1073/pnas.0509227103 – volume: 29 start-page: 767 year: 2007 ident: 10.1016/S1474-4422(12)70238-7_bib43 article-title: Increased ER stress during motor neuron degeneration in a transgenic mouse model of amyotrophic lateral sclerosis publication-title: Neurol Res doi: 10.1179/016164107X229803 – volume: 117 start-page: 448 year: 2007 ident: 10.1016/S1474-4422(12)70238-7_bib16 article-title: The integrated stress response prevents demyelination by protecting oligodendrocytes against immune-mediated damage publication-title: J Clin Invest doi: 10.1172/JCI29571 – volume: 6 start-page: 81 year: 2011 ident: 10.1016/S1474-4422(12)70238-7_bib133 article-title: Dantrolene is neuroprotective in Huntington's disease transgenic mouse model publication-title: Mol Neurodegener doi: 10.1186/1750-1326-6-81 – volume: 30 start-page: 3924 year: 2010 ident: 10.1016/S1474-4422(12)70238-7_bib2 article-title: Loss of HRD1-mediated protein degradation causes amyloid precursor protein accumulation and amyloid-β generation publication-title: J Neurosci doi: 10.1523/JNEUROSCI.2422-09.2010 – volume: 56 start-page: 216 year: 2010 ident: 10.1016/S1474-4422(12)70238-7_bib76 article-title: Homocysteine induces X-box-binding protein 1 splicing in the mice brain publication-title: Neurochem Int doi: 10.1016/j.neuint.2009.12.005 – volume: 4 start-page: 265 year: 2003 ident: 10.1016/S1474-4422(12)70238-7_bib79 article-title: A time-dependent phase shift in the Mammalian unfolded protein response publication-title: Dev Cell doi: 10.1016/S1534-5807(03)00022-4 – volume: 485 start-page: 507 year: 2012 ident: 10.1016/S1474-4422(12)70238-7_bib9 article-title: Sustained translational repression by eIF2α-P mediates prion neurodegeneration publication-title: Nature doi: 10.1038/nature11058 – volume: 24 start-page: 2352 year: 2004 ident: 10.1016/S1474-4422(12)70238-7_bib12 article-title: Mutations causing childhood ataxia with central nervous system hypomyelination reduce eukaryotic initiation factor 2B complex formation and activity publication-title: Mol Cell Biol doi: 10.1128/MCB.24.6.2352-2363.2004 – volume: 52 start-page: 261 year: 2005 ident: 10.1016/S1474-4422(12)70238-7_bib96 article-title: CHOP plays a pivotal role in the astrocyte death induced by oxygen and glucose deprivation publication-title: Glia doi: 10.1002/glia.20242 – volume: 54 start-page: 403 year: 2009 ident: 10.1016/S1474-4422(12)70238-7_bib54 article-title: Apolipoprotein E-deficient mice are more vulnerable to ER stress after transient forebrain ischemia publication-title: Neurochem Int doi: 10.1016/j.neuint.2009.01.010 – volume: 57 start-page: 393 year: 2008 ident: 10.1016/S1474-4422(12)70238-7_bib15 article-title: Ablation of the UPR-mediator CHOP restores motor function and reduces demyelination in Charcot-Marie-Tooth 1B mice publication-title: Neuron doi: 10.1016/j.neuron.2007.12.021 – volume: 14 start-page: 3801 year: 2005 ident: 10.1016/S1474-4422(12)70238-7_bib124 article-title: Endoplasmic reticulum stress and mitochondrial cell death pathways mediate A53T mutant alpha-synuclein-induced toxicity publication-title: Hum Mol Genet doi: 10.1093/hmg/ddi396 – volume: 18 start-page: 3066 year: 2004 ident: 10.1016/S1474-4422(12)70238-7_bib62 article-title: CHOP induces death by promoting protein synthesis and oxidation in the stressed endoplasmic reticulum publication-title: Genes Dev doi: 10.1101/gad.1250704 – volume: 25 start-page: 41 year: 2005 ident: 10.1016/S1474-4422(12)70238-7_bib95 article-title: Damage to the endoplasmic reticulum and activation of apoptotic machinery by oxidative stress in ischemic neurons publication-title: J Cereb Blood Flow Metab doi: 10.1038/sj.jcbfm.9600005 – volume: 1 start-page: 479 year: 1999 ident: 10.1016/S1474-4422(12)70238-7_bib103 article-title: Presenilin-1 mutations downregulate the signalling pathway of the unfolded-protein response publication-title: Nat Cell Biol doi: 10.1038/70265 – volume: 1349 start-page: 90 year: 2010 ident: 10.1016/S1474-4422(12)70238-7_bib4 article-title: Protein disulfide isomerase-immunopositive inclusions in patients with Alzheimer disease publication-title: Brain Res doi: 10.1016/j.brainres.2010.06.016 – volume: 75 start-page: 284 year: 2011 ident: 10.1016/S1474-4422(12)70238-7_bib137 article-title: Quinotrierixin inhibited ER stress-induced XBP1 mRNA splicing through inhibition of protein synthesis publication-title: Biosci Biotechnol Biochem doi: 10.1271/bbb.100622 – volume: 41 start-page: 380 year: 2006 ident: 10.1016/S1474-4422(12)70238-7_bib105 article-title: The unfolded protein response affects neuronal cell cycle protein expression: implications for Alzheimer's disease pathogenesis publication-title: Exp Gerontol doi: 10.1016/j.exger.2006.01.013 – volume: 19 start-page: 3502 year: 2010 ident: 10.1016/S1474-4422(12)70238-7_bib52 article-title: The early-onset torsion dystonia-associated protein, torsinA, is a homeostatic regulator of endoplasmic reticulum stress response publication-title: Hum Mol Genet doi: 10.1093/hmg/ddq266 – volume: 31 start-page: 454 year: 2008 ident: 10.1016/S1474-4422(12)70238-7_bib112 article-title: Neuronal calcium mishandling and the pathogenesis of Alzheimer's disease publication-title: Trends Neurosci doi: 10.1016/j.tins.2008.06.005 – volume: 165 start-page: 347 year: 2004 ident: 10.1016/S1474-4422(12)70238-7_bib91 article-title: Involvement of caspase-4 in endoplasmic reticulum stress-induced apoptosis and Aβ-induced cell death publication-title: J Cell Biol doi: 10.1083/jcb.200310015 – volume: 28 start-page: 111 year: 2006 ident: 10.1016/S1474-4422(12)70238-7_bib107 article-title: β-amyloid and endoplasmic reticulum stress responses in primary neurons: effects of drugs that interact with the cytoskeleton publication-title: J Mol Neurosci doi: 10.1385/JMN:28:2:111 – volume: 58 start-page: 35 year: 2011 ident: 10.1016/S1474-4422(12)70238-7_bib34 article-title: Endoplasmic reticulum stress inducers provide protection against 6-hydroxydopamine-induced cytotoxicity publication-title: Neurochem Int doi: 10.1016/j.neuint.2010.10.006 – volume: 7 start-page: 317 year: 2001 ident: 10.1016/S1474-4422(12)70238-7_bib101 article-title: ORP150 protects against hypoxia/ischemia-induced neuronal death publication-title: Nat Med doi: 10.1038/85463 – volume: 58 start-page: 344 year: 2011 ident: 10.1016/S1474-4422(12)70238-7_bib128 article-title: Derlin-1 overexpression ameliorates mutant SOD1-induced endoplasmic reticulum stress by reducing mutant SOD1 accumulation publication-title: Neurochem Int doi: 10.1016/j.neuint.2010.12.010 – volume: 86 start-page: 2091 year: 2008 ident: 10.1016/S1474-4422(12)70238-7_bib21 article-title: ER stress is involved in Aβ-induced GSK-3β activation and tau phosphorylation publication-title: J Neurosci Res doi: 10.1002/jnr.21648 – volume: 293 start-page: 263 year: 2001 ident: 10.1016/S1474-4422(12)70238-7_bib122 article-title: Ubiquitination of a new form of α-synuclein by parkin from human brain: implications for Parkinson's disease publication-title: Science doi: 10.1126/science.1060627 – volume: 32 start-page: 3306 year: 2012 ident: 10.1016/S1474-4422(12)70238-7_bib32 article-title: Endoplasmic reticulum stress is important for the manifestations of α-synucleinopathy in vivo publication-title: J Neurosci doi: 10.1523/JNEUROSCI.5367-11.2012 – volume: 208 start-page: 169 year: 2007 ident: 10.1016/S1474-4422(12)70238-7_bib109 article-title: NF-κB activated by ER calcium release inhibits Aβ-mediated expression of CHOP protein: enhancement by AD-linked mutant presenilin 1 publication-title: Exp Neurol doi: 10.1016/j.expneurol.2007.04.009 – volume: 106 start-page: 189 year: 2012 ident: 10.1016/S1474-4422(12)70238-7_bib67 article-title: Phosphoproteins in stress-induced disease publication-title: Prog Mol Biol Transl Sci doi: 10.1016/B978-0-12-396456-4.00003-1 – volume: 28 start-page: 2168 year: 2008 ident: 10.1016/S1474-4422(12)70238-7_bib59 article-title: Eif-2a protects brainstem motoneurons in a murine model of sleep apnea publication-title: J Neurosci doi: 10.1523/JNEUROSCI.5232-07.2008 – volume: 23 start-page: 2294 year: 2009 ident: 10.1016/S1474-4422(12)70238-7_bib127 article-title: XBP-1 deficiency in the nervous system protects against amyotrophic lateral sclerosis by increasing autophagy publication-title: Genes Dev doi: 10.1101/gad.1830709 – volume: 60 start-page: 598 year: 2008 ident: 10.1016/S1474-4422(12)70238-7_bib6 article-title: Mutant prion protein expression causes motor and memory deficits and abnormal sleep patterns in a transgenic mouse model publication-title: Neuron doi: 10.1016/j.neuron.2008.09.008 – volume: 20 start-page: 261 year: 2010 ident: 10.1016/S1474-4422(12)70238-7_bib24 article-title: Presenilin-1 holoprotein is an interacting partner of sarco endoplasmic reticulum calcium-ATPase and confers resistance to endoplasmic reticulum stress publication-title: J Alzheimers Dis doi: 10.3233/JAD-2010-1360 – volume: 120 start-page: 744 year: 2010 ident: 10.1016/S1474-4422(12)70238-7_bib51 article-title: Wolfram syndrome 1 gene negatively regulates ER stress signaling in rodent and human cells publication-title: J Clin Invest doi: 10.1172/JCI39678 – volume: 118 start-page: 491 year: 2003 ident: 10.1016/S1474-4422(12)70238-7_bib89 article-title: Activation of caspase-12 by endoplasmic reticulum stress induced by transient middle cerebral artery occlusion in mice publication-title: Neuroscience doi: 10.1016/S0306-4522(02)00910-7 – volume: 172 start-page: 201 year: 2006 ident: 10.1016/S1474-4422(12)70238-7_bib65 article-title: Activation-dependent substrate recruitment by the eukaryotic translation initiation factor 2 kinase PERK publication-title: J Cell Biol doi: 10.1083/jcb.200508099 – volume: 57 start-page: 1 year: 2010 ident: 10.1016/S1474-4422(12)70238-7_bib56 article-title: Characterization of neuronal and astroglial responses to ER stress in the hippocampal CA1 area in mice following transient forebrain ischemia publication-title: Neurochem Int doi: 10.1016/j.neuint.2010.03.017 – volume: 22 start-page: 1451 year: 2008 ident: 10.1016/S1474-4422(12)70238-7_bib46 article-title: ALS-linked mutant SOD1 induces ER stress- and ASK1-dependent motor neuron death by targeting Derlin-1 publication-title: Genes Dev doi: 10.1101/gad.1640108 – volume: 110 start-page: 956 year: 2009 ident: 10.1016/S1474-4422(12)70238-7_bib93 article-title: Increased vulnerability of hippocampal pyramidal neurons to the toxicity of kainic acid in OASIS-deficient mice publication-title: J Neurochem doi: 10.1111/j.1471-4159.2009.06188.x – volume: 84 start-page: 94 year: 2011 ident: 10.1016/S1474-4422(12)70238-7_bib50 article-title: Involvement of IRE1α signaling in the hippocampus in patients with mesial temporal lobe epilepsy publication-title: Brain Res Bull doi: 10.1016/j.brainresbull.2010.10.004 – volume: 118 start-page: 99 year: 2005 ident: 10.1016/S1474-4422(12)70238-7_bib10 article-title: Heightened stress response in primary fibroblasts expressing mutant eIF2B genes from CACH/VWM leukodystrophy patients publication-title: Hum Genet doi: 10.1007/s00439-005-0024-x – volume: 17 start-page: 189 year: 2010 ident: 10.1016/S1474-4422(12)70238-7_bib1 article-title: Endoplasmic reticulum stress plays critical role in brain damage after cerebral ischemia/reperfusion in rats publication-title: Neurotox Res doi: 10.1007/s12640-009-9110-5 – volume: 129 start-page: 1306 year: 2006 ident: 10.1016/S1474-4422(12)70238-7_bib17 article-title: Interferon-γ inhibits central nervous system remyelination through a process modulated by endoplasmic reticulum stress publication-title: Brain doi: 10.1093/brain/awl044 – volume: 307 start-page: 1776 year: 2005 ident: 10.1016/S1474-4422(12)70238-7_bib69 article-title: Uncharged tRNA and sensing of amino acid deficiency in mammalian piriform cortex publication-title: Science doi: 10.1126/science.1104882 – volume: 1037 start-page: 52 year: 2005 ident: 10.1016/S1474-4422(12)70238-7_bib82 article-title: HMG CoA reductase inhibitors reduce ischemic brain injury of Wistar rats through decreasing oxidative stress on neurons publication-title: Brain Res doi: 10.1016/j.brainres.2004.12.051 – volume: 22 start-page: 63 year: 1997 ident: 10.1016/S1474-4422(12)70238-7_bib131 article-title: The ER-overload response: activation of NF-κB publication-title: Trends Biochem Sci doi: 10.1016/S0968-0004(96)10073-6 – volume: 78 start-page: 779 year: 2001 ident: 10.1016/S1474-4422(12)70238-7_bib87 article-title: Changes in the phosphorylation of initiation factor eIF-2α, elongation factor eEF-2 and p70 S6 kinase after transient focal cerebral ischaemia in mice publication-title: J Neurochem doi: 10.1046/j.1471-4159.2001.00462.x – volume: 448 start-page: 704 year: 2007 ident: 10.1016/S1474-4422(12)70238-7_bib37 article-title: Global changes to the ubiquitin system in Huntington's disease publication-title: Nature doi: 10.1038/nature06022 – volume: 6 start-page: e19339 year: 2011 ident: 10.1016/S1474-4422(12)70238-7_bib5 article-title: Expression of mutant or cytosolic PrP in transgenic mice and cells is not associated with endoplasmic reticulum stress or proteasome dysfunction publication-title: PLoS One doi: 10.1371/journal.pone.0019339 – volume: 63 start-page: 700 year: 2011 ident: 10.1016/S1474-4422(12)70238-7_bib25 article-title: Endoplasmic reticulum Ca2+ handling in excitable cells in health and disease publication-title: Pharmacol Rev doi: 10.1124/pr.110.003814 – volume: 47 start-page: 122 year: 2010 ident: 10.1016/S1474-4422(12)70238-7_bib83 article-title: Calcium, ischemia and excitotoxicity publication-title: Cell Calcium doi: 10.1016/j.ceca.2010.01.003 – volume: 307 start-page: 935 year: 2005 ident: 10.1016/S1474-4422(12)70238-7_bib72 article-title: A selective inhibitor of eIF2α dephosphorylation protects cells from ER stress publication-title: Science doi: 10.1126/science.1101902 – volume: 27 start-page: 901 year: 2007 ident: 10.1016/S1474-4422(12)70238-7_bib99 article-title: Endoplasmic reticulum stress inhibition protects against excitotoxic neuronal injury in the rat brain publication-title: J Neurosci doi: 10.1523/JNEUROSCI.4289-06.2007 – volume: 284 start-page: 18202 year: 2009 ident: 10.1016/S1474-4422(12)70238-7_bib47 article-title: Neuroserpin polymers activate NF-κB by a calcium signalling pathway that is independent of the unfolded protein response publication-title: J Biol Chem doi: 10.1074/jbc.M109.010744 – volume: 106 start-page: 333 year: 2008 ident: 10.1016/S1474-4422(12)70238-7_bib29 article-title: Changes in endoplasmic reticulum stress proteins and aldolase A in cells exposed to dopamine publication-title: J Neurochem doi: 10.1111/j.1471-4159.2008.05392.x – volume: 96 start-page: 30 year: 2001 ident: 10.1016/S1474-4422(12)70238-7_bib108 article-title: Aβ(1-42) and aluminum induce stress in the endoplasmic reticulum in rabbit hippocampus, involving nuclear translocation of gadd 153 and NF-κB publication-title: Brain Res Mol Brain Res doi: 10.1016/S0169-328X(01)00256-X – volume: 924 start-page: 159 year: 2002 ident: 10.1016/S1474-4422(12)70238-7_bib85 article-title: Depletion of intracellular calcium stores is toxic to SH-SY5Y neuronal cells publication-title: Brain Res doi: 10.1016/S0006-8993(01)03229-2 – volume: 174 start-page: 1241 year: 2009 ident: 10.1016/S1474-4422(12)70238-7_bib20 article-title: The unfolded protein response is activated in pretangle neurons in Alzheimer's disease hippocampus publication-title: Am J Pathol doi: 10.2353/ajpath.2009.080814 – volume: 36 start-page: 585 year: 2002 ident: 10.1016/S1474-4422(12)70238-7_bib13 article-title: The unfolded protein response modulates disease severity in Pelizaeus-Mezbacher disease publication-title: Neuron doi: 10.1016/S0896-6273(02)01045-0 – volume: 7 start-page: 186 year: 2005 ident: 10.1016/S1474-4422(12)70238-7_bib74 article-title: OASIS, a CREB/ATF-family member, modulates UPR signalling in astrocytes publication-title: Nat Cell Biol doi: 10.1038/ncb1213 – volume: 90 start-page: 694 year: 2004 ident: 10.1016/S1474-4422(12)70238-7_bib97 article-title: GADD34 protein levels increase after transient ischemia in the cortex but not in the CA1 subfield: implications for post-ischemic recovery of protein synthesis in ischemia-resistant cells publication-title: J Neurochem doi: 10.1111/j.1471-4159.2004.02555.x – volume: 101 start-page: 1491 year: 2007 ident: 10.1016/S1474-4422(12)70238-7_bib33 article-title: Neurodegeneration of mouse nigrostriatal dopaminergic system induced by repeated oral administration of rotenone is prevented by 4-phenylbutyrate, a chemical chaperone publication-title: J Neurochem doi: 10.1111/j.1471-4159.2006.04440.x – volume: 5 start-page: 56 year: 2010 ident: 10.1016/S1474-4422(12)70238-7_bib135 article-title: ER stress response plays an important role in aggregation of α-synuclein publication-title: Mol Neurodegener doi: 10.1186/1750-1326-5-56 – volume: 15 start-page: 767 year: 2004 ident: 10.1016/S1474-4422(12)70238-7_bib78 article-title: Degradation of misfolded proteins prevents ER-derived oxidative stress and cell death publication-title: Mol Cell doi: 10.1016/j.molcel.2004.08.025 – volume: 397 start-page: 271 year: 1999 ident: 10.1016/S1474-4422(12)70238-7_bib63 article-title: Translation and protein folding are coupled by an endoplasmic reticulum resident kinase publication-title: Nature doi: 10.1038/16729 – volume: 69 start-page: 346 year: 2010 ident: 10.1016/S1474-4422(12)70238-7_bib39 article-title: Endoplasmic reticulum stress in motor neurons of the spinal cord in sporadic amyotrophic lateral sclerosis publication-title: J Neuropathol Exp Neurol doi: 10.1097/NEN.0b013e3181d44992 – volume: 284 start-page: 18167 year: 2009 ident: 10.1016/S1474-4422(12)70238-7_bib125 article-title: Rrs1 is involved in endoplasmic reticulum stress response in Huntington disease publication-title: J Biol Chem doi: 10.1074/jbc.M109.018325 – volume: 94 start-page: 1235 year: 2005 ident: 10.1016/S1474-4422(12)70238-7_bib64 article-title: PERK is responsible for the increased phosphorylation of eIF2α and the severe inhibition of protein synthesis after transient global brain ischemia publication-title: J Neurochem doi: 10.1111/j.1471-4159.2005.03276.x – volume: 78 start-page: 659 year: 2006 ident: 10.1016/S1474-4422(12)70238-7_bib90 article-title: Spread of an inactive form of caspase-12 in humans is due to recent positive selection publication-title: Am J Hum Genet doi: 10.1086/503116 – volume: 25 start-page: 302 year: 2000 ident: 10.1016/S1474-4422(12)70238-7_bib120 article-title: Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase publication-title: Nat Genet doi: 10.1038/77060 – volume: 83 start-page: 673 year: 2002 ident: 10.1016/S1474-4422(12)70238-7_bib111 article-title: Involvement of Gadd153 in the pathogenic action of presenilin-1 mutations publication-title: J Neurochem doi: 10.1046/j.1471-4159.2002.01165.x – volume: 11 start-page: 619 year: 2003 ident: 10.1016/S1474-4422(12)70238-7_bib68 article-title: An integrated stress response regulates amino acid metabolism and resistance to oxidative stress publication-title: Mol Cell doi: 10.1016/S1097-2765(03)00105-9 – volume: 11 start-page: 403 year: 2004 ident: 10.1016/S1474-4422(12)70238-7_bib94 article-title: Ischemia-induced neuronal cell death is mediated by the endoplasmic reticulum stress pathway involving CHOP publication-title: Cell Death Differ doi: 10.1038/sj.cdd.4401365 – volume: 1257 start-page: 16 year: 2009 ident: 10.1016/S1474-4422(12)70238-7_bib27 article-title: Protective effect against Parkinson's disease-related insults through the activation of XBP1 publication-title: Brain Res doi: 10.1016/j.brainres.2008.11.104 – volume: 20 start-page: 2144 year: 2011 ident: 10.1016/S1474-4422(12)70238-7_bib110 article-title: The ER stress factor XBP1s prevents amyloid-β neurotoxicity publication-title: Hum Mol Genet doi: 10.1093/hmg/ddr100 – volume: 1 start-page: 273 year: 2005 ident: 10.1016/S1474-4422(12)70238-7_bib70 article-title: The GCN2 kinase biases feeding behavior to maintain amino acid homeostasis in omnivores publication-title: Cell Metab doi: 10.1016/j.cmet.2005.03.004 – volume: 28 start-page: F96 year: 2009 ident: 10.1016/S1474-4422(12)70238-7_bib84 article-title: Calcium binding chaperones of the endoplasmic reticulum publication-title: Gen Physiol Biophys – volume: 11 start-page: 619 year: 2003 ident: 10.1016/S1474-4422(12)70238-7_bib66 article-title: An integrated stress response regulates amino acid metabolism and resistance to oxidative stress publication-title: Mol Cell doi: 10.1016/S1097-2765(03)00105-9 – volume: 124 start-page: 3332 year: 2011 ident: 10.1016/S1474-4422(12)70238-7_bib36 article-title: Changes in BiP availability reveal hypersensitivity to acute endoplasmic reticulum stress in cells expressing mutant huntingtin publication-title: J Cell Sci doi: 10.1242/jcs.087510 – volume: 6 start-page: 158 year: 2011 ident: 10.1016/S1474-4422(12)70238-7_bib53 article-title: Ca2+ homeostasis modulation enhances the amenability of L444P glucosylcerebrosidase to proteostasis regulation in patient-derived fibroblasts publication-title: ACS Chem Biol doi: 10.1021/cb100321m – volume: 1087 start-page: 60 year: 2006 ident: 10.1016/S1474-4422(12)70238-7_bib80 article-title: Prolonged bihemispheric alterations in unfolded protein response related gene expression after experimental stroke publication-title: Brain Res doi: 10.1016/j.brainres.2006.02.095 – volume: 147 start-page: 957 year: 2007 ident: 10.1016/S1474-4422(12)70238-7_bib81 article-title: Involvement of endoplasmic reticulum stress after middle cerebral artery occlusion in mice publication-title: Neuroscience doi: 10.1016/j.neuroscience.2007.04.017 – volume: 18 start-page: 106 year: 1998 ident: 10.1016/S1474-4422(12)70238-7_bib123 article-title: Ala30Pro mutation in the gene encoding α-synuclein in Parkinson's disease publication-title: Nat Genet doi: 10.1038/ng0298-106 – volume: 20 start-page: 1008 year: 2011 ident: 10.1016/S1474-4422(12)70238-7_bib45 article-title: The unfolded protein response in familial amyotrophic lateral sclerosis publication-title: Hum Mol Genet doi: 10.1093/hmg/ddq546 – volume: 1034 start-page: 51 year: 2005 ident: 10.1016/S1474-4422(12)70238-7_bib98 article-title: Evolution of GADD34 expression after focal cerebral ischaemia publication-title: Brain Res doi: 10.1016/j.brainres.2004.11.058 – volume: 60 start-page: 988 year: 2008 ident: 10.1016/S1474-4422(12)70238-7_bib26 article-title: Phosphorylation of the translation initiation factor eIF2α increases BACE1 levels and promotes amyloidogenesis publication-title: Neuron doi: 10.1016/j.neuron.2008.10.047 – volume: 332 start-page: 91 year: 2011 ident: 10.1016/S1474-4422(12)70238-7_bib73 article-title: Selective inhibition of a regulatory subunit of protein phosphatase 1 restores proteostasis publication-title: Science doi: 10.1126/science.1201396 – volume: 109 start-page: E869 year: 2012 ident: 10.1016/S1474-4422(12)70238-7_bib138 article-title: The molecular basis for selective inhibition of unconventional mRNA splicing by an IRE1-binding small molecule publication-title: Proc Natl Acad Sci USA doi: 10.1073/pnas.1115623109 – volume: 329 start-page: 229 year: 2010 ident: 10.1016/S1474-4422(12)70238-7_bib132 article-title: An autophagy-enhancing drug promotes degradation of mutant α1-antitrypsin Z and reduces hepatic fibrosis publication-title: Science doi: 10.1126/science.1190354 – volume: 286 start-page: 33942 year: 2011 ident: 10.1016/S1474-4422(12)70238-7_bib7 article-title: Proteasomal dysfunction and endoplasmic reticulum stress enhance trafficking of prion protein aggregates through the secretory pathway and increase accumulation of pathologic prion protein publication-title: J Biol Chem doi: 10.1074/jbc.M111.272617 – volume: 178 start-page: 33 year: 2011 ident: 10.1016/S1474-4422(12)70238-7_bib60 article-title: Valproate reduces CHOP levels and preserves oligodendrocytes and axons after spinal cord injury publication-title: Neuroscience doi: 10.1016/j.neuroscience.2011.01.012 – volume: 17 start-page: 1527 year: 2008 ident: 10.1016/S1474-4422(12)70238-7_bib130 article-title: The intracellular accumulation of polymeric neuroserpin explains the severity of the dementia FENIB publication-title: Hum Mol Genet doi: 10.1093/hmg/ddn041 – volume: 415 start-page: 92 year: 2002 ident: 10.1016/S1474-4422(12)70238-7_bib75 article-title: IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA publication-title: Nature doi: 10.1038/415092a – volume: 42 start-page: 386 year: 2010 ident: 10.1016/S1474-4422(12)70238-7_bib3 article-title: Induction of the unfolded protein response and cell death pathway in Alzheimer's disease, but not in aged Tg2576 mice publication-title: Exp Mol Med doi: 10.3858/emm.2010.42.5.040 – volume: 15 start-page: 359 year: 2008 ident: 10.1016/S1474-4422(12)70238-7_bib8 article-title: Reduced translocation of nascent prion protein during ER stress contributes to neurodegeneration publication-title: Dev Cell doi: 10.1016/j.devcel.2008.06.015 – volume: 68 start-page: 865 year: 2010 ident: 10.1016/S1474-4422(12)70238-7_bib38 article-title: Mechanism of ER stress-induced brain damage by IP3 receptor publication-title: Neuron doi: 10.1016/j.neuron.2010.11.010 – volume: 488 start-page: 11 year: 2011 ident: 10.1016/S1474-4422(12)70238-7_bib115 article-title: Proteomic insights into the protective mechanisms of an in vitro oxidative stress model of early stage Parkinson's disease publication-title: Neurosci Lett doi: 10.1016/j.neulet.2010.10.071 – volume: 155 start-page: 302 year: 1999 ident: 10.1016/S1474-4422(12)70238-7_bib100 article-title: The endoplasmic reticulum stress-responsive protein GRP78 protects neurons against excitotoxicity and apoptosis: suppression of oxidative stress and stabilization of calcium homeostasis publication-title: Exp Neurol doi: 10.1006/exnr.1998.7002 – volume: 104 start-page: 20606 year: 2007 ident: 10.1016/S1474-4422(12)70238-7_bib41 article-title: Deletion of the BH3-only protein puma protects motoneurons from ER stress-induced apoptosis and delays motoneuron loss in ALS mice publication-title: Proc Natl Acad Sci USA doi: 10.1073/pnas.0707906105 – volume: 11 start-page: 279 year: 2011 ident: 10.1016/S1474-4422(12)70238-7_bib57 article-title: Overexpressing GRP78 influences Ca2+ handling and function of mitochondria in astrocytes after ischemia-like stress publication-title: Mitochondrion doi: 10.1016/j.mito.2010.10.007 – volume: 392 start-page: 605 year: 1998 ident: 10.1016/S1474-4422(12)70238-7_bib119 article-title: Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism publication-title: Nature doi: 10.1038/33416 – volume: 65 start-page: 348 year: 2006 ident: 10.1016/S1474-4422(12)70238-7_bib106 article-title: Endoplasmic reticulum stress features are prominent in Alzheimer disease but not in prion diseases in vivo publication-title: J Neuropathol Exp Neurol doi: 10.1097/01.jnen.0000218445.30535.6f – volume: 15 start-page: 364 year: 2008 ident: 10.1016/S1474-4422(12)70238-7_bib58 article-title: A molecular chaperone inducer protects neurons from ER stress publication-title: Cell Death Differ doi: 10.1038/sj.cdd.4402276 – volume: 37 start-page: 974 year: 2005 ident: 10.1016/S1474-4422(12)70238-7_bib18 article-title: Protein accumulation and neurodegeneration in the woozy mutant mouse is caused by disruption of SIL1, a cochaperone of BiP publication-title: Nat Genet doi: 10.1038/ng1620 – volume: 22 start-page: 3308 year: 2008 ident: 10.1016/S1474-4422(12)70238-7_bib35 article-title: Impaired ERAD and ER stress are early and specific events in polyglutamine toxicity publication-title: Genes Dev doi: 10.1101/gad.1673408 – volume: 151 start-page: 109 year: 2008 ident: 10.1016/S1474-4422(12)70238-7_bib55 article-title: Involvement of endoplasmic reticulum stress in the neuronal death induced by transient forebrain ischemia in gerbil publication-title: Neuroscience doi: 10.1016/j.neuroscience.2007.10.047 – volume: 12 start-page: 627 year: 2009 ident: 10.1016/S1474-4422(12)70238-7_bib44 article-title: A role for motoneuron subtype-selective ER stress in disease manifestations of FALS mice publication-title: Nat Neurosci doi: 10.1038/nn.2297 |
| SSID | ssj0021481 |
| Score | 2.572192 |
| SecondaryResourceType | review_article |
| Snippet | Endoplasmic reticulum (ER) dysfunction might have an important part to play in a range of neurological disorders, including cerebral ischaemia, sleep apnoea,... Summary Endoplasmic reticulum (ER) dysfunction might have an important part to play in a range of neurological disorders, including cerebral ischaemia, sleep... Endoplasmic reticulum (ER) dysfunction is important in the pathogenesis of many neurological diseases. In this review, we examine the evidence for ER... |
| SourceID | hal proquest pubmed crossref elsevier |
| SourceType | Open Access Repository Aggregation Database Index Database Enrichment Source Publisher |
| StartPage | 105 |
| SubjectTerms | Alzheimer's disease Amyloid beta-Peptides Amyloid beta-Peptides - genetics Amyotrophic lateral sclerosis Animals Ataxia beta -Amyloid Cellular Biology Cognitive ability Disease Endoplasmic Reticulum Endoplasmic Reticulum - pathology Endoplasmic Reticulum - physiology Enzymes Epilepsy Humans Inclusion bodies Ischemia Life Sciences Movement disorders Multiple sclerosis Mutation Nervous System Diseases Nervous System Diseases - genetics Nervous System Diseases - pathology Nervous System Diseases - physiopathology Neurodegenerative diseases Neurological diseases Neurology neuroserpin Prion protein Protein Folding Reperfusion Signal Transduction Signal Transduction - physiology Sleep Sleep disorders Stress Stroke Unfolded Protein Response Unfolded Protein Response - genetics |
| Title | Endoplasmic reticulum dysfunction in neurological disease |
| URI | https://www.clinicalkey.com/#!/content/1-s2.0-S1474442212702387 https://www.clinicalkey.es/playcontent/1-s2.0-S1474442212702387 https://dx.doi.org/10.1016/S1474-4422(12)70238-7 https://www.ncbi.nlm.nih.gov/pubmed/23237905 https://www.proquest.com/docview/1237170089 https://www.proquest.com/docview/1239061171 https://www.proquest.com/docview/1272732764 https://inserm.hal.science/inserm-01296824 |
| Volume | 12 |
| WOSCitedRecordID | wos000312429400025&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D |
| hasFullText | 1 |
| inHoldings | 1 |
| isFullTextHit | |
| isPrint | |
| journalDatabaseRights | – providerCode: PRVPQU databaseName: Nursing & allied health premium. customDbUrl: eissn: 1474-4465 dateEnd: 20251009 omitProxy: false ssIdentifier: ssj0021481 issn: 1474-4422 databaseCode: 7RV dateStart: 20020501 isFulltext: true titleUrlDefault: https://search.proquest.com/nahs providerName: ProQuest – providerCode: PRVPQU databaseName: ProQuest Central customDbUrl: eissn: 1474-4465 dateEnd: 20251009 omitProxy: false ssIdentifier: ssj0021481 issn: 1474-4422 databaseCode: BENPR dateStart: 20020501 isFulltext: true titleUrlDefault: https://www.proquest.com/central providerName: ProQuest – providerCode: PRVPQU databaseName: ProQuest Health & Medical Collection customDbUrl: eissn: 1474-4465 dateEnd: 20251009 omitProxy: false ssIdentifier: ssj0021481 issn: 1474-4422 databaseCode: 7X7 dateStart: 20020501 isFulltext: true titleUrlDefault: https://search.proquest.com/healthcomplete providerName: ProQuest – providerCode: PRVPQU databaseName: Psychology Database customDbUrl: eissn: 1474-4465 dateEnd: 20251009 omitProxy: false ssIdentifier: ssj0021481 issn: 1474-4422 databaseCode: M2M dateStart: 20020501 isFulltext: true titleUrlDefault: https://www.proquest.com/psychology providerName: ProQuest |
| link | http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV3da9wwDBe76xh92fdHtq5ksMH2kPbsc23naXTjSh96R-m2cm8msR12sOauzbWw_36S46QvazvYSyAfInakSD9JtgTwHhGskxTX4KzUmSgLmeXC68z7SpSVR48sBNxOj9Rspufz_DgG3Jq4rLLTiUFRu6WlGPkualhFteR0_nl1nlHXKMquxhYaA9igSmViCBtfJrPjk97lQrAfXC6hRCYE59d7eHa_9Rc_Mv5Jke3K1E3WafCTlknehEGDLTp49L-zeAwPIwpN91uxeQL3fP0UHkxjnv0Z5JPaLVcIrM8WNg37HClImLrfDdlB4mW6qNNQCzPqzjRmep7Dj4PJ96-HWWyykFn0ndYZ3_NjZsesFB6dlRLhitRWa-f3VM5HlWOVUAX6UdZJ771lwhe5U6wqfOWqEfPjFzCsl7V_BWlecnSIhHSFrkRRleWIu0LY3CH3hZRlAqL7uMbGCuTUCOOX6ZeaEU8M8cQwbgJPjEpgpydbtSU47iKQHedMt78UNaJBI3EXofoboW_if90YZhpuRi01EVPeHkmRUveUEbq0kORfXvoBhaufGZX7Ptw_MosaVdCZoTih1FxcsQS2OpEy1-Pp5SmBd_1t1BCU9ilqv7wMz-SI2phitz1DOJYrKRJ42Yp2PyLE3GMq4_b69gG8gU0eWoVQeGoLhuuLS_8W7tur9aK52IaBOjml41yFo96OvyqeTfn0DxDIPJU |
| linkProvider | ProQuest |
| linkToHtml | http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMw1V3dT9RAEJ8AGuXFb6WCWhNJ5KFyu7fsbh-IIQo5wnExioS3td3dxkukd9IDwz_l3-jM9oMXAV948LXttNv2tzPzm52dAXiDHqyTFNfgLNeJyDOZpMLrxPtC5IVHRhYCbodDNRrpo6P00xz8bvfCUFplqxODonYTSzHyddSwimrJ6fT99GdCXaNodbVtoVHDYs-f_0LKVm3ufsT_u8r5zvbBh0HSdBVILJKFWcI3fJ_ZPsuFR-88R_sstdXa-Q2V8l7hWCFUhsTBOum9t0z4LHWKFZkvXNFjvo_3nYdbqMcZpZCpz4cdwUNqEQieUCIRgvOLHUPrX7qDbxlfU2QpE3WZLZz_TkmZl3m8wfLt3P_fvtkDuNf42PFWPSkewpwvH8Gd_SaL4DGk26WbTJE2HI9tHHZxUgg0ducVWXlCajwu41Dps7EMcbOO9QS-3sjAn8JCOSn9EsRpzpHuCekyXYisyPMed5mwqUNsCynzCET7M41t6qtTm48fpkukIwwYwoBh3AQMGBXBu05sWhcYuU5Atkgx7e5Z1PcGTeB1gupvgr5qtFZlmKm46dXSJExZCSiKkrqTbByz2uH6l4euIpi7N6Ni5oOtoRmXqGCPDUVBpebijEWw0kLYXIynw28Er7vTqP9oUSsr_eQ0XJOiT8oUu-oa8tK5kiKCZ_VU6kaEjKJPReqeXz2AV3B3cLA_NMPd0d4yLPLQFIUCcSuwMDs59S_gtj2bjauTl0ElxPDtpufTH9KAlpc |
| linkToPdf | http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMw1V1Lb9QwEB61BVVceD8CBYJEJTiEXXu9dnJAqKJdteruqhIP9WYSP8RKNLs026L-NX4dM86jF9py6YFrkkmc5PPMfOPxDMBr9GCtpLgGZ0WaiCKXSSZcmjjnReEdMrIQcPs6VtNpeniYHazA73YvDKVVtjoxKGo7NxQj76GGVVRLLs16vkmLONgefVj8TKiDFK20tu00aojsu7NfSN-q93vb-K83OR_tfP64mzQdBhKDxGGZ8KEbMDNghXDoqRdoq2Vq0tS6ocp431vmhcqRRBgrnXOGCZdnVjGfO299n7kB3ncVbigxHFL3hAmfdGQPaUYge0KJRAjOz3cP9T51B98w_laR1UzURXZx9TslaF7k_QYrOLrzP3-_u3C78b3jrXqy3IMVV96H9UmTXfAAsp3SzhdIJ45mJg67Oyk0Gtuziqw_ITielXGoANpYjLhZ33oIX65l4I9grZyX7gnEWcGRBgpp89SL3BdFn9tcmMwi5oWURQSi_bHaNHXXqf3HD90l2BEeNOFBM64DHrSK4F0ntqgLj1wlIFvU6HZXLdoBjabxKkH1N0FXNdqs0kxXXPdraRKmbAUURcm0k2wcttoR-5eHbiKwuzejIue7W2M9K1HxHmmKjsqUi1MWwUYLZ30-ng7LEbzqTqNepMWuvHTzk3BNhr4qU-yya8h750qKCB7X06obETKNARWve3r5AF7COk4jPd6b7j-DWzz0SqH43AasLY9P3HO4aU6Xs-r4RdAOMXy77un0BwDiny4 |
| openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Endoplasmic+reticulum+dysfunction+in+neurological+disease&rft.jtitle=Lancet+neurology&rft.au=Roussel%2C+Benoit+D%2C+PhD&rft.au=Kruppa%2C+Antonina+J%2C+PhD&rft.au=Miranda%2C+Elena%2C+PhD&rft.au=Crowther%2C+Damian+C%2C+PhD&rft.date=2013&rft.issn=1474-4422&rft.volume=12&rft.issue=1&rft.spage=105&rft.epage=118&rft_id=info:doi/10.1016%2FS1474-4422%2812%2970238-7&rft.externalDBID=ECK1-s2.0-S1474442212702387&rft.externalDocID=1_s2_0_S1474442212702387 |
| thumbnail_m | http://cvtisr.summon.serialssolutions.com/2.0.0/image/custom?url=https%3A%2F%2Fcdn.clinicalkey.com%2Fck-thumbnails%2F14744422%2FS1474442212X70261%2Fcov150h.gif |