Structure, function, aging and turnover of aggrecan in the intervertebral disc
Aggrecan is the major non-collagenous component of the intervertebral disc. It is a large proteoglycan possessing numerous glycosaminoglycan chains and the ability to form aggregates in association with hyaluronan. Its abundance and unique molecular features provide the disc with its osmotic propert...
Gespeichert in:
| Veröffentlicht in: | Biochimica et biophysica acta Jg. 1840; H. 10; S. 3181 - 3189 |
|---|---|
| Hauptverfasser: | , , |
| Format: | Journal Article |
| Sprache: | Englisch |
| Veröffentlicht: |
Netherlands
Elsevier B.V
01.10.2014
|
| Schlagworte: | |
| ISSN: | 0304-4165, 0006-3002, 1872-8006 |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| Abstract | Aggrecan is the major non-collagenous component of the intervertebral disc. It is a large proteoglycan possessing numerous glycosaminoglycan chains and the ability to form aggregates in association with hyaluronan. Its abundance and unique molecular features provide the disc with its osmotic properties and ability to withstand compressive loads. Degradation and loss of aggrecan result in impairment of disc function and the onset of degeneration.
This review summarizes current knowledge concerning the structure and function of aggrecan in the normal intervertebral disc and how and why these change in aging and degenerative disc disease. It also outlines how supplementation with aggrecan or a biomimetic may be of therapeutic value in treating the degenerate disc.
Aggrecan abundance reaches a plateau in the early twenties, declining thereafter due to proteolysis, mainly by matrix metalloproteinases and aggrecanases, though degradation of hyaluronan and non-enzymic glycation may also participate. Aggrecan loss is an early event in disc degeneration, although it is a lengthy process as degradation products may accumulate in the disc for decades. The low turnover rate of the remaining aggrecan is an additional contributing factor, preventing protein renewal. It may be possible to retard the degenerative process by restoring the aggrecan content of the disc, or by supplementing with a bioimimetic possessing similar osmotic properties.
This review provides a basis for scientists and clinicians to understand and appreciate the central role of aggrecan in the function, degeneration and repair of the intervertebral disc.
•Aggrecan abundance reaches a plateau in the early twenties, then slowly declines.•Aggrecan abundance declines due to proteolysis, mainly by MMPs and aggrecanases.•Aggrecan loss is an early event in disc degeneration.•The low turnover rate of the degraded aggrecan prevents its replacement.•Aggrecan restoration or bioimimetic supplementation may retard disc degeneration. |
|---|---|
| AbstractList | Aggrecan is the major non-collagenous component of the intervertebral disc. It is a large proteoglycan possessing numerous glycosaminoglycan chains and the ability to form aggregates in association with hyaluronan. Its abundance and unique molecular features provide the disc with its osmotic properties and ability to withstand compressive loads. Degradation and loss of aggrecan result in impairment of disc function and the onset of degeneration.BACKGROUNDAggrecan is the major non-collagenous component of the intervertebral disc. It is a large proteoglycan possessing numerous glycosaminoglycan chains and the ability to form aggregates in association with hyaluronan. Its abundance and unique molecular features provide the disc with its osmotic properties and ability to withstand compressive loads. Degradation and loss of aggrecan result in impairment of disc function and the onset of degeneration.This review summarizes current knowledge concerning the structure and function of aggrecan in the normal intervertebral disc and how and why these change in aging and degenerative disc disease. It also outlines how supplementation with aggrecan or a biomimetic may be of therapeutic value in treating the degenerate disc.SCOPE OF REVIEWThis review summarizes current knowledge concerning the structure and function of aggrecan in the normal intervertebral disc and how and why these change in aging and degenerative disc disease. It also outlines how supplementation with aggrecan or a biomimetic may be of therapeutic value in treating the degenerate disc.Aggrecan abundance reaches a plateau in the early twenties, declining thereafter due to proteolysis, mainly by matrix metalloproteinases and aggrecanases, though degradation of hyaluronan and non-enzymic glycation may also participate. Aggrecan loss is an early event in disc degeneration, although it is a lengthy process as degradation products may accumulate in the disc for decades. The low turnover rate of the remaining aggrecan is an additional contributing factor, preventing protein renewal. It may be possible to retard the degenerative process by restoring the aggrecan content of the disc, or by supplementing with a bioimimetic possessing similar osmotic properties.MAJOR CONCLUSIONSAggrecan abundance reaches a plateau in the early twenties, declining thereafter due to proteolysis, mainly by matrix metalloproteinases and aggrecanases, though degradation of hyaluronan and non-enzymic glycation may also participate. Aggrecan loss is an early event in disc degeneration, although it is a lengthy process as degradation products may accumulate in the disc for decades. The low turnover rate of the remaining aggrecan is an additional contributing factor, preventing protein renewal. It may be possible to retard the degenerative process by restoring the aggrecan content of the disc, or by supplementing with a bioimimetic possessing similar osmotic properties.This review provides a basis for scientists and clinicians to understand and appreciate the central role of aggrecan in the function, degeneration and repair of the intervertebral disc.GENERAL SIGNIFICANCEThis review provides a basis for scientists and clinicians to understand and appreciate the central role of aggrecan in the function, degeneration and repair of the intervertebral disc. Aggrecan is the major non-collagenous component of the intervertebral disc. It is a large proteoglycan possessing numerous glycosaminoglycan chains and the ability to form aggregates in association with hyaluronan. Its abundance and unique molecular features provide the disc with its osmotic properties and ability to withstand compressive loads. Degradation and loss of aggrecan result in impairment of disc function and the onset of degeneration. This review summarizes current knowledge concerning the structure and function of aggrecan in the normal intervertebral disc and how and why these change in aging and degenerative disc disease. It also outlines how supplementation with aggrecan or a biomimetic may be of therapeutic value in treating the degenerate disc. Aggrecan abundance reaches a plateau in the early twenties, declining thereafter due to proteolysis, mainly by matrix metalloproteinases and aggrecanases, though degradation of hyaluronan and non-enzymic glycation may also participate. Aggrecan loss is an early event in disc degeneration, although it is a lengthy process as degradation products may accumulate in the disc for decades. The low turnover rate of the remaining aggrecan is an additional contributing factor, preventing protein renewal. It may be possible to retard the degenerative process by restoring the aggrecan content of the disc, or by supplementing with a bioimimetic possessing similar osmotic properties. This review provides a basis for scientists and clinicians to understand and appreciate the central role of aggrecan in the function, degeneration and repair of the intervertebral disc. •Aggrecan abundance reaches a plateau in the early twenties, then slowly declines.•Aggrecan abundance declines due to proteolysis, mainly by MMPs and aggrecanases.•Aggrecan loss is an early event in disc degeneration.•The low turnover rate of the degraded aggrecan prevents its replacement.•Aggrecan restoration or bioimimetic supplementation may retard disc degeneration. Aggrecan is the major non-collagenous component of the intervertebral disc. It is a large proteoglycan possessing numerous glycosaminoglycan chains and the ability to form aggregates in association with hyaluronan. Its abundance and unique molecular features provide the disc with its osmotic properties and ability to withstand compressive loads. Degradation and loss of aggrecan result in impairment of disc function and the onset of degeneration.This review summarizes current knowledge concerning the structure and function of aggrecan in the normal intervertebral disc and how and why these change in aging and degenerative disc disease. It also outlines how supplementation with aggrecan or a biomimetic may be of therapeutic value in treating the degenerate disc.Aggrecan abundance reaches a plateau in the early twenties, declining thereafter due to proteolysis, mainly by matrix metalloproteinases and aggrecanases, though degradation of hyaluronan and non-enzymic glycation may also participate. Aggrecan loss is an early event in disc degeneration, although it is a lengthy process as degradation products may accumulate in the disc for decades. The low turnover rate of the remaining aggrecan is an additional contributing factor, preventing protein renewal. It may be possible to retard the degenerative process by restoring the aggrecan content of the disc, or by supplementing with a bioimimetic possessing similar osmotic properties.This review provides a basis for scientists and clinicians to understand and appreciate the central role of aggrecan in the function, degeneration and repair of the intervertebral disc. Aggrecan is the major non-collagenous component of the intervertebral disc. It is a large proteoglycan possessing numerous glycosaminoglycan chains and the ability to form aggregates in association with hyaluronan. Its abundance and unique molecular features provide the disc with its osmotic properties and ability to withstand compressive loads. Degradation and loss of aggrecan result in impairment of disc function and the onset of degeneration. This review summarizes current knowledge concerning the structure and function of aggrecan in the normal intervertebral disc and how and why these change in aging and degenerative disc disease. It also outlines how supplementation with aggrecan or a biomimetic may be of therapeutic value in treating the degenerate disc. Aggrecan abundance reaches a plateau in the early twenties, declining thereafter due to proteolysis, mainly by matrix metalloproteinases and aggrecanases, though degradation of hyaluronan and non-enzymic glycation may also participate. Aggrecan loss is an early event in disc degeneration, although it is a lengthy process as degradation products may accumulate in the disc for decades. The low turnover rate of the remaining aggrecan is an additional contributing factor, preventing protein renewal. It may be possible to retard the degenerative process by restoring the aggrecan content of the disc, or by supplementing with a bioimimetic possessing similar osmotic properties. This review provides a basis for scientists and clinicians to understand and appreciate the central role of aggrecan in the function, degeneration and repair of the intervertebral disc. |
| Author | Wachtel, Ellen Roughley, Peter Sivan, Sarit Sara |
| Author_xml | – sequence: 1 givenname: Sarit Sara surname: Sivan fullname: Sivan, Sarit Sara email: ssivan@braude.ac.il organization: Department of Biotechnology Engineering, ORT Braude College, Karmiel 21982 Israel – sequence: 2 givenname: Ellen surname: Wachtel fullname: Wachtel, Ellen organization: Faculty of Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel – sequence: 3 givenname: Peter surname: Roughley fullname: Roughley, Peter organization: Shriners Hospital for Children, Genetics Unit, 1529 Cedar Avenue, Montreal, Quebec H3G 1A6, Canada |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/25065289$$D View this record in MEDLINE/PubMed |
| BookMark | eNqFkU1PJCEQhonR6PjxD4zpowe7BRoaxoPJxri7JkYP6pnQUIxMemgF2mT_vUxGPexB61KEet4qqHcfbYcxAELHBDcEk-582fS9XkBoKCaswaLBpN1CMyIFrSXG3Taa4RazmpGO76H9lJa4BJ_zXbRHOe44lfMZunvIcTJ5inBWuSmY7MdwVumFD4tKB1uVShjfIFajK7eLCEaHyocqP0NJGWKpZeijHirrkzlEO04PCY4-8gF6-n39ePW3vr3_c3P167Y27ZznmnedlYyWcOtTy6wztqO4N0CEcKLlkhHOtbROSOek7o01vekZZx1lFrcH6HTT9yWOrxOkrFZlOgyDDjBOSdHyVUoYk-xHlJTHMEyFmBf05AOd-hVY9RL9Ssd_6nNdBWAbwMQxpQjuCyFYrV1RS7VxRa1dUVio4kqRXfwnMz7r9apz1H74SXy5EUPZ55uHqJLxEAxYX9zIyo7--wbvIj6pWA |
| CitedBy_id | crossref_primary_10_1155_2022_1274580 crossref_primary_10_1002_jsp2_1037 crossref_primary_10_1080_19476337_2023_2245008 crossref_primary_10_2106_JBJS_17_00396 crossref_primary_10_1038_s41598_018_25851_5 crossref_primary_10_1016_j_bioadv_2022_213192 crossref_primary_10_1007_s12079_021_00650_2 crossref_primary_10_1016_j_biopha_2017_06_101 crossref_primary_10_1097_BRS_0000000000001556 crossref_primary_10_1002_sctm_17_0181 crossref_primary_10_3390_metabo11030132 crossref_primary_10_1002_jcp_29684 crossref_primary_10_1155_2022_1792412 crossref_primary_10_1007_s10856_020_06480_9 crossref_primary_10_1096_fj_202001021R crossref_primary_10_1007_s00586_019_06227_3 crossref_primary_10_3390_biom12121804 crossref_primary_10_1016_j_matbio_2018_03_019 crossref_primary_10_3389_fcell_2021_817099 crossref_primary_10_3892_mmr_2017_6334 crossref_primary_10_3390_biom10091244 crossref_primary_10_1177_1535370216657444 crossref_primary_10_1002_jmri_24945 crossref_primary_10_1111_jcmm_14488 crossref_primary_10_3390_antiox11081571 crossref_primary_10_1111_jcmm_15971 crossref_primary_10_1007_s11626_025_01108_0 crossref_primary_10_1002_jsp2_1298 crossref_primary_10_1007_s40291_024_00729_7 crossref_primary_10_1186_s13018_018_0838_6 crossref_primary_10_1155_2016_7031397 crossref_primary_10_1038_s41598_025_04388_4 crossref_primary_10_3390_ijms23136915 crossref_primary_10_1016_j_clinbiomech_2021_105506 crossref_primary_10_1016_j_jbiomech_2019_109573 crossref_primary_10_1089_gtmb_2016_0256 crossref_primary_10_1007_s00441_022_03662_5 crossref_primary_10_7554_eLife_103073_3 crossref_primary_10_1002_jor_24188 crossref_primary_10_1038_s41419_019_1985_3 crossref_primary_10_1002_jsp2_1224 crossref_primary_10_1039_D1BM01589C crossref_primary_10_3390_jcm9051377 crossref_primary_10_1002_sstr_202400330 crossref_primary_10_1038_s41374_018_0036_5 crossref_primary_10_1007_s11010_022_04501_5 crossref_primary_10_1016_j_matbio_2024_10_005 crossref_primary_10_1111_acel_13148 crossref_primary_10_1371_journal_pone_0202640 crossref_primary_10_1002_jsp2_70092 crossref_primary_10_1016_j_bas_2022_100872 crossref_primary_10_1096_fj_202201622RR crossref_primary_10_1002_jbm_a_37594 crossref_primary_10_1016_j_ejrad_2017_03_017 crossref_primary_10_1002_jor_22991 crossref_primary_10_1002_jbm_b_34339 crossref_primary_10_1007_s40279_015_0444_2 crossref_primary_10_1016_j_biochi_2023_05_015 crossref_primary_10_1177_23094990211068203 crossref_primary_10_3892_ijmm_2020_4621 crossref_primary_10_18632_aging_206316 crossref_primary_10_1007_s11033_024_09766_1 crossref_primary_10_1155_2019_3904923 crossref_primary_10_3389_fphys_2021_723220 crossref_primary_10_1002_adfm_202502028 crossref_primary_10_1002_jsp2_1192 crossref_primary_10_1002_jcla_24508 crossref_primary_10_1038_srep33836 crossref_primary_10_3390_ijms22116015 crossref_primary_10_1038_s41467_025_58946_5 crossref_primary_10_1016_j_matbio_2018_02_025 crossref_primary_10_1016_j_biomaterials_2015_12_013 crossref_primary_10_1177_08853282231173115 crossref_primary_10_1002_jor_24880 crossref_primary_10_1210_jc_2016_3313 crossref_primary_10_1016_j_matbio_2019_02_004 crossref_primary_10_1177_0018720816657235 crossref_primary_10_1186_s12920_021_00926_x crossref_primary_10_3892_mmr_2018_9384 crossref_primary_10_1371_journal_pone_0276626 crossref_primary_10_1016_j_arr_2016_04_011 crossref_primary_10_1002_mgg3_2439 crossref_primary_10_1080_03008207_2018_1499731 crossref_primary_10_1002_jbm_a_35858 crossref_primary_10_1002_jsp2_1089 crossref_primary_10_3389_fcell_2022_841831 crossref_primary_10_1016_j_mbplus_2020_100036 crossref_primary_10_3390_biom14040393 crossref_primary_10_3390_life12111866 crossref_primary_10_1016_j_matbio_2020_09_003 crossref_primary_10_1038_s41598_017_17472_1 crossref_primary_10_3390_nu15132872 crossref_primary_10_7554_eLife_103073 crossref_primary_10_1186_s13075_022_02895_7 crossref_primary_10_4158_EP_2019_0518 crossref_primary_10_1016_j_spinee_2019_11_003 crossref_primary_10_3390_ijms221910408 crossref_primary_10_1002_advs_202309032 crossref_primary_10_1089_scd_2022_0007 crossref_primary_10_1002_jor_23583 crossref_primary_10_1186_s12891_023_06891_z crossref_primary_10_1039_C5FD00160A crossref_primary_10_1038_s41434_024_00504_7 crossref_primary_10_1016_j_meatsci_2023_109172 crossref_primary_10_1038_jhg_2017_33 crossref_primary_10_1111_acel_12800 crossref_primary_10_1016_j_arr_2024_102633 crossref_primary_10_1097_GME_0000000000000964 crossref_primary_10_3389_fcell_2022_1083983 crossref_primary_10_3389_fimmu_2022_882407 crossref_primary_10_1155_2023_6210885 crossref_primary_10_1016_j_mad_2017_08_007 crossref_primary_10_1007_s00586_015_4189_2 crossref_primary_10_1038_s41419_020_2543_8 crossref_primary_10_1016_j_intimp_2024_113620 crossref_primary_10_1002_cbin_11767 crossref_primary_10_1111_papr_70062 crossref_primary_10_1080_03008207_2019_1665652 crossref_primary_10_1002_jsp2_1143 crossref_primary_10_1016_j_ajpath_2023_10_011 crossref_primary_10_1016_j_matbio_2024_05_006 crossref_primary_10_1016_j_biopha_2016_08_062 |
| Cites_doi | 10.1520/JFS13449J 10.1016/j.spinee.2012.12.003 10.1002/art.10585 10.1073/pnas.72.8.2891 10.1016/j.actbio.2013.11.010 10.1179/030801882789801304 10.1042/bj3370077 10.1097/00007632-199812010-00009 10.1042/BJ20060579 10.1073/pnas.98.3.944 10.1093/oxfordjournals.jbchem.a022166 10.1074/jbc.270.35.20516 10.1520/JFS14339J 10.3109/03008209309014239 10.1086/444401 10.1073/pnas.071066498 10.1007/s00586-006-0127-7 10.1074/jbc.273.21.12999 10.1126/science.6857259 10.1186/ar3423 10.1016/j.joca.2012.03.012 10.1111/j.1749-6632.1992.tb38648.x 10.1111/j.1469-7580.2010.01227.x 10.22203/eCM.v026a08 10.1038/262279b0 10.1074/jbc.271.31.18456 10.1016/j.actbio.2012.08.041 10.1159/000212218 10.1074/jbc.M109.077503 10.1016/S0021-9258(19)49491-X 10.1016/S0945-053X(02)00069-0 10.1002/mabi.201300112 10.1074/jbc.M512531200 10.1007/s00586-008-0749-z 10.1042/bj2610801 10.1016/j.spinee.2010.09.015 10.1002/art.10627 10.1006/geno.1994.1396 10.1016/S0021-9258(19)75855-4 10.1074/jbc.M113.451948 10.1074/jbc.274.22.15892 10.1016/j.matbio.2010.10.007 10.1016/0021-9150(92)90132-Z 10.1016/0304-4165(90)90168-V 10.1016/j.biotechadv.2007.07.001 10.1111/j.1749-6632.2000.tb06187.x 10.1016/j.spinee.2013.01.041 10.1038/245308a0 10.1002/jcb.10479 10.1016/S0021-9258(18)41799-1 10.1111/j.1749-6632.1996.tb56273.x 10.1097/01.brs.0000162624.95262.73 10.1002/jor.21456 10.1016/j.bbagen.2012.06.010 10.1042/bj3040887 10.1016/S0021-9258(18)45444-0 10.1016/S0021-9258(17)34045-0 10.1016/j.ajhg.2009.12.018 10.1074/jbc.M111.264549 10.1073/pnas.75.3.1204 10.1111/j.1533-2500.2007.00171.x 10.1074/jbc.M006700200 10.1002/jor.1100130211 10.1016/0076-6879(84)06011-0 10.1038/268071a0 10.1016/S0021-9258(19)51154-1 10.1042/bst0180799 10.1097/00007632-199912010-00006 10.1016/0921-8734(91)90016-5 10.1006/abbi.2000.1955 10.1074/jbc.M701523200 10.1074/jbc.M709885200 10.1016/j.joca.2006.02.008 10.1016/j.actbio.2011.12.029 10.1002/1529-0131(200201)46:1<114::AID-ART10025>3.0.CO;2-P 10.1074/jbc.M600296200 10.1186/ar4113 10.1097/01.brs.0000231761.73859.2c 10.1042/bj3300345 10.1007/BF01923584 10.1016/S0945-053X(01)00158-5 10.1016/S0021-9258(17)35257-2 10.1042/bj3260235 10.1074/jbc.272.44.28057 10.1016/0304-4165(82)90017-4 10.1074/jbc.272.21.13974 10.1016/0047-6374(79)90019-8 10.1016/S0021-9258(18)53661-9 10.1016/S0021-9258(19)86286-5 10.1016/0945-053X(94)90198-8 10.1210/jc.2014-1332 10.1016/S0945-053X(01)00170-6 10.1111/j.1365-2133.2003.05618.x 10.1016/S0021-9258(19)85345-0 10.1006/abbi.1997.0261 10.1074/jbc.M006783200 10.1007/s00414-009-0392-1 10.1016/j.ajhg.2008.12.001 |
| ContentType | Journal Article |
| Copyright | 2014 Elsevier B.V. Copyright © 2014 Elsevier B.V. All rights reserved. |
| Copyright_xml | – notice: 2014 Elsevier B.V. – notice: Copyright © 2014 Elsevier B.V. All rights reserved. |
| DBID | AAYXX CITATION CGR CUY CVF ECM EIF NPM 7X8 7S9 L.6 |
| DOI | 10.1016/j.bbagen.2014.07.013 |
| DatabaseName | CrossRef Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed MEDLINE - Academic AGRICOLA AGRICOLA - Academic |
| DatabaseTitle | CrossRef MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) MEDLINE - Academic AGRICOLA AGRICOLA - Academic |
| DatabaseTitleList | MEDLINE - Academic AGRICOLA MEDLINE |
| 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: 7X8 name: MEDLINE - Academic url: https://search.proquest.com/medline sourceTypes: Aggregation Database |
| DeliveryMethod | fulltext_linktorsrc |
| Discipline | Chemistry Biology |
| EISSN | 1872-8006 |
| EndPage | 3189 |
| ExternalDocumentID | 25065289 10_1016_j_bbagen_2014_07_013 S0304416514002517 |
| Genre | Journal Article Review |
| GroupedDBID | --- --K --M .~1 0R~ 1B1 1RT 1~. 1~5 23N 3O- 4.4 457 4G. 53G 5GY 5RE 5VS 7-5 71M 8P~ 9JM AACTN AAEDT AAEDW AAIAV AAIKJ AAKOC AALRI AAOAW AAQFI AAQXK AAXUO ABEFU ABFNM ABGSF ABMAC ABUDA ABXDB ABYKQ ACDAQ ACIUM ACRLP ADBBV ADEZE ADMUD ADUVX AEBSH AEHWI AEKER AFKWA AFTJW AFXIZ AGHFR AGRDE AGUBO AGYEJ AHHHB AIEXJ AIKHN AITUG AJBFU AJOXV ALMA_UNASSIGNED_HOLDINGS AMFUW AMRAJ ASPBG AVWKF AXJTR AZFZN BKOJK BLXMC CS3 DOVZS EBS EFJIC EFLBG EJD EO8 EO9 EP2 EP3 FDB FEDTE FGOYB FIRID FNPLU FYGXN G-2 G-Q GBLVA HLW HVGLF HZ~ IHE J1W KOM LX3 M41 MO0 N9A O-L O9- OAUVE OHT OZT P-8 P-9 PC. Q38 R2- ROL RPZ SBG SCC SDF SDG SDP SES SEW SPCBC SSU SSZ T5K UQL WH7 WUQ XJT XPP ~G- 9DU AAHBH AATTM AAXKI AAYWO AAYXX ABWVN ACLOT ACRPL ACVFH ADCNI ADNMO AEIPS AEUPX AFJKZ AFPUW AGQPQ AIGII AIIUN AKBMS AKRWK AKYEP ANKPU APXCP CITATION EFKBS ~HD -~X .55 .GJ AAYJJ ABJNI AFFNX AI. CGR CUY CVF ECM EIF F5P H~9 K-O MVM NPM RIG TWZ UHS VH1 X7M Y6R YYP ZE2 ZGI ~KM 7X8 7S9 L.6 |
| ID | FETCH-LOGICAL-c395t-566d842222f66d834dfcd620bce177f73584155a8df78ff8abcdcbcb454624d03 |
| ISICitedReferencesCount | 152 |
| ISICitedReferencesURI | http://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=Summon&SrcAuth=ProQuest&DestLinkType=CitingArticles&DestApp=WOS_CPL&KeyUT=000341675900024&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D |
| ISSN | 0304-4165 0006-3002 |
| IngestDate | Sun Sep 28 09:07:55 EDT 2025 Wed Oct 01 14:50:46 EDT 2025 Thu Apr 03 07:09:03 EDT 2025 Sat Nov 29 01:38:00 EST 2025 Tue Nov 18 22:19:00 EST 2025 Fri Feb 23 02:32:43 EST 2024 |
| IsPeerReviewed | true |
| IsScholarly | true |
| Issue | 10 |
| Keywords | CRP NP TNFα ADAMTS Biomimetics Intervertebral disc HYALs Turnover Degeneration Repair Asp CML EGF AF IGD MMPs KS OSM AGEs CEL GAG BMP7 GDF5 ECM IL1 CS IVD TGFβ HA Aggrecan |
| Language | English |
| License | Copyright © 2014 Elsevier B.V. All rights reserved. |
| LinkModel | OpenURL |
| MergedId | FETCHMERGED-LOGICAL-c395t-566d842222f66d834dfcd620bce177f73584155a8df78ff8abcdcbcb454624d03 |
| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 ObjectType-Review-3 content type line 23 |
| PMID | 25065289 |
| PQID | 1566402779 |
| PQPubID | 23479 |
| PageCount | 9 |
| ParticipantIDs | proquest_miscellaneous_2000214484 proquest_miscellaneous_1566402779 pubmed_primary_25065289 crossref_primary_10_1016_j_bbagen_2014_07_013 crossref_citationtrail_10_1016_j_bbagen_2014_07_013 elsevier_sciencedirect_doi_10_1016_j_bbagen_2014_07_013 |
| PublicationCentury | 2000 |
| PublicationDate | 2014-10-01 |
| PublicationDateYYYYMMDD | 2014-10-01 |
| PublicationDate_xml | – month: 10 year: 2014 text: 2014-10-01 day: 01 |
| PublicationDecade | 2010 |
| PublicationPlace | Netherlands |
| PublicationPlace_xml | – name: Netherlands |
| PublicationTitle | Biochimica et biophysica acta |
| PublicationTitleAlternate | Biochim Biophys Acta |
| PublicationYear | 2014 |
| Publisher | Elsevier B.V |
| Publisher_xml | – name: Elsevier B.V |
| References | Doege, Sasaki, Horigan, Hassell, Yamada (bb0010) 1987; 262 Antoniou, Wang, Alaseem, Haglund, Roughley, Mwale (bb0485) 2012; 14 Gawri, Antoniou, Ouellet, Awwad, Steffen, Roughley, Haglund, Mwale (bb0475) 2013; 26 Sajdok, Kotrbova-Kozak, Pilin (bb0390) 2001; 46 Fulop, Walcz, Valyon, Glant (bb0105) 1993; 268 Nilsson, Guo, Dunbar, Popovic, Flynn, Jacobsen, Lui, Hirschhorn, Baron, Dauber (bb0135) 2014 Powell, Vine, Crossman (bb0250) 1992; 97 Sharma, Lee, Choi, Kim, Youn, Trippel, Panitch (bb0510) 2013; 13 Vilim, Fosang (bb0365) 1994; 304 Ohtani, Matsushima, Kobayashi, Kishi (bb0275) 1998; 43 Fosang, Neame, Last, Hardingham, Murphy, Hamilton (bb0060) 1992; 267 Johnson, Caterson, Eisenstein, Roberts (bb0160) 2005; 30 Roughley, Melching, Heathfield, Pearce, Mort (bb0155) 2006; 15 Roher, Lowenson, Clarke, Wolkow, Wang, Cotter, Reardon, Zurcher-Neely, Heinrikson, Ball (bb0425) 1993; 268 Stadtman, Levine (bb0340) 2000; 899 Verzijl, DeGroot, Bank, Bayliss, Bijlsma, Lafeber, Maroudas, TeKoppele (bb0255) 2001; 20 Hristova, Jarzem, Ouellet, Roughley, Epure, Antoniou, Mwale (bb0170) 2011; 29 Stattin, Wiklund, Lindblom, Onnerfjord, Jonsson, Tegner, Sasaki, Struglics, Lohmander, Dahl, Heinegard, Aspberg (bb0140) 2010; 86 Raj (bb0460) 2008; 8 Doege, Sasaki, Kimura, Yamada (bb0015) 1991; 266 Bada (bb0225) 1984; 106 Sivan, Wachtel, Tsitron, Sakkee, van der Ham, Degroot, Roberts, Maroudas (bb0305) 2008; 283 Lowenson, Clarke (bb0415) 1988; 14 Helfman, Bada, Shou (bb0405) 1977; 23 Bada (bb0355) 1984; 106 Ritz-Timme, Laumeier, Collins (bb0265) 2003; 149 Barry, Rosenberg, Gaw, Gaw, Koob, Neame (bb0055) 1995; 270 Neame, Barry (bb0050) 1993; 49 Sivan, Roberts, Urban, Menage, Bramhill, Campbell, Franklin, Lydon, Merkher, Maroudas, Tighe (bb0500) 2014; 10 Iatridis, Godburn, Wuertz, Alini, Roughley (bb0180) 2010 Mwale, Demers, Petit, Roughley, Poole, Steffen, Aebi, Antoniou (bb0470) 2003; 88 Santer, White, Roughley (bb0070) 1982; 716 Tomiyama, Asano, Furiya, Shirasawa, Endo, Mori (bb0435) 1994; 269 Sztrolovics, Alini, Roughley, Mort (bb0175) 1997; 326 Michalek, Buckley, Bonassar, Cohen, Iatridis (bb0495) 2010; 10 Sivan, Van El, Merkher, Schmelzer, Zuurmond, Heinz, Wachtel, Varga, Lazary, Brayda-Bruno, Maroudas (bb0300) 2012; 1820 Kepler, Ponnappan, Tannoury, Risbud, Anderson (bb0445) 2013; 13 Thorpe, Streeter, Pinchbeck, Goodship, Clegg, Birch (bb0280) 2010; 285 Bolton, Dudhia, Bayliss (bb0370) 1999; 337 Barry, Neame, Sasse, Pearson (bb0075) 1994; 14 Sivan, Tsitron, Wachtel, Roughley, Sakkee, van der Ham, Degroot, Maroudas (bb0220) 2006; 399 Tortorella, Liu, Burn, Newton, Arner (bb0195) 2002; 21 Rodriguez, Roughley (bb0215) 2006; 14 Fosang, Hardingham (bb0065) 1989; 261 Walcz, Deak, Erhardt, Coulter, Fulop, Horvath, Doege, Glant (bb0025) 1994; 22 Chen, Temple, Ng, Verzijl, DeGroot, TeKoppele, Sah (bb0330) 2002; 46 Verzijl, DeGroot, Ben, Brau-Benjamin, Maroudas, Bank, Mizrahi, Schalkwijk, Thorpe, Baynes, Bijlsma, Lafeber, TeKoppele (bb0345) 2002; 46 Robinson, Robinson (bb0410) 2001; 98 Olin, Morgelin, Sasaki, Timpl, Heinegard, Aspberg (bb0110) 2001; 276 Bayliss, Osborne, Woodhouse, Davidson (bb0035) 1999; 274 Bailey, Wotton, Sims, Thompson (bb0320) 1993; 29 Willett, Kandel, De Croos, Avery, Grynpas (bb0350) 2012; 20 Masters, Bada, Zigler (bb0245) 1977; 268 Tompson, Merriman, Funari, Fresquet, Lachman, Rimoin, Nelson, Briggs, Cohn, Krakow (bb0145) 2009; 84 Melching, Roughley (bb0120) 1990; 1035 Watanabe, Cheung, Itano, Kimata, Yamada (bb0045) 1997; 272 Stern, Kogan, Jedrzejas, Soltes (bb0210) 2007; 25 Johnson, Caterson, Eisenstein, Hynds, Snow, Roberts (bb0165) 2002; 46 Masuda (bb0465) 2008; 17 Masters, Bada, Zigler (bb0420) 1978; 75 Verzijl, DeGroot, Thorpe, Bank, Shaw, Lyons, Bijlsma, Lafeber, Baynes, TeKoppele (bb0260) 2000; 275 Sivan, Tsitron, Wachtel, Roughley, Sakkee, van der Ham, DeGroot, Roberts, Maroudas (bb0295) 2006; 281 Watanabe, Yamada, Kimata (bb0005) 1998; 124 London, West, Shemin, Rittenberg (bb0310) 1950; 184 Garcia-Cosamalon, del Valle, Calavia, Garcia-Suarez, Lopez-Muniz, Otero, Vega (bb0455) 2010; 217 Lepperdinger, Mullegger, Kreil (bb0205) 2001; 20 Rattan, Derventzi, Clark (bb0335) 1992; 663 Mayer, Iatridis, Chan, Qureshi, Gottesman, Hecht (bb0450) 2013; 13 Kawaguchi, Osada, Kanamori, Ishihara, Ohmori, Matsui, Kimura (bb0090) 1999; 24 Bada, Kvenvolden, Peterson (bb0270) 1973; 245 Dudhia, Davidson, Wells, Hardingham, Bayliss (bb0115) 1996; 785 Durigova, Nagase, Mort, Roughley (bb0190) 2011; 30 Man, Sandhouse, Burg, Fisher (bb0240) 1983; 220 Adams, Roughley (bb0440) 2006; 31 Duance, Crean, Sims, Avery, Smith, Menage, Eisenstein, Roberts (bb0315) 1998; 23 Bada (bb0400) 1982; 7 Roughley, White (bb0095) 1980; 255 Rossi, Bonaventure, Delezoide, Cetta, Superti-Furga (bb0150) 1996; 271 Zheng, Luo, Tanzer (bb0100) 1998; 273 Doege, Coulter, Meek, Maslen, Wood (bb0085) 1997; 272 Hering, Kollar, Huynh (bb0020) 1997; 345 Li, Schwartz, Vertel (bb0030) 1993; 268 Shimizu, Watanabe, Ogawara, Mori, Shirasawa (bb0430) 2000; 381 Deutsch, Midura, Plaas (bb0040) 1995; 13 Helfman, Bada (bb0235) 1976; 262 Rodriguez, Roland, Plaas, Roughley (bb0080) 2006; 281 Gleghorn, Ramesar, Beighton, Wallis (bb0130) 2005; 77 Bank, Bayliss, Lafeber, Maroudas, Tekoppele (bb0325) 1998; 330 Ritz, Schutz (bb0290) 1993; 38 Wang, Markova, Anderson, Zheng, Shapiro, Risbud (bb0185) 2011; 286 Mwale, Masuda, Pichika, Epure, Yoshikawa, Hemmad, Roughley, Antoniou (bb0490) 2011; 13 Bayliss (bb0360) 1990; 18 Helfman, Bada (bb0230) 1975; 72 Gendron, Kashiwagi, Lim, Enghild, Thogersen, Hughes, Caterson, Nagase (bb0200) 2007; 282 Bernhard, Panitch (bb0505) 2012; 8 Geiger, Clarke (bb0395) 1987; 262 Dobberstein, Tung, Ritz-Timme (bb0285) 2009; 124 Wang, Weitzmann, Sangadala, Hutton, Yoon (bb0480) 2013; 288 McKerrow (bb0375) 1979; 10 Robinson, Robinson (bb0380) 2001; 98 Sharma, Panitch, Neu (bb0515) 2013; 9 Hascall (bb0125) 1988; 1 Rosenberger (bb0385) 1991; 256 Bolton (10.1016/j.bbagen.2014.07.013_bb0370) 1999; 337 Deutsch (10.1016/j.bbagen.2014.07.013_bb0040) 1995; 13 Sajdok (10.1016/j.bbagen.2014.07.013_bb0390) 2001; 46 Mayer (10.1016/j.bbagen.2014.07.013_bb0450) 2013; 13 Neame (10.1016/j.bbagen.2014.07.013_bb0050) 1993; 49 Li (10.1016/j.bbagen.2014.07.013_bb0030) 1993; 268 Robinson (10.1016/j.bbagen.2014.07.013_bb0380) 2001; 98 Kepler (10.1016/j.bbagen.2014.07.013_bb0445) 2013; 13 Bada (10.1016/j.bbagen.2014.07.013_bb0355) 1984; 106 Dobberstein (10.1016/j.bbagen.2014.07.013_bb0285) 2009; 124 Johnson (10.1016/j.bbagen.2014.07.013_bb0160) 2005; 30 Fosang (10.1016/j.bbagen.2014.07.013_bb0060) 1992; 267 Helfman (10.1016/j.bbagen.2014.07.013_bb0405) 1977; 23 Santer (10.1016/j.bbagen.2014.07.013_bb0070) 1982; 716 Sivan (10.1016/j.bbagen.2014.07.013_bb0300) 2012; 1820 Johnson (10.1016/j.bbagen.2014.07.013_bb0165) 2002; 46 Shimizu (10.1016/j.bbagen.2014.07.013_bb0430) 2000; 381 Bayliss (10.1016/j.bbagen.2014.07.013_bb0360) 1990; 18 Masuda (10.1016/j.bbagen.2014.07.013_bb0465) 2008; 17 Bada (10.1016/j.bbagen.2014.07.013_bb0270) 1973; 245 Sivan (10.1016/j.bbagen.2014.07.013_bb0295) 2006; 281 Dudhia (10.1016/j.bbagen.2014.07.013_bb0115) 1996; 785 Stern (10.1016/j.bbagen.2014.07.013_bb0210) 2007; 25 Vilim (10.1016/j.bbagen.2014.07.013_bb0365) 1994; 304 Ritz-Timme (10.1016/j.bbagen.2014.07.013_bb0265) 2003; 149 Adams (10.1016/j.bbagen.2014.07.013_bb0440) 2006; 31 Doege (10.1016/j.bbagen.2014.07.013_bb0010) 1987; 262 Wang (10.1016/j.bbagen.2014.07.013_bb0185) 2011; 286 Barry (10.1016/j.bbagen.2014.07.013_bb0055) 1995; 270 Roher (10.1016/j.bbagen.2014.07.013_bb0425) 1993; 268 Watanabe (10.1016/j.bbagen.2014.07.013_bb0045) 1997; 272 Masters (10.1016/j.bbagen.2014.07.013_bb0245) 1977; 268 Bank (10.1016/j.bbagen.2014.07.013_bb0325) 1998; 330 Garcia-Cosamalon (10.1016/j.bbagen.2014.07.013_bb0455) 2010; 217 Sivan (10.1016/j.bbagen.2014.07.013_bb0305) 2008; 283 Michalek (10.1016/j.bbagen.2014.07.013_bb0495) 2010; 10 Hascall (10.1016/j.bbagen.2014.07.013_bb0125) 1988; 1 McKerrow (10.1016/j.bbagen.2014.07.013_bb0375) 1979; 10 Robinson (10.1016/j.bbagen.2014.07.013_bb0410) 2001; 98 Mwale (10.1016/j.bbagen.2014.07.013_bb0470) 2003; 88 Raj (10.1016/j.bbagen.2014.07.013_bb0460) 2008; 8 Fulop (10.1016/j.bbagen.2014.07.013_bb0105) 1993; 268 Watanabe (10.1016/j.bbagen.2014.07.013_bb0005) 1998; 124 Fosang (10.1016/j.bbagen.2014.07.013_bb0065) 1989; 261 Sivan (10.1016/j.bbagen.2014.07.013_bb0500) 2014; 10 Tortorella (10.1016/j.bbagen.2014.07.013_bb0195) 2002; 21 Durigova (10.1016/j.bbagen.2014.07.013_bb0190) 2011; 30 Helfman (10.1016/j.bbagen.2014.07.013_bb0230) 1975; 72 Bailey (10.1016/j.bbagen.2014.07.013_bb0320) 1993; 29 Wang (10.1016/j.bbagen.2014.07.013_bb0480) 2013; 288 Sztrolovics (10.1016/j.bbagen.2014.07.013_bb0175) 1997; 326 Willett (10.1016/j.bbagen.2014.07.013_bb0350) 2012; 20 Stadtman (10.1016/j.bbagen.2014.07.013_bb0340) 2000; 899 Chen (10.1016/j.bbagen.2014.07.013_bb0330) 2002; 46 Doege (10.1016/j.bbagen.2014.07.013_bb0085) 1997; 272 London (10.1016/j.bbagen.2014.07.013_bb0310) 1950; 184 Gawri (10.1016/j.bbagen.2014.07.013_bb0475) 2013; 26 Hering (10.1016/j.bbagen.2014.07.013_bb0020) 1997; 345 Verzijl (10.1016/j.bbagen.2014.07.013_bb0260) 2000; 275 Nilsson (10.1016/j.bbagen.2014.07.013_bb0135) 2014 Tompson (10.1016/j.bbagen.2014.07.013_bb0145) 2009; 84 Tomiyama (10.1016/j.bbagen.2014.07.013_bb0435) 1994; 269 Olin (10.1016/j.bbagen.2014.07.013_bb0110) 2001; 276 Hristova (10.1016/j.bbagen.2014.07.013_bb0170) 2011; 29 Gleghorn (10.1016/j.bbagen.2014.07.013_bb0130) 2005; 77 Geiger (10.1016/j.bbagen.2014.07.013_bb0395) 1987; 262 Sharma (10.1016/j.bbagen.2014.07.013_bb0510) 2013; 13 Rodriguez (10.1016/j.bbagen.2014.07.013_bb0080) 2006; 281 Walcz (10.1016/j.bbagen.2014.07.013_bb0025) 1994; 22 Antoniou (10.1016/j.bbagen.2014.07.013_bb0485) 2012; 14 Roughley (10.1016/j.bbagen.2014.07.013_bb0095) 1980; 255 Bayliss (10.1016/j.bbagen.2014.07.013_bb0035) 1999; 274 Kawaguchi (10.1016/j.bbagen.2014.07.013_bb0090) 1999; 24 Helfman (10.1016/j.bbagen.2014.07.013_bb0235) 1976; 262 Gendron (10.1016/j.bbagen.2014.07.013_bb0200) 2007; 282 Bada (10.1016/j.bbagen.2014.07.013_bb0225) 1984; 106 Melching (10.1016/j.bbagen.2014.07.013_bb0120) 1990; 1035 Doege (10.1016/j.bbagen.2014.07.013_bb0015) 1991; 266 Thorpe (10.1016/j.bbagen.2014.07.013_bb0280) 2010; 285 Barry (10.1016/j.bbagen.2014.07.013_bb0075) 1994; 14 Bernhard (10.1016/j.bbagen.2014.07.013_bb0505) 2012; 8 Rossi (10.1016/j.bbagen.2014.07.013_bb0150) 1996; 271 Ritz (10.1016/j.bbagen.2014.07.013_bb0290) 1993; 38 Iatridis (10.1016/j.bbagen.2014.07.013_bb0180) 2010 Sivan (10.1016/j.bbagen.2014.07.013_bb0220) 2006; 399 Verzijl (10.1016/j.bbagen.2014.07.013_bb0255) 2001; 20 Rattan (10.1016/j.bbagen.2014.07.013_bb0335) 1992; 663 Verzijl (10.1016/j.bbagen.2014.07.013_bb0345) 2002; 46 Duance (10.1016/j.bbagen.2014.07.013_bb0315) 1998; 23 Powell (10.1016/j.bbagen.2014.07.013_bb0250) 1992; 97 Mwale (10.1016/j.bbagen.2014.07.013_bb0490) 2011; 13 Masters (10.1016/j.bbagen.2014.07.013_bb0420) 1978; 75 Rodriguez (10.1016/j.bbagen.2014.07.013_bb0215) 2006; 14 Sharma (10.1016/j.bbagen.2014.07.013_bb0515) 2013; 9 Rosenberger (10.1016/j.bbagen.2014.07.013_bb0385) 1991; 256 Bada (10.1016/j.bbagen.2014.07.013_bb0400) 1982; 7 Lowenson (10.1016/j.bbagen.2014.07.013_bb0415) 1988; 14 Stattin (10.1016/j.bbagen.2014.07.013_bb0140) 2010; 86 Ohtani (10.1016/j.bbagen.2014.07.013_bb0275) 1998; 43 Man (10.1016/j.bbagen.2014.07.013_bb0240) 1983; 220 Zheng (10.1016/j.bbagen.2014.07.013_bb0100) 1998; 273 Lepperdinger (10.1016/j.bbagen.2014.07.013_bb0205) 2001; 20 Roughley (10.1016/j.bbagen.2014.07.013_bb0155) 2006; 15 |
| References_xml | – volume: 13 start-page: 1228 year: 2013 end-page: 1237 ident: bb0510 article-title: Biomimetic aggrecan reduces cartilage extracellular matrix from degradation and lowers catabolic activity in ex vivo and in vivo models publication-title: Macromol. Biosci. – volume: 283 start-page: 8796 year: 2008 end-page: 8801 ident: bb0305 article-title: Collagen turnover in normal and degenerate human intervertebral discs as determined by the racemization of aspartic acid publication-title: J. Biol. Chem. – volume: 77 start-page: 484 year: 2005 end-page: 490 ident: bb0130 article-title: A mutation in the variable repeat region of the aggrecan gene (AGC1) causes a form of spondyloepiphyseal dysplasia associated with severe, premature osteoarthritis publication-title: Am. J. Hum. Genet. – volume: 46 start-page: 2658 year: 2002 end-page: 2664 ident: bb0165 article-title: Human intervertebral disc aggrecan inhibits nerve growth in vitro publication-title: Arthritis Rheum. – volume: 14 start-page: 323 year: 1994 end-page: 328 ident: bb0075 article-title: Length variation in the keratan sulfate domain of mammalian aggrecan publication-title: Matrix Biol. – volume: 20 start-page: 509 year: 2001 end-page: 514 ident: bb0205 article-title: Hyal2—less active, but more versatile? publication-title: Matrix Biol. – volume: 23 start-page: 2545 year: 1998 end-page: 2551 ident: bb0315 article-title: Changes in collagen cross-linking in degenerative disc disease and scoliosis publication-title: Spine – volume: 13 start-page: 299 year: 2013 end-page: 317 ident: bb0450 article-title: Genetic polymorphisms associated with intervertebral disc degeneration publication-title: Spine J. – volume: 286 start-page: 39738 year: 2011 end-page: 39749 ident: bb0185 article-title: TNF-alpha and IL-1beta promote a disintegrin-like and metalloprotease with thrombospondin type I motif-5-mediated aggrecan degradation through syndecan-4 in intervertebral disc publication-title: J. Biol. Chem. – volume: 10 start-page: 1124 year: 2014 end-page: 1133 ident: bb0500 article-title: Injectable hydrogels with high fixed charge density and swelling pressure for nucleus pulposus repair: biomimetic glycosaminoglycan analogues publication-title: Acta Biomater. – volume: 106 start-page: 98 year: 1984 end-page: 115 ident: bb0355 article-title: In vivo racemization in mammalian proteins publication-title: Posttranslational modifications, in: Methods Enzymol – volume: 29 start-page: 1888 year: 2011 end-page: 1895 ident: bb0170 article-title: Calcification in human intervertebral disc degeneration and scoliosis publication-title: J. Orthop. Res. – volume: 256 start-page: 255 year: 1991 end-page: 262 ident: bb0385 article-title: Senescence and the accumulation of abnormal proteins publication-title: Mutat. Res. – volume: 899 start-page: 191 year: 2000 end-page: 208 ident: bb0340 article-title: Protein oxidation publication-title: Ann. N. Y. Acad. Sci. – volume: 75 start-page: 1204 year: 1978 end-page: 1208 ident: bb0420 article-title: Aspartic acid racemization in heavy molecular weight crystallins and water insoluble protein from normal human lenses and cataracts publication-title: Proc. Natl. Acad. Sci. – volume: 10 start-page: 371 year: 1979 end-page: 377 ident: bb0375 article-title: Non-enzymatic, post-translational, amino acid modifications in ageing. A brief review publication-title: Mech. Ageing Dev. – volume: 46 start-page: 114 year: 2002 end-page: 123 ident: bb0345 article-title: Crosslinking by advanced glycation end products increases the stiffness of the collagen network in human articular cartilage: a possible mechanism through which age is a risk factor for osteoarthritis publication-title: Arthritis Rheum. – year: 2014 ident: bb0135 article-title: Short stature, accelerated bone maturation, and early growth cessation due to heterozygous aggrecan mutations publication-title: J. Clin. Endocrinol. Metab. – volume: 97 start-page: 201 year: 1992 end-page: 208 ident: bb0250 article-title: On the accumulation of D-aspartate in elastin and other proteins of the ageing aorta publication-title: Atherosclerosis – volume: 281 start-page: 13009 year: 2006 end-page: 13014 ident: bb0295 article-title: Aggrecan turnover in human intervertebral disc as determined by the racemization of aspartic acid publication-title: J. Biol. Chem. – volume: 98 start-page: 4367 year: 2001 end-page: 4372 ident: bb0380 article-title: Prediction of protein deamidation rates from primary and three-dimensional structure publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 13 start-page: R120 year: 2011 ident: bb0490 article-title: The efficacy of Link N as a mediator of repair in a rabbit model of intervertebral disc degeneration publication-title: Arthritis Res. Ther. – volume: 1 start-page: 198 year: 1988 ident: bb0125 article-title: Proteoglycans: the chondroitin sulfate/keratan sulfate proteoglycan of cartilage publication-title: ISI Atlas Sci. Biochem. – volume: 266 start-page: 894 year: 1991 end-page: 902 ident: bb0015 article-title: Complete coding sequence and deduced primary structure of the human cartilage large aggregating proteoglycan, aggrecan. Human-specific repeats, and additional alternatively spliced forms publication-title: J. Biol. Chem. – volume: 106 start-page: 98 year: 1984 end-page: 115 ident: bb0225 article-title: In vivo racemization in mammalian proteins publication-title: Methods Enzymol. – volume: 9 start-page: 4618 year: 2013 end-page: 4625 ident: bb0515 article-title: Incorporation of an aggrecan mimic prevents proteolytic degradation of anisotropic cartilage analogs publication-title: Acta Biomater. – volume: 30 start-page: 1139 year: 2005 end-page: 1147 ident: bb0160 article-title: Human intervertebral disc aggrecan inhibits endothelial cell adhesion and cell migration in vitro publication-title: Spine (Phila Pa 1976) – volume: 149 start-page: 951 year: 2003 end-page: 959 ident: bb0265 article-title: Aspartic acid racemization: evidence for marked longevity of elastin in human skin publication-title: Br. J. Dermatol. – volume: 88 start-page: 1202 year: 2003 end-page: 1213 ident: bb0470 article-title: A synthetic peptide of link protein stimulates the biosynthesis of collagens II, IX and proteoglycan by cells of the intervertebral disc publication-title: J. Cell. Biochem. – volume: 86 start-page: 126 year: 2010 end-page: 137 ident: bb0140 article-title: A missense mutation in the aggrecan C-type lectin domain disrupts extracellular matrix interactions and causes dominant familial osteochondritis dissecans publication-title: Am. J. Hum. Genet. – volume: 124 start-page: 269 year: 2009 end-page: 275 ident: bb0285 article-title: Aspartic acid racemisation in purified elastin from arteries as basis for age estimation publication-title: Int. J. Legal Med. – volume: 98 start-page: 944 year: 2001 end-page: 949 ident: bb0410 article-title: Molecular Clocks publication-title: Proc. Natl. Acad. Sci. USA – volume: 326 start-page: 235 year: 1997 end-page: 241 ident: bb0175 article-title: Aggrecan degradation in human intervertebral disc and articular cartilage publication-title: Biochem. J. – volume: 23 start-page: 419 year: 1977 end-page: 425 ident: bb0405 article-title: Considerations on the role of aspartic acid racemization in the aging process publication-title: Gerontology – volume: 381 start-page: 225 year: 2000 end-page: 234 ident: bb0430 article-title: Isoaspartate formation and neurodegeneration in Alzheimer's disease publication-title: Arch. Biochem. Biophys. – volume: 272 start-page: 13974 year: 1997 end-page: 13979 ident: bb0085 article-title: A human-specific polymorphism in the coding region of the aggrecan gene. Variable number of tandem repeats produce a range of core protein sizes in the general population publication-title: J. Biol. Chem. – volume: 281 start-page: 18444 year: 2006 end-page: 18450 ident: bb0080 article-title: The glycosaminoglycan attachment regions of human aggrecan publication-title: J. Biol. Chem. – volume: 21 start-page: 499 year: 2002 end-page: 511 ident: bb0195 article-title: Characterization of human aggrecanase 2 (ADAM-TS5): substrate specificity studies and comparison with aggrecanase 1 (ADAM-TS4) publication-title: Matrix Biol. – volume: 285 start-page: 15674 year: 2010 end-page: 15681 ident: bb0280 article-title: Aspartic acid racemization and collagen degradation markers reveal an accumulation of damage in tendon collagen that is enhanced with aging publication-title: J. Biol. Chem. – volume: 268 start-page: 17377 year: 1993 end-page: 17383 ident: bb0105 article-title: Expression of alternatively spliced epidermal growth factor-like domains in aggrecans of different species. Evidence for a novel module publication-title: J. Biol. Chem. – volume: 43 start-page: 949 year: 1998 end-page: 953 ident: bb0275 article-title: Evaluation of aspartic acid racemization ratios in the human femur for age estimation publication-title: J. Forensic Sci. – volume: 72 start-page: 2891 year: 1975 end-page: 2894 ident: bb0230 article-title: Aspartic acid racemization in tooth enamel from living humans publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 220 start-page: 1407 year: 1983 end-page: 1408 ident: bb0240 article-title: Accumulation of D-aspartic acid with age in the human brain publication-title: Science – volume: 24 start-page: 2456 year: 1999 end-page: 2460 ident: bb0090 article-title: Association between an aggrecan gene polymorphism and lumbar disc degeneration publication-title: Spine (Phila Pa 1976) – volume: 26 start-page: 107 year: 2013 end-page: 119 ident: bb0475 article-title: Link-N can stimulate proteoglycan synthesis in the degenerated human intervertebral discs publication-title: Eur. Cell Mater. – volume: 716 start-page: 277 year: 1982 end-page: 282 ident: bb0070 article-title: O-Linked oligosaccharides of human articular cartilage proteoglycan publication-title: Biochim. Biophys. Acta – volume: 337 start-page: 77 year: 1999 end-page: 82 ident: bb0370 article-title: Age-related changes in the synthesis of link protein and aggrecan in human articular cartilage: implications for aggregate stability publication-title: Biochem. J. – volume: 330 start-page: 345 year: 1998 end-page: 351 ident: bb0325 article-title: Ageing and zonal variation in post-translational modification of collagen in normal human articular cartilage. The age-related increase in non-enzymatic glycation affects biomechanical properties of cartilage publication-title: Biochem. J. – volume: 46 start-page: 5 year: 2001 end-page: 8 ident: bb0390 article-title: Age determination using peptide mapping of non-collagenous proteins in human dentin publication-title: Soud. Lek. – volume: 49 start-page: 393 year: 1993 end-page: 402 ident: bb0050 article-title: The link proteins publication-title: Experientia – volume: 20 start-page: 409 year: 2001 end-page: 417 ident: bb0255 article-title: Age-related accumulation of the advanced glycation endproduct pentosidine in human articular cartilage aggrecan: the use of pentosidine levels as a quantitative measure of protein turnover publication-title: Matrix Biol. – volume: 245 start-page: 308 year: 1973 end-page: 310 ident: bb0270 article-title: Racemization of amino acids in bones publication-title: Nature – volume: 8 start-page: 1543 year: 2012 end-page: 1550 ident: bb0505 article-title: Synthesis and characterization of an aggrecan mimic publication-title: Acta Biomater. – volume: 20 start-page: 736 year: 2012 end-page: 744 ident: bb0350 article-title: Enhanced level of non-enzymatic glycation and pentosidine crosslinking in spontaneous osteoarthritis progression publication-title: Osteoarthritis Cartilage – volume: 268 start-page: 23504 year: 1993 end-page: 23511 ident: bb0030 article-title: cDNA cloning of chick cartilage chondroitin sulfate (aggrecan) core protein and identification of a stop codon in the aggrecan gene associated with the chondrodystrophy, nanomelia publication-title: J. Biol. Chem. – volume: 184 start-page: 351 year: 1950 end-page: 358 ident: bb0310 article-title: On the origin of bile pigment in normal man publication-title: J. Biol. Chem. – volume: 10 start-page: 1098 year: 2010 end-page: 1105 ident: bb0495 article-title: The effects of needle puncture injury on microscale shear strain in the intervertebral disc annulus fibrosus publication-title: Spine J. – volume: 17 start-page: 441 year: 2008 end-page: 451 ident: bb0465 article-title: Biological repair of the degenerated intervertebral disc by the injection of growth factors publication-title: Eur. Spine J. – volume: 267 start-page: 19470 year: 1992 end-page: 19474 ident: bb0060 article-title: The interglobular domain of cartilage aggrecan is cleaved by PUMP, gelatinases, and cathepsin B publication-title: J. Biol. Chem. – volume: 273 start-page: 12999 year: 1998 end-page: 13006 ident: bb0100 article-title: Aggrecan synthesis and secretion. A paradigm for molecular and cellular coordination of multiglobular protein folding and intracellular trafficking publication-title: J. Biol. Chem. – volume: 268 start-page: 3072 year: 1993 end-page: 3083 ident: bb0425 article-title: Structural alterations in the peptide backbone of beta-amyloid core protein may account for its deposition and stability in Alzheimer's disease publication-title: J. Biol. Chem. – volume: 14 start-page: 823 year: 2006 end-page: 829 ident: bb0215 article-title: Link protein can retard the degradation of hyaluronan in proteoglycan aggregates publication-title: Osteoarthritis Cartilage – volume: 38 start-page: 633 year: 1993 end-page: 640 ident: bb0290 article-title: Aspartic acid racemization in intervertebral discs as an aid to postmortem estimation of age at death publication-title: J. Forensic Sci. – volume: 288 start-page: 28243 year: 2013 end-page: 28253 ident: bb0480 article-title: Link protein N-terminal peptide binds to bone morphogenetic protein (BMP) type II receptor and drives matrix protein expression in rabbit intervertebral disc cells publication-title: J. Biol. Chem. – volume: 1820 start-page: 1671 year: 2012 end-page: 1677 ident: bb0300 article-title: Longevity of elastin in human intervertebral disc as probed by the racemization of aspartic acid publication-title: Biochim. Biophys. Acta – volume: 25 start-page: 537 year: 2007 end-page: 557 ident: bb0210 article-title: The many ways to cleave hyaluronan publication-title: Biotechnol. Adv. – volume: 7 start-page: 30 year: 1982 end-page: 46 ident: bb0400 article-title: Racemization of amino acids in nature publication-title: Interdisc. Sci. Rev. – volume: 271 start-page: 18456 year: 1996 end-page: 18464 ident: bb0150 article-title: Undersulfation of proteoglycans synthesized by chondrocytes from a patient with achondrogenesis type 1B homozygous for an L483P substitution in the diastrophic dysplasia sulfate transporter publication-title: J. Biol. Chem. – volume: 785 start-page: 245 year: 1996 end-page: 247 ident: bb0115 article-title: Studies on the G3 domain of aggrecan from human cartilage publication-title: Ann. N. Y. Acad. Sci. – volume: 270 start-page: 20516 year: 1995 end-page: 20524 ident: bb0055 article-title: N- and O-linked keratan sulfate on the hyaluronan binding region of aggrecan from mature and immature bovine cartilage publication-title: J. Biol. Chem. – volume: 8 start-page: 18 year: 2008 end-page: 44 ident: bb0460 article-title: Intervertebral disc: anatomy–physiology–pathophysiology–treatment publication-title: Pain Pract. – volume: 84 start-page: 72 year: 2009 end-page: 79 ident: bb0145 article-title: A recessive skeletal dysplasia, SEMD aggrecan type, results from a missense mutation affecting the C-type lectin domain of aggrecan publication-title: Am. J. Hum. Genet. – volume: 217 start-page: 1 year: 2010 end-page: 15 ident: bb0455 article-title: Intervertebral disc, sensory nerves and neurotrophins: who is who in discogenic pain? publication-title: J. Anat. – volume: 272 start-page: 28057 year: 1997 end-page: 28065 ident: bb0045 article-title: Identification of hyaluronan-binding domains of aggrecan publication-title: J. Biol. Chem. – start-page: 203 year: 2010 end-page: 209 ident: bb0180 article-title: Region-dependent aggrecan degradation patterns in the rat Intervertebral disc are affected by mechanical loading in vivo publication-title: Spine – volume: 269 start-page: 10205 year: 1994 end-page: 10208 ident: bb0435 article-title: Racemization of Asp23 residue affects the aggregation properties of Alzheimer amyloid beta protein analogues publication-title: J. Biol. Chem. – volume: 399 start-page: 29 year: 2006 end-page: 35 ident: bb0220 article-title: Age-related accumulation of pentosidine in aggrecan and collagen from normal and degenerate human intervertebral discs publication-title: Biochem. J. – volume: 18 start-page: 799 year: 1990 end-page: 802 ident: bb0360 article-title: Proteoglycan structure and metabolism during maturation and ageing of human articular cartilage publication-title: Biochem. Soc. Trans. – volume: 262 start-page: 17757 year: 1987 end-page: 17767 ident: bb0010 article-title: Complete primary structure of the rat cartilage proteoglycan core protein deduced from cDNA clones publication-title: J. Biol. Chem. – volume: 276 start-page: 1253 year: 2001 end-page: 1261 ident: bb0110 article-title: The proteoglycans aggrecan and versican form networks with fibulin-2 through their lectin domain binding publication-title: J. Biol. Chem. – volume: 304 start-page: 887 year: 1994 end-page: 894 ident: bb0365 article-title: Proteoglycans isolated from dissociative extracts of differently aged human articular cartilage: characterization of naturally occurring hyaluronan-binding fragments of aggrecan publication-title: Biochem. J. – volume: 345 start-page: 259 year: 1997 end-page: 270 ident: bb0020 article-title: Complete coding sequence of bovine aggrecan: comparative structural analysis publication-title: Arch. Biochem. Biophys. – volume: 31 start-page: 2151 year: 2006 end-page: 2161 ident: bb0440 article-title: What is intervertebral disc degeneration, and what causes it? publication-title: Spine (Phila Pa 1976) – volume: 275 start-page: 39027 year: 2000 end-page: 39031 ident: bb0260 article-title: Effect of collagen turnover on the accumulation of advanced glycation end products publication-title: J. Biol. Chem. – volume: 46 start-page: 3212 year: 2002 end-page: 3217 ident: bb0330 article-title: Induction of advanced glycation end products and alterations of the tensile properties of articular cartilage publication-title: Arthritis Rheum. – volume: 14 start-page: R267 year: 2012 ident: bb0485 article-title: The effect of Link N on differentiation of human bone marrow-derived mesenchymal stem cells publication-title: Arthritis Res. Ther. – volume: 268 start-page: 71 year: 1977 end-page: 73 ident: bb0245 article-title: Aspartic acid racemisation in the human lens during ageing and in cataract formation publication-title: Nature – volume: 124 start-page: 687 year: 1998 end-page: 693 ident: bb0005 article-title: Roles of aggrecan, a large chondroitin sulfate proteoglycan, in cartilage structure and function publication-title: J. Biochem. – volume: 29 start-page: 119 year: 1993 end-page: 132 ident: bb0320 article-title: Biochemical changes in the collagen of human osteoporotic bone matrix publication-title: Connect. Tissue Res. – volume: 262 start-page: 279 year: 1976 end-page: 281 ident: bb0235 article-title: Aspartic acid racemisation in dentine as a measure of ageing publication-title: Nature – volume: 14 start-page: 103 year: 1988 end-page: 118 ident: bb0415 article-title: Does the chemical instability of aspartyl and asparaginyl residues in proteins contribute to erythrocyte aging? The role of protein carboxyl methylation reactions publication-title: Blood Cells – volume: 30 start-page: 145 year: 2011 end-page: 153 ident: bb0190 article-title: MMPs are less efficient than ADAMTS5 in cleaving aggrecan core protein publication-title: Matrix Biol. – volume: 274 start-page: 15892 year: 1999 end-page: 15900 ident: bb0035 article-title: Sulfation of chondroitin sulfate in human articular cartilage. The effect of age, topographical position, and zone of cartilage on tissue composition publication-title: J. Biol. Chem. – volume: 262 start-page: 785 year: 1987 end-page: 794 ident: bb0395 article-title: Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides. Succinimide-linked reactions that contribute to protein degradation publication-title: J. Biol. Chem. – volume: 22 start-page: 364 year: 1994 end-page: 371 ident: bb0025 article-title: Complete coding sequence, deduced primary structure, chromosomal localization, and structural analysis of murine aggrecan publication-title: Genomics – volume: 15 start-page: S326 year: 2006 end-page: S332 ident: bb0155 article-title: The structure and degradation of aggrecan in human intervertebral disc publication-title: Eur. Spine J. – volume: 255 start-page: 217 year: 1980 end-page: 224 ident: bb0095 article-title: Age-related changes in the structure of the proteoglycan subunits from human articular cartilage publication-title: J. Biol. Chem. – volume: 282 start-page: 18294 year: 2007 end-page: 18306 ident: bb0200 article-title: Proteolytic activities of human ADAMTS-5: comparative studies with ADAMTS-4 publication-title: J. Biol. Chem. – volume: 13 start-page: 318 year: 2013 end-page: 330 ident: bb0445 article-title: The molecular basis of intervertebral disc degeneration publication-title: Spine J. – volume: 261 start-page: 801 year: 1989 end-page: 809 ident: bb0065 article-title: Isolation of the N-terminal globular protein domains from cartilage proteoglycans. Identification of G2 domain and its lack of interaction with hyaluronate and link protein publication-title: Biochem. J. – volume: 13 start-page: 230 year: 1995 end-page: 239 ident: bb0040 article-title: Structure of chondroitin sulfate on aggrecan isolated from bovine tibial and costochondral growth plates publication-title: J. Orthop. Res. – volume: 663 start-page: 48 year: 1992 end-page: 62 ident: bb0335 article-title: Protein synthesis, posttranslational modifications, and aging publication-title: Ann. N. Y. Acad. Sci. – volume: 1035 start-page: 20 year: 1990 end-page: 28 ident: bb0120 article-title: Studies on the interaction of newly secreted proteoglycan subunits with hyaluronate in human articular cartilage publication-title: Biochim. Biophys. Acta – volume: 38 start-page: 633 year: 1993 ident: 10.1016/j.bbagen.2014.07.013_bb0290 article-title: Aspartic acid racemization in intervertebral discs as an aid to postmortem estimation of age at death publication-title: J. Forensic Sci. doi: 10.1520/JFS13449J – volume: 13 start-page: 318 year: 2013 ident: 10.1016/j.bbagen.2014.07.013_bb0445 article-title: The molecular basis of intervertebral disc degeneration publication-title: Spine J. doi: 10.1016/j.spinee.2012.12.003 – volume: 46 start-page: 2658 year: 2002 ident: 10.1016/j.bbagen.2014.07.013_bb0165 article-title: Human intervertebral disc aggrecan inhibits nerve growth in vitro publication-title: Arthritis Rheum. doi: 10.1002/art.10585 – volume: 72 start-page: 2891 year: 1975 ident: 10.1016/j.bbagen.2014.07.013_bb0230 article-title: Aspartic acid racemization in tooth enamel from living humans publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.72.8.2891 – volume: 10 start-page: 1124 year: 2014 ident: 10.1016/j.bbagen.2014.07.013_bb0500 article-title: Injectable hydrogels with high fixed charge density and swelling pressure for nucleus pulposus repair: biomimetic glycosaminoglycan analogues publication-title: Acta Biomater. doi: 10.1016/j.actbio.2013.11.010 – volume: 7 start-page: 30 year: 1982 ident: 10.1016/j.bbagen.2014.07.013_bb0400 article-title: Racemization of amino acids in nature publication-title: Interdisc. Sci. Rev. doi: 10.1179/030801882789801304 – volume: 337 start-page: 77 issue: Pt. 1 year: 1999 ident: 10.1016/j.bbagen.2014.07.013_bb0370 article-title: Age-related changes in the synthesis of link protein and aggrecan in human articular cartilage: implications for aggregate stability publication-title: Biochem. J. doi: 10.1042/bj3370077 – volume: 23 start-page: 2545 year: 1998 ident: 10.1016/j.bbagen.2014.07.013_bb0315 article-title: Changes in collagen cross-linking in degenerative disc disease and scoliosis publication-title: Spine doi: 10.1097/00007632-199812010-00009 – volume: 399 start-page: 29 year: 2006 ident: 10.1016/j.bbagen.2014.07.013_bb0220 article-title: Age-related accumulation of pentosidine in aggrecan and collagen from normal and degenerate human intervertebral discs publication-title: Biochem. J. doi: 10.1042/BJ20060579 – volume: 98 start-page: 944 year: 2001 ident: 10.1016/j.bbagen.2014.07.013_bb0410 article-title: Molecular Clocks publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.98.3.944 – volume: 124 start-page: 687 year: 1998 ident: 10.1016/j.bbagen.2014.07.013_bb0005 article-title: Roles of aggrecan, a large chondroitin sulfate proteoglycan, in cartilage structure and function publication-title: J. Biochem. doi: 10.1093/oxfordjournals.jbchem.a022166 – volume: 270 start-page: 20516 year: 1995 ident: 10.1016/j.bbagen.2014.07.013_bb0055 article-title: N- and O-linked keratan sulfate on the hyaluronan binding region of aggrecan from mature and immature bovine cartilage publication-title: J. Biol. Chem. doi: 10.1074/jbc.270.35.20516 – volume: 43 start-page: 949 year: 1998 ident: 10.1016/j.bbagen.2014.07.013_bb0275 article-title: Evaluation of aspartic acid racemization ratios in the human femur for age estimation publication-title: J. Forensic Sci. doi: 10.1520/JFS14339J – volume: 29 start-page: 119 year: 1993 ident: 10.1016/j.bbagen.2014.07.013_bb0320 article-title: Biochemical changes in the collagen of human osteoporotic bone matrix publication-title: Connect. Tissue Res. doi: 10.3109/03008209309014239 – volume: 77 start-page: 484 year: 2005 ident: 10.1016/j.bbagen.2014.07.013_bb0130 article-title: A mutation in the variable repeat region of the aggrecan gene (AGC1) causes a form of spondyloepiphyseal dysplasia associated with severe, premature osteoarthritis publication-title: Am. J. Hum. Genet. doi: 10.1086/444401 – volume: 98 start-page: 4367 year: 2001 ident: 10.1016/j.bbagen.2014.07.013_bb0380 article-title: Prediction of protein deamidation rates from primary and three-dimensional structure publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.071066498 – volume: 15 start-page: S326 issue: Suppl. 3 year: 2006 ident: 10.1016/j.bbagen.2014.07.013_bb0155 article-title: The structure and degradation of aggrecan in human intervertebral disc publication-title: Eur. Spine J. doi: 10.1007/s00586-006-0127-7 – volume: 273 start-page: 12999 year: 1998 ident: 10.1016/j.bbagen.2014.07.013_bb0100 article-title: Aggrecan synthesis and secretion. A paradigm for molecular and cellular coordination of multiglobular protein folding and intracellular trafficking publication-title: J. Biol. Chem. doi: 10.1074/jbc.273.21.12999 – volume: 220 start-page: 1407 year: 1983 ident: 10.1016/j.bbagen.2014.07.013_bb0240 article-title: Accumulation of D-aspartic acid with age in the human brain publication-title: Science doi: 10.1126/science.6857259 – volume: 13 start-page: R120 year: 2011 ident: 10.1016/j.bbagen.2014.07.013_bb0490 article-title: The efficacy of Link N as a mediator of repair in a rabbit model of intervertebral disc degeneration publication-title: Arthritis Res. Ther. doi: 10.1186/ar3423 – volume: 20 start-page: 736 year: 2012 ident: 10.1016/j.bbagen.2014.07.013_bb0350 article-title: Enhanced level of non-enzymatic glycation and pentosidine crosslinking in spontaneous osteoarthritis progression publication-title: Osteoarthritis Cartilage doi: 10.1016/j.joca.2012.03.012 – volume: 663 start-page: 48 year: 1992 ident: 10.1016/j.bbagen.2014.07.013_bb0335 article-title: Protein synthesis, posttranslational modifications, and aging publication-title: Ann. N. Y. Acad. Sci. doi: 10.1111/j.1749-6632.1992.tb38648.x – volume: 217 start-page: 1 year: 2010 ident: 10.1016/j.bbagen.2014.07.013_bb0455 article-title: Intervertebral disc, sensory nerves and neurotrophins: who is who in discogenic pain? publication-title: J. Anat. doi: 10.1111/j.1469-7580.2010.01227.x – volume: 26 start-page: 107 year: 2013 ident: 10.1016/j.bbagen.2014.07.013_bb0475 article-title: Link-N can stimulate proteoglycan synthesis in the degenerated human intervertebral discs publication-title: Eur. Cell Mater. doi: 10.22203/eCM.v026a08 – volume: 262 start-page: 279 year: 1976 ident: 10.1016/j.bbagen.2014.07.013_bb0235 article-title: Aspartic acid racemisation in dentine as a measure of ageing publication-title: Nature doi: 10.1038/262279b0 – volume: 271 start-page: 18456 year: 1996 ident: 10.1016/j.bbagen.2014.07.013_bb0150 article-title: Undersulfation of proteoglycans synthesized by chondrocytes from a patient with achondrogenesis type 1B homozygous for an L483P substitution in the diastrophic dysplasia sulfate transporter publication-title: J. Biol. Chem. doi: 10.1074/jbc.271.31.18456 – volume: 9 start-page: 4618 year: 2013 ident: 10.1016/j.bbagen.2014.07.013_bb0515 article-title: Incorporation of an aggrecan mimic prevents proteolytic degradation of anisotropic cartilage analogs publication-title: Acta Biomater. doi: 10.1016/j.actbio.2012.08.041 – volume: 23 start-page: 419 year: 1977 ident: 10.1016/j.bbagen.2014.07.013_bb0405 article-title: Considerations on the role of aspartic acid racemization in the aging process publication-title: Gerontology doi: 10.1159/000212218 – volume: 285 start-page: 15674 year: 2010 ident: 10.1016/j.bbagen.2014.07.013_bb0280 article-title: Aspartic acid racemization and collagen degradation markers reveal an accumulation of damage in tendon collagen that is enhanced with aging publication-title: J. Biol. Chem. doi: 10.1074/jbc.M109.077503 – volume: 268 start-page: 23504 year: 1993 ident: 10.1016/j.bbagen.2014.07.013_bb0030 article-title: cDNA cloning of chick cartilage chondroitin sulfate (aggrecan) core protein and identification of a stop codon in the aggrecan gene associated with the chondrodystrophy, nanomelia publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(19)49491-X – volume: 21 start-page: 499 year: 2002 ident: 10.1016/j.bbagen.2014.07.013_bb0195 article-title: Characterization of human aggrecanase 2 (ADAM-TS5): substrate specificity studies and comparison with aggrecanase 1 (ADAM-TS4) publication-title: Matrix Biol. doi: 10.1016/S0945-053X(02)00069-0 – volume: 13 start-page: 1228 year: 2013 ident: 10.1016/j.bbagen.2014.07.013_bb0510 article-title: Biomimetic aggrecan reduces cartilage extracellular matrix from degradation and lowers catabolic activity in ex vivo and in vivo models publication-title: Macromol. Biosci. doi: 10.1002/mabi.201300112 – volume: 281 start-page: 18444 year: 2006 ident: 10.1016/j.bbagen.2014.07.013_bb0080 article-title: The glycosaminoglycan attachment regions of human aggrecan publication-title: J. Biol. Chem. doi: 10.1074/jbc.M512531200 – volume: 17 start-page: 441 issue: Suppl. 4 year: 2008 ident: 10.1016/j.bbagen.2014.07.013_bb0465 article-title: Biological repair of the degenerated intervertebral disc by the injection of growth factors publication-title: Eur. Spine J. doi: 10.1007/s00586-008-0749-z – volume: 261 start-page: 801 year: 1989 ident: 10.1016/j.bbagen.2014.07.013_bb0065 article-title: Isolation of the N-terminal globular protein domains from cartilage proteoglycans. Identification of G2 domain and its lack of interaction with hyaluronate and link protein publication-title: Biochem. J. doi: 10.1042/bj2610801 – volume: 14 start-page: 103 year: 1988 ident: 10.1016/j.bbagen.2014.07.013_bb0415 article-title: Does the chemical instability of aspartyl and asparaginyl residues in proteins contribute to erythrocyte aging? The role of protein carboxyl methylation reactions publication-title: Blood Cells – volume: 10 start-page: 1098 year: 2010 ident: 10.1016/j.bbagen.2014.07.013_bb0495 article-title: The effects of needle puncture injury on microscale shear strain in the intervertebral disc annulus fibrosus publication-title: Spine J. doi: 10.1016/j.spinee.2010.09.015 – volume: 46 start-page: 3212 year: 2002 ident: 10.1016/j.bbagen.2014.07.013_bb0330 article-title: Induction of advanced glycation end products and alterations of the tensile properties of articular cartilage publication-title: Arthritis Rheum. doi: 10.1002/art.10627 – volume: 22 start-page: 364 year: 1994 ident: 10.1016/j.bbagen.2014.07.013_bb0025 article-title: Complete coding sequence, deduced primary structure, chromosomal localization, and structural analysis of murine aggrecan publication-title: Genomics doi: 10.1006/geno.1994.1396 – volume: 262 start-page: 785 year: 1987 ident: 10.1016/j.bbagen.2014.07.013_bb0395 article-title: Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides. Succinimide-linked reactions that contribute to protein degradation publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(19)75855-4 – volume: 288 start-page: 28243 year: 2013 ident: 10.1016/j.bbagen.2014.07.013_bb0480 article-title: Link protein N-terminal peptide binds to bone morphogenetic protein (BMP) type II receptor and drives matrix protein expression in rabbit intervertebral disc cells publication-title: J. Biol. Chem. doi: 10.1074/jbc.M113.451948 – volume: 274 start-page: 15892 year: 1999 ident: 10.1016/j.bbagen.2014.07.013_bb0035 article-title: Sulfation of chondroitin sulfate in human articular cartilage. The effect of age, topographical position, and zone of cartilage on tissue composition publication-title: J. Biol. Chem. doi: 10.1074/jbc.274.22.15892 – volume: 30 start-page: 145 year: 2011 ident: 10.1016/j.bbagen.2014.07.013_bb0190 article-title: MMPs are less efficient than ADAMTS5 in cleaving aggrecan core protein publication-title: Matrix Biol. doi: 10.1016/j.matbio.2010.10.007 – volume: 97 start-page: 201 year: 1992 ident: 10.1016/j.bbagen.2014.07.013_bb0250 article-title: On the accumulation of D-aspartate in elastin and other proteins of the ageing aorta publication-title: Atherosclerosis doi: 10.1016/0021-9150(92)90132-Z – volume: 1035 start-page: 20 year: 1990 ident: 10.1016/j.bbagen.2014.07.013_bb0120 article-title: Studies on the interaction of newly secreted proteoglycan subunits with hyaluronate in human articular cartilage publication-title: Biochim. Biophys. Acta doi: 10.1016/0304-4165(90)90168-V – volume: 25 start-page: 537 year: 2007 ident: 10.1016/j.bbagen.2014.07.013_bb0210 article-title: The many ways to cleave hyaluronan publication-title: Biotechnol. Adv. doi: 10.1016/j.biotechadv.2007.07.001 – volume: 899 start-page: 191 year: 2000 ident: 10.1016/j.bbagen.2014.07.013_bb0340 article-title: Protein oxidation publication-title: Ann. N. Y. Acad. Sci. doi: 10.1111/j.1749-6632.2000.tb06187.x – volume: 13 start-page: 299 year: 2013 ident: 10.1016/j.bbagen.2014.07.013_bb0450 article-title: Genetic polymorphisms associated with intervertebral disc degeneration publication-title: Spine J. doi: 10.1016/j.spinee.2013.01.041 – volume: 245 start-page: 308 year: 1973 ident: 10.1016/j.bbagen.2014.07.013_bb0270 article-title: Racemization of amino acids in bones publication-title: Nature doi: 10.1038/245308a0 – volume: 88 start-page: 1202 year: 2003 ident: 10.1016/j.bbagen.2014.07.013_bb0470 article-title: A synthetic peptide of link protein stimulates the biosynthesis of collagens II, IX and proteoglycan by cells of the intervertebral disc publication-title: J. Cell. Biochem. doi: 10.1002/jcb.10479 – volume: 267 start-page: 19470 year: 1992 ident: 10.1016/j.bbagen.2014.07.013_bb0060 article-title: The interglobular domain of cartilage aggrecan is cleaved by PUMP, gelatinases, and cathepsin B publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)41799-1 – volume: 785 start-page: 245 year: 1996 ident: 10.1016/j.bbagen.2014.07.013_bb0115 article-title: Studies on the G3 domain of aggrecan from human cartilage publication-title: Ann. N. Y. Acad. Sci. doi: 10.1111/j.1749-6632.1996.tb56273.x – volume: 30 start-page: 1139 year: 2005 ident: 10.1016/j.bbagen.2014.07.013_bb0160 article-title: Human intervertebral disc aggrecan inhibits endothelial cell adhesion and cell migration in vitro publication-title: Spine (Phila Pa 1976) doi: 10.1097/01.brs.0000162624.95262.73 – volume: 29 start-page: 1888 year: 2011 ident: 10.1016/j.bbagen.2014.07.013_bb0170 article-title: Calcification in human intervertebral disc degeneration and scoliosis publication-title: J. Orthop. Res. doi: 10.1002/jor.21456 – volume: 1820 start-page: 1671 year: 2012 ident: 10.1016/j.bbagen.2014.07.013_bb0300 article-title: Longevity of elastin in human intervertebral disc as probed by the racemization of aspartic acid publication-title: Biochim. Biophys. Acta doi: 10.1016/j.bbagen.2012.06.010 – volume: 304 start-page: 887 issue: Pt. 3 year: 1994 ident: 10.1016/j.bbagen.2014.07.013_bb0365 article-title: Proteoglycans isolated from dissociative extracts of differently aged human articular cartilage: characterization of naturally occurring hyaluronan-binding fragments of aggrecan publication-title: Biochem. J. doi: 10.1042/bj3040887 – volume: 262 start-page: 17757 year: 1987 ident: 10.1016/j.bbagen.2014.07.013_bb0010 article-title: Complete primary structure of the rat cartilage proteoglycan core protein deduced from cDNA clones publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)45444-0 – volume: 269 start-page: 10205 year: 1994 ident: 10.1016/j.bbagen.2014.07.013_bb0435 article-title: Racemization of Asp23 residue affects the aggregation properties of Alzheimer amyloid beta protein analogues publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(17)34045-0 – volume: 86 start-page: 126 year: 2010 ident: 10.1016/j.bbagen.2014.07.013_bb0140 article-title: A missense mutation in the aggrecan C-type lectin domain disrupts extracellular matrix interactions and causes dominant familial osteochondritis dissecans publication-title: Am. J. Hum. Genet. doi: 10.1016/j.ajhg.2009.12.018 – volume: 286 start-page: 39738 year: 2011 ident: 10.1016/j.bbagen.2014.07.013_bb0185 article-title: TNF-alpha and IL-1beta promote a disintegrin-like and metalloprotease with thrombospondin type I motif-5-mediated aggrecan degradation through syndecan-4 in intervertebral disc publication-title: J. Biol. Chem. doi: 10.1074/jbc.M111.264549 – volume: 75 start-page: 1204 year: 1978 ident: 10.1016/j.bbagen.2014.07.013_bb0420 article-title: Aspartic acid racemization in heavy molecular weight crystallins and water insoluble protein from normal human lenses and cataracts publication-title: Proc. Natl. Acad. Sci. doi: 10.1073/pnas.75.3.1204 – volume: 8 start-page: 18 year: 2008 ident: 10.1016/j.bbagen.2014.07.013_bb0460 article-title: Intervertebral disc: anatomy–physiology–pathophysiology–treatment publication-title: Pain Pract. doi: 10.1111/j.1533-2500.2007.00171.x – volume: 275 start-page: 39027 year: 2000 ident: 10.1016/j.bbagen.2014.07.013_bb0260 article-title: Effect of collagen turnover on the accumulation of advanced glycation end products publication-title: J. Biol. Chem. doi: 10.1074/jbc.M006700200 – volume: 13 start-page: 230 year: 1995 ident: 10.1016/j.bbagen.2014.07.013_bb0040 article-title: Structure of chondroitin sulfate on aggrecan isolated from bovine tibial and costochondral growth plates publication-title: J. Orthop. Res. doi: 10.1002/jor.1100130211 – volume: 106 start-page: 98 year: 1984 ident: 10.1016/j.bbagen.2014.07.013_bb0225 article-title: In vivo racemization in mammalian proteins publication-title: Methods Enzymol. doi: 10.1016/0076-6879(84)06011-0 – start-page: 203 year: 2010 ident: 10.1016/j.bbagen.2014.07.013_bb0180 article-title: Region-dependent aggrecan degradation patterns in the rat Intervertebral disc are affected by mechanical loading in vivo publication-title: Spine – volume: 268 start-page: 71 year: 1977 ident: 10.1016/j.bbagen.2014.07.013_bb0245 article-title: Aspartic acid racemisation in the human lens during ageing and in cataract formation publication-title: Nature doi: 10.1038/268071a0 – volume: 184 start-page: 351 year: 1950 ident: 10.1016/j.bbagen.2014.07.013_bb0310 article-title: On the origin of bile pigment in normal man publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(19)51154-1 – volume: 18 start-page: 799 year: 1990 ident: 10.1016/j.bbagen.2014.07.013_bb0360 article-title: Proteoglycan structure and metabolism during maturation and ageing of human articular cartilage publication-title: Biochem. Soc. Trans. doi: 10.1042/bst0180799 – volume: 24 start-page: 2456 year: 1999 ident: 10.1016/j.bbagen.2014.07.013_bb0090 article-title: Association between an aggrecan gene polymorphism and lumbar disc degeneration publication-title: Spine (Phila Pa 1976) doi: 10.1097/00007632-199912010-00006 – volume: 256 start-page: 255 year: 1991 ident: 10.1016/j.bbagen.2014.07.013_bb0385 article-title: Senescence and the accumulation of abnormal proteins publication-title: Mutat. Res. doi: 10.1016/0921-8734(91)90016-5 – volume: 381 start-page: 225 year: 2000 ident: 10.1016/j.bbagen.2014.07.013_bb0430 article-title: Isoaspartate formation and neurodegeneration in Alzheimer's disease publication-title: Arch. Biochem. Biophys. doi: 10.1006/abbi.2000.1955 – volume: 282 start-page: 18294 year: 2007 ident: 10.1016/j.bbagen.2014.07.013_bb0200 article-title: Proteolytic activities of human ADAMTS-5: comparative studies with ADAMTS-4 publication-title: J. Biol. Chem. doi: 10.1074/jbc.M701523200 – volume: 283 start-page: 8796 year: 2008 ident: 10.1016/j.bbagen.2014.07.013_bb0305 article-title: Collagen turnover in normal and degenerate human intervertebral discs as determined by the racemization of aspartic acid publication-title: J. Biol. Chem. doi: 10.1074/jbc.M709885200 – volume: 106 start-page: 98 year: 1984 ident: 10.1016/j.bbagen.2014.07.013_bb0355 article-title: In vivo racemization in mammalian proteins – volume: 14 start-page: 823 year: 2006 ident: 10.1016/j.bbagen.2014.07.013_bb0215 article-title: Link protein can retard the degradation of hyaluronan in proteoglycan aggregates publication-title: Osteoarthritis Cartilage doi: 10.1016/j.joca.2006.02.008 – volume: 8 start-page: 1543 year: 2012 ident: 10.1016/j.bbagen.2014.07.013_bb0505 article-title: Synthesis and characterization of an aggrecan mimic publication-title: Acta Biomater. doi: 10.1016/j.actbio.2011.12.029 – volume: 46 start-page: 114 year: 2002 ident: 10.1016/j.bbagen.2014.07.013_bb0345 article-title: Crosslinking by advanced glycation end products increases the stiffness of the collagen network in human articular cartilage: a possible mechanism through which age is a risk factor for osteoarthritis publication-title: Arthritis Rheum. doi: 10.1002/1529-0131(200201)46:1<114::AID-ART10025>3.0.CO;2-P – volume: 281 start-page: 13009 year: 2006 ident: 10.1016/j.bbagen.2014.07.013_bb0295 article-title: Aggrecan turnover in human intervertebral disc as determined by the racemization of aspartic acid publication-title: J. Biol. Chem. doi: 10.1074/jbc.M600296200 – volume: 14 start-page: R267 year: 2012 ident: 10.1016/j.bbagen.2014.07.013_bb0485 article-title: The effect of Link N on differentiation of human bone marrow-derived mesenchymal stem cells publication-title: Arthritis Res. Ther. doi: 10.1186/ar4113 – volume: 31 start-page: 2151 year: 2006 ident: 10.1016/j.bbagen.2014.07.013_bb0440 article-title: What is intervertebral disc degeneration, and what causes it? publication-title: Spine (Phila Pa 1976) doi: 10.1097/01.brs.0000231761.73859.2c – volume: 330 start-page: 345 issue: Pt 1 year: 1998 ident: 10.1016/j.bbagen.2014.07.013_bb0325 article-title: Ageing and zonal variation in post-translational modification of collagen in normal human articular cartilage. The age-related increase in non-enzymatic glycation affects biomechanical properties of cartilage publication-title: Biochem. J. doi: 10.1042/bj3300345 – volume: 49 start-page: 393 year: 1993 ident: 10.1016/j.bbagen.2014.07.013_bb0050 article-title: The link proteins publication-title: Experientia doi: 10.1007/BF01923584 – volume: 20 start-page: 409 year: 2001 ident: 10.1016/j.bbagen.2014.07.013_bb0255 article-title: Age-related accumulation of the advanced glycation endproduct pentosidine in human articular cartilage aggrecan: the use of pentosidine levels as a quantitative measure of protein turnover publication-title: Matrix Biol. doi: 10.1016/S0945-053X(01)00158-5 – volume: 266 start-page: 894 year: 1991 ident: 10.1016/j.bbagen.2014.07.013_bb0015 article-title: Complete coding sequence and deduced primary structure of the human cartilage large aggregating proteoglycan, aggrecan. Human-specific repeats, and additional alternatively spliced forms publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(17)35257-2 – volume: 326 start-page: 235 issue: Pt 1 year: 1997 ident: 10.1016/j.bbagen.2014.07.013_bb0175 article-title: Aggrecan degradation in human intervertebral disc and articular cartilage publication-title: Biochem. J. doi: 10.1042/bj3260235 – volume: 272 start-page: 28057 year: 1997 ident: 10.1016/j.bbagen.2014.07.013_bb0045 article-title: Identification of hyaluronan-binding domains of aggrecan publication-title: J. Biol. Chem. doi: 10.1074/jbc.272.44.28057 – volume: 716 start-page: 277 year: 1982 ident: 10.1016/j.bbagen.2014.07.013_bb0070 article-title: O-Linked oligosaccharides of human articular cartilage proteoglycan publication-title: Biochim. Biophys. Acta doi: 10.1016/0304-4165(82)90017-4 – volume: 272 start-page: 13974 year: 1997 ident: 10.1016/j.bbagen.2014.07.013_bb0085 article-title: A human-specific polymorphism in the coding region of the aggrecan gene. Variable number of tandem repeats produce a range of core protein sizes in the general population publication-title: J. Biol. Chem. doi: 10.1074/jbc.272.21.13974 – volume: 10 start-page: 371 year: 1979 ident: 10.1016/j.bbagen.2014.07.013_bb0375 article-title: Non-enzymatic, post-translational, amino acid modifications in ageing. A brief review publication-title: Mech. Ageing Dev. doi: 10.1016/0047-6374(79)90019-8 – volume: 268 start-page: 3072 year: 1993 ident: 10.1016/j.bbagen.2014.07.013_bb0425 article-title: Structural alterations in the peptide backbone of beta-amyloid core protein may account for its deposition and stability in Alzheimer's disease publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)53661-9 – volume: 255 start-page: 217 year: 1980 ident: 10.1016/j.bbagen.2014.07.013_bb0095 article-title: Age-related changes in the structure of the proteoglycan subunits from human articular cartilage publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(19)86286-5 – volume: 14 start-page: 323 year: 1994 ident: 10.1016/j.bbagen.2014.07.013_bb0075 article-title: Length variation in the keratan sulfate domain of mammalian aggrecan publication-title: Matrix Biol. doi: 10.1016/0945-053X(94)90198-8 – year: 2014 ident: 10.1016/j.bbagen.2014.07.013_bb0135 article-title: Short stature, accelerated bone maturation, and early growth cessation due to heterozygous aggrecan mutations publication-title: J. Clin. Endocrinol. Metab. doi: 10.1210/jc.2014-1332 – volume: 46 start-page: 5 year: 2001 ident: 10.1016/j.bbagen.2014.07.013_bb0390 article-title: Age determination using peptide mapping of non-collagenous proteins in human dentin publication-title: Soud. Lek. – volume: 20 start-page: 509 year: 2001 ident: 10.1016/j.bbagen.2014.07.013_bb0205 article-title: Hyal2—less active, but more versatile? publication-title: Matrix Biol. doi: 10.1016/S0945-053X(01)00170-6 – volume: 149 start-page: 951 year: 2003 ident: 10.1016/j.bbagen.2014.07.013_bb0265 article-title: Aspartic acid racemization: evidence for marked longevity of elastin in human skin publication-title: Br. J. Dermatol. doi: 10.1111/j.1365-2133.2003.05618.x – volume: 268 start-page: 17377 year: 1993 ident: 10.1016/j.bbagen.2014.07.013_bb0105 article-title: Expression of alternatively spliced epidermal growth factor-like domains in aggrecans of different species. Evidence for a novel module publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(19)85345-0 – volume: 1 start-page: 198 year: 1988 ident: 10.1016/j.bbagen.2014.07.013_bb0125 article-title: Proteoglycans: the chondroitin sulfate/keratan sulfate proteoglycan of cartilage publication-title: ISI Atlas Sci. Biochem. – volume: 345 start-page: 259 year: 1997 ident: 10.1016/j.bbagen.2014.07.013_bb0020 article-title: Complete coding sequence of bovine aggrecan: comparative structural analysis publication-title: Arch. Biochem. Biophys. doi: 10.1006/abbi.1997.0261 – volume: 276 start-page: 1253 year: 2001 ident: 10.1016/j.bbagen.2014.07.013_bb0110 article-title: The proteoglycans aggrecan and versican form networks with fibulin-2 through their lectin domain binding publication-title: J. Biol. Chem. doi: 10.1074/jbc.M006783200 – volume: 124 start-page: 269 year: 2009 ident: 10.1016/j.bbagen.2014.07.013_bb0285 article-title: Aspartic acid racemisation in purified elastin from arteries as basis for age estimation publication-title: Int. J. Legal Med. doi: 10.1007/s00414-009-0392-1 – volume: 84 start-page: 72 year: 2009 ident: 10.1016/j.bbagen.2014.07.013_bb0145 article-title: A recessive skeletal dysplasia, SEMD aggrecan type, results from a missense mutation affecting the C-type lectin domain of aggrecan publication-title: Am. J. Hum. Genet. doi: 10.1016/j.ajhg.2008.12.001 |
| SSID | ssj0000595 ssj0025309 |
| Score | 2.5035527 |
| SecondaryResourceType | review_article |
| Snippet | Aggrecan is the major non-collagenous component of the intervertebral disc. It is a large proteoglycan possessing numerous glycosaminoglycan chains and the... |
| SourceID | proquest pubmed crossref elsevier |
| SourceType | Aggregation Database Index Database Enrichment Source Publisher |
| StartPage | 3181 |
| SubjectTerms | Aggrecan Aggrecans - metabolism Aging - metabolism Aging - pathology Animals Biomimetics Degeneration glycation Humans hyaluronic acid Intervertebral disc Intervertebral Disc - metabolism Intervertebral Disc - pathology Intervertebral Disc Degeneration - metabolism Intervertebral Disc Degeneration - pathology intervertebral disks metalloproteinases proteoglycans proteolysis Repair scientists Structure-Activity Relationship Turnover |
| Title | Structure, function, aging and turnover of aggrecan in the intervertebral disc |
| URI | https://dx.doi.org/10.1016/j.bbagen.2014.07.013 https://www.ncbi.nlm.nih.gov/pubmed/25065289 https://www.proquest.com/docview/1566402779 https://www.proquest.com/docview/2000214484 |
| Volume | 1840 |
| WOSCitedRecordID | wos000341675900024&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: PRVESC databaseName: Elsevier SD Freedom Collection Journals 2021 customDbUrl: eissn: 1872-8006 dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0000595 issn: 0304-4165 databaseCode: AIEXJ dateStart: 19950118 isFulltext: true titleUrlDefault: https://www.sciencedirect.com providerName: Elsevier |
| link | http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwtV3db9MwELe6DgQvCAaD8jEZibcuU5I6tf04TUWARDWpQ-pbFNtJm2lKpzWdxt_CP8udHacroxog8RIlqZO6vl_P932EfMhjrNltkmDIClBQCskCZRhcZkmOXjSQYpVtNsHHYzGdytNO54fPhbm-4FUlbm7k5X8lNdwDYmPq7F-Qu30p3IBzIDocgexw_CPCT2xF2JWzLeO2ZcM3MEhz5hMS4dMKQzdtEMAMNG5khU3AY-mCIK9q9ChbB47ecPyWCz0vscZAP6_7qlw400iGRTmyI1_Fur9cKTTwtAL7xDucJqCb19YOvTbl63ntYgVG2Ndl7QJazeaNRX0dRdwYKCLWhro1VrM7mTMuWytkAQiDzqOdO-YrOHDnMBxucmdXzsnjMLzFbYEfRbd2briUv90VnIHi_EgpGIZFbyNmK7a6LNhf6m1PcGo4M1A9bUG3HbIb80SKLtk9_jyafllv9Ilt6tP-FJ-ZacMH737XNslnm2ZjJZyzp-RJo5rQYwepZ6STV3vkoWtW-n2PPDrxvQGfk3ELskPqIXZILcAoAIx6gNFFQT3AaFlRABjdBBhFgL0g3z6Ozk4-BU1njkAPZFIHoAMYgcbDuMCzATOFNsM4VDqPOC_4AMRaEFQzYQouikJkShuttGIJG8bMhIN90q0WVf6KUA0qvFZCGplj7wIlMxPqCO2RsJcaHvXIwK9aqpuy9dg95SL18YnnqVvrFNc6DXkKa90jQfvUpSvbcs947gmSNqKnEylTwNA9T7739EuBCOhuy6p8sVqmaBlhGCIht4_BRDksWihYj7x0xG_nC5xymMRCvv7nub0hj9d_yLekC9DI35EH-roul1cHZIdPxUEDargan379CaU7ypE |
| linkProvider | Elsevier |
| 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=Structure%2C+function%2C+aging+and+turnover+of+aggrecan+in+the+intervertebral+disc&rft.jtitle=Biochimica+et+biophysica+acta.+General+subjects&rft.au=Sivan%2C+Sarit+Sara&rft.au=Wachtel%2C+Ellen&rft.au=Roughley%2C+Peter&rft.date=2014-10-01&rft.pub=Elsevier+B.V&rft.issn=0304-4165&rft.eissn=1872-8006&rft.volume=1840&rft.issue=10&rft.spage=3181&rft.epage=3189&rft_id=info:doi/10.1016%2Fj.bbagen.2014.07.013&rft.externalDocID=S0304416514002517 |
| thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0304-4165&client=summon |
| thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0304-4165&client=summon |
| thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0304-4165&client=summon |