Suchergebnisse - "Cell Nucleolus/metabolism"

Probing condensate microenvironments with a micropeptide killswitch

Autoren: Yaotian Zhang Ida Stöppelkamp Pablo Fernandez-Pernas et al.

Quelle: Nature
Nature, vol. 643, no. 8073, pp. 1107-1116

Schlagwörter: Cell biology, Nuclear organization, Mechanisms of disease, Biowissenschaften, Biologie, Humans, Nucleophosmin, Peptides/chemistry, Peptides/metabolism, Biomolecular Condensates/metabolism, Biomolecular Condensates/chemistry, Cell Nucleolus/metabolism, Cell Nucleolus/chemistry, Single-Domain Antibodies/immunology, Single-Domain Antibodies/metabolism, Single-Domain Antibodies/chemistry, Nuclear Proteins/metabolism, Capsid Proteins/metabolism, Cell Proliferation/drug effects, Cellular Microenvironment, Cell Line, Tumor, Ribosomal Proteins/metabolism, Leukemia/pathology, Leukemia/metabolism, Hydrophobic and Hydrophilic Interactions, Article, Imaging

Dateibeschreibung: application/pdf

Zugangs-URL: https://serval.unil.ch/notice/serval:BIB_E354BC5C82D1
http://nbn-resolving.org/urn/resolver.pl?urn=urn:nbn:ch:serval-BIB_E354BC5C82D11
https://serval.unil.ch/resource/serval:BIB_E354BC5C82D1.P001/REF.pdf
https://refubium.fu-berlin.de/handle/fub188/48906
https://doi.org/10.17169/refubium-48629
https://doi.org/10.1038/s41586-025-09141-5

Nucleolar reorganization after cellular stress is orchestrated by SMN shuttling between nuclear compartments

Autoren: Musawi, Shaqraa Donnio, Lise-Marie Zhao, Zehui et al.

Weitere Verfasser: Musawi, Shaqraa Donnio, Lise-Marie Zhao, Zehui et al.

Quelle: Nat Commun
Nature Communications, Vol 14, Iss 1, Pp 1-17 (2023)

Schlagwörter: Muscular Atrophy, Spinal/metabolism, Cell Nucleolus/metabolism, Protein-Arginine N-Methyltransferases, Science, Nerve Tissue Proteins/metabolism, General Physics and Astronomy, Nerve Tissue Proteins, Coiled Bodies, SMN Complex Proteins/metabolism, Biochimie, biophysique & biologie moléculaire, General Biochemistry, Genetics and Molecular Biology, Article, Muscular Atrophy, Spinal, Physics and Astronomy (all), Coiled Bodies/metabolism, [SDV.BC.BC] Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC], Humans, Motor Neurons, Biochemistry, Genetics and Molecular Biology (all), Multidisciplinary, Repressor Proteins/metabolism, Chemistry (all), [SDV.NEU.NB] Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiology, RNA-Binding Proteins, SMN Complex Proteins, General Chemistry, Life sciences, Protein-Arginine N-Methyltransferases/metabolism, Repressor Proteins, Sciences du vivant, RNA-Binding Proteins/metabolism, PRMT1 protein, human, Motor Neurons/metabolism, Muscular Atrophy, Spinal/genetics, Cell Nucleolus, Biochemistry, biophysics & molecular biology

Dateibeschreibung: application/pdf

Zugangs-URL: https://pubmed.ncbi.nlm.nih.gov/37968267
https://doaj.org/article/50248904959c4a86860e553b2d011862
https://hdl.handle.net/2268/311189
https://doi.org/10.1038/s41467-023-42390-4
https://hal.science/hal-04297657v1
https://doi.org/10.1038/s41467-023-42390-4
https://hal.science/hal-04297657v1/document

Is the coiled body involved in nucleolar functions?

Autoren: Malatesta, M. Zancanaro, C. Martin, T.E. et al.

Schlagwörter: Animals, Antibodies, Monoclonal, Cell Nucleolus/metabolism, Cell Nucleolus/ultrastructure, Chromosomal Proteins, Non-Histone/metabolism, Hibernation, Liver/metabolism, Liver/ultrastructure, Microscopy, Immunoelectron, Nuclear Proteins/immunology, Nuclear Proteins/metabolism, RNA Precursors/metabolism, Ribonucleoproteins, Small Nuclear/metabolism, Rodentia

Relation: Experimental Cell Research; https://iris.unil.ch/handle/iris/94577; serval:BIB_0DCF85BE7754; A1994NE89700032; 8143790

Verfügbarkeit: https://iris.unil.ch/handle/iris/94577
https://doi.org/10.1006/excr.1994.1106

Ultrastructural analysis of transcription and splicing in the cell nucleus after bromo-UTP microinjection.

Autoren: Cmarko, D. Verschure, P.J. Martin, T.E. et al.

Schlagwörter: Cell Line, Cell Nucleolus/metabolism, Cell Nucleolus/ultrastructure, Cell Nucleus/metabolism, Cell Nucleus/ultrastructure, Chromatin/metabolism, Chromatin/ultrastructure, Cytoplasm/metabolism, Cytoplasm/ultrastructure, Humans, Microinjections, Microscopy, Confocal, Immunoelectron, RNA Splicing, RNA, Heterogeneous Nuclear/genetics, Heterogeneous Nuclear/metabolism, Transcription, Genetic, Uridine Triphosphate/administration & dosage, Uridine Triphosphate/analogs & derivatives

Relation: Molecular Biology of the Cell; https://iris.unil.ch/handle/iris/51314; serval:BIB_13301; 000079475600018; 9880337

Verfügbarkeit: https://iris.unil.ch/handle/iris/51314
https://doi.org/10.1091/mbc.10.1.211

Different concentrations of Mg++ ions affect nuclear matrix protein distribution during thermal stabilization of isolated nuclei.

Autoren: Neri, L.M. Riederer, B.M. Valmori, A. et al.

Schlagwörter: Antigens, Nuclear, Cell Nucleolus/metabolism, Cell Nucleus/drug effects, Cell Nucleus/metabolism, Fluorescent Antibody Technique, Indirect, Hot Temperature, Humans, Image Processing, Computer-Assisted, Leukemia, Erythroblastic, Acute/metabolism, Magnesium/pharmacokinetics, Microscopy, Confocal, Nuclear Proteins/drug effects, Nuclear Proteins/metabolism, Ribonucleoproteins/metabolism, Tumor Cells, Cultured

Relation: Journal of Histochemistry & Cytochemistry; https://iris.unil.ch/handle/iris/257353; serval:BIB_FDA04849D78F; A1997XX34700001; 9313794

Verfügbarkeit: https://iris.unil.ch/handle/iris/257353

Phosphorylation by casein kinase 2 facilitates rRNA gene transcription by promoting dissociation of TIF-IA from elongating RNA polymerase I.

Autoren: Bierhoff, H. Dundr, M. Michels, A.A. et al.

Schlagwörter: Amino Acid Sequence, Animals, Casein Kinase II/metabolism, Cell Cycle, Cell Nucleolus/metabolism, Cell Proliferation, DNA, Ribosomal/genetics, Humans, Mice, Models, Biological, Molecular Sequence Data, NIH 3T3 Cells, Phosphoprotein Phosphatases/metabolism, Phosphorylation, Phosphoserine/metabolism, Pol1 Transcription Initiation Complex Proteins, Promoter Regions, Genetic/genetics, Protein Binding, RNA Polymerase I/metabolism, RNA Precursors/biosynthesis, RNA, Transcription Factors/chemistry, Transcription Factors/metabolism, Transcription, Genetic

Relation: Molecular and Cellular Biology; 1098-5549[electronic], 0270-7306[linking]; https://iris.unil.ch/handle/iris/253051; serval:BIB_F422FF61B727; 000258195200007

Verfügbarkeit: https://iris.unil.ch/handle/iris/253051
https://doi.org/10.1128/MCB.00492-08

Functional characterization of the N terminus of Sir3p.

Autoren: Gotta, M. Palladino, F. Gasser, S.M.

Schlagwörter: Cell Nucleolus/metabolism, Chromatin, DNA, Fungal, Ribosomal, Fungal Proteins/genetics, Fungal Proteins/metabolism, Gene Deletion, Saccharomyces cerevisiae/genetics, Silent Information Regulator Proteins, Saccharomyces cerevisiae, Telomere, Trans-Activators/genetics, Trans-Activators/metabolism

Relation: Molecular and Cellular Biology; https://iris.unil.ch/handle/iris/166250; serval:BIB_9093; 000075980900050; 9742128

Verfügbarkeit: https://iris.unil.ch/handle/iris/166250
https://doi.org/10.1128/MCB.18.10.6110

Altered RNA structural constituents in aging and vitamin E deficiency.

Autoren: Malatesta, M. Bertoni-Freddari, C. Fattoretti, P. et al.

Schlagwörter: Aging/genetics, Aging/metabolism, Animals, Cell Nucleolus/genetics, Cell Nucleolus/metabolism, Female, Hepatocytes/ultrastructure, Microscopy, Electron, Oxidative Stress, RNA/metabolism, RNA/ultrastructure, Rats, Wistar, Vitamin E Deficiency/genetics, Vitamin E Deficiency/metabolism

Relation: Mechanisms of Ageing and Development; https://iris.unil.ch/handle/iris/102314; serval:BIB_28172; 000182099800005

Verfügbarkeit: https://iris.unil.ch/handle/iris/102314
https://doi.org/10.1016/S0047-6374(02)00117-3

Mammalian and yeast U3 snoRNPs are matured in specific and related nuclear compartments

Autoren: Verheggen, C. Lafontaine, D. L. Samarsky, D. et al.

Weitere Verfasser: Verheggen, C. Lafontaine, D. L. Samarsky, D. et al.

Quelle: The EMBO Journal. 21:2736-2745

Schlagwörter: 0301 basic medicine, Cell Nucleus -- metabolism, Chromosomal Proteins, Non-Histone, Xenopus, Fluorescence Nuclear Proteins/metabolism Nucleic Acid Conformation Plasmids/metabolism Precipitin Tests Protein Binding Protein Structure, DNA -- metabolism, Ribonucleoproteins, Small Nucleolar, In Situ Hybridization, Animals Cell Line Cell Nucleolus/metabolism Cell Nucleus/*metabolism Chromosomal Proteins, Microscopy, 0303 health sciences, Non-Histone/metabolism Coiled Bodies/metabolism DNA/metabolism DNA Methylation Hela Cells Humans In Situ Hybridization Microscopy, Nuclear Proteins, Non-Histone -- metabolism, Small Nucleolar -- metabolism -- physiology, Chromosomal Proteins, Ribonucleoproteins, Plasmids -- metabolism, Cell Nucleolus, Plasmids, Protein Binding, Protein Structure, Saccharomyces cerevisiae Proteins, Cell Nucleolus -- metabolism, Coiled Bodies, Saccharomyces cerevisiae, Fluorescence, Cell Line, Tertiary Ribonucleoproteins, 03 medical and health sciences, [SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology, Animals, Humans, Saccharomyces cerevisiae -- metabolism, Cell Nucleus, Small Nucleolar/*metabolism/*physiology Saccharomyces cerevisiae/metabolism Saccharomyces cerevisiae Proteins Xenopus, synthèse des protéines, Biologie moléculaire, DNA, DNA Methylation, Precipitin Tests, Coiled Bodies -- metabolism, Protein Structure, Tertiary, Microscopy, Fluorescence, Nucleic Acid Conformation, Biologie cellulaire, Nuclear Proteins -- metabolism, Acides nucléiques, Tertiary, HeLa Cells

Dateibeschreibung: 2 full-text file(s): application/pdf; application/pdf

Zugangs-URL: https://europepmc.org/articles/pmc126019?pdf=render
https://pubmed.ncbi.nlm.nih.gov/12032086
http://onlinelibrary.wiley.com/doi/10.1093/emboj/21.11.2736/full
https://europepmc.org/abstract/MED/12032086
https://www.embopress.org/doi/full/10.1093/emboj/21.11.2736
https://difusion.ulb.ac.be/vufind/Record/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/110873/Details
https://emboj.embopress.org/content/embojnl/21/11/2736.full.pdf
https://hal.archives-ouvertes.fr/hal-02197512

Box C/D small nucleolar RNA trafficking involves small nucleolar RNP proteins, nucleolar factors and a novel nuclear domain

Autoren: David Tollervey Céline Verheggen Marie Françoise Thiry et al.

Weitere Verfasser: David Tollervey Céline Verheggen Marie Françoise Thiry et al.

Quelle: The EMBO Journal. 20:5480-5490

Schlagwörter: 0301 basic medicine, SnoRNA, Saccharomyces cerevisiae Proteins, Cajal body, Phosphoproteins -- metabolism, Small Nucleolar/*metabolism Saccharomyces cerevisiae *Saccharomyces cerevisiae Proteins, Active Transport, Cell Nucleus, Cell Nucleolus -- metabolism, Coiled Bodies, Saccharomyces cerevisiae, Cell Nucleus Cell Compartmentation Cell Nucleolus/*metabolism Coiled Bodies/metabolism Fungal Proteins/metabolism Models, Models, Biological, Fungal Proteins, 03 medical and health sciences, Models, Ribonucleoproteins, Small Nucleolar, [SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology, RNA, Small Nucleolar, Cell Nucleus, 0303 health sciences, Trafficking, Serine-Arginine Splicing Factors, Fungal Proteins -- metabolism, Small Nucleolar -- metabolism, synthèse des protéines, Biologie moléculaire, Nuclear Proteins, RNA-Binding Proteins, Nucleolus, Biological, Phosphoproteins, Small Nucleolar/*metabolism *RNA-Binding Proteins Ribonucleoproteins, Active Transport, Coiled Bodies -- metabolism, Cell Compartmentation, Ribonucleoproteins, RNA, Biologie cellulaire, Nuclear Proteins -- metabolism, Biological Nuclear Proteins/metabolism Phosphoproteins/metabolism RNA, Acides nucléiques, Cell Nucleolus

Dateibeschreibung: 2 full-text file(s): application/pdf; application/pdf

Zugangs-URL: https://europepmc.org/articles/pmc125276?pdf=render
https://pubmed.ncbi.nlm.nih.gov/11574480
https://difusion.ulb.ac.be/vufind/Record/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/110874/Details
https://www.embopress.org/doi/pdf/10.1093/emboj/20.19.5480
https://dumas.ccsd.cnrs.fr/IGMM/hal-02197472
http://onlinelibrary.wiley.com/doi/10.1093/emboj/20.19.5480/abstract
https://europepmc.org/abstract/MED/11574480
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC125276/

Subcellular localization of Mdm2 expression and prognosis of breast cancer

Autoren: Seung Il Kim Seho Park Hyung Seok Park et al.

Weitere Verfasser: Seung Il Kim Seho Park Hyung Seok Park et al.

Quelle: International Journal of Clinical Oncology. 19:842-851

Schlagwörter: p53, Adult, Cell Nucleolus/metabolism, Cytoplasm, Breast Neoplasms/pathology, Prognosis, Receptor, ErbB-2, Cell Nucleolus/genetics, Proto-oncogene proteins c-mdm2, Breast Neoplasms, Breast Neoplasms/genetics, Disease-Free Survival, Mice, 03 medical and health sciences, 0302 clinical medicine, Neoplasms, Biomarkers, Tumor, Animals, Humans, Proto-Oncogene Proteins c-mdm2/genetics, Breast, Neoplastic, Proto-Oncogene Proteins c-mdm2, Middle Aged, Cytoplasm/genetics, Cytoplasm/metabolism, 3. Good health, Gene Expression Regulation, Neoplastic, Gene Expression Regulation, Breast Neoplasms/metabolism, Tissue Array Analysis, Tumor/genetics, Proto-Oncogene Proteins c-mdm2/biosynthesis, Tumor Suppressor Protein p53/genetics, Female, Tumor Suppressor Protein p53, Biomarkers, Cell Nucleolus, Tumor/biosynthesis, Receptor, ErbB-2/genetics

Dateibeschreibung: 842~851

Zugangs-URL: https://pubmed.ncbi.nlm.nih.gov/24292333
https://yonsei.pure.elsevier.com/en/publications/subcellular-localization-of-mdm2-expression-and-prognosis-of-brea
https://pubmed.ncbi.nlm.nih.gov/24292333/
https://www.ncbi.nlm.nih.gov/pubmed/24292333
https://ir.ymlib.yonsei.ac.kr/handle/22282913/100361
https://europepmc.org/article/MED/24292333
https://link.springer.com/article/10.1007/s10147-013-0639-1

CRM1 plays a nuclear role in transporting snoRNPs to nucleoli in higher eukaryotes

Autoren: Verheggen, C. Bertrand, Edouard Adele, Sarah

Weitere Verfasser: Verheggen, C. Bertrand, Edouard Adele, Sarah

Quelle: Nucleus. 3:132-137

Schlagwörter: Cell Nucleus Amino Acid Sequence Cell Nucleolus/*metabolism Humans Karyopherins/chemistry/*metabolism Methyltransferases/chemistry/metabolism Molecular Sequence Data Receptors, 0301 basic medicine, 0303 health sciences, Small Nucleolar/biosynthesis/*metabolism Saccharomyces cerevisiae/cytology/metabolism, Molecular Sequence Data, Active Transport, Cell Nucleus, Receptors, Cytoplasmic and Nuclear, Exportin 1 Protein, Methyltransferases, Saccharomyces cerevisiae, Karyopherins, Active Transport, 03 medical and health sciences, Ribonucleoproteins, Small Nucleolar, Cytoplasmic and Nuclear/chemistry/*metabolism Ribonucleoproteins, [SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology, Humans, Amino Acid Sequence, Cell Nucleolus

Zugangs-URL: https://www.tandfonline.com/doi/pdf/10.4161/nucl.19266?needAccess=true
https://pubmed.ncbi.nlm.nih.gov/22555597
https://europepmc.org/articles/PMC3383567
https://www.tandfonline.com/doi/full/10.4161/nucl.19266
https://pubmed.ncbi.nlm.nih.gov/22555597/
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3383567/

Nucleolar stress is an early response to myocardial damage involving nucleolar proteins nucleostemin and nucleophosmin

Autoren: Avitabile, Daniele Bailey, Brandi Cottage, Christopher T et al.

Quelle: Proceedings of the National Academy of Sciences. 108:6145-6150

Schlagwörter: Pathologic - pathology, Carrier Proteins - metabolism, 0301 basic medicine, Cells, Physiological, Myocardial Infarction, Apoptosis, Constriction, Pathologic, Stress, Mice, 03 medical and health sciences, GTP-Binding Proteins, Stress, Physiological, Myocardial Infarction - pathology, Myocardium - metabolism, Animals, Humans, Myocytes, Cardiac, Cell Nucleolus - metabolism, Aorta, Cells, Cultured, Myocytes, 0303 health sciences, Cultured, Myocardium, Myocardial Infarction - metabolism, Aorta - pathology, Nuclear Proteins, RNA-Binding Proteins, Myocardium - pathology, Constriction, Ribosomal - biosynthesis, Aorta - metabolism, Rats, Cardiac - metabolism, RNA, Ribosomal, Pathologic - metabolism, Nuclear Proteins - metabolism, Cell Nucleolus - pathology, RNA, Carrier Proteins, Cardiac - pathology, Nucleophosmin, Cell Nucleolus

Zugangs-URL: https://www.pnas.org/content/pnas/108/15/6145.full.pdf
https://pubmed.ncbi.nlm.nih.gov/21444791
https://pubmed.ncbi.nlm.nih.gov/21444791/
https://www.ncbi.nlm.nih.gov/pubmed/21444791
https://www.pnas.org/content/pnas/108/15/6145.full.pdf
https://www.jstor.org/stable/41126621
http://europepmc.org/abstract/MED/21444791
https://europepmc.org/abstract/MED/21444791

A Proteomic Screen for Nucleolar SUMO Targets Shows SUMOylation Modulates the Function of Nop5/Nop58

Autoren: Westman, B. J. Verheggen, C. Hutten, S. et al.

Weitere Verfasser: Westman, B. J. Verheggen, C. Hutten, S. et al.

Quelle: Mol Cell
Molecular Cell; Vol 39
Molecular Cell

Schlagwörter: Proteomics, 0301 basic medicine, Chromosomal Proteins, Non-Histone, Recombinant Fusion Proteins, BIOGENESIS, Molecular Sequence Data, SUMO-1 Protein, Post-Translational *Proteomics/methods Rats Recombinant Fusion Proteins/metabolism Ribonucleoproteins, PROTEIN SUMOYLATION, Transfection, UBIQUITIN, Article, PATHWAY, 03 medical and health sciences, Ribonucleoproteins, Small Nucleolar, BOX C/D SNORNPS, [SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology, Animals, Humans, Amino Acid Sequence, Molecular Biology, Small Nucleolar/genetics/*metabolism SUMO-1 Protein/metabolism Small Ubiquitin-Related Modifier Proteins/*metabolism Transfection Ubiquitins/metabolism, Small Nuclear/metabolism Ribonucleoproteins, 0303 health sciences, Binding Sites, IDENTIFICATION, Lysine, Nuclear Proteins, Cell Biology, Amino Acid Sequence Animals Binding Sites Cell Nucleolus/*metabolism Chromosomal Proteins, Ribonucleoproteins, Small Nuclear, TOPOISOMERASE-I, COMPONENT, Rats, PROTEASES, RIBONUCLEOPROTEINS, Mutation, Small Ubiquitin-Related Modifier Proteins, Protein Processing, Post-Translational, Cell Nucleolus, Non-Histone/metabolism HeLa Cells Humans Lysine Molecular Sequence Data Mutation Nuclear Proteins/genetics/*metabolism *Protein Processing, HeLa Cells

Zugangs-URL: http://www.cell.com/article/S1097276510005721/pdf
https://pubmed.ncbi.nlm.nih.gov/20797632
http://www.cell.com/molecular-cell/abstract/S1097-2765(10)00572-1
http://www.cell.com/molecular-cell/comments/S1097-2765(10)00572-1
https://www.sciencedirect.com/science/article/pii/S1097276510005721
http://core.ac.uk/display/20452250
http://europepmc.org/articles/PMC2938476
https://www.ncbi.nlm.nih.gov/pubmed/20797632

Hsp70 translocates to the nuclei and nucleoli, binds to XRCC1 and PARP-1, and protects HeLa cells from single-strand DNA breaks

Autoren: Kotoglou, P. (Polychronis) Kalaitzakis, A. (Alexandros) Vezyraki, P. (Patra) et al.

Weitere Verfasser: Kotoglou, P. (Polychronis) Kalaitzakis, A. (Alexandros) Vezyraki, P. (Patra) et al.

Quelle: Cell Stress and Chaperones. 14:391-406

Schlagwörter: 0301 basic medicine, Hot Temperature, Active Transport, Cell Nucleus, Poly (ADP-Ribose) Polymerase-1, DNA, Single-Stranded, HSP70 Heat-Shock Proteins/analysis/*metabolism/physiology, Apoptosis, RNA, Small Interfering/metabolism, 03 medical and health sciences, Cell Line, Tumor, [SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology, Humans, Cell Nucleus/*metabolism, HSP70 Heat-Shock Proteins, DNA Breaks, Single-Stranded, DNA-Binding Proteins/*metabolism, RNA, Small Interfering, Cell Nucleus, 0303 health sciences, Sciences du Vivant [q-bio]/Biotechnologies, Protein Structure, Tertiary, DNA-Binding Proteins, Poly(ADP-ribose) Polymerases/*metabolism, X-ray Repair Cross Complementing Protein 1, DNA, Single-Stranded/metabolism, Poly(ADP-ribose) Polymerases, Cell Nucleolus/*metabolism, Cell Nucleolus, HeLa Cells

Zugangs-URL: https://europepmc.org/articles/pmc2728274?pdf=render
https://pubmed.ncbi.nlm.nih.gov/19089598
https://www.jstor.org/stable/20532931
https://link.springer.com/article/10.1007%2Fs12192-008-0093-6/fulltext.html
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2728274/
https://pubmed.ncbi.nlm.nih.gov/19089598/
https://link.springer.com/article/10.1007%2Fs12192-008-0093-6
http://www.europepmc.org/articles/PMC2728274/
http://olympias.lib.uoi.gr/jspui/handle/123456789/21146
http://link.springer.com/10.1007/s12192-008-0093-6

Human PinX1 Mediates TRF1 Accumulation in Nucleolus and Enhances TRF1 Binding to Telomeres

Autoren: Young Nyun Park Jeong Eun Yoo Bong-Kyeong Oh et al.

Weitere Verfasser: Young Nyun Park Jeong Eun Yoo Bong-Kyeong Oh et al.

Quelle: Journal of Molecular Biology. 388:928-940

Schlagwörter: 0301 basic medicine, Protein Structure, Telomere/metabolism, ALT, Cell Nucleolus/metabolism, Recombinant Fusion Proteins, Cell Cycle Proteins, TRF1, Tumor Suppressor Proteins/genetics, Tumor Suppressor Proteins/chemistry, Telomeric Repeat Binding Protein 1/metabolism, Mice, 03 medical and health sciences, Animals, Humans, Tumor Suppressor Proteins/metabolism, Telomeric Repeat Binding Protein 1, nucleolus, Recombinant Fusion Proteins/genetics, Cell Nucleus, telomere, 0303 health sciences, Tumor Suppressor Proteins, Cell Cycle, Telomere, Telomeric Repeat Binding Protein 1/genetics, Protein Structure, Tertiary, Telomeric Repeat Binding Protein 1/chemistry, human PinX1, Cell Nucleus/metabolism, Recombinant Fusion Proteins/metabolism, Cell Cycle/physiology, Tertiary, Cell Nucleolus, HeLa Cells, Protein Binding

Zugangs-URL: https://pubmed.ncbi.nlm.nih.gov/19265708
https://www.ncbi.nlm.nih.gov/pubmed/19265708
https://europepmc.org/article/MED/19265708
https://ir.ymlib.yonsei.ac.kr/handle/22282913/103896
http://europepmc.org/abstract/MED/19265708
https://www.sciencedirect.com/science/article/pii/S0022283609002034

Fatty acid acylation regulates trafficking of the unusual Plasmodium falciparum calpain to the nucleolus

Autoren: Russo, Ilaria Oksman, Anna Goldberg, Daniel E.

Quelle: Mol Microbiol
Russo, I, Oksman, A & Goldberg, D E 2009, 'Fatty acid acylation regulates trafficking of the unusual Plasmodium falciparum calpain to the nucleolus', Molecular Microbiology, vol. 72, no. 1, pp. 229-245. https://doi.org/10.1111/j.1365-2958.2009.06639.x

Schlagwörter: 0301 basic medicine, Calpain, QH, Acylation, Lipoylation, Fatty Acids, Nuclear Localization Signals, Plasmodium falciparum, Protozoan Proteins, Fatty Acids/*metabolism, Transfection, Plasmodium falciparum/genetics/*metabolism, Protozoan Proteins/genetics/*metabolism, 3. Good health, Calpain/genetics/*metabolism, Cell Line, QH301, Protein Transport, 03 medical and health sciences, Animals, Humans, Cell Nucleolus/*metabolism, Research Articles, Cell Nucleolus, Phylogeny

Dateibeschreibung: application/pdf

Zugangs-URL: https://onlinelibrary.wiley.com/doi/pdfdirect/10.1111/j.1365-2958.2009.06639.x
https://pubmed.ncbi.nlm.nih.gov/19239622
http://onlinelibrary.wiley.com/doi/10.1111/j.1365-2958.2009.06639.x/full
https://www.research.manchester.ac.uk/portal/en/publications/fatty-acid-acylation-regulates-trafficking-of-the-unusual-plasmodium-falciparum-calpain-to-the-nucleolus(e1d40041-5837-4be8-86cc-f82900836255).html
https://onlinelibrary.wiley.com/doi/10.1111/j.1365-2958.2009.06639.x
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2746569/pdf
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2746569/
https://www.cabdirect.org/cabdirect/abstract/20093110123

The nuclear poly(A) polymerase and Exosome cofactor Trf5 is recruited cotranscriptionally to nucleolar surveillance

Autoren: Wery, Maxime Ruidant, Sabine Schillewaert, Stéphanie et al.

Quelle: RNA. 15:406-419

Schlagwörter: 0301 basic medicine, Chromatin Immunoprecipitation, Saccharomyces cerevisiae Proteins, Transcription, Genetic, U3 snornp/ssu processome, Cell Nucleolus -- metabolism, Pre-rRNA processing, Saccharomyces cerevisiae, RNA Precursors -- genetics -- metabolism, Small, 03 medical and health sciences, Genetic, Gene Expression Regulation, Fungal, Ribosome Subunits, RNA Precursors, Ribosome synthesis, Humans, Eukaryotic -- genetics, Ribosome Subunits, Small, Eukaryotic, Saccharomyces cerevisiae Proteins -- metabolism, 0303 health sciences, Saccharomyces cerevisiae -- genetics -- metabolism, synthèse des protéines, Biologie moléculaire, Nucleolus, DNA-Directed RNA Polymerases, DNA-Directed RNA Polymerases -- metabolism, Exosome, Fungal, Gene Expression Regulation, Cotranscriptional assembly, Biologie cellulaire, Transcription, Acides nucléiques, Cell Nucleolus

Dateibeschreibung: 1 full-text file(s): application/pdf

Zugangs-URL: http://rnajournal.cshlp.org/content/15/3/406.full.pdf
https://pubmed.ncbi.nlm.nih.gov/19141608
http://europepmc.org/articles/PMC2657017
https://jglobal.jst.go.jp/public/201002216341371835
https://www.ncbi.nlm.nih.gov/pubmed/19141608
https://difusion.ulb.ac.be/vufind/Record/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/110860/Details
https://core.ac.uk/display/8915139
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2657017

Bidirectional nucleolar dysfunction in C9orf72 frontotemporal lobar degeneration

Autoren: Friedrich A. Grässer Rubika Balendra Charlotte E. Ridler et al.

Quelle: Acta Neuropathol Commun
Acta Neuropathologica Communications, Vol 5, Iss 1, Pp 1-11 (2017)
Mizielinska, S, Ridler, C E, Balendra, R, Thoeng, A, Woodling, N S, Grässer, F A, Plagnol, V, Lashley, T, Partridge, L & Isaacs, A M 2017, ' Bidirectional nucleolar dysfunction in C9orf72 frontotemporal lobar degeneration ', Acta Neuropathologica Communications, vol. 5, no. 1, 29 . https://doi.org/10.1186/s40478-017-0432-x
Acta Neuropathologica Communications

Schlagwörter: 0301 basic medicine, Frontal Lobe/metabolism, Intranuclear Inclusion Bodies, Neurons/metabolism, Fluorescent Antibody Technique, Intranuclear Inclusion Bodies/metabolism, Dipeptide repeat proteins, Imaging, Animals, Genetically Modified, C9orf72, Physiological/genetics, In Situ Hybridization, In Situ Hybridization, Fluorescence, Neurons, 2. Zero hunger, Microscopy, 0303 health sciences, DNA Repeat Expansion, Microscopy, Confocal, Cell Nucleus Size/genetics, Frontal Lobe, Confocal, Cell Nucleus Size, Proteins/genetics, Drosophila, FTLD, Nucleolar stress, Cell Nucleolus, Cell Nucleolus/metabolism, Poly(GR), Physiological, Genetically Modified, Stress, Fluorescence, 03 medical and health sciences, Imaging, Three-Dimensional, Stress, Physiological, Animals, Humans, RC346-429, C9orf72 Protein, Research, RNA foci, Proteins, Three-Dimensional, Frontotemporal Lobar Degeneration/genetics, Neurology. Diseases of the nervous system, Frontotemporal Lobar Degeneration, Stress, Physiological/genetics

Dateibeschreibung: application/pdf

Zugangs-URL: https://actaneurocomms.biomedcentral.com/track/pdf/10.1186/s40478-017-0432-x
https://pubmed.ncbi.nlm.nih.gov/28420437
https://doaj.org/article/f0c320103fb14149a797a496a8654551
https://core.ac.uk/display/81683035
https://link.springer.com/article/10.1186/s40478-017-0432-x
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5395972
https://link.springer.com/content/pdf/10.1186%2Fs40478-017-0432-x.pdf
https://actaneurocomms.biomedcentral.com/articles/10.1186/s40478-017-0432-x
https://www.ncbi.nlm.nih.gov/pubmed/28420437
http://hdl.handle.net/21.11116/0000-000B-4F59-A
https://kclpure.kcl.ac.uk/en/publications/54381054-d4ae-49c6-87e5-c3ff9ada4067
https://kclpure.kcl.ac.uk/portal/en/publications/54381054-d4ae-49c6-87e5-c3ff9ada4067
https://discovery-pp.ucl.ac.uk/id/eprint/1552913/

TOR regulates the subcellular distribution of DIM2, a KH domain protein required for cotranscriptional ribosome assembly and pre-40S ribosome export

Autoren: Vanrobays, Emmanuel Leplus, Alexius Osheim, Yvonne N et al.

Quelle: RNA. 14:2061-2073

Schlagwörter: 0301 basic medicine, Protein Structure, Saccharomyces cerevisiae Proteins, Transcription, Genetic, Protein Conformation, Molecular Sequence Data, Cell Nucleolus -- metabolism, Pre-rRNA processing, Saccharomyces cerevisiae, Protein Serine-Threonine Kinases, Small, Ribosomal -- metabolism, Ribosome export, 03 medical and health sciences, Genetic, Saccharomyces cerevisiae -- drug effects -- genetics -- metabolism, Osmotic Pressure, Ribosome Subunits, Ribosome synthesis, Animals, Humans, Target of rapamycin (TOR), Amino Acid Sequence, Saccharomyces cerevisiae Proteins -- genetics -- metabolism -- physiology, Nuclear Export Signals, Ribosome Subunits, Small, Eukaryotic, Sirolimus, 0303 health sciences, Eukaryotic -- metabolism, synthèse des protéines, Biologie moléculaire, Nuclear Proteins, Nucleolus, Nuclear Proteins -- genetics -- metabolism, Protein Structure, Tertiary, KH domain, Oxidative Stress, Protein Transport, Sirolimus -- pharmacology, RNA, Ribosomal, RNA, Biologie cellulaire, Protein-Serine-Threonine Kinases -- genetics -- physiology, Transcription, Acides nucléiques, Tertiary, Cell Nucleolus

Dateibeschreibung: 1 full-text file(s): application/pdf

Zugangs-URL: http://rnajournal.cshlp.org/content/14/10/2061.full.pdf
https://pubmed.ncbi.nlm.nih.gov/18755838
https://core.ac.uk/display/8915198
https://www.ncbi.nlm.nih.gov/pubmed/18755838
https://difusion.ulb.ac.be/vufind/Record/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/110920/Details
https://europepmc.org/abstract/MED/18755838
https://pubmed.ncbi.nlm.nih.gov/18755838/