TRF1 is degraded by ubiquitin-mediated proteolysis after release from telomeres
about
TIN2 is a tankyrase 1 PARP modulator in the TRF1 telomere length control complexThe F-box protein FBX4 targets PIN2/TRF1 for ubiquitin-mediated degradation and regulates telomere maintenanceVault poly(ADP-ribose) polymerase is associated with mammalian telomerase and is dispensable for telomerase function and vault structure in vivoTankyrase-1 assembly to large protein complexes blocks its telomeric functionProtein requirements for sister telomere association in human cellsLoss of Tankyrase-mediated destruction of 3BP2 is the underlying pathogenic mechanism of cherubismStructural basis of selective ubiquitination of TRF1 by SCFFbx4Telosome, a mammalian telomere-associated complex formed by multiple telomeric proteinsPinX1, a telomere repeat-binding factor 1 (TRF1)-interacting protein, maintains telomere integrity by modulating TRF1 homeostasis, the process in which human telomerase reverse Transcriptase (hTERT) plays dual rolesTelomere dysfunction and cell survival: roles for distinct TIN2-containing complexesDisruption of Wnt/β-Catenin Signaling and Telomeric Shortening Are Inextricable Consequences of Tankyrase Inhibition in Human CellsTankyrase 1 regulates centrosome function by controlling CPAP stabilityInhibition of Epstein-Barr virus OriP function by tankyrase, a telomere-associated poly-ADP ribose polymerase that binds and modifies EBNA1Shelterin complex and associated factors at human telomeresFunctional subdomain in the ankyrin domain of tankyrase 1 required for poly(ADP-ribosyl)ation of TRF1 and telomere elongationHistone deacetylase 8 safeguards the human ever-shorter telomeres 1B (hEST1B) protein from ubiquitin-mediated degradationNucleostemin delays cellular senescence and negatively regulates TRF1 protein stabilityIn silico characterization of the family of PARP-like poly(ADP-ribosyl)transferases (pARTs)Telomerase Regulation from Beginning to the EndGNL3L stabilizes the TRF1 complex and promotes mitotic transitionTelomerase inhibitor Imetelstat (GRN163L) limits the lifespan of human pancreatic cancer cellsTankyrase 2 poly(ADP-ribose) polymerase domain-deleted mice exhibit growth defects but have normal telomere length and cappingUbiquitin ligase RNF146 regulates tankyrase and Axin to promote Wnt signalingNuMA is a major acceptor of poly(ADP-ribosyl)ation by tankyrase 1 in mitosis.Tankyrase 1 and tankyrase 2 are essential but redundant for mouse embryonic developmentGcn5 and SAGA regulate shelterin protein turnover and telomere maintenance.Tankyrase1-mediated poly(ADP-ribosyl)ation of TRF1 maintains cell survival after telomeric DNA damage.Computationally designed peptide inhibitors of the ubiquitin E3 ligase SCF(Fbx4).The protein network surrounding the human telomere repeat binding factors TRF1, TRF2, and POT1.Evolutionary history of the poly(ADP-ribose) polymerase gene family in eukaryotes.The E3 ubiquitin ligase Rnf8 stabilizes Tpp1 to promote telomere end protection.The role of deubiquitinating enzymes in chromatin regulation.Fanconi anemia protein FANCD2 inhibits TRF1 polyADP-ribosylation through tankyrase1-dependent mannerTelomeres and aging.Poly-ADP ribosylation of PTEN by tankyrases promotes PTEN degradation and tumor growthAnalysis of poly(ADP-Ribose) polymerases in Arabidopsis telomere biology.The Drosophila tankyrase regulates Wg signaling depending on the concentration of Daxin.Nucleostemin inhibits TRF1 dimerization and shortens its dynamic association with the telomere.Tankyrase-1 function at telomeres and during mitosis is regulated by Polo-like kinase-1-mediated phosphorylation.Arabidopsis thaliana telomeric DNA-binding protein 1 is required for telomere length homeostasis and its Myb-extension domain stabilizes plant telomeric DNA binding.
P2860
Q24292755-0C5BBCD1-B714-4760-BA1D-F71C5C650450Q24293991-E2815CE6-8381-45E1-BDAC-206E5FC33516Q24294689-2CC828D9-6109-4A66-B8FE-ACAE3DF0EFC0Q24294752-6EC125E0-F4EF-4EDD-9D24-73617C635783Q24298717-4256E719-1776-439F-9928-64A70EECE947Q24299210-88C2028D-EF05-46CF-96C6-C2750ACC033DQ24299395-0E2CD648-9266-489B-AB79-1B43157D5193Q24304989-24C8F78F-F0C9-4E11-A65B-A5EC9097A3D7Q24319715-39B1184C-1274-451F-A726-4818989CCF60Q24336203-633D1BE5-4716-4B88-A22C-71109E263E82Q24337325-2CDF1280-9F26-4321-8A44-052C49AF6950Q24338290-57C181A7-8251-4C7A-832A-78BF23542626Q24520598-03C8E7C4-1DBC-4C06-956A-3DCEA59DF6F6Q24601577-358F62EA-4C72-4A6A-9EAF-AAF850506D75Q24607672-3E7471B2-1913-4F14-8588-4C1BCE09439FQ24671304-2E453C38-D29F-4267-9617-C11CBD8B75E3Q24672458-0740A24E-C707-447E-9446-B4B20D333842Q24816599-929F62BD-3F3B-4AF5-9160-574122426C5DQ28075938-8338FD5E-8FE9-49F8-8FB0-C8598A07DD4CQ28118811-8F3FFB20-02B9-4B67-9418-14397862E7A7Q28538403-D4D015EB-FAC9-4340-8D23-316657240FCAQ28593281-0128A308-6D6A-4213-A751-1489609FDE3AQ28742180-358A1689-6B78-4E15-BE04-75B9A1C7EE6DQ29871495-27D789E7-CD2F-4F4C-A608-9E4E1462C81EQ33350164-9F5E2DAB-E6F0-4201-AF88-D696B390E3EFQ33493740-DA76409B-D06F-422D-AFBE-461F3CB892E7Q33580476-96D63F4A-69C5-4C98-900A-89DA9E6A3681Q33637957-E7E91582-DE14-4A78-A38C-6BB7B5563FC5Q33682203-9BBA40AF-0D19-4FEE-B582-E4C707ABCCA7Q33717573-BDD6B175-D4B7-46BB-B705-2C3ADE67A9C8Q34079012-4AC6AD06-6BF4-414E-B9A5-D3746131F443Q34564968-FC918A37-1972-4EB6-930B-4A5A597728F1Q34623241-4191BD60-30F5-4A07-B48E-DA59DE07B942Q34768068-C66074D4-5365-46B2-A150-67F876F19A09Q34981637-E079ACA9-125B-4EDE-BC50-944C6CE95600Q35097621-96E5E279-21BE-4DDC-B53B-17BA98375668Q35136575-D2201202-A131-4E45-9B3C-659501411B85Q35548414-F329E8AF-90FE-4418-BB1D-08EA3FD4CB6DQ35687096-2B3ABE44-1945-433A-A48B-C7BDCFE5A59AQ35749737-BEFAD293-C682-4DD5-8B2E-F4462A4BDBBA
P2860
TRF1 is degraded by ubiquitin-mediated proteolysis after release from telomeres
description
2003 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի հունիսին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2003
@ast
im Juni 2003 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2003/06/01)
@sk
vědecký článek publikovaný v roce 2003
@cs
wetenschappelijk artikel (gepubliceerd op 2003/06/01)
@nl
наукова стаття, опублікована в червні 2003
@uk
مقالة علمية (نشرت في يونيو 2003)
@ar
name
TRF1 is degraded by ubiquitin-mediated proteolysis after release from telomeres
@ast
TRF1 is degraded by ubiquitin-mediated proteolysis after release from telomeres
@en
TRF1 is degraded by ubiquitin-mediated proteolysis after release from telomeres
@nl
type
label
TRF1 is degraded by ubiquitin-mediated proteolysis after release from telomeres
@ast
TRF1 is degraded by ubiquitin-mediated proteolysis after release from telomeres
@en
TRF1 is degraded by ubiquitin-mediated proteolysis after release from telomeres
@nl
prefLabel
TRF1 is degraded by ubiquitin-mediated proteolysis after release from telomeres
@ast
TRF1 is degraded by ubiquitin-mediated proteolysis after release from telomeres
@en
TRF1 is degraded by ubiquitin-mediated proteolysis after release from telomeres
@nl
P2093
P2860
P921
P3181
P356
P1433
P1476
TRF1 is degraded by ubiquitin-mediated proteolysis after release from telomeres
@en
P2093
Jasmin N. Dynek
Susan Smith
William Chang
P2860
P304
P3181
P356
10.1101/GAD.1077103
P577
2003-06-01T00:00:00Z