about
Role for the related poly(ADP-Ribose) polymerases tankyrase 1 and 2 at human telomeresPOT1-interacting protein PIP1: a telomere length regulator that recruits POT1 to the TIN2/TRF1 complexA critical role for TPP1 and TIN2 interaction in high-order telomeric complex assemblyGenome-wide YFP fluorescence complementation screen identifies new regulators for telomere signaling in human cellsA quantitative telomeric chromatin isolation protocol identifies different telomeric statesCharacterization and cell cycle regulation of the related human telomeric proteins Pin2 and TRF1 suggest a role in mitosisIn vivo stoichiometry of shelterin componentsHuman telomeres contain two distinct Myb-related proteins, TRF1 and TRF2How the human telomeric proteins TRF1 and TRF2 recognize telomeric DNA: a view from high-resolution crystal structuresInhibition of Epstein-Barr virus OriP function by tankyrase, a telomere-associated poly-ADP ribose polymerase that binds and modifies EBNA1The human telomere-associated protein TIN2 stimulates interactions between telomeric DNA tracts in vitroSATB1 cleavage by caspase 6 disrupts PDZ domain-mediated dimerization, causing detachment from chromatin early in T-cell apoptosisControl of human telomere length by TRF1 and TRF2Shelterin complex and associated factors at human telomeresHuman telomerase contains evolutionarily conserved catalytic and structural subunitsFunctional subdomain in the ankyrin domain of tankyrase 1 required for poly(ADP-ribosyl)ation of TRF1 and telomere elongationCharacterization of the yeast telomere nucleoprotein core: Rap1 binds independently to each recognition siteOxidative damage in telomeric DNA disrupts recognition by TRF1 and TRF2Multiple facets of TPP1 in telomere maintenanceA shared docking motif in TRF1 and TRF2 used for differential recruitment of telomeric proteinsStructure of the DNA-binding domain of NgTRF1 reveals unique features of plant telomere-binding proteinsStructural bases of dimerization of yeast telomere protein Cdc13 and its interaction with the catalytic subunit of DNA polymerase αMRE11-RAD50-NBS1 and ATM function as co-mediators of TRF1 in telomere length controlDNA binding features of human POT1: a nonamer 5'-TAGGGTTAG-3' minimal binding site, sequence specificity, and internal binding to multimeric sitesA comprehensive model for the recognition of human telomeres by TRF1Telomeric localization of TRF2, a novel human telobox proteinDNA damage-induced cell cycle checkpoints involve both p53-dependent and -independent pathways: role of telomere repeat binding factor 2The TRF1-binding protein TERB1 promotes chromosome movement and telomere rigidity in meiosisGeneration and characterization of telomere length maintenance in tankyrase 2-deficient mice.Characterization of telomeric repeats in metaphase chromosomes and interphase nuclei of Syrian Hamster FibroblastsSuper-resolution fluorescence imaging of telomeres reveals TRF2-dependent T-loop formationTimeless preserves telomere length by promoting efficient DNA replication through human telomeresTRF2 and lamin A/C interact to facilitate the functional organization of chromosome endsSequence-specific binding to telomeric DNA by CEH-37, a homeodomain protein in the nematode Caenorhabditis elegans.Multiple POT1-TPP1 proteins coat and compact long telomeric single-stranded DNA.Resolution of telomere associations by TRF1 cleavage in mouse embryonic stem cellsPlant interstitial telomere motifs participate in the control of gene expression in root meristems.Suppression of subtelomeric VSG switching by Trypanosoma brucei TRF requires its TTAGGG repeat-binding activity.Sequence-specific DNA recognition by the Myb-like domain of plant telomeric protein RTBP1.Unwinding protein complexes in ALTernative telomere maintenance.
P2860
Q24291989-3F4AD4D0-6AD2-4A14-BCDC-7C7D7D743231Q24298357-4ED3A05E-358E-407C-AD1E-67716239C39AQ24298475-78631518-582F-416F-A6B1-6E010AA9EF14Q24305322-781EF9A1-DFDB-4352-853E-430218802E22Q24309504-D378191D-89DF-4C23-BFD9-4DA94068C762Q24311518-9F0B4FE9-CFE0-4781-A4D7-8A77132C760EQ24312021-2AF27C65-3F04-4CBD-9F90-9E029396D7A9Q24317670-F13E4303-7914-475B-8A0B-3FBFF182195AQ24323494-158B4B83-AA80-42F8-9D2D-04236A182B93Q24520598-4D054A6A-0DA0-4A65-88AA-2EFE890FA6FEQ24536029-0A153E33-8A78-4306-A445-0F69D33D693EQ24550879-16AC7308-1434-4315-9E1C-739DFC0DBB0DQ24554302-97F7BC60-ED52-46B5-B51E-68F5DDC32570Q24601577-1050D87F-A51F-4CAA-8D5B-8E3A9C8FD4ECQ24604009-D346E17A-859E-40AF-BCD8-112CC48B4957Q24607672-700722DC-D239-479B-9AF7-5EBF1BCABB65Q24612886-98051421-C976-41F2-852E-4A51588619E4Q24793970-A005965C-8906-41FF-AEF4-3AC048A5B57CQ26859063-5E749A50-91EF-4A89-B7AD-4C3740F716EFQ27649552-BE298854-4F4A-4D10-8D06-57B2DBBFEDBAQ27650163-3224901A-F09C-4112-8C74-0AE1E421F38DQ27664722-095C8EAB-2B0D-4E63-A0BD-EEC3DC81901CQ28115619-57A9EA00-F8B0-4B36-9168-3DB957B3CB04Q28238009-0D1A7BAD-1CBD-497B-822F-ECFA16B6D9E2Q28291302-5D171B49-58BF-4723-A0A2-67640A85FF52Q28314941-A91D8394-F12A-4B1D-B62D-EEB24ADFE426Q28352650-06EBB874-BBE7-45FB-B12E-D2C864AD6F40Q28505967-9F93D2C0-93BC-41B1-96ED-5F332AF537CBQ28590926-24CCBAF2-96C5-4D06-864F-4D152BB61002Q28714273-61A5C66A-6BCA-436B-9511-F992EC17D2C0Q28854371-7103E1D6-B605-4617-B053-4A501941D408Q29041627-2FA9D5DE-CDC9-4715-9A7C-FF266156243EQ29147479-ABBEEBBC-4C6B-486E-BCDC-A50AB1CFA2A4Q30332771-118A38C5-907D-461D-B472-8D6C3E8E44D7Q30453497-B116AF56-601E-4499-83EF-02B669A4BDDFQ30581726-8DEDB8C1-A786-432A-846D-5D5E079E7C1EQ30835366-E1663026-B3E7-419D-95F5-2C52E0B3A198Q30860113-8A8565EE-7B1F-46C1-B02B-0CE0532C92FCQ30870709-D736B681-64F3-4626-9AD1-7F0D01E9D7B3Q30884429-7ACBB0BB-28A7-4EE0-8F96-DBA6F7867F44
P2860
description
1997 nî lūn-bûn
@nan
1997 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
name
TRF1 is a dimer and bends telomeric DNA
@ast
TRF1 is a dimer and bends telomeric DNA
@en
TRF1 is a dimer and bends telomeric DNA
@en-gb
TRF1 is a dimer and bends telomeric DNA
@nl
type
label
TRF1 is a dimer and bends telomeric DNA
@ast
TRF1 is a dimer and bends telomeric DNA
@en
TRF1 is a dimer and bends telomeric DNA
@en-gb
TRF1 is a dimer and bends telomeric DNA
@nl
prefLabel
TRF1 is a dimer and bends telomeric DNA
@ast
TRF1 is a dimer and bends telomeric DNA
@en
TRF1 is a dimer and bends telomeric DNA
@en-gb
TRF1 is a dimer and bends telomeric DNA
@nl
P2093
P2860
P3181
P356
P1433
P1476
TRF1 is a dimer and bends telomeric DNA
@en
P2093
P2860
P304
P3181
P356
10.1093/EMBOJ/16.7.1785
P407
P577
1997-04-01T00:00:00Z