Yeast Tdp1 regulates the fidelity of nonhomologous end joining.
about
SUMO-targeted ubiquitin ligase, Rad60, and Nse2 SUMO ligase suppress spontaneous Top1-mediated DNA damage and genome instability.End-processing during non-homologous end-joining: a role for exonuclease 1A multistep genomic screen identifies new genes required for repair of DNA double-strand breaks in Saccharomyces cerevisiae.Frameshift mutagenesis: the roles of primer-template misalignment and the nonhomologous end-joining pathway in Saccharomyces cerevisiae.Overhang polarity of chromosomal double-strand breaks impacts kinetics and fidelity of yeast non-homologous end joiningDiscovery of selective inhibitors of tyrosyl-DNA phosphodiesterase 2 by targeting the enzyme DNA-binding cleft.Epigenetic and genetic inactivation of tyrosyl-DNA-phosphodiesterase 1 (TDP1) in human lung cancer cells from the NCI-60 panelTo live or to die: a matter of processing damaged DNA termini in neurons.Detection and repair of ionizing radiation-induced DNA double strand breaks: new developments in nonhomologous end joining.Repair of double-strand breaks by end joining.Is non-homologous end-joining really an inherently error-prone process?Consider the workhorse: Nonhomologous end-joining in budding yeast.SUMO modification of the neuroprotective protein TDP1 facilitates chromosomal single-strand break repair.TDP1 promotes assembly of non-homologous end joining protein complexes on DNA.HTLV-1 bZIP factor suppresses TDP1 expression through inhibition of NRF-1 in adult T-cell leukemia.RNA-Seq analysis discloses early senescence and nucleolar dysfunction triggered by Tdp1α depletion in Medicago truncatula.Tyrosyl-DNA phosphodiesterases: rescuing the genome from the risks of relaxation.Structural basis for DNA 3'-end processing by human tyrosyl-DNA phosphodiesterase 1.Ku DNA End-Binding Activity Promotes Repair Fidelity and Influences End-Processing During Nonhomologous End-Joining in Saccharomyces cerevisiae.Depletion of tyrosyl-DNA phosphodiesterase 1α (MtTdp1α) affects transposon expression in Medicago truncatula.TDP1 suppresses mis-joining of radiomimetic DNA double-strand breaks and cooperates with Artemis to promote optimal nonhomologous end joining
P2860
Q33847786-F1CE1D9B-742C-4646-AB12-819D6F477D89Q34559710-8C7F78FC-A3AD-452A-8CB4-A4D9549FD170Q34668593-A8A2C416-8446-46CF-A947-63BDBDBA70DBQ35748265-D6AEBCC1-2070-4558-825C-ACE222681D86Q36775535-C89C2C8C-C268-4396-9C00-BAC95D78EEC2Q37081410-D0040D77-455D-4A90-B192-DC46D2601E64Q37572609-87C195CA-09B8-4C5D-A9A1-06D07D3D0BEAQ37830005-C1F2A101-7504-4426-86C0-85CAD289A877Q38083939-205C7286-7190-4129-8B91-5665A11C6741Q38103528-4C288A20-24CE-4CBD-8B19-88C8147545C4Q38181069-E329BF42-9316-4D96-9CEF-ED63F8BE3BECQ38848161-FE40E16A-F6A6-43CE-8AEB-821FF2A2441AQ39380131-2F7E2118-C6B3-43C2-A33E-48E3F9D5BA2CQ41116917-2CD74532-0913-4080-809C-EC72FF03BC56Q41921241-02DE772D-AB4C-4D6E-9D75-FB13B3021C0BQ42773644-419820F3-998B-4F31-B505-382369E37433Q46431649-B827470A-A6F5-45FC-8307-B55390955BD3Q47236725-5FE54329-EFAC-4E1A-AC9C-2F2A1EFD8C42Q52676508-939E37CE-E7DE-4E90-93A0-A82B02762F4BQ53646915-1E18B5E6-4234-4418-AE68-D6A74D869581Q58800814-AA0F7270-9F9E-4D9D-86AD-1A245A1C2057
P2860
Yeast Tdp1 regulates the fidelity of nonhomologous end joining.
description
2010 nî lūn-bûn
@nan
2010 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Yeast Tdp1 regulates the fidelity of nonhomologous end joining.
@ast
Yeast Tdp1 regulates the fidelity of nonhomologous end joining.
@en
type
label
Yeast Tdp1 regulates the fidelity of nonhomologous end joining.
@ast
Yeast Tdp1 regulates the fidelity of nonhomologous end joining.
@en
prefLabel
Yeast Tdp1 regulates the fidelity of nonhomologous end joining.
@ast
Yeast Tdp1 regulates the fidelity of nonhomologous end joining.
@en
P2860
P356
P1476
Yeast Tdp1 regulates the fidelity of nonhomologous end joining.
@en
P2093
Karim Bahmed
Karin C Nitiss
P2860
P304
P356
10.1073/PNAS.0909917107
P577
2010-02-16T00:00:00Z