Interaction with PCNA is essential for yeast DNA polymerase eta function.
about
Role of PCNA-dependent stimulation of 3'-phosphodiesterase and 3'-5' exonuclease activities of human Ape2 in repair of oxidative DNA damageThe processivity factor beta controls DNA polymerase IV traffic during spontaneous mutagenesis and translesion synthesis in vivoStimulation of DNA synthesis activity of human DNA polymerase kappa by PCNA.Physical and functional interactions of human DNA polymerase eta with PCNARad18 guides poleta to replication stalling sites through physical interaction and PCNA monoubiquitinationMouse Rev1 protein interacts with multiple DNA polymerases involved in translesion DNA synthesisEukaryotic translesion polymerases and their roles and regulation in DNA damage toleranceBase excision repair intermediates are mutagenic in mammalian cellsA broad requirement for TLS polymerases η and κ, and interacting sumoylation and nuclear pore proteins, in lesion bypass during C. elegans embryogenesisStructure of a Mutant Form of Proliferating Cell Nuclear Antigen That Blocks Translesion DNA Synthesis † ‡Structural Basis for Novel Interactions between Human Translesion Synthesis Polymerases and Proliferating Cell Nuclear AntigenStructure of monoubiquitinated PCNA and implications for translesion synthesis and DNA polymerase exchangePCNA monoubiquitylation and DNA polymerase eta ubiquitin-binding domain are required to prevent 8-oxoguanine-induced mutagenesis in Saccharomyces cerevisiae.Trf4 and Trf5 proteins of Saccharomyces cerevisiae exhibit poly(A) RNA polymerase activity but no DNA polymerase activity.Def1 promotes the degradation of Pol3 for polymerase exchange to occur during DNA-damage--induced mutagenesis in Saccharomyces cerevisiae.Importance of Polη for damage-induced cohesion reveals differential regulation of cohesion establishment at the break site and genome-wideThe 9-1-1 checkpoint clamp physically interacts with polzeta and is partially required for spontaneous polzeta-dependent mutagenesis in Saccharomyces cerevisiae.A ubiquitin-binding motif in the translesion DNA polymerase Rev1 mediates its essential functional interaction with ubiquitinated proliferating cell nuclear antigen in response to DNA damage.Yeast Rad5 protein required for postreplication repair has a DNA helicase activity specific for replication fork regression.Stimulation of 3'-->5' exonuclease and 3'-phosphodiesterase activities of yeast apn2 by proliferating cell nuclear antigen.Reversal of PCNA ubiquitylation by Ubp10 in Saccharomyces cerevisiae.Comparative analysis of in vivo interactions between Rev1 protein and other Y-family DNA polymerases in animals and yeasts.Human DNA polymerase lambda functionally and physically interacts with proliferating cell nuclear antigen in normal and translesion DNA synthesisThe Proliferating Cell Nuclear Antigen (PCNA)-interacting Protein (PIP) Motif of DNA Polymerase η Mediates Its Interaction with the C-terminal Domain of Rev1Subtle alterations in PCNA-partner interactions severely impair DNA replication and repairDNA repair mechanisms and the bypass of DNA damage in Saccharomyces cerevisiaeControl of spontaneous and damage-induced mutagenesis by SUMO and ubiquitin conjugationA hybrid machine learning-based method for classifying the Cushing's Syndrome with comorbid adrenocortical lesions.Targeting of human DNA polymerase iota to the replication machinery via interaction with PCNA.PCNA is required for initiation of recombination-associated DNA synthesis by DNA polymerase delta.Effects of accessory proteins on the bypass of a cis-syn thymine-thymine dimer by Saccharomyces cerevisiae DNA polymerase eta.A single domain in human DNA polymerase iota mediates interaction with PCNA: implications for translesion DNA synthesisProcessivity factor of DNA polymerase and its expanding role in normal and translesion DNA synthesisCoordinating DNA polymerase traffic during high and low fidelity synthesis.Variations on a theme: eukaryotic Y-family DNA polymerasesIdentification of two functional PCNA-binding domains in human DNA polymerase κPre-Steady-State Kinetic Analysis of Truncated and Full-Length Saccharomyces cerevisiae DNA Polymerase Eta.Ubiquitinated proliferating cell nuclear antigen activates translesion DNA polymerases eta and REV1Role of the ubiquitin-binding domain of Polη in Rad18-independent translesion DNA synthesis in human cell extracts.Computational protein design suggests that human PCNA-partner interactions are not optimized for affinity.
P2860
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P2860
Interaction with PCNA is essential for yeast DNA polymerase eta function.
description
2001 nî lūn-bûn
@nan
2001 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年学术文章
@wuu
2001年学术文章
@zh-cn
2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
@zh-sg
2001年學術文章
@yue
name
Interaction with PCNA is essential for yeast DNA polymerase eta function.
@ast
Interaction with PCNA is essential for yeast DNA polymerase eta function.
@en
Interaction with PCNA is essential for yeast DNA polymerase eta function.
@nl
type
label
Interaction with PCNA is essential for yeast DNA polymerase eta function.
@ast
Interaction with PCNA is essential for yeast DNA polymerase eta function.
@en
Interaction with PCNA is essential for yeast DNA polymerase eta function.
@nl
prefLabel
Interaction with PCNA is essential for yeast DNA polymerase eta function.
@ast
Interaction with PCNA is essential for yeast DNA polymerase eta function.
@en
Interaction with PCNA is essential for yeast DNA polymerase eta function.
@nl
P2093
P3181
P1433
P1476
Interaction with PCNA is essential for yeast DNA polymerase eta function.
@en
P2093
P304
P3181
P356
10.1016/S1097-2765(01)00319-7
P407
P577
2001-08-01T00:00:00Z