REV1 protein interacts with PCNA: significance of the REV1 BRCT domain in vitro and in vivo.
about
Proliferating cell nuclear antigen (PCNA)-binding protein C1orf124 is a regulator of translesion synthesisRegulation of Rev1 by the Fanconi anemia core complexSeparate roles of structured and unstructured regions of Y-family DNA polymerasesFunctional Evolution of BRCT Domains from Binding DNA to ProteinHow the fanconi anemia pathway guards the genomeEukaryotic translesion polymerases and their roles and regulation in DNA damage toleranceGetting Ready for the Dance: FANCJ Irons Out DNA WrinklesThe Fanconi anemia pathway and DNA interstrand cross-link repairEukaryotic DNA polymerase ζKeeping chromatin quiet: how nucleosome remodeling restores heterochromatin after replicationStructural Basis for Novel Interactions between Human Translesion Synthesis Polymerases and Proliferating Cell Nuclear AntigenUnconventional Ubiquitin Recognition by the Ubiquitin-Binding Motif within the Y Family DNA Polymerases ι and Rev1Structural Basis of Ubiquitin Recognition by Translesion Synthesis DNA Polymerase ιStructural insights into the assembly of human translesion polymerase complexesStructure and Functional Analysis of the BRCT Domain of Translesion Synthesis DNA Polymerase Rev1NMR Structure and Dynamics of the C-Terminal Domain from Human Rev1 and Its Complex with Rev1 Interacting Region of DNA Polymerase ηThe mechanisms of UV mutagenesis.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.Comparative analysis of in vivo interactions between Rev1 protein and other Y-family DNA polymerases in animals and yeasts.Regulation of translesion DNA synthesis: Posttranslational modification of lysine residues in key proteinsThe Proliferating Cell Nuclear Antigen (PCNA)-interacting Protein (PIP) Motif of DNA Polymerase η Mediates Its Interaction with the C-terminal Domain of Rev1The transcription factor TFII-I promotes DNA translesion synthesis and genomic stabilityAn overview of Y-Family DNA polymerases and a case study of human DNA polymerase ηThe vital role of polymerase ζ and REV1 in mutagenic, but not correct, DNA synthesis across benzo[a]pyrene-dG and recruitment of polymerase ζ by REV1 to replication-stalled siteDifferential roles for DNA polymerases eta, zeta, and REV1 in lesion bypass of intrastrand versus interstrand DNA cross-links.Processivity 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 polymerasesParkin regulates translesion DNA synthesis in response to UV radiationKinetic basis of nucleotide selection employed by a protein template-dependent DNA polymeraseRegulation of DNA cross-link repair by the Fanconi anemia/BRCA pathwayThe DNA polymerase activity of Saccharomyces cerevisiae Rev1 is biologically significant.The Werner syndrome protein limits the error-prone 8-oxo-dG lesion bypass activity of human DNA polymerase kappa.Analysis of CPD ultraviolet lesion bypass in chicken DT40 cells: polymerase η and PCNA ubiquitylation play identical rolesMouse DNA polymerase kappa has a functional role in the repair of DNA strand breaksDNA polymerase zeta (pol zeta) in higher eukaryotes.Sequential assembly of translesion DNA polymerases at UV-induced DNA damage sitesMolecular chaperone Hsp90 regulates REV1-mediated mutagenesis.Starvation promotes REV1 SUMOylation and p53-dependent sensitization of melanoma and breast cancer cells.The non-canonical protein binding site at the monomer-monomer interface of yeast proliferating cell nuclear antigen (PCNA) regulates the Rev1-PCNA interaction and Polζ/Rev1-dependent translesion DNA synthesis.
P2860
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P2860
REV1 protein interacts with PCNA: significance of the REV1 BRCT domain in vitro and in vivo.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
2006年论文
@zh
2006年论文
@zh-cn
name
REV1 protein interacts with PC ...... T domain in vitro and in vivo.
@en
type
label
REV1 protein interacts with PC ...... T domain in vitro and in vivo.
@en
prefLabel
REV1 protein interacts with PC ...... T domain in vitro and in vivo.
@en
P2093
P1433
P1476
REV1 protein interacts with PC ...... T domain in vitro and in vivo.
@en
P2093
Aleksandra B Bielen
Caixia Guo
Eiichiro Sonoda
Errol C Friedberg
Shunichi Takeda
Tie-Shan Tang
P304
P356
10.1016/J.MOLCEL.2006.05.038
P577
2006-07-01T00:00:00Z