Human replication protein A-Rad52-single-stranded DNA complex: stoichiometry and evidence for strand transfer regulation by phosphorylation.
about
Human single-stranded DNA binding proteins are essential for maintaining genomic stabilityTyrosine phosphorylation enhances RAD52-mediated annealing by modulating its DNA binding.Increased RPA1 gene dosage affects genomic stability potentially contributing to 17p13.3 duplication syndromeOverexpression of RAD51 suppresses recombination defects: a possible mechanism to reverse genomic instability.Human Rad52 binds and wraps single-stranded DNA and mediates annealing via two hRad52-ssDNA complexes.Replication protein A: directing traffic at the intersection of replication and repair.Identification of the DNA-Binding Domains of Human Replication Protein A That Recognize G-Quadruplex DNAInterplay of DNA damage and cell cycle signaling at the level of human replication protein AReplication protein A (RPA) hampers the processive action of APOBEC3G cytosine deaminase on single-stranded DNAReplication-mediated disassociation of replication protein A-XPA complex upon DNA damage: implications for RPA handing off.Phosphorylated hMSH6: DNA mismatch versus DNA damage recognition.Human single-stranded DNA binding proteins: guardians of genome stability.Homologous recombination and its regulationMechanistic Modelling and Bayesian Inference Elucidates the Variable Dynamics of Double-Strand Break Repair.Physical and functional interaction between yeast Pif1 helicase and Rim1 single-stranded DNA binding proteinHeterozygous PALB2 c.1592delT mutation channels DNA double-strand break repair into error-prone pathways in breast cancer patients.DNA-pairing and annealing processes in homologous recombination and homology-directed repair.NF-κB-dependent DNA damage-signaling differentially regulates DNA double-strand break repair mechanisms in immature and mature human hematopoietic cells.
P2860
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P2860
Human replication protein A-Rad52-single-stranded DNA complex: stoichiometry and evidence for strand transfer regulation by phosphorylation.
description
2009 nî lūn-bûn
@nan
2009 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Human replication protein A-Ra ...... regulation by phosphorylation.
@ast
Human replication protein A-Ra ...... regulation by phosphorylation.
@en
type
label
Human replication protein A-Ra ...... regulation by phosphorylation.
@ast
Human replication protein A-Ra ...... regulation by phosphorylation.
@en
prefLabel
Human replication protein A-Ra ...... regulation by phosphorylation.
@ast
Human replication protein A-Ra ...... regulation by phosphorylation.
@en
P2093
P2860
P356
P1433
P1476
Human replication protein A-Ra ...... regulation by phosphorylation.
@en
P2093
Aishwarya Prakash
Carol Kolar
Gilson S Baia
Gloria E O Borgstahl
Kajari Dhar
Xiaoyi Deng
P2860
P304
P356
10.1021/BI900564K
P407
P577
2009-07-01T00:00:00Z