Replication protein A interactions with DNA. III. Molecular basis of recognition of damaged DNA.
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Cellular functions of human RPA1. Multiple roles of domains in replication, repair, and checkpointsEvidence for direct contact between the RPA3 subunit of the human replication protein A and single-stranded DNANMR chemical shift and relaxation measurements provide evidence for the coupled folding and binding of the p53 transactivation domainSurface Reengineering of RPA70N Enables Cocrystallization with an Inhibitor of the Replication Protein A Interaction Motif of ATR Interacting ProteinStructural Analysis of Replication Protein A Recruitment of the DNA Damage Response Protein SMARCAL1Aberrant mobility phenomena of the DNA repair protein XPAPolarity of human replication protein A binding to DNATorsional regulation of hRPA-induced unwinding of double-stranded DNA.Stopped-flow kinetic analysis of replication protein A-binding DNA: damage recognition and affinity for single-stranded DNA reveal differential contributions of k(on) and k(off) rate constants.Double-check probing of DNA bending and unwinding by XPA-RPA: an architectural function in DNA repair.Proteome analysis of a human heptocellular carcinoma cell line, HCC-M: an update.FANCJ helicase uniquely senses oxidative base damage in either strand of duplex DNA and is stimulated by replication protein A to unwind the damaged DNA substrate in a strand-specific manner.The phosphorylation domain of the 32-kDa subunit of replication protein A (RPA) modulates RPA-DNA interactions. Evidence for an intersubunit interaction.Chemical shift changes provide evidence for overlapping single-stranded DNA- and XPA-binding sites on the 70 kDa subunit of human replication protein AThe weak interdomain coupling observed in the 70 kDa subunit of human replication protein A is unaffected by ssDNA bindingXeroderma pigmentosum complementation group A protein (XPA) modulates RPA-DNA interactions via enhanced complex stability and inhibition of strand separation activity.UV light-damaged DNA and its interaction with human replication protein A: an atomic force microscopy study.Interactions of human replication protein A with single-stranded DNA adducts.NMR study on the interaction between RPA and DNA decamer containing cis-syn cyclobutane pyrimidine dimer in the presence of XPA: implication for damage verification and strand-specific dual incision in nucleotide excision repair.Modulation of replication protein A function by its hyperphosphorylation-induced conformational change involving DNA binding domain B.Recognition of oxidized thymine base on the single-stranded DNA by replication protein A.Regulatory functions of the N-terminal domain of the 70-kDa subunit of replication protein A (RPA)Inhibitory effects of Baicalin on ultraviolet B-induced photo-damage in keratinocyte cell line.Functional characterization of a cancer causing mutation in human replication protein ALocalization of xeroderma pigmentosum group A protein and replication protein A on damaged DNA in nucleotide excision repair.Photonic-plasmonic hybrid single-molecule nanosensor measures the effect of fluorescent labels on DNA-protein dynamicsIdentification of the DNA-Binding Domains of Human Replication Protein A That Recognize G-Quadruplex DNAAccurate prediction of the binding free energy and analysis of the mechanism of the interaction of replication protein A (RPA) with ssDNA.Theoretical prediction of the binding free energy for mutants of replication protein A.Repair-specific functions of replication protein A.Secondary structure and dynamics of an intrinsically unstructured linker domain.The biochemical basis and in vivo regulation of SOS-induced mutagenesis promoted by Escherichia coli DNA polymerase V (UmuD'2C).Leishmania braziliensis replication protein A subunit 1: molecular modelling, protein expression and analysis of its affinity for both DNA and RNA.Molecular Evolution and Functional Diversification of Replication Protein A1 in Plants.Force regulated dynamics of RPA on a DNA forkRPA activates the XPF-ERCC1 endonuclease to initiate processing of DNA interstrand crosslinks.Five repair pathways in one context: chromatin modification during DNA repair.hSSB1 (NABP2/OBFC2B) is regulated by oxidative stressRPA and XPA interaction with DNA structures mimicking intermediates of the late stages in nucleotide excision repair.
P2860
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P2860
Replication protein A interactions with DNA. III. Molecular basis of recognition of damaged DNA.
description
2000 nî lūn-bûn
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2000 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Replication protein A interact ...... of recognition of damaged DNA.
@ast
Replication protein A interact ...... of recognition of damaged DNA.
@en
type
label
Replication protein A interact ...... of recognition of damaged DNA.
@ast
Replication protein A interact ...... of recognition of damaged DNA.
@en
prefLabel
Replication protein A interact ...... of recognition of damaged DNA.
@ast
Replication protein A interact ...... of recognition of damaged DNA.
@en
P2093
P356
P1433
P1476
Replication protein A interact ...... of recognition of damaged DNA.
@en
P2093
P304
P356
10.1021/BI991704S
P407
P577
2000-02-01T00:00:00Z