Replication protein A: a heterotrimeric, single-stranded DNA-binding protein required for eukaryotic DNA metabolism
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Multiple ATR-Chk1 pathway proteins preferentially associate with checkpoint-inducing DNA substratesUnwinding and rewinding: double faces of helicase?Phosphorylation: the molecular switch of double-strand break repairFunctional and physical interaction between WRN helicase and human replication protein APhosphorylation of replication protein A middle subunit (RPA32) leads to a disassembly of the RPA heterotrimerReconstitution of proliferating cell nuclear antigen-dependent repair of apurinic/apyrimidinic sites with purified human proteinsFuzziness: linking regulation to protein dynamicsNuclear structure in normal and Bloom syndrome cellsReplication protein A physically interacts with the Bloom's syndrome protein and stimulates its helicase activityRBT1, a novel transcriptional co-activator, binds the second subunit of replication protein AStrong functional interactions of TFIIH with XPC and XPG in human DNA nucleotide excision repair, without a preassembled repairosomeStructure of the RPA trimerization core and its role in the multistep DNA-binding mechanism of RPAReplication protein A prevents accumulation of single-stranded telomeric DNA in cells that use alternative lengthening of telomeresStructure of RPA32 bound to the N-terminus of SMARCAL1 redefines the binding interface between RPA32 and its interacting proteinsE3 ligase RFWD3 participates in replication checkpoint controlInteraction and colocalization of Rad9/Rad1/Hus1 checkpoint complex with replication protein A in human cellsCircadian control of XPA and excision repair of cisplatin-DNA damage by cryptochrome and HERC2 ubiquitin ligaseA dominant-negative mutant of human DNA helicase B blocks the onset of chromosomal DNA replicationPhysical and functional mapping of the replication protein a interaction domain of the werner and bloom syndrome helicasesHuman Mcm proteins at a replication origin during the G1 to S phase transitionCellular functions of human RPA1. Multiple roles of domains in replication, repair, and checkpointsStreamline proteomic approach for characterizing protein-protein interaction network in a RAD52 protein complexAn alternative form of replication protein a prevents viral replication in vitroHSSB1 and hSSB2 form similar multiprotein complexes that participate in DNA damage responseEvidence for direct contact between the RPA3 subunit of the human replication protein A and single-stranded DNAHuman DNA glycosylases of the bacterial Fpg/MutM superfamily: an alternative pathway for the repair of 8-oxoguanine and other oxidation products in DNASumoylation of the novel protein hRIP{beta} is involved in replication protein A deposition in PML nuclear bodiesThe SIOD disorder protein SMARCAL1 is an RPA-interacting protein involved in replication fork restartThe annealing helicase HARP is recruited to DNA repair sites via an interaction with RPAThe evolutionarily conserved zinc finger motif in the largest subunit of human replication protein A is required for DNA replication and mismatch repair but not for nucleotide excision repairA naturally occurring human RPA subunit homolog does not support DNA replication or cell-cycle progressionSOSS complexes participate in the maintenance of genomic stabilityDifferent activities of the largest subunit of replication protein A cooperate during SV40 DNA replicationAn alternative form of replication protein a expressed in normal human tissues supports DNA repair4E-BP3 regulates eIF4E-mediated nuclear mRNA export and interacts with replication protein A2hPrimpol1/CCDC111 is a human DNA primase-polymerase required for the maintenance of genome integrityPhosphorylation of the replication protein A large subunit in the Saccharomyces cerevisiae checkpoint responseReplication-mediated DNA damage by camptothecin induces phosphorylation of RPA by DNA-dependent protein kinase and dissociates RPA:DNA-PK complexesPreferential localization of hyperphosphorylated replication protein A to double-strand break repair and checkpoint complexes upon DNA damageInteraction of human rad51 recombination protein with single-stranded DNA binding protein, RPA
P2860
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P2860
Replication protein A: a heterotrimeric, single-stranded DNA-binding protein required for eukaryotic DNA metabolism
description
1997 nî lūn-bûn
@nan
1997 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
name
Replication protein A: a heter ...... for eukaryotic DNA metabolism
@ast
Replication protein A: a heter ...... for eukaryotic DNA metabolism
@en
Replication protein A: a heter ...... for eukaryotic DNA metabolism
@nl
type
label
Replication protein A: a heter ...... for eukaryotic DNA metabolism
@ast
Replication protein A: a heter ...... for eukaryotic DNA metabolism
@en
Replication protein A: a heter ...... for eukaryotic DNA metabolism
@nl
altLabel
REPLICATION PROTEIN A:A Hetero ...... for Eukaryotic DNA Metabolism
@en
prefLabel
Replication protein A: a heter ...... for eukaryotic DNA metabolism
@ast
Replication protein A: a heter ...... for eukaryotic DNA metabolism
@en
Replication protein A: a heter ...... for eukaryotic DNA metabolism
@nl
P3181
P1476
REPLICATION PROTEIN A:A Hetero ...... for Eukaryotic DNA Metabolism
@en
Replication protein A: a heter ...... for eukaryotic DNA metabolism
@en
P2093
Marc S. Wold
P3181
P356
10.1146/ANNUREV.BIOCHEM.66.1.61
P407
P577
1997-06-01T00:00:00Z