The weak interdomain coupling observed in the 70 kDa subunit of human replication protein A is unaffected by ssDNA binding
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Structure of the RPA trimerization core and its role in the multistep DNA-binding mechanism of RPAEvidence 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 domainDynamic binding of replication protein a is required for DNA repair.A flexible linker region in Fip1 is needed for efficient mRNA polyadenylationReplication Protein A Presents Canonical Functions and Is Also Involved in the Differentiation Capacity of Trypanosoma cruziA dynamic model for replication protein A (RPA) function in DNA processing pathwaysSingle-stranded DNA mimicry in the p53 transactivation domain interaction with replication protein AThe 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 AIndependent and coordinated functions of replication protein A tandem high affinity single-stranded DNA binding domains.Human replication protein A (RPA) binds a primer-template junction in the absence of its major ssDNA-binding domains.Denaturation of replication protein A reveals an alternative conformation with intact domain structure and oligonucleotide binding activityStructural characterization of human RPA sequential binding to single-stranded DNA using ssDNA as a molecular ruler.Regulatory functions of the N-terminal domain of the 70-kDa subunit of replication protein A (RPA)The annealing helicase HARP protects stalled replication forksStructural dynamics and single-stranded DNA binding activity of the three N-terminal domains of the large subunit of replication protein A from small angle X-ray scatteringReplication protein A: directing traffic at the intersection of replication and repair.Accurate 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.A small molecule directly inhibits the p53 transactivation domain from binding to replication protein A.A new structural framework for integrating replication protein A into DNA processing machinery.Diffusion of human replication protein A along single-stranded DNA.Architecture and ssDNA interaction of the Timeless-Tipin-RPA complex.Molecular Evolution and Functional Diversification of Replication Protein A1 in Plants.Essential functions of the 32 kDa subunit of yeast replication protein A.Catalysis of strand annealing by replication protein A derives from its strand melting properties.Structural models of protein-DNA complexes based on interface prediction and docking.
P2860
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P2860
The weak interdomain coupling observed in the 70 kDa subunit of human replication protein A is unaffected by ssDNA binding
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年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
The weak interdomain coupling ...... is unaffected by ssDNA binding
@ast
The weak interdomain coupling ...... is unaffected by ssDNA binding
@en
type
label
The weak interdomain coupling ...... is unaffected by ssDNA binding
@ast
The weak interdomain coupling ...... is unaffected by ssDNA binding
@en
prefLabel
The weak interdomain coupling ...... is unaffected by ssDNA binding
@ast
The weak interdomain coupling ...... is unaffected by ssDNA binding
@en
P2093
P2860
P356
P1476
The weak interdomain coupling ...... is unaffected by ssDNA binding
@en
P2093
C Arrowsmith
G W Daughdrill
J Ackerman
M V Botuyan
P2860
P304
P356
10.1093/NAR/29.15.3270
P407
P577
2001-08-01T00:00:00Z