Human replication protein A: global fold of the N-terminal RPA-70 domain reveals a basic cleft and flexible C-terminal linker
about
Structure of the RPA trimerization core and its role in the multistep DNA-binding mechanism of RPAPhysical and functional mapping of the replication protein a interaction domain of the werner and bloom syndrome helicasesNMR chemical shift and relaxation measurements provide evidence for the coupled folding and binding of the p53 transactivation domainRPA-coated single-stranded DNA as a platform for post-translational modifications in the DNA damage responseConcentration-dependent exchange of replication protein A on single-stranded DNA revealed by single-molecule imagingDynamic binding of replication protein a is required for DNA repair.Structure of the major single-stranded DNA-binding domain of replication protein A suggests a dynamic mechanism for DNA binding.Insights into ssDNA recognition by the OB fold from a structural and thermodynamic study of Sulfolobus SSB proteinCrystal structures of RMI1 and RMI2, two OB-fold regulatory subunits of the BLM complexStructural bases of dimerization of yeast telomere protein Cdc13 and its interaction with the catalytic subunit of DNA polymerase αA flexible linker region in Fip1 is needed for efficient mRNA polyadenylationCharacteristics and concepts of dynamic hub proteins in DNA processing machinery from studies of RPANucleic acid recognition by OB-fold proteinsOligonucleotide/oligosaccharide-binding fold proteins: a growing family of genome guardiansA dynamic model for replication protein A (RPA) function in DNA processing pathwaysSingle-stranded DNA mimicry in the p53 transactivation domain interaction with replication protein AFunctional analysis of the four DNA binding domains of replication protein A. The role of RPA2 in ssDNA binding.Bimodal interaction between replication-protein A and Dna2 is critical for Dna2 function both in vivo and in vitro.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 bindingMass spectrometric identification of lysines involved in the interaction of human replication protein a with single-stranded DNA.Independent and coordinated functions of replication protein A tandem high affinity single-stranded DNA binding domains.Physical interaction between replication protein A and Rad51 promotes exchange on single-stranded DNA.Denaturation of replication protein A reveals an alternative conformation with intact domain structure and oligonucleotide binding activityModulation of replication protein A function by its hyperphosphorylation-induced conformational change involving DNA binding domain B.Structural 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 basic cleft of RPA70N binds multiple checkpoint proteins, including RAD9, to regulate ATR signaling.Physical interaction between replication protein A (RPA) and MRN: involvement of RPA2 phosphorylation and the N-terminus of RPA1.Structural 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.Preparation of the modular multi-domain protein RPA for study by NMR spectroscopy.In vitro analysis of the role of replication protein A (RPA) and RPA phosphorylation in ATR-mediated checkpoint signalingSample preparation methods to analyze DNA-induced structural changes in 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.The tenacious recognition of yeast telomere sequence by Cdc13 is fully exerted by a single OB-fold domain.Leishmania braziliensis replication protein A subunit 1: molecular modelling, protein expression and analysis of its affinity for both DNA and RNA.RPA70 depletion induces hSSB1/2-INTS3 complex to initiate ATR signaling.
P2860
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P2860
Human replication protein A: global fold of the N-terminal RPA-70 domain reveals a basic cleft and flexible C-terminal linker
description
1999 nî lūn-bûn
@nan
1999 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Human replication protein A: g ...... and flexible C-terminal linker
@ast
Human replication protein A: g ...... and flexible C-terminal linker
@en
Human replication protein A: g ...... and flexible C-terminal linker
@nl
type
label
Human replication protein A: g ...... and flexible C-terminal linker
@ast
Human replication protein A: g ...... and flexible C-terminal linker
@en
Human replication protein A: g ...... and flexible C-terminal linker
@nl
prefLabel
Human replication protein A: g ...... and flexible C-terminal linker
@ast
Human replication protein A: g ...... and flexible C-terminal linker
@en
Human replication protein A: g ...... and flexible C-terminal linker
@nl
P2093
P3181
P356
P1476
Human replication protein A: g ...... and flexible C-terminal linker
@en
P2093
A S Lipton
D M Jacobs
G W Daughdrill
P2888
P304
P3181
P356
10.1023/A:1008373009786
P577
1999-08-01T00:00:00Z
P6179
1040969374