Structure of the major single-stranded DNA-binding domain of replication protein A suggests a dynamic mechanism for DNA binding.
about
Structure of the RPA trimerization core and its role in the multistep DNA-binding mechanism of RPAStructure of RPA32 bound to the N-terminus of SMARCAL1 redefines the binding interface between RPA32 and its interacting proteinsEvidence for direct contact between the RPA3 subunit of the human replication protein A and single-stranded DNADifferent activities of the largest subunit of replication protein A cooperate during SV40 DNA replicationThe oligomerization and ligand-binding properties of Sm-like archaeal proteins (SmAPs)Solution structure of the DNA-binding domain of RPA from Saccharomyces cerevisiae and its interaction with single-stranded DNA and SV40 T antigenRPA-coated single-stranded DNA as a platform for post-translational modifications in the DNA damage responseDynamic binding of replication protein a is required for DNA repair.Insights into ssDNA recognition by the OB fold from a structural and thermodynamic study of Sulfolobus SSB proteinCrystal structure of the Agrobacterium virulence complex VirE1-VirE2 reveals a flexible protein that can accommodate different partnersPhysical Interactions between Mcm10, DNA, and DNA PolymeraseStructure and conformational change of a replication protein A heterotrimer bound to ssDNAThe structural basis of DNA binding by the single-stranded DNA-binding protein from Sulfolobus solfataricusRPA-like proteins mediate yeast telomere function.Characteristics 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 guardiansInterferon-inducible protein 16: insight into the interaction with tumor suppressor p53MEIOB exhibits single-stranded DNA-binding and exonuclease activities and is essential for meiotic recombinationA dynamic model for replication protein A (RPA) function in DNA processing pathwaysSaccharomyces cerevisiae replication protein A binds to single-stranded DNA in multiple salt-dependent modesSingle-stranded DNA mimicry in the p53 transactivation domain interaction with replication protein ATorsional regulation of hRPA-induced unwinding of double-stranded DNA.Functional analysis of the four DNA binding domains of replication protein A. The role of RPA2 in ssDNA binding.Human replication protein A. The C-terminal RPA70 and the central RPA32 domains are involved in the interactions with the 3'-end of a primer-template DNA.Bimodal interaction between replication-protein A and Dna2 is critical for Dna2 function both in vivo and in vitro.Recruitment of replication protein A by the papillomavirus E1 protein and modulation by single-stranded DNARecruitment of the priming protein pTP and DNA binding occur by overlapping Oct-1 POU homeodomain surfacesMass 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.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.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 activityDNA damage induced hyperphosphorylation of replication protein A. 1. Identification of novel sites of phosphorylation in response to DNA damage.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.Structural mechanism of RPA loading on DNA during activation of a simple pre-replication complex.Structural characterization of human RPA sequential binding to single-stranded DNA using ssDNA as a molecular ruler.Sequential recruitment of the repair factors during NER: the role of XPG in initiating the resynthesis step.Regulatory functions of the N-terminal domain of the 70-kDa subunit of replication protein A (RPA)
P2860
Q24293001-DDC89DDD-80D7-478A-9CAA-F0483067890CQ24299074-F4C1B6F2-F985-4724-A092-BE4AFA8F17F4Q24314908-5A795992-877F-49EF-98BB-103C4E5FE408Q24336061-B10BA1A4-2558-4361-9E66-C2F5CB3FA17FQ24644821-4673E3AE-7A64-40A0-86A4-4C52ADCBA49AQ24814735-B86A487D-6A1C-46AC-AECE-65BC15543585Q26827954-004FE649-5ED5-4003-8BE4-95B118D0C27EQ27323422-B6E8F739-44E2-49D5-A92D-8F7E55A53285Q27641337-6BB5453F-5A75-4E7A-9135-4C8030D819D6Q27651409-2BF31AE8-211F-4079-90CC-D8E6ED845BEAQ27656496-E4071ED7-E11E-450B-9545-D7EE30627130Q27674555-2E70B946-9639-4D0A-A34A-EE5F8DC9BEBEQ27696128-5782D347-D34E-4960-9ACB-E249E02362FCQ27939798-0E108549-FF7A-437A-ACBC-8660F60E6565Q28087630-043F5A87-4881-46D8-9922-01DC1C8EF444Q28211138-6F0A09C7-1157-4D38-8446-FA05BD0B8F0EQ28283925-4D665C86-826F-43FA-84D8-D1129B640F7DQ28307165-91CD4C18-28F8-471F-8C10-FEE6444A6BD4Q28593795-1660CB84-019A-4F13-A883-461160849908Q29614213-810EE220-96C6-42E0-9775-B8ACC69D0190Q30441264-EFE113F3-C021-48AD-BBE2-AD50ED60B3FEQ30446685-EF9D28C1-F438-4ED1-B64D-D5DD972D640FQ30495260-B0A54C8F-EF1A-4F72-923D-7DA84D85E4D5Q30695523-3C90F91B-5955-41A0-98E6-71740B423014Q30724515-33CFC8AD-EC32-462D-B74F-E3D377308AB6Q30727947-835D0D53-1DFC-414F-9811-5D6C76C8CBE1Q31038703-496A1603-DA21-4497-84CB-A5881B303C29Q31038852-1D7BAAFE-7CB7-4244-97C7-F49D7D6E4E06Q31141904-88E939DB-D3A1-4E4D-8295-AD10137FE08AQ31150799-9207A147-8AC9-4A51-B7D1-E08CDA254BC7Q31153117-0F4ACCCE-CC03-40E9-956A-F9F77D0C253AQ33200370-ACF9E71D-631B-4AC2-89D7-65B276595949Q33201968-20C43620-2A96-433D-A371-3F1CEDF5885FQ33216530-E741BE78-67AB-4328-A431-8896D8F5C005Q33218577-8568C5D6-09A7-4767-927C-00D9862CDF4CQ33250054-7D65AC85-2FA1-437A-A18B-75F91DB08250Q33263880-E43B7046-DEBD-4A08-BCC9-03EBDAE5F27AQ33288423-90632BAD-C4CE-4417-A1A4-F8634729B0D6Q33310274-4BB164EB-29CD-4A19-9EC9-14B5795EA7E1Q33339291-8EA66629-3835-4C2C-82AC-080E3DF89D72
P2860
Structure of the major single-stranded DNA-binding domain of replication protein A suggests a dynamic mechanism for DNA binding.
description
2001 nî lūn-bûn
@nan
2001 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի փետրվարին 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
Structure of the major single- ...... amic mechanism for DNA binding
@nl
Structure of the major single- ...... mic mechanism for DNA binding.
@ast
Structure of the major single- ...... mic mechanism for DNA binding.
@en
type
label
Structure of the major single- ...... amic mechanism for DNA binding
@nl
Structure of the major single- ...... mic mechanism for DNA binding.
@ast
Structure of the major single- ...... mic mechanism for DNA binding.
@en
prefLabel
Structure of the major single- ...... amic mechanism for DNA binding
@nl
Structure of the major single- ...... mic mechanism for DNA binding.
@ast
Structure of the major single- ...... mic mechanism for DNA binding.
@en
P2093
P2860
P3181
P356
P1433
P1476
Structure of the major single- ...... mic mechanism for DNA binding.
@en
P2093
A Bochkarev
E Bochkareva
P2860
P304
P3181
P356
10.1093/EMBOJ/20.3.612
P407
P577
2001-02-01T00:00:00Z