Recombinant human replication protein A binds to polynucleotides with low cooperativity.
about
Influence of the human cohesion establishment factor Ctf4/AND-1 on DNA replicationA conserved lysine residue of plant Whirly proteins is necessary for higher order protein assembly and protection against DNA damageSaccharomyces cerevisiae replication protein A binds to single-stranded DNA in multiple salt-dependent modesTorsional 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.Functional analysis of the four DNA binding domains of replication protein A. The role of RPA2 in ssDNA binding.Interaction of the p70 subunit of RPA with a DNA template directs p32 to the 3'-end of nascent DNA.Replication protein A modulates its interface with the primed DNA template during RNA-DNA primer elongation in replicating SV40 chromosomes.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.Photocrosslinking locates a binding site for the large subunit of human replication protein A to the damaged strand of cisplatin-modified DNARPA subunit arrangement near the 3'-end of the primer is modulated by the length of the template strand and cooperative protein interactionsThe phosphorylation domain of the 32-kDa subunit of replication protein A (RPA) modulates RPA-DNA interactions. Evidence for an intersubunit interaction.Interactions of human replication protein A with single-stranded DNA adducts.Mass spectrometric identification of lysines involved in the interaction of human replication protein a with single-stranded DNA.Order of assembly of human DNA repair excision nuclease.Identification and characterization of a single-stranded DNA-binding protein from the archaeon Methanococcus jannaschii.Identification and characterization of the fourth single-stranded-DNA binding domain of replication protein AThe middle subunit of replication protein A contacts growing RNA-DNA primers in replicating simian virus 40 chromosomesDNA annealing by RAD52 protein is stimulated by specific interaction with the complex of replication protein A and single-stranded DNAHuman 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 lesion-specific co-localization of the Mre11/Rad50/Nbs1 (MRN) complex and replication protein A (RPA) to repair foci.Functions of human replication protein A (RPA): from DNA replication to DNA damage and stress responsesStructural characterization of human RPA sequential binding to single-stranded DNA using ssDNA as a molecular ruler.Human replication protein A-Rad52-single-stranded DNA complex: stoichiometry and evidence for strand transfer regulation by phosphorylation.The impact of base stacking on the conformations and electrostatics of single-stranded DNA.Localization of xeroderma pigmentosum group A protein and replication protein A on damaged DNA in nucleotide excision repair.Prognostic significance of replication protein A (RPA) expression levels in bladder urothelial carcinoma.Identification of a region of the herpes simplex virus single-stranded DNA-binding protein involved in cooperative bindingIdentification 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.Replication protein A unfolds G-quadruplex structures with varying degrees of efficiency.A DNA helicase purified by replication protein A (RPA) affinity chromatography from mouse FM3A cells.Characterization of Werner syndrome protein DNA helicase activity: directionality, substrate dependence and stimulation by replication protein ARPA-mediated unfolding of systematically varying G-quadruplex structures.Mechanochemical regulations of RPA's binding to ssDNA.Diffusion of human replication protein A along single-stranded DNA.Dual DNA-binding domains shape the interaction of Brh2 with DNA.
P2860
Q24617845-5A341C85-C740-46E0-9662-0AB21702550CQ27673752-51D46644-113B-48E8-827A-8C0DFF9F9149Q30441264-9E22C378-39C4-45AC-B11D-3FB5C66B089BQ30495260-6556C1E1-FD30-4D33-AF1B-F2CED69B81E5Q30661563-4EB88FF8-A108-454F-953D-F3F07C7E26F9Q30695523-62A56841-9577-4996-B8F8-BDC218B2F86FQ30704781-0217CEDB-8755-4E9B-A2A3-9F15400DD930Q30718522-139F5C8D-5406-467E-B7D4-D5E816E8C15CQ30724515-ECA1BBB9-79D5-40E7-A483-5FB93608B6D8Q30755683-B2050796-CACB-4340-A771-23C5B99EC64FQ30789768-745DCE83-2B0A-45DE-867B-14A3581199BDQ30951152-8990ACD0-957E-4949-BD5D-E6BCB285AA98Q31111443-E154EFB8-B4EA-4B9E-9E04-EDC7E0E1B966Q31141904-3A3B3268-BAEE-47D0-B063-737559BC3D44Q31326797-300EE744-CD8D-47B1-9071-FB79216D2D56Q31960108-09A65C37-4876-41C8-81E9-9D788DE66E64Q31973924-AF391765-6F2F-45B5-885C-B6C445B1448FQ31998506-2F129405-3FEF-4114-83D8-C301A5F7934CQ32062848-45D3313A-0076-4745-92B1-253345EA958CQ33200370-12E28E87-4C50-4CA6-9802-186A8AFED0C5Q33201968-29DF9946-B37D-45E6-8528-B0995D429463Q33210943-B17CB543-4D25-404E-9C8E-F714D6A7BA69Q33235763-6B520F41-550A-4F96-AF1A-C0B2DA1FBE78Q33288423-932140DC-7384-4467-8B89-FE2AD6C9AD8FQ33468536-B230DD94-1D6D-4962-A924-77CB1BA1B7E3Q33580487-D2505118-D531-49F0-9DEB-E0F445AF481FQ33652377-0E7AD4F4-96DA-4C8D-A96D-5D26B9CDA8DFQ33742674-A1E7496F-AA8C-46E5-B6F5-0827F4D312BCQ33781954-C921F513-4732-4E43-A1B9-16F4BEC68EE2Q33966014-6E1A5061-132F-4AAA-9F29-ADD80723D68DQ34083570-AEE6AB6A-4C12-416F-BCAB-F71368370926Q34097061-499277E5-7C0E-4DA6-9F21-308FDC9AE8C8Q34104803-E5B3F06C-3978-443A-8DE3-3C5608122683Q34231778-506CC52A-93B5-47B8-83F3-BF53254F1131Q34637176-257CEAEE-7FD6-4230-9F39-B55D6855EBF2Q34669156-D4286E79-1A2F-4577-8CD2-1D439EF4FA20Q34740767-8AA67D07-65E3-4EF6-8F62-69CF5D38EE4AQ35193716-C3C22B7C-3441-469D-B52F-745958CEDEA2Q35212587-EBEA4443-C4AB-46E5-9E19-6D2EB8A91655Q35226160-B87D9AE0-AA43-4A3A-BAFF-A4AECC11B8CE
P2860
Recombinant human replication protein A binds to polynucleotides with low cooperativity.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
1995年论文
@zh
1995年论文
@zh-cn
name
Recombinant human replication protein A binds to polynucleotides with low cooperativity.
@ast
Recombinant human replication protein A binds to polynucleotides with low cooperativity.
@en
type
label
Recombinant human replication protein A binds to polynucleotides with low cooperativity.
@ast
Recombinant human replication protein A binds to polynucleotides with low cooperativity.
@en
prefLabel
Recombinant human replication protein A binds to polynucleotides with low cooperativity.
@ast
Recombinant human replication protein A binds to polynucleotides with low cooperativity.
@en
P356
P1433
P1476
Recombinant human replication protein A binds to polynucleotides with low cooperativity.
@en
P304
P356
10.1021/BI00006A028
P407
P577
1995-02-01T00:00:00Z