about
Human single-stranded DNA binding proteins are essential for maintaining genomic stabilityPhosphorylation: the molecular switch of double-strand break repairStructure of the RPA trimerization core and its role in the multistep DNA-binding mechanism of RPAA PP4 phosphatase complex dephosphorylates RPA2 to facilitate DNA repair via homologous recombinationE3 ligase RFWD3 participates in replication checkpoint controlInteraction and colocalization of Rad9/Rad1/Hus1 checkpoint complex with replication protein A in human cellsCellular functions of human RPA1. Multiple roles of domains in replication, repair, and checkpointsHSSB1 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 DNAThe annealing helicase HARP is recruited to DNA repair sites via an interaction with RPAA naturally occurring human RPA subunit homolog does not support DNA replication or cell-cycle progressionAn alternative form of replication protein a expressed in normal human tissues supports DNA repairThe 32-kilodalton subunit of replication protein A interacts with menin, the product of the MEN1 tumor suppressor genePreferential localization of hyperphosphorylated replication protein A to double-strand break repair and checkpoint complexes upon DNA damageStress-dependent nucleolin mobilization mediated by p53-nucleolin complex formationCell cycle-dependent recruitment of telomerase RNA and Cajal bodies to human telomeresNMR chemical shift and relaxation measurements provide evidence for the coupled folding and binding of the p53 transactivation domainSolution structure of the DNA-binding domain of RPA from Saccharomyces cerevisiae and its interaction with single-stranded DNA and SV40 T antigenBacterial single-stranded DNA-binding proteins are phosphorylated on tyrosine.Role of the XPA protein in the NER pathway: A perspective on the function of structural disorder in macromolecular assemblyHuman RAD18 interacts with ubiquitylated chromatin components and facilitates RAD9 recruitment to DNA double strand breaksStructure of the major single-stranded DNA-binding domain of replication protein A suggests a dynamic mechanism for DNA binding.Structure and conformational change of a replication protein A heterotrimer bound to ssDNADisplacement of the canonical single-stranded DNA-binding protein in the ThermoprotealesThe structural basis of DNA binding by the single-stranded DNA-binding protein from Sulfolobus solfataricusThe karyopherin Kap142p/Msn5p mediates nuclear import and nuclear export of different cargo proteins.RPA-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 proteins53BP1 is associated with replication protein A and is required for RPA2 hyperphosphorylation following DNA damageSpy1 expression prevents normal cellular responses to DNA damage: inhibition of apoptosis and checkpoint activationThe interaction of p53 with replication protein A mediates suppression of homologous recombinationMicrohomology-mediated end joining: new players join the teamNABP1, a novel RORgamma-regulated gene encoding a single-stranded nucleic-acid-binding proteinPolarity of human replication protein A binding to DNAHuman replication protein A unfolds telomeric G-quadruplexesA dynamic model for replication protein A (RPA) function in DNA processing pathwaysDistinguishing the roles of Topoisomerases I and II in relief of transcription-induced torsional stress in yeast rRNA genes.Saccharomyces cerevisiae replication protein A binds to single-stranded DNA in multiple salt-dependent modesTorsional regulation of hRPA-induced unwinding of double-stranded DNA.
P2860
Q21263027-D6277F12-8B62-4152-B120-37A139CAE8D5Q21296796-6CA7F43C-6706-4365-A25A-B9ECE21B82E4Q24293001-710F0BA8-18F4-49D3-B17B-DDAA4B3D9A26Q24299264-A6AB66EB-59BA-4504-988E-E7BD68A53878Q24300010-728E0090-A3D7-4926-BB76-DBF1D5BA942DQ24302320-62C632EE-A52D-41DA-9C09-68A4E3BB4F01Q24311398-3509AE5A-ADC8-4793-AB5E-009FAEF02503Q24314871-58EE7FF2-445D-4760-B1E2-8F5D43EE3385Q24314908-3B6FB47E-CF6D-4F03-8B1E-6F38F54CD6BFQ24319860-C5E3B3D7-EBD1-4514-BFBD-ED48BB88DDA8Q24321940-0D54AFAA-B305-441F-87D9-0699C82F1AEEQ24336962-26BACAC2-1F47-49AB-9BB9-398CEBE03844Q24338184-E3025546-01C6-444F-84BE-B09E3BFDE031Q24537139-1FFE3BD0-C4AF-43B4-9B5B-31D68A3F0303Q24537692-8F2DCBD5-0F8A-4FC2-9112-ECC2FA749F6EQ24540232-DE849668-5466-499B-AA4B-5EC133CC9168Q24792064-ADD83D47-0233-4D99-82FA-2472BE4EF947Q24814735-BD079A5E-8C2A-4B6F-8834-BE1B8FA64397Q25255885-1899EEA2-155B-4249-9C06-7132730ABB3EQ26766647-D23F2668-3829-4EB0-A6B3-84FDD7B17EA4Q27325197-12F74E24-5DD8-4E3A-8A63-40C24AC95B58Q27629271-ED41E8FA-9CC4-4E9F-B23F-48AC5C3BC943Q27674555-5AFDF3F4-7E5D-440F-A72C-ABFE3190431DQ27675747-D7D796CF-3240-48B4-8F8A-046F0685E653Q27696128-169ADDE2-7040-49A5-B6F5-D540BAFEF442Q27933902-7013A7D3-5C10-4C66-B4F5-C58B49113850Q27939798-E3CA5B6C-FB8C-48BB-87F7-67E2F182193CQ28087630-47151467-6E05-45F1-8B21-73133B96E211Q28211138-D9C3E8A7-E49C-46D9-B0B0-FF0D18E8E358Q28247101-1F4DA87B-D355-4E45-8C31-6D26C16FC873Q28261764-ACD8551C-1502-466E-8F03-EF5E8B62A0E2Q28288360-3BE257CC-563D-4A28-9441-0734B723C90CQ28468576-51E6806E-7248-41CC-B152-C33C4E7D75E9Q28590992-171F73E5-E452-4F85-AC20-0FDC0FB084CCQ28647355-83527775-B6B8-4744-BA20-A468BBE1DE39Q29147418-5C153CB8-84A1-44F6-B54A-2D87500B98A4Q29614213-B5A6661E-ABE8-4E4B-AC07-5EF1496B8A97Q30431283-F6EB5B90-680B-4185-9C8D-17583A7E7091Q30441264-9B6AA071-9B07-40EA-AED5-B15D1D19FEF7Q30495260-1D98BD94-A2FF-42B5-8EDA-C757EBFA4B19
P2860
description
1999 nî lūn-bûn
@nan
1999 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հունվարին 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
Replication Protein A (RPA): The Eukaryotic SSB
@ast
Replication Protein A (RPA): The Eukaryotic SSB
@en
Replication Protein A (RPA): The Eukaryotic SSB
@en-gb
Replication Protein A (RPA): The Eukaryotic SSB
@nl
type
label
Replication Protein A (RPA): The Eukaryotic SSB
@ast
Replication Protein A (RPA): The Eukaryotic SSB
@en
Replication Protein A (RPA): The Eukaryotic SSB
@en-gb
Replication Protein A (RPA): The Eukaryotic SSB
@nl
altLabel
Replication protein A (RPA): the eukaryotic SSB
@en
prefLabel
Replication Protein A (RPA): The Eukaryotic SSB
@ast
Replication Protein A (RPA): The Eukaryotic SSB
@en
Replication Protein A (RPA): The Eukaryotic SSB
@en-gb
Replication Protein A (RPA): The Eukaryotic SSB
@nl
P3181
P1476
Replication protein A (RPA): the eukaryotic SSB
@en
P2093
P304
P3181
P356
10.1080/10409239991209255
P407
P577
1999-01-01T00:00:00Z