Phosphorylated and unphosphorylated forms of human single-stranded DNA-binding protein are equally active in simian virus 40 DNA replication and in nucleotide excision repair.
about
Interaction and colocalization of Rad9/Rad1/Hus1 checkpoint complex with replication protein A in human cellsPreferential localization of hyperphosphorylated replication protein A to double-strand break repair and checkpoint complexes upon DNA damageIdentification of DNA replication and cell cycle proteins that interact with PCNABacterial single-stranded DNA-binding proteins are phosphorylated on tyrosine.Roles of replication protein-A subunits 2 and 3 in DNA replication fork movement in Saccharomyces cerevisiae.Quaternary structure of ATR and effects of ATRIP and replication protein A on its DNA binding and kinase activitiesInvolvement of DNA-dependent protein kinase in UV-induced replication arrest.DNA replication but not nucleotide excision repair is required for UVC-induced replication protein A phosphorylation in mammalian cellsZinc finger of replication protein A, a non-DNA binding element, regulates its DNA binding activity through redox.Re-oxygenation of hypoxic simian virus 40 (SV40)-infected CV1 cells causes distinct changes of SV40 minichromosome-associated replication proteins.DNA damage induced hyperphosphorylation of replication protein A. 2. Characterization of DNA binding activity, protein interactions, and activity in DNA replication and repair.The phosphorylation domain of the 32-kDa subunit of replication protein A (RPA) modulates RPA-DNA interactions. Evidence for an intersubunit interaction.Replication protein A (RPA) phosphorylation prevents RPA association with replication centers.Functional analysis of human replication protein A in nucleotide excision repair.DNA damage induced hyperphosphorylation of replication protein A. 1. Identification of novel sites of phosphorylation in response to DNA damage.Functions of human replication protein A (RPA): from DNA replication to DNA damage and stress responsesRegulation of replication protein A functions in DNA mismatch repair by phosphorylation.Regulatory functions of the N-terminal domain of the 70-kDa subunit of replication protein A (RPA)Human RPA phosphorylation by ATR stimulates DNA synthesis and prevents ssDNA accumulation during DNA-replication stressPhosphorylated RPA recruits PALB2 to stalled DNA replication forks to facilitate fork recovery.Multiple roles for kinases in DNA replication.In vitro analysis of the role of replication protein A (RPA) and RPA phosphorylation in ATR-mediated checkpoint signalingMapping of amino acid residues in the p34 subunit of human single-stranded DNA-binding protein phosphorylated by DNA-dependent protein kinase and Cdc2 kinase in vitro.Sites of UV-induced phosphorylation of the p34 subunit of replication protein A from HeLa cells.Phosphorylation of human replication protein A by the DNA-dependent protein kinase is involved in the modulation of DNA replicationExcision repair in mammalian cells.The DNA damage response in DNA-dependent protein kinase-deficient SCID mouse cells: replication protein A hyperphosphorylation and p53 induction.Phosphorylation of the PCNA binding domain of the large subunit of replication factor C on Thr506 by cyclin-dependent kinases regulates binding to PCNASingle-stranded-DNA binding alters human replication protein A structure and facilitates interaction with DNA-dependent protein kinaseStudies on the in vitro phosphorylation of HSSB-p34 and -p107 by cyclin-dependent kinases. Cyclin-substrate interactions dictate the efficiency of phosphorylation.The ATM homologue MEC1 is required for phosphorylation of replication protein A in yeastPurification, gene cloning, and reconstitution of the heterotrimeric single-stranded DNA-binding protein from Schizosaccharomyces pombe.The catalytic subunit DNA-dependent protein kinase (DNA-PKcs) facilitates recovery from radiation-induced inhibition of DNA replicationReversible protein phosphorylation modulates nucleotide excision repair of damaged DNA by human cell extracts.Complex formation between p53 and replication protein A inhibits the sequence-specific DNA binding of p53 and is regulated by single-stranded DNACharacterization of the p125 subunit of human DNA polymerase delta and its deletion mutants. Interaction with cyclin-dependent kinase-cyclins.Phosphorylation of xeroderma pigmentosum group C regulates ultraviolet-induced DNA damage repair.
P2860
Q24302320-FC4DDED9-3680-476E-B1D8-6336B3960B7BQ24537139-62F0A652-7CAD-4CFE-97F6-801D761EBBBAQ24545747-3230FC7C-BEE9-4784-867F-8D3666E97BCDQ25255885-EADA604F-4DF7-424D-9BDA-AF401267B308Q27930616-873FE832-B994-420D-8E32-0E87C27B67B1Q28610054-FF48C6A3-85EE-4110-BCE0-153A73928F0EQ30638467-FE5C7532-BB3E-40EC-B682-2648CA2047E4Q30653070-33F4E2B1-DF50-489C-A5D4-3A71F7E4A5B7Q30782786-D4ED6CB1-BBDB-4303-8710-B1DD5CEC0407Q30835095-0B36129A-1DC0-4E36-B3CC-C635D4E2BB85Q30854499-C946DA73-4773-4052-A474-FC2CC392EA6BQ30951152-D790F7BB-B266-4B0E-B070-C477B67C5104Q31048017-A22543E7-B25F-4F6F-911E-C162E4D4C4B4Q32069526-314C846F-90A2-4DA1-9AED-5C914CDF8D8DQ33216530-99B0F41B-9607-4090-BD96-71B2CA820E94Q33235763-83FEF858-58DB-470F-9052-4FC163A48F04Q33244982-2D45E09A-C50B-4684-A80A-C8624B973EA7Q33339291-20C3B62F-783C-44B1-9BAF-E90AFEF9FA1CQ33511571-2D9F2690-031D-404D-9554-45136C846777Q34062530-9C7C1749-472D-4C91-A396-A6F81ABAC474Q34228156-21C0EDCE-473B-4FF3-852B-F40AAEC6F6F2Q34403175-CBD5493F-AFA3-41D5-85F5-E58DBEFB1273Q34424988-F94E9E35-AC7A-46DD-842D-D84598F1EFE2Q34439017-CB2B4E5A-B22B-4467-88CB-4B824B773B27Q34604946-4F071F21-203D-4FD2-A9A9-41AA8FE085B6Q34720551-345EED4E-F924-44D1-95D7-F074EF166E6CQ35932187-4124D982-FB38-4401-B59F-911CF61A7747Q36247484-E785028E-D61D-40A9-B205-E9F8F4A38C37Q36562044-86FA4CF4-7132-45CB-B5A6-22995106ABAFQ36818739-15FFCDED-33B4-4471-B73E-53364389D063Q36840988-D960626B-F14E-4284-B78F-D9D6BC4B2EA4Q38353881-F4B36699-5A62-497B-A79A-2F0D0B587B0EQ39542617-B7691B36-A5C2-4364-B6A9-4CCA9A0DF941Q39715390-6FE957A7-1D97-449C-82FF-5B7387FCD480Q40021927-82D4232B-ADDD-413D-9BD6-1DFA937BE17AQ41041364-35264CD9-7554-4A06-A5F3-A16170477BFBQ52585806-59048ADA-859B-4D17-BC39-38FF9464FB1F
P2860
Phosphorylated and unphosphorylated forms of human single-stranded DNA-binding protein are equally active in simian virus 40 DNA replication and in nucleotide excision repair.
description
1995 nî lūn-bûn
@nan
1995 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի մայիսին հրատարակված գիտական հոդված
@hy
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
name
Phosphorylated and unphosphory ...... in nucleotide excision repair.
@ast
Phosphorylated and unphosphory ...... in nucleotide excision repair.
@en
Phosphorylated and unphosphory ...... in nucleotide excision repair.
@nl
type
label
Phosphorylated and unphosphory ...... in nucleotide excision repair.
@ast
Phosphorylated and unphosphory ...... in nucleotide excision repair.
@en
Phosphorylated and unphosphory ...... in nucleotide excision repair.
@nl
prefLabel
Phosphorylated and unphosphory ...... in nucleotide excision repair.
@ast
Phosphorylated and unphosphory ...... in nucleotide excision repair.
@en
Phosphorylated and unphosphory ...... in nucleotide excision repair.
@nl
P2093
P2860
P356
P1476
Phosphorylated and unphosphory ...... in nucleotide excision repair.
@en
P2093
P2860
P304
P356
10.1073/PNAS.92.10.4636
P407
P577
1995-05-01T00:00:00Z