Replication protein A (RPA) phosphorylation prevents RPA association with replication centers.
about
Human single-stranded DNA binding proteins are essential for maintaining genomic stabilityPhosphorylation: the molecular switch of double-strand break repairA PP4 phosphatase complex dephosphorylates RPA2 to facilitate DNA repair via homologous recombinationChk1 phosphorylation of Metnase enhances DNA repair but inhibits replication fork restartInteraction and colocalization of Rad9/Rad1/Hus1 checkpoint complex with replication protein A in human cellsA genome-wide camptothecin sensitivity screen identifies a mammalian MMS22L-NFKBIL2 complex required for genomic stabilityCellular functions of human RPA1. Multiple roles of domains in replication, repair, and checkpointsA naturally occurring human RPA subunit homolog does not support DNA replication or cell-cycle progressionPreferential localization of hyperphosphorylated replication protein A to double-strand break repair and checkpoint complexes upon DNA damageBacterial single-stranded DNA-binding proteins are phosphorylated on tyrosine.RPA-coated single-stranded DNA as a platform for post-translational modifications in the DNA damage responseIdentification of Small Molecule Proliferating Cell Nuclear Antigen (PCNA) Inhibitor That Disrupts Interactions with PIP-box Proteins and Inhibits DNA ReplicationSpy1 expression prevents normal cellular responses to DNA damage: inhibition of apoptosis and checkpoint activationA dynamic model for replication protein A (RPA) function in DNA processing pathwaysMitotic crisis: the unmasking of a novel role for RPANovel checkpoint response to genotoxic stress mediated by nucleolin-replication protein a complex formation.DNA stimulates Mec1-mediated phosphorylation of replication protein A.Replication protein A and the Mre11.Rad50.Nbs1 complex co-localize and interact at sites of stalled replication forks.Coordinated regulation of replication protein A activities by its subunits p14 and p32.DNA lesion-specific co-localization of the Mre11/Rad50/Nbs1 (MRN) complex and replication protein A (RPA) to repair foci.Inhibition of the herpes simplex virus type 1 DNA polymerase induces hyperphosphorylation of replication protein A and its accumulation at S-phase-specific sites of DNA damage during infection.DNA 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.Evidence of meiotic crossover control in Saccharomyces cerevisiae through Mec1-mediated phosphorylation of replication protein A.Differential involvement of phosphatidylinositol 3-kinase-related protein kinases in hyperphosphorylation of replication protein A2 in response to replication-mediated DNA double-strand breaks.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.Herpes simplex virus type I disrupts the ATR-dependent DNA-damage response during lytic infection.Autoantibodies against the replication protein A complex in systemic lupus erythematosus and other autoimmune diseases.RPA2 is a direct downstream target for ATR to regulate the S-phase checkpoint.The 32 kDa subunit of replication protein A (RPA) participates in the DNA replication of Mung bean yellow mosaic India virus (MYMIV) by interacting with the viral Rep protein.The checkpoint clamp activates Mec1 kinase during initiation of the DNA damage checkpoint.Structural characterization of human RPA sequential binding to single-stranded DNA using ssDNA as a molecular ruler.Sequential and synergistic modification of human RPA stimulates chromosomal DNA repair.Regulatory functions of the N-terminal domain of the 70-kDa subunit of replication protein A (RPA)RPA phosphorylation facilitates mitotic exit in response to mitotic DNA damage.Homologous recombinational repair factors are recruited and loaded onto the viral DNA genome in Epstein-Barr virus replication compartments.Ionizing radiation-dependent and independent phosphorylation of the 32-kDa subunit of replication protein A during mitosisProtein phosphatase 2A-dependent dephosphorylation of replication protein A is required for the repair of DNA breaks induced by replication stressHyperphosphorylation of replication protein A in cisplatin-resistant and -sensitive head and neck squamous cell carcinoma cell lines
P2860
Q21263027-5E16784E-C555-4E3C-A6C4-AF9646193599Q21296796-3D5870C9-3D0C-4B1A-B9B5-39E9B305736DQ24299264-5F5A76A0-312D-4183-8266-462DC1C9CC51Q24301492-96F87CFD-DF76-4D21-839E-1B31D8F85548Q24302320-65DB2D99-560A-479D-BCCA-04903ECAB5E0Q24306107-D311FBDF-9DBB-4F10-B3CA-4556B1B71056Q24311398-B462E3B2-C5B1-4280-9602-8CBB11ED0C82Q24321940-2C25B5F2-19A5-4058-81CA-BBB3CC6654B9Q24537139-52959A05-D624-4D3B-BFAC-D285EDD7AA53Q25255885-6DCE1849-EE05-4E46-B80E-3552611D72F0Q26827954-D6670676-4CAA-4A35-80E7-ADD1361A4A52Q27677564-F7BC2D2F-129D-4B7C-9F55-B85650FBA2ABQ28261764-77197750-3F6C-423A-8E95-9480D8C1A96EQ29614213-01084FFB-45A2-4CFD-9519-539A89783891Q30857441-3DFFFA90-C13C-44C0-B2A3-DC365356D06DQ31150971-ACE3BA0A-EB6F-4A43-8F33-850D54BD69B0Q33201421-457A51EC-CB8D-455F-96DF-EE6050CDE3FDQ33203493-A2460AC2-D33B-47C1-9FDC-66CA9C725332Q33203905-5D93DB68-C904-486C-9489-4321D8794639Q33210943-46885D02-FFBC-4207-ABBD-F20C3612EAF9Q33214993-CB21C4EF-F51A-4997-9AA9-211FD1D77D09Q33216530-E5D62B6F-6A3B-48DF-9EDD-60E9C3B69698Q33218577-1F5B3220-E0D3-440B-8B81-5022426EAEEBQ33222159-020443EA-31BA-49DF-BC67-E7BB9E2013D1Q33234136-ED944AB7-44CE-4F03-83C9-4A7EFC77C758Q33235763-A0AA2D46-FF44-46C6-9B5C-E51DA074B90CQ33244982-B821A474-315E-44EF-9BC0-AB0415C04B57Q33245944-A9D3D917-B29B-4174-AB55-A5344885304AQ33250439-779973CB-EB8B-4155-9704-D262177A7536Q33260135-AD5449D5-AAD7-4856-BA70-12F6CA47694AQ33267233-9632342A-8D89-43C6-8E93-D45B968E81FAQ33267615-EAA6F055-07A3-447D-AFD1-CC6778D46B87Q33288423-B8F3C3EC-C2E7-4D93-958B-0DF8083920BAQ33302234-EF939504-7787-406A-8E18-5695D0E8649EQ33339291-A3F6E19C-3773-47CD-BFB7-AA382D85FE32Q33362855-345B0190-4009-430F-9A4F-AA9279E4B880Q33433812-A599F72D-9CD2-4D1A-B87D-9CBAC9769909Q33492639-EC3B17F0-7F08-473C-BD2C-0BA9FF2EC7A4Q33496409-5E101DE3-68DF-4996-B8DF-BAC32082B118Q33507350-DE04F8D8-6469-4D99-B46C-EC3F0FE4A5DB
P2860
Replication protein A (RPA) phosphorylation prevents RPA association with replication centers.
description
2004 nî lūn-bûn
@nan
2004 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի մարտին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Replication protein A (RPA) ph ...... tion with replication centers.
@ast
Replication protein A (RPA) ph ...... tion with replication centers.
@en
type
label
Replication protein A (RPA) ph ...... tion with replication centers.
@ast
Replication protein A (RPA) ph ...... tion with replication centers.
@en
prefLabel
Replication protein A (RPA) ph ...... tion with replication centers.
@ast
Replication protein A (RPA) ph ...... tion with replication centers.
@en
P2093
P2860
P1476
Replication protein A (RPA) ph ...... tion with replication centers.
@en
P2093
James A Borowiec
Marc S Wold
Vitaly M Vassin
P2860
P304
P356
10.1128/MCB.24.5.1930-1943.2004
P407
P577
2004-03-01T00:00:00Z