RPA mediates recombination repair during replication stress and is displaced from DNA by checkpoint signalling in human cells (Q24338859)

Replication protein A2

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Replication protein A3

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double-strand break repair via homologous recombination

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author

Thomas Helleday

6

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Jiří Bártek

5

object named as

Jiri Bartek

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Natalia Issaeva

3

object named as

Natalia Issaeva

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author name string

Kate M Sleeth

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Claus Storgaard Sørensen

2

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Jaroslaw Dziegielewski

Journal of Molecular Biology

4

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language of work or name

English

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publication date

12 October 2007

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published in

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volume

373

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issue

1

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page(s)

38-47

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cites work

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An ATR- and Cdc7-dependent DNA damage checkpoint that inhibits initiation of DNA replication

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RPA phosphorylation in mitosis alters DNA binding and protein-protein interactions.

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The 32- and 14-Kilodalton Subunits of Replication Protein A Are Responsible for Species-Specific Interactions with Single-Stranded DNA

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Synergistic actions of Rad51 and Rad52 in recombination and DNA repair

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Stimulation by Rad52 of yeast Rad51- mediated recombination

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Rad52 protein stimulates DNA strand exchange by Rad51 and replication protein A

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Mutation in Rpa1 results in defective DNA double-strand break repair, chromosomal instability and cancer in mice

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Checking on DNA damage in S phase

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Rad52-mediated DNA annealing after Rad51-mediated DNA strand exchange promotes second ssDNA capture

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ATRIP associates with replication protein A-coated ssDNA through multiple interactions

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Nuclear foci of mammalian Rad51 recombination protein in somatic cells after DNA damage and its localization in synaptonemal complexes

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DNA annealing by Rad52 Protein is stimulated by specific interaction with the complex of replication protein A and single-stranded DNA

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Physical interaction between human RAD52 and RPA is required for homologous recombination in mammalian cells

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A sequence in the N-terminal region of human uracil-DNA glycosylase with homology to XPA interacts with the C-terminal part of the 34-kDa subunit of replication protein A

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The Chk1 protein kinase and the Cdc25C regulatory pathways are targets of the anticancer agent UCN-01

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DNA replication defects, spontaneous DNA damage, and ATM-dependent checkpoint activation in replication protein A-deficient cells

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Structural basis for Chk1 inhibition by UCN-01

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Rad52 protein associates with replication protein A (RPA)-single-stranded DNA to accelerate Rad51-mediated displacement of RPA and presynaptic complex formation

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Replication protein A and the Mre11.Rad50.Nbs1 complex co-localize and interact at sites of stalled replication forks

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Sister chromatid gene conversion is a prominent double-strand break repair pathway in mammalian cells

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Interaction of human rad51 recombination protein with single-stranded DNA binding protein, RPA

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Conservative homologous recombination preferentially repairs DNA double-strand breaks in the S phase of the cell cycle in human cells

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Sensing DNA damage through ATRIP recognition of RPA-ssDNA complexes

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Claspin operates downstream of TopBP1 to direct ATR signaling towards Chk1 activation

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Targeted inactivation of mouse RAD52 reduces homologous recombination but not resistance to ionizing radiation

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Nonperiodic activity of the human anaphase-promoting complex-Cdh1 ubiquitin ligase results in continuous DNA synthesis uncoupled from mitosis

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Different roles for nonhomologous end joining and homologous recombination following replication arrest in mammalian cells

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Spontaneous homologous recombination is induced by collapsed replication forks that are caused by endogenous DNA single-strand breaks

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Inhibition of human Chk1 causes increased initiation of DNA replication, phosphorylation of ATR targets, and DNA breakage

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Role of Saccharomyces single-stranded DNA-binding protein RPA in the strand invasion step of double-strand break repair

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Identifiers

DOI

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

17765923

1 reference

Consolidated OpenCitations Corpus – April 2017