Structure of an XRCC1 BRCT domain: a new protein-protein interaction module (Q24533379)

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author name string

S Moréra

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P A Bates

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P C Whitehead

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A I Coffer

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K Hainbucher

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R A Nash

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M J Sternberg

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P S Freemont

BRCA1 protein is linked to the RNA polymerase II holoenzyme complex via RNA helicase A

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language of work or name

English

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publication date

2 November 1998

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published in

The EMBO Journal

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volume

17

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issue

21

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page(s)

6404-11

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cites work

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XRCC1 is specifically associated with poly(ADP-ribose) polymerase and negatively regulates its activity following DNA damage

24 March 2017

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BRCA1 regulates p53-dependent gene expression

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Mammalian DNA double-strand break repair protein XRCC4 interacts with DNA ligase IV

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BRCA1 is a component of the RNA polymerase II holoenzyme

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Reconstitution of DNA base excision-repair with purified human proteins: interaction between DNA polymerase beta and the XRCC1 protein

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Characterization of the XRCC1-DNA ligase III complex in vitro and its absence from mutant hamster cells

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24 March 2017

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A strong candidate for the breast and ovarian cancer susceptibility gene BRCA1

24 March 2017

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Role of a BRCT domain in the interaction of DNA ligase III-alpha with the DNA repair protein XRCC1

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From BRCA1 to RAP1: a widespread BRCT module closely associated with DNA repair

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BRCA1 protein products ... Functional motifs...

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30 May 2018

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Germline mutations of the BRCA1 gene in breast and ovarian cancer families provide evidence for a genotype–phenotype correlation

21 January 2018

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21 January 2018

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Transcriptional activation by BRCA1

29 November 2018

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Breast cancer genes--what are the real risks?

21 January 2018

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Specific versus non-specific contacts in protein crystals

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Altered DNA ligase III activity in the CHO EM9 mutant

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