The RING heterodimer BRCA1-BARD1 is a ubiquitin ligase inactivated by a breast cancer-derived mutation (Q28207617)

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I Maeda

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H Nishikawa

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D Oyake

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Y Yabuki

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H Ogata

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T Ohta

Journal of Biological Chemistry

8

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language of work or name

English

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publication date

4 May 2001

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published in

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volume

276

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issue

18

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page(s)

14537-40

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cites work

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Centrosome amplification and a defective G2-M cell cycle checkpoint induce genetic instability in BRCA1 exon 11 isoform-deficient cells

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Identification of a RING protein that can interact in vivo with the BRCA1 gene product

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Mapping the functional domains of BRCA1. Interaction of the ring finger domains of BRCA1 and BARD1

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ROC1, a homolog of APC11, represents a family of cullin partners with an associated ubiquitin ligase activity

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Recruitment of a ROC1-CUL1 ubiquitin ligase by Skp1 and HOS to catalyze the ubiquitination of I kappa B alpha

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Rbx1, a component of the VHL tumor suppressor complex and SCF ubiquitin ligase

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Cdc53/cullin and the essential Hrt1 RING-H2 subunit of SCF define a ubiquitin ligase module that activates the E2 enzyme Cdc34

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SCF and APC: the Yin and Yang of cell cycle regulated proteolysis

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Activity of MDM2, a ubiquitin ligase, toward p53 or itself is dependent on the RING finger domain of the ligase

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The tyrosine kinase negative regulator c-Cbl as a RING-type, E2-dependent ubiquitin-protein ligase

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Ubiquitin protein ligase activity of IAPs and their degradation in proteasomes in response to apoptotic stimuli

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RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination

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Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases

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BRCA1 proteins are transported to the nucleus in the absence of serum and splice variants BRCA1a, BRCA1b are tyrosine phosphoproteins that associate with E2F, cyclins and cyclin dependent kinases

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Functional interaction of BRCA1-associated BARD1 with polyadenylation factor CstF-50

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The cancer-predisposing mutation C61G disrupts homodimer formation in the NH2-terminal BRCA1 RING finger domain

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Cell cycle-dependent colocalization of BARD1 and BRCA1 proteins in discrete nuclear domains

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Mutations in the BRCA1-associated RING domain (BARD1) gene in primary breast, ovarian and uterine cancers

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Identifiers

DOI

10.1074/JBC.C000881200

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Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

11278247

1 reference

Consolidated OpenCitations Corpus – April 2017