BRCA1 Associated RING Domain 1 Protein

Known as: BARD-1, BRCA1-Associated RING Domain 1, BRCA1 Associated RING Domain Protein 1 
BRCA1-associated RING domain protein 1 (777 aa, ~87 kDa) is encoded by the human BARD1 gene. This protein plays a role in cell cycle progression, DNA… (More)
National Institutes of Health

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23 relations
Ankyrin RepeatApoptosisApoptosis PromoterBARD1 Pathway
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BRCA1 Protein

Papers overview

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Highly Cited
2009
Highly Cited
2009
BRCA1-associated protein 1 interferes with BRCA1/BARD1 RING heterodimer activity.
The breast and ovarian tumor suppressor BRCA1 constitutes a RING heterodimer E3 ligase with BARD1. BRCA1-associated protein 1… (More)
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Highly Cited
2004
Highly Cited
2004
BRCA1 : BARD1 induces the formation of conjugated ubiquitin structures, dependent on K6 of ubiquitin, in cells during DNA replication and repair.
The N-terminus of the BRCA1 protein bears a RING finger domain that functions as an E3 ubiquitin ligase in vitro where it is able… (More)
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Highly Cited
2003
Highly Cited
2003
Enhancement of BRCA1 E3 ubiquitin ligase activity through direct interaction with the BARD1 protein.
The breast and ovarian cancer-specific tumor suppressor RING finger protein BRCA1 has been identified as an E3 ubiquitin (Ub… (More)
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Highly Cited
2002
Highly Cited
2002
Autoubiquitination of the BRCA1*BARD1 RING ubiquitin ligase.
The RING finger of BRCA1 confers ubiquitin ligase activity that is markedly enhanced when complexed with another RING-containing… (More)
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Highly Cited
2002
Highly Cited
2002
BARD1 induces BRCA1 intranuclear foci formation by increasing RING-dependent BRCA1 nuclear import and inhibiting BRCA1 nuclear export.
BRCA1 is a tumor suppressor with several important nuclear functions. BRCA1 has no known cytoplasmic functions. We show here that… (More)
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Highly Cited
2002
Highly Cited
2002
Activation of the E3 ligase function of the BRCA1/BARD1 complex by polyubiquitin chains.
Loss of the tumour suppressor BRCA1 results in profound chromosomal instability. The fundamental defect underlying this… (More)
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Highly Cited
2001
Highly Cited
2001
The RING heterodimer BRCA1-BARD1 is a ubiquitin ligase inactivated by a breast cancer-derived mutation.
BRCA1-BARD1 constitutes a heterodimeric RING finger complex associated through its N-terminal regions. Here we demonstrate that… (More)
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Highly Cited
2001
Highly Cited
2001
Structure of a BRCA1–BARD1 heterodimeric RING–RING complex
The RING domain of the breast and ovarian cancer tumor suppressor BRCA1 interacts with multiple cognate proteins, including the… (More)
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1998
1998
Mutations in the BRCA1-associated RING domain (BARD1) gene in primary breast, ovarian and uterine cancers.
Germline alterations of BRCA1 result in susceptibility to breast and ovarian cancer. The protein encoded by BRCA1 interacts in… (More)
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1998
1998
In Vitro Repression of Brca1-associated RING Domain Gene, Bard1, Induces Phenotypic Changes in Mammary Epithelial Cells
BRCA1-associated RING domain (BARD1) was identified as a protein interacting with the breast cancer gene product BRCA1. The… (More)
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