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

THE UBIQUITIN SYSTEM

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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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ROC1, a Homolog of APC11, Represents a Family of Cullin Partners with an Associated Ubiquitin Ligase Activity

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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 Cdc34Preprint

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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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Recruitment of a ROC1–CUL1 Ubiquitin Ligase by Skp1 and HOS to Catalyze the Ubiquitination of IκBα

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Functional Interaction of BRCA1-Associated BARD1 with Polyadenylation Factor CstF-50

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

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Mapping the Functional Domains of BRCA1

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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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The Cancer-predisposing Mutation C61G Disrupts Homodimer Formation in the NH2-terminal BRCA1 RING Finger Domain

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Activation of Transcription in Vitro by the BRCA1 Carboxyl-terminal Domain

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Phosphorylation- and Skp1-independent in vitro ubiquitination of E2F1 by multiple ROC-cullin ligases.

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Breast Cancer Genes and DNA Repair

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Association with cullin partners protects ROC proteins from proteasome-dependent degradation

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RING Domain E3 Ubiquitin Ligases

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Regulation of DNA repair throughout the cell cycle

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Abraxas and RAP80 Form a BRCA1 Protein Complex Required for the DNA Damage Response

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A mutational signature reveals alterations underlying deficient homologous recombination repair in breast cancer

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Ubiquitin-Binding Protein RAP80 Mediates BRCA1-Dependent DNA Damage Response

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The p53 orchestra: Mdm2 and Mdmx set the tone

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Recombinational DNA repair and human disease

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HdmX stimulates Hdm2-mediated ubiquitination and degradation of p53

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E2-BRCA1 RING interactions dictate synthesis of mono- or specific polyubiquitin chain linkages

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Binding and recognition in the assembly of an active BRCA1/BARD1 ubiquitin-ligase complex

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Structure of the MDM2/MDMX RING domain heterodimer reveals dimerization is required for their ubiquitylation in trans

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BRCA1 tumor suppression depends on BRCT phosphoprotein binding, but not its E3 ligase activity

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The p53 inhibitors MDM2/MDMX complex is required for control of p53 activity in vivo

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NBA1, a new player in the Brca1 A complex, is required for DNA damage resistance and checkpoint control

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Mechanisms of BRCA1 Tumor Suppression

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Discovery of Mdm2-MdmX E3 Ligase Inhibitors Using a Cell-Based Ubiquitination Assay

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Familial breast cancer screening reveals an alteration in the RAP80 UIM domain that impairs DNA damage response function

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SIRT2 promotes BRCA1-BARD1 heterodimerization through deacetylation

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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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Herpes Simplex Virus Type 1 Immediate-Early Protein ICP0 and Its Isolated RING Finger Domain Act as Ubiquitin E3 Ligases In Vitro

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Characterisation of human RING finger protein TRIM69, a novel testis E3 ubiquitin ligase and its subcellular localisation

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Alphaherpesvirus Proteins Related to Herpes Simplex Virus Type 1 ICP0 Induce the Formation of Colocalizing, Conjugated Ubiquitin

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