The BRCA1/BARD1 heterodimer assembles polyubiquitin chains through an unconventional linkage involving lysine residue K6 of ubiquitin (Q24312959)

BRCA1 DNA repair associated

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BRCA1 associated RING domain 1

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ubiquitin-protein transferase activity

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author name string

Foon Wu-Baer

1

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Karen Lagrazon

2

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Wei Yuan

3

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Richard Baer

Journal of Biological Chemistry

4

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language of work or name

English

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publication date

12 September 2003

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published in

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volume

278

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page(s)

34743-6

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issue

37

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Activation of the E3 ligase function of the BRCA1/BARD1 complex by polyubiquitin chains

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

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Control of biochemical reactions through supramolecular RING domain self-assembly

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Mechanisms underlying ubiquitination

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Themes and variations on ubiquitylation

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A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein

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Stress resistance in Saccharomyces cerevisiae is strongly correlated with assembly of a novel type of multiubiquitin chain

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inferred from DOI database lookup

7 January 2021

based on heuristic

Construct for high-level expression and low misincorporation of lysine for arginine during expression of pET-encoded eukaryotic proteins in Escherichia coli

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inferred from DOI database lookup

7 January 2021

based on heuristic

Identifiers

DOI

10.1074/JBC.C300249200

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Consolidated OpenCitations Corpus – April 2017

755046

755046

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Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

1 reference