Inhibition of ubiquitin-protein ligase (E3) by mono- and bifunctional phenylarsenoxides. Evidence for essential vicinal thiols and a proximal nucleophile.-Reference-Cited by-同舟云学术

Inhibition of ubiquitin-protein ligase (E3) by mono- and bifunctional phenylarsenoxides. Evidence for essential vicinal thiols and a proximal nucleophile.

Published:1992-08 Issue:23 Volume:267 Page:16403-16411
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Berleth E.S.,Kasperek E.M.,Grill S.P.,Braunscheidel J.A.,Graziani L.A.,Pickart C.M.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference31 articles.

1. The ubiquitin pathway for protein degradation

2. Ubiquitin-conjugating enzymes: novel regulators of eukaryotic cells

3. Components of ubiquitin-protein ligase system. Resolution, affinity purification, and role in protein breakdown.

4. Functional heterogeneity of ubiquitin carrier proteins.

5. Levels of active ubiquitin carrier proteins decline during erythroid maturation.

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