Quantitative Proteomics Reveals the Function of Unconventional Ubiquitin Chains in Proteasomal Degradation-Reference-Cited by-同舟云学术

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Quantitative Proteomics Reveals the Function of Unconventional Ubiquitin Chains in Proteasomal Degradation

Published:2009-04 Issue:1 Volume:137 Page:133-145
ISSN:0092-8674
Container-title:Cell
language:en
Short-container-title:Cell

Author:

Xu Ping,Duong Duc M.,Seyfried Nicholas T.,Cheng Dongmei,Xie Yang,Robert Jessica,Rush John,Hochstrasser Mark,Finley Daniel,Peng Junmin

Publisher

Elsevier BV

Subject

General Biochemistry, Genetics and Molecular Biology

Reference43 articles.

1. UBXD7 binds multiple ubiquitin ligases and implicates p97 in HIF1alpha turnover;Alexandru;Cell,2008

2. Analysis of the deubiquitinating enzymes of the yeast Saccharomyces cerevisiae;Amerik;Biol. Chem.,2000

3. The Doa4 deubiquitinating enzyme is functionally linked to the vacuolar protein-sorting and endocytic pathways;Amerik;Mol. Biol. Cell,2000

4. Gene ontology: tool for the unification of biology. The Gene Ontology Consortium;Ashburner;Nat. Genet.,2000

5. Novel multiubiquitin chain linkages catalyzed by the conjugating enzymes E2EPF and RAD6 are recognized by 26 S proteasome subunit 5;Baboshina;J. Biol. Chem.,1996

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