Catalytically Important Residues of E6AP Ubiquitin Ligase Identified Using Acid-Cleavable Photo-Cross-Linkers-Reference-Cited by-同舟云学术

Catalytically Important Residues of E6AP Ubiquitin Ligase Identified Using Acid-Cleavable Photo-Cross-Linkers

Published:2015-07-20 Issue:29 Volume:54 Page:4411-4414
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Krist David T.¹,Statsyuk Alexander V.¹

Affiliation:

1. Chemistry of Life Processes Institute, Department of Chemistry, Northwestern University, Silverman Hall, 2145 Sheridan Road, Evanston, Illinois 60208, United States

Funder

Northwestern University

Pew Charitable Trusts

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.5b00625

Reference19 articles.

1. The Ubiquitin System, an Immense Realm

2. Protein ubiquitination involving an E1–E2–E3 enzyme ubiquitin thioester cascade

3. UBE3A/E6-AP mutations cause Angelman syndrome

4. The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53

5. Cloning of Human Ubiquitin-conjugating Enzymes UbcH6 and UbcH7 (E2-F1) and Characterization of Their Interaction with E6-AP and RSP5

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