The substrate binding domains of human SIAH E3 ubiquitin ligases are now crystal clear-Reference-Cited by-同舟云学术

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The substrate binding domains of human SIAH E3 ubiquitin ligases are now crystal clear

Published:2017-01 Issue:1 Volume:1861 Page:3095-3105
ISSN:0304-4165
Container-title:Biochimica et Biophysica Acta (BBA) - General Subjects
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - General Subjects

Author:

Zhang Qi,Wang Zhongduo,Hou Feng,Harding Rachel,Huang Xinyi^ORCID,Dong Aiping,Walker John R.,Tong Yufeng^ORCID

Funder

AbbVie

Bayer Pharma AG

Boehringer Ingelheim

Canada Foundation for Innovation

Eshelman Institute for Innovation

Genome Canada through Ontario Genomics Institute

Innovative Medicines Initiative

Janssen, Merck & Co.

Novartis Pharma AG

Ontario Ministry of Economic Development and Innovation

Pfizer

São Paulo Research Foundation-FAPESP

Takeda

Wellcome Trust

UChicago Argonne, LLC

U.S. Department of Energy, Office of Biological and Environmental Research

National Natural Science Foundation of China

Excellent Young Teachers Program of Guangdong Province

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics

Reference88 articles.

1. Siah-1 N-terminal RING domain is required for proteolysis function, and C-terminal sequences regulate oligomerization and binding to target proteins;Hu;Mol. Cell. Biol.,1999

2. Siah proteins: novel drug targets in the Ras and hypoxia pathways;House;Cancer Res.,2009

3. Estrogen down-regulation of the corepressor N-CoR: mechanism and implications for estrogen derepression of N-CoR-regulated genes;Frasor;Proc. Natl. Acad. Sci. U. S. A.,2005

4. Control of HIPK2 stability by ubiquitin ligase Siah-1 and checkpoint kinases ATM and ATR;Winter;Nat. Cell Biol.,2008

5. Regulation of Tumor Suppressor EAF2 Polyubiquitination by ELL1 and SIAH2 in Prostate Cancer Cells;Yu,2016

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