Analysis of acetylation stoichiometry suggests that SIRT 3 repairs nonenzymatic acetylation lesions-Reference-Cited by-同舟云学术

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Analysis of acetylation stoichiometry suggests that SIRT 3 repairs nonenzymatic acetylation lesions

Published:2015-09-10 Issue:21 Volume:34 Page:2620-2632
ISSN:0261-4189
Container-title:The EMBO Journal
language:en
Short-container-title:EMBO J

Author:

Weinert Brian T¹,Moustafa Tarek²,Iesmantavicius Vytautas¹,Zechner Rudolf³,Choudhary Chunaram¹

Affiliation:

1. The NNF Center for Protein Research Faculty of Health Sciences University of Copenhagen Copenhagen Denmark

2. Division of Gastroenterology and Hepatology Medical University Graz Graz Austria

3. Institute of Molecular Biosciences University of Graz Graz Austria

Publisher

EMBO

Subject

General Immunology and Microbiology,General Biochemistry, Genetics and Molecular Biology,Molecular Biology,General Neuroscience

Link

https://onlinelibrary.wiley.com/doi/pdf/10.15252/embj.201591271

Reference48 articles.

1. Lysine Acetylation Targets Protein Complexes and Co-Regulates Major Cellular Functions

2. Andromeda: A Peptide Search Engine Integrated into the MaxQuant Environment

3. Sirt5 Is a NAD-Dependent Protein Lysine Demalonylase and Desuccinylase

4. Tyr Phosphorylation of PDP1 Toggles Recruitment between ACAT1 and SIRT3 to Regulate the Pyruvate Dehydrogenase Complex

5. Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS

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