Deacylation Mechanism by SIRT2 Revealed in the 1′-SH-2′-O-Myristoyl Intermediate Structure-Reference-Cited by-同舟云学术

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Deacylation Mechanism by SIRT2 Revealed in the 1′-SH-2′-O-Myristoyl Intermediate Structure

Published:2017-03 Issue:3 Volume:24 Page:339-345
ISSN:2451-9456
Container-title:Cell Chemical Biology
language:en
Short-container-title:Cell Chemical Biology

Author:

Wang Yi,Fung Yi Man Eva,Zhang Weizhe,He Bin,Chung Matthew Wai Heng,Jin Jing,Hu Jing,Lin Hening,Hao Quan

Funder

NIH

Publisher

Elsevier BV

Subject

Clinical Biochemistry,Drug Discovery,Pharmacology,Molecular Biology,Molecular Medicine,Biochemistry

Reference34 articles.

1. Structure of trypanothione reductase from Crithidia fasciculata at 2.6 A resolution; enzyme-NADP interactions at 2.8 A resolution;Bailey;Acta Crystallogr. D Biol. Crystallogr.,1994

2. Identification of 'erasers' for lysine crotonylated histone marks using a chemical proteomics approach;Bao;ELife,2014

3. SIRT1 deacetylation and repression of p300 involves lysine residues 1020/1024 within the cell cycle regulatory domain 1;Bouras;J. Biol. Chem.,2005

4. Silent information regulator 2 potentiates Foxo1-mediated transcription through its deacetylase activity;Daitoku;Proc. Natl. Acad. Sci. USA,2004

5. Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase;Du;Science,2011

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