相关参考文献
注意：仅列出部分参考文献，下载原文获取全部文献信息。Activation of the Protein Deacetylase SIRT6 by Long-chain Fatty Acids and Widespread Deacylation by Mammalian Sirtuins
Jessica L. Feldman et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2013)
SIRT6 regulates TNF-α secretion through hydrolysis of long-chain fatty acyl lysine
Hong Jiang et al.
NATURE (2013)
Evidence for a Common Mechanism of SIRT1 Regulation by Allosteric Activators
Basil P. Hubbard et al.
SCIENCE (2013)
Profiling of Substrates for Zinc-dependent Lysine Deacylase Enzymes: HDAC3 Exhibits Decrotonylase Activity In Vitro
Andreas S. Madsen et al.
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION (2012)
Structural Basis for Sirtuin Activity and Inhibition
Hua Yuan et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2012)
Quantitative Chemical Proteomics Approach To Identify Post-translational Modification-Mediated Protein-Protein Interactions
Xiang Li et al.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2012)
SIRT3 Functions in the Nucleus in the Control of Stress-Related Gene Expression
Toshinori Iwahara et al.
MOLECULAR AND CELLULAR BIOLOGY (2012)
Sirtuins as regulators of metabolism and healthspan
Riekelt H. Houtkooper et al.
NATURE REVIEWS MOLECULAR CELL BIOLOGY (2012)
Identification of 67 Histone Marks and Histone Lysine Crotonylation as a New Type of Histone Modification
Minjia Tan et al.
CELL (2011)
The First Identification of Lysine Malonylation Substrates and Its Regulatory Enzyme
Chao Peng et al.
MOLECULAR & CELLULAR PROTEOMICS (2011)
Sirt5 Is a NAD-Dependent Protein Lysine Demalonylase and Desuccinylase
Jintang Du et al.
SCIENCE (2011)
Approach to Profile Proteins That Recognize Post-Translationally Modified Histone Tails
Xiang Li et al.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2010)
Mechanism and regulation of acetylated histone binding by the tandem PHD finger of DPF3b
Lei Zeng et al.
NATURE (2010)
Crystal Structures of Human SIRT3 Displaying Substrate-induced Conformational Changes
Lei Jin et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2009)
The many roles of histone deacetylases in development and physiology: implications for disease and therapy
Michael Haberland et al.
NATURE REVIEWS GENETICS (2009)
Lysine acetylation: Codified crosstalk with other posttranslational modifications
Xiang-Jiao Yang et al.
MOLECULAR CELL (2008)
The Rpd3/Hda1 family of lysine deacetylases: from bacteria and yeast to mice and men
Xiang-Jiao Yang et al.
NATURE REVIEWS MOLECULAR CELL BIOLOGY (2008)
How chromatin-binding modules interpret histone modifications: lessons from professional pocket pickers
Sean D. Taverna et al.
NATURE STRUCTURAL & MOLECULAR BIOLOGY (2007)
SirT3 is a nuclear NAD+-dependent histone deacetylase that translocates to the mitochondria upon cellular stress
Michael B. Scher et al.
GENES & DEVELOPMENT (2007)
Epigenetics: A landscape takes shape
Aaron D. Goldberg et al.
CELL (2007)
Chromatin modifications and their function
Tony Kouzarides
CELL (2007)
Extraction, purification and analysis of histones
David Shechter et al.
NATURE PROTOCOLS (2007)
Reading protein modifications with interaction domains
Bruce T. Seet et al.
NATURE REVIEWS MOLECULAR CELL BIOLOGY (2006)
Histone H4-K16 acetylation controls chromatin structure and protein interactions
M Shogren-Knaak et al.
SCIENCE (2006)
The diverse functions of histone lysine methylation
C Martin et al.
NATURE REVIEWS MOLECULAR CELL BIOLOGY (2005)
Structural basis for the mechanism and regulation of Sir2 enzymes
JL Avalos et al.
MOLECULAR CELL (2004)
Structure and function of bromodomains in chromatin-regulating complexes
R Marmorstein et al.
GENE (2001)
Structure of the histone deacetylase SIRT2
MS Finnin et al.
NATURE STRUCTURAL BIOLOGY (2001)
Silent information regulator 2 family of NAD-dependent histone/protein deacetylases generates a unique product, 1-O-acetyl-ADP-ribose
KG Tanner et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2000)
The silencing protein SIR2 and its homologs are MAD-dependent protein deacetylases
J Landry et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2000)
Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
S Imai et al.
NATURE (2000)
分享论文
