SIRT1 Shows No Substrate Specificity in Vitro-Reference-Cited by-同舟云学术

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SIRT1 Shows No Substrate Specificity in Vitro

Published:2005-03 Issue:11 Volume:280 Page:9780-9785
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Blander Gil,Olejnik Jerzy,Krzymanska-Olejnik Edyta,McDonagh Thomas,Haigis Marcia,Yaffe Michael B.,Guarente Leonard

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference31 articles.

1. Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase

2. The Sir2 Family of Protein Deacetylases

3. The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms

4. Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans

5. Characterization of Five Human cDNAs with Homology to the Yeast SIR2 Gene: Sir2-like Proteins (Sirtuins) Metabolize NAD and May Have Protein ADP-Ribosyltransferase Activity

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1. Quantitative structure–activity relationship modeling reveals the minimal sequence requirement and amino acid preference of sirtuin-1’s deacetylation substrates in diabetes mellitus;Journal of Bioinformatics and Computational Biology;2022-04-21

2. Substrate-Dependent Sensitivity of SIRT1 to Nicotinamide Inhibition;Biomolecules;2021-02-18

3. Fluorogenic probes for detecting deacylase and demethylase activity towards post-translationally-modified lysine residues;Chemical Science;2021

4. Human SIRT1 Multispecificity Is Modulated by Active-Site Vicinity Substitutions during Natural Evolution;Molecular Biology and Evolution;2020-09-21

5. The evolution of human SIRT1 for multi-specificity is enabled by active-site adaptation;2020-01-14

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