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A Chemical Biology Approach to Reveal Sirt6-targeted Histone H3 Sites in Nucleosomes.The Current State of NAD(+) -Dependent Histone Deacetylases (Sirtuins) as Novel Therapeutic Targets.Rewiring protein synthesis: From natural to synthetic amino acids.Vascular Smooth Muscle Sirtuin-1 Protects Against Diet-Induced Aortic Stiffness.Chemical biology approaches for studying posttranslational modifications.Thienopyrimidinone Based Sirtuin-2 (SIRT2)-Selective Inhibitors Bind in the Ligand Induced Selectivity Pocket.Evolving the N-Terminal Domain of Pyrrolysyl-tRNA Synthetase for Improved Incorporation of Noncanonical Amino Acids.LC-MS/MS-based quantitative study of the acyl group- and site-selectivity of human sirtuins to acylated nucleosomes.
P2860
Q33817548-318F309D-DF04-4E95-8DE5-4C850771BDE4Q39091771-BC6D394B-1B04-427B-8BAD-DFDB9DA33B65Q39092037-0286800F-79AA-4EF2-A371-AAD334C012F9Q42111057-7B1535BC-413A-46C9-8AAC-10A51AE7E92DQ47810690-481E5AF7-283C-482C-BE6E-82BEF2455EDEQ48298219-BFF2CB47-BF88-4863-BAC8-3B4ECD0D5F1CQ48374893-C487E7D4-EF77-435B-8164-FA0F3EF60A62Q50106782-7D4639CA-FE86-4E0F-8F01-918DC20F61C9
P2860
description
2016 nî lūn-bûn
@nan
2016年の論文
@ja
2016年論文
@yue
2016年論文
@zh-hant
2016年論文
@zh-hk
2016年論文
@zh-mo
2016年論文
@zh-tw
2016年论文
@wuu
2016年论文
@zh
2016年论文
@zh-cn
name
Sirtuins 1 and 2 Are Universal Histone Deacetylases.
@en
type
label
Sirtuins 1 and 2 Are Universal Histone Deacetylases.
@en
prefLabel
Sirtuins 1 and 2 Are Universal Histone Deacetylases.
@en
P1433
P1476
Sirtuins 1 and 2 Are Universal Histone Deacetylases.
@en
P2093
P304
P356
10.1021/ACSCHEMBIO.5B00886
P50
P577
2016-01-28T00:00:00Z