Structural basis for potent inhibition of SIRT2 deacetylase by a macrocyclic peptide inducing dynamic structural change
about
Structure-Based Development of an Affinity Probe for Sirtuin 2The sirtuin-2 inhibitor AK7 is neuroprotective in models of Parkinson's disease but not amyotrophic lateral sclerosis and cerebral ischemiaA continuous sirtuin activity assay without any coupling to enzymatic or chemical reactions.Selective Sirt2 inhibition by ligand-induced rearrangement of the active site.Insights into Lysine Deacetylation of Natively Folded Substrate Proteins by Sirtuins.Selectivity hot-spots of sirtuin catalytic cores.Insight into the Mechanism of Intramolecular Inhibition of the Catalytic Activity of Sirtuin 2 (SIRT2).Finding Potent Sirt Inhibitor in Coffee: Isolation, Confirmation and Synthesis of Javamide-II (N-Caffeoyltryptophan) as Sirt1/2 InhibitorMacrocycle peptides delineate locked-open inhibition mechanism for microorganism phosphoglycerate mutases.New Modalities for Challenging Targets in Drug Discovery.Seeding for sirtuins: microseed matrix seeding to obtain crystals of human Sirt3 and Sirt2 suitable for soaking.The Current State of NAD(+) -Dependent Histone Deacetylases (Sirtuins) as Novel Therapeutic Targets.Lysine-acetylation as a fundamental regulator of Ran function: Implications for signaling of proteins of the Ras-superfamily.Kinetic and Structural Basis for Acyl-Group Selectivity and NAD(+) Dependence in Sirtuin-Catalyzed DeacylationMax-Bergmann award lecture:A RaPID way to discover bioactive nonstandard peptides assisted by the flexizyme and FIT systems.The crystal structure of the Leishmania infantum Silent Information Regulator 2 related protein 1: Implications to protein function and drug design.Non-competitive cyclic peptides for targeting enzyme-substrate complexes.Model foldamers: applications and structures of stable macrocyclic peptides identified using in vitro selectionIdentification of a novel small molecule that inhibits deacetylase but not defatty-acylase reaction catalysed by SIRT2
P2860
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P2860
Structural basis for potent inhibition of SIRT2 deacetylase by a macrocyclic peptide inducing dynamic structural change
description
2014 nî lūn-bûn
@nan
2014 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
name
Structural basis for potent in ...... cing dynamic structural change
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Structural basis for potent in ...... cing dynamic structural change
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Structural basis for potent in ...... cing dynamic structural change
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type
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Structural basis for potent in ...... cing dynamic structural change
@ast
Structural basis for potent in ...... cing dynamic structural change
@en
Structural basis for potent in ...... cing dynamic structural change
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prefLabel
Structural basis for potent in ...... cing dynamic structural change
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Structural basis for potent in ...... cing dynamic structural change
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Structural basis for potent in ...... cing dynamic structural change
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P2093
P50
P1433
P1476
Structural basis for potent in ...... cing dynamic structural change
@en
P2093
Hiroaki Suga
Hiroshi Nishimasu
Jumpei Morimoto
Kenichiro Yamagata
Norihiko Takeda
Ryozo Nagai
P304
P356
10.1016/J.STR.2013.12.001
P577
2014-02-04T00:00:00Z