SIRT1 contains N- and C-terminal regions that potentiate deacetylase activity. - Wikidata - awgldk - TriplyDB

SIRT1 contains N- and C-terminal regions that potentiate deacetylase activity.

SIRT1 contains N- and C-terminal regions that potentiate deacetylase activity.

http://www.wikidata.org/entity/Q35709871

about

Structural basis for sirtuin activity and inhibition Structural and Functional Analysis of Human SIRT1 Crystal structure of the N-terminal domain of human SIRT7 reveals a three-helical domain architecture Evidence for a common mechanism of SIRT1 regulation by allosteric activators Small-molecule allosteric activators of sirtuins.Sirt1 carboxyl-domain is an ATP-repressible domain that is transferrable to other proteins.Energy restriction and potential energy restriction mimetics.The multifunctional sorting protein PACS-2 regulates SIRT1-mediated deacetylation of p53 to modulate p21-dependent cell-cycle arrest.Structural basis for allosteric, substrate-dependent stimulation of SIRT1 activity by resveratrol Using mitochondrial sirtuins as drug targets: disease implications and available compounds.The N-Terminal Domain of SIRT1 Is a Positive Regulator of Endogenous SIRT1-Dependent Deacetylation and Transcriptional Outputs Deacetylation by SIRT1 Reprograms Inflammation and Cancer The emerging and diverse roles of sirtuins in cancer: a clinical perspective.Unreported intrinsic disorder in proteins: Building connections to the literature on IDPs.The sirtuin class of histone deacetylases: regulation and roles in lipid metabolism.Chemical and structural biology of protein lysine deacetylases Biochemistry. Red wine, toast of the town (again)Jamming up the "β-staple": regulation of SIRT1 activity by its C-terminal regulatory segment (CTR).Molecular architecture of the human protein deacetylase Sirt1 and its regulation by AROS and resveratrol.Crystallographic structure of a small molecule SIRT1 activator-enzyme complex.A novel sirtuin 2 (SIRT2) inhibitor with p53-dependent pro-apoptotic activity in non-small cell lung cancer.Mechanism of Sirt1 NAD+-dependent Protein Deacetylase Inhibition by Cysteine S-Nitrosation.Sirt1 interaction with active Smad2 modulates transforming growth factor-β regulated transcription.The crystal structure of the Leishmania infantum Silent Information Regulator 2 related protein 1: Implications to protein function and drug design.

P2860

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P2860

SIRT1 contains N- and C-terminal regions that potentiate deacetylase activity.

http://www.wikidata.org/entity/Q35709871

description

2011 nî lūn-bûn

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2011年の論文

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2011年論文

@yue

2011年論文

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2011年論文

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2011年論文

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2011年論文

@zh-tw

2011年论文

@wuu

2011年论文

@zh

2011年论文

@zh-cn

name

SIRT1 contains N- and C-terminal regions that potentiate deacetylase activity.

@ast

SIRT1 contains N- and C-terminal regions that potentiate deacetylase activity.

@en

type

label

SIRT1 contains N- and C-terminal regions that potentiate deacetylase activity.

@ast

SIRT1 contains N- and C-terminal regions that potentiate deacetylase activity.

@en

prefLabel

SIRT1 contains N- and C-terminal regions that potentiate deacetylase activity.

@ast

SIRT1 contains N- and C-terminal regions that potentiate deacetylase activity.

@en

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P356

JBC.M111.285031

P1433

Journal of Biological Chemistry

P1476

SIRT1 contains N- and C-terminal regions that potentiate deacetylase activity.

@en

P2093

Emily Chen Ding

http://www.w3.org/2001/XMLSchema#string

Hua Yuan

http://www.w3.org/2001/XMLSchema#string

Michael Brent

http://www.w3.org/2001/XMLSchema#string

Min Pan

http://www.w3.org/2001/XMLSchema#string

Ronen Marmorstein

http://www.w3.org/2001/XMLSchema#string

P2860

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

Sir2 mediates longevity in the fly through a pathway related to calorie restriction

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

SRT1720, SRT2183, SRT1460, and resveratrol are not direct activators of SIRT1

Small molecule activators of SIRT1 as therapeutics for the treatment of type 2 diabetes

Structure and autoregulation of the yeast Hst2 homolog of Sir2

Structural basis of inhibition of the human NAD+-dependent deacetylase SIRT5 by suramin

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

The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases.

Nuclear export modulates the cytoplasmic Sir2 homologue Hst2.

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2468-2476

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scholarly article

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10.1074/JBC.M111.285031

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4

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287

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2011-12-07T00:00:00Z

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22157016

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3268407

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