(Q37788970)

23 August 2017

title

Sirtuin mechanism and inhibition: explored with N(ε)-acetyl-lysine analogs (English)

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23 August 2017

Brett M Hirsch

1

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23 August 2017

Weiping Zheng

series ordinal

2

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23 August 2017

publication date

15 September 2010

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23 August 2017

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23 August 2017

volume

7

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23 August 2017

issue

1

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23 August 2017

page(s)

16-28

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Acetylation: a regulatory modification to rival phosphorylation?

23 August 2017

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Substrates and regulation mechanisms for the human mitochondrial sirtuins Sirt3 and Sirt5

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SIRT5 Deacetylates carbamoyl phosphate synthetase 1 and regulates the urea cycle

21 January 2018

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SIRT6 is a histone H3 lysine 9 deacetylase that modulates telomeric chromatin

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Sirt1 physically interacts with Tip60 and negatively regulates Tip60-mediated acetylation of H2AX.

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CobB regulates Escherichia coli chemotaxis by deacetylating the response regulator CheY.

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Structure of a Sir2 substrate, Alba, reveals a mechanism for deacetylation-induced enhancement of DNA binding

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Regulation of succinate dehydrogenase activity by SIRT3 in mammalian mitochondria

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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Mechanism of Nicotinamide Inhibition and Transglycosidation by Sir2 Histone/Protein Deacetylases

21 January 2018

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Sir2 protein deacetylases: evidence for chemical intermediates and functions of a conserved histidine.

21 January 2018

1 reference

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Plasmodium falciparum Sir2 is an NAD+-dependent deacetylase and an acetyllysine-dependent and acetyllysine-independent NAD+ glycohydrolase

21 January 2018

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Structural Insights into Intermediate Steps in the Sir2 Deacetylation Reaction

21 January 2018

1 reference

https://api.crossref.org/works/10.1039%2FC0MB00033G

Mechanism-based inhibition of Sir2 deacetylases by thioacetyl-lysine peptide

21 January 2018

1 reference

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Thiasugars: potential glycosidase inhibitors.

21 January 2018

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Sir2 deacetylases exhibit nucleophilic participation of acetyl-lysine in NAD+ cleavage.

21 January 2018

1 reference

https://api.crossref.org/works/10.1039%2FC0MB00033G

Highly dissociative and concerted mechanism for the nicotinamide cleavage reaction in Sir2Tm enzyme suggested by ab initio QM/MM molecular dynamics simulations

21 January 2018

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Quantitative assays for characterization of the Sir2 family of NAD(+)-dependent deacetylases

21 January 2018

1 reference

https://api.crossref.org/works/10.1039%2FC0MB00033G

Unstructured conformations are a substrate requirement for the Sir2 family of NAD-dependent protein deacetylases

21 January 2018

1 reference

https://api.crossref.org/works/10.1039%2FC0MB00033G

Use of substrate analogs and mutagenesis to study substrate binding and catalysis in the Sir2 family of NAD-dependent protein deacetylases

21 January 2018

1 reference

https://api.crossref.org/works/10.1039%2FC0MB00033G

Acetyl-lysine analog peptides as mechanistic probes of protein deacetylases

21 January 2018

1 reference

https://api.crossref.org/works/10.1039%2FC0MB00033G

Structural basis for the mechanism and regulation of Sir2 enzymes.

21 January 2018

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Molecular characterization of propionyllysines in non-histone proteins

21 January 2018

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Subtype selective substrates for histone deacetylases

21 January 2018

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https://api.crossref.org/works/10.1039%2FC0MB00033G

N-lysine propionylation controls the activity of propionyl-CoA synthetase

21 January 2018

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https://api.crossref.org/works/10.1039%2FC0MB00033G

Inhibition of human sirtuins by in situ generation of an acetylated lysine-ADP-ribose conjugate.

21 January 2018

1 reference

https://api.crossref.org/works/10.1039%2FC0MB00033G

Substrate specificity of SIRT1-catalyzed lysine Nepsilon-deacetylation reaction probed with the side chain modified Nepsilon-acetyl-lysine analogs

21 January 2018

1 reference

https://api.crossref.org/works/10.1039%2FC0MB00033G

Substituting N(epsilon)-thioacetyl-lysine for N(epsilon)-acetyl-lysine in peptide substrates as a general approach to inhibiting human NAD(+)-dependent protein deacetylases

21 January 2018

1 reference

https://api.crossref.org/works/10.1039%2FC0MB00033G

N(epsilon)-thioacetyl-lysine-containing tri-, tetra-, and pentapeptides as SIRT1 and SIRT2 inhibitors.

21 January 2018

1 reference

https://api.crossref.org/works/10.1039%2FC0MB00033G

Identification of a cell-active non-peptide sirtuin inhibitor containing N-thioacetyl lysine

21 January 2018

1 reference

https://api.crossref.org/works/10.1039%2FC0MB00033G

N(epsilon)-Modified lysine containing inhibitors for SIRT1 and SIRT2.

21 January 2018

1 reference

https://api.crossref.org/works/10.1039%2FC0MB00033G

Insights into the Sirtuin Mechanism from Ternary Complexes Containing NAD+ and Acetylated Peptide

21 January 2018

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https://api.crossref.org/works/10.1039%2FC0MB00033G

21 January 2018

Identifiers

DOI

10.1039/C0MB00033G

1 reference

23 August 2017

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