(Q46977934)

27 December 2017

title

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

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27 December 2017

author name string

Ahlia N Khan

series ordinal

1

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27 December 2017

Peter N Lewis

series ordinal

2

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27 December 2017

language of work or name

English

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publication date

6 March 2006

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27 December 2017

Journal of Biological Chemistry

published in

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27 December 2017

volume

281

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27 December 2017

issue

17

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27 December 2017

page(s)

11702-11711

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27 December 2017

Substrate specificity and kinetic mechanism of the Sir2 family of NAD+-dependent histone/protein deacetylases

cites work

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511482200

Chemistry of gene silencing: the mechanism of NAD+-dependent deacetylation reactions

21 January 2018

1 reference

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Structural identification of 2'- and 3'-O-acetyl-ADP-ribose as novel metabolites derived from the Sir2 family of beta -NAD+-dependent histone/protein deacetylases

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511482200

A cytosolic NAD-dependent deacetylase, Hst2p, can modulate nucleolar and telomeric silencing in yeast

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511482200

The Sir2 family of protein deacetylases

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511482200

Histone acetylation and deacetylation in yeast

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511482200

hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511482200

The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511482200

Crystal structure of a SIR2 homolog-NAD complex

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511482200

Structural basis for the NAD-dependent deacetylase mechanism of Sir2

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511482200

Structure of a Sir2 enzyme bound to an acetylated p53 peptide

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511482200

Structural basis for the mechanism and regulation of Sir2 enzymes.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511482200

Structure and autoregulation of the yeast Hst2 homolog of Sir2

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511482200

Structure of the Yeast Hst2 Protein Deacetylase in Ternary Complex with 2′-O-Acetyl ADP Ribose and Histone Peptide

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511482200

Structure of the histone deacetylase SIRT2

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511482200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511482200

HST2 mediates SIR2-independent life-span extension by calorie restriction

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511482200

CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511482200

NPS@: network protein sequence analysis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511482200

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/10.1074%2FJBC.M511482200

Coupling of histone deacetylation to NAD breakdown by the yeast silencing protein Sir2: Evidence for acetyl transfer from substrate to an NAD breakdown product

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511482200

Mutations in Saccharomyces cerevisiae gene SIR2 can have differential effects on in vivo silencing phenotypes and in vitro histone deacetylation activity

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511482200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511482200

Sir2 regulation by nicotinamide results from switching between base exchange and deacetylation chemistry

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511482200

Poly(ADP-ribose) polymerases: managing genome stability

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M511482200

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511482200

Nicotinamide and PNC1 govern lifespan extension by calorie restriction in Saccharomyces cerevisiae

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511482200

Nicotinamide clearance by Pnc1 directly regulates Sir2-mediated silencing and longevity

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511482200

Identification of a small molecule inhibitor of Sir2p

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511482200

SIRT1 shows no substrate specificity in vitro

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M511482200

21 January 2018

Identifiers

DOI

10.1074/JBC.M511482200

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27 December 2017

PubMed ID

16520376

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27 December 2017