Structural basis for the mechanism and regulation of Sir2 enzymes. (Q44800960)

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25 December 2019

title

Structural basis for the mechanism and regulation of Sir2 enzymes (English)

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25 December 2019

2

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25 December 2019

Jose L Avalos

1

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25 December 2019

Cynthia Wolberger

3

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25 December 2019

author name string

José L Avalos

1

1 reference

6 December 2017

Cynthia Wolberger

3

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6 December 2017

1 March 2004

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25 December 2019

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25 December 2019

volume

13

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25 December 2019

issue

5

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25 December 2019

page(s)

639-648

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

25 December 2019

cites work

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

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Structure of a Sir2 enzyme bound to an acetylated p53 peptide

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Unusual conformation of nicotinamide adenine dinucleotide (NAD) bound to diphtheria toxin: a comparison with NAD bound to the oxidoreductase enzymes

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Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast sir2 and human SIRT1

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Transcriptional silencing in yeast is associated with reduced nucleosome acetylation

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Structural basis for the NAD-dependent deacetylase mechanism of Sir2

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7 January 2021

Structure of the histone deacetylase SIRT2

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Sir2 regulates skeletal muscle differentiation as a potential sensor of the redox state

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A new role for a yeast transcriptional silencer gene, SIR2, in regulation of recombination in ribosomal DNA.

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

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7 January 2021

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

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Improved methods for building protein models in electron density maps and the location of errors in these models

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

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7 January 2021

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

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7 January 2021

Requirement of NAD and SIR2 for life-span extension by calorie restriction in Saccharomyces cerevisiae

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7 January 2021

Negative control of p53 by Sir2alpha promotes cell survival under stress

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7 January 2021

XtalView/Xfit--A versatile program for manipulating atomic coordinates and electron density

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7 January 2021

Crystal structure of a SIR2 homolog-NAD complex

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7 January 2021

Acetylation of TAF(I)68, a subunit of TIF-IB/SL1, activates RNA polymerase I transcription

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7 January 2021

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

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7 January 2021

The amide rotational barriers in picolinamide and nicotinamide: NMR and ab initio studies

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7 January 2021

Processing of X-ray diffraction data collected in oscillation mode

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7 January 2021

Uracil-DNA glycosylase-DNA substrate and product structures: conformational strain promotes catalytic efficiency by coupled stereoelectronic effects

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7 January 2021

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

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7 January 2021

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

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7 January 2021

A phylogenetically conserved NAD+-dependent protein deacetylase activity in the Sir2 protein family.

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7 January 2021

SIR2 family of NAD(+)-dependent protein deacetylases.

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7 January 2021

Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine

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7 January 2021

Silent information regulator 2 family of NAD- dependent histone/protein deacetylases generates a unique product, 1-O-acetyl-ADP-ribose

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7 January 2021

Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans

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7 January 2021

Structure and catalytic mechanism of a SET domain protein methyltransferase

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7 January 2021

MOLREP: an Automated Program for Molecular Replacement

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7 January 2021

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

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7 January 2021

Structure and autoregulation of the yeast Hst2 homolog of Sir2

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7 January 2021

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

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7 January 2021

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Identifiers

DOI

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15023335%20AND%20SRC:MED&resulttype=core&format=json

25 December 2019

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