Characterization of CobB kinetics and inhibition by nicotinamide.

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Characterization of CobB kinetics and inhibition by nicotinamide.

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2017 nî lūn-bûn

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2017年の論文

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年學術文章

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2017年學術文章

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Characterization of CobB kinetics and inhibition by nicotinamide.

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Characterization of CobB kinetics and inhibition by nicotinamide.

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Characterization of CobB kinetics and inhibition by nicotinamide.

@en

Characterization of CobB kinetics and inhibition by nicotinamide.

@nl

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Characterization of CobB kinetics and inhibition by nicotinamide.

@en

Characterization of CobB kinetics and inhibition by nicotinamide.

@nl

P1476

Characterization of CobB kinetics and inhibition by nicotinamide

@en

P2093

Ana Écija Conesa

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

Gema Lozano Terol

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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

Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2

Regulation of cellular metabolism by protein lysine acetylation

Acetylation of histones and transcription-related factors

Structural basis for nicotinamide cleavage and ADP-ribose transfer by NAD(+)-dependent Sir2 histone/protein deacetylases

Acylation of Biomolecules in Prokaryotes: a Widespread Strategy for the Control of Biological Function and Metabolic Stress

Structural basis for sirtuin activity and inhibition

Structure and mechanism of non-histone protein acetyltransferase enzymes

From sirtuin biology to human diseases: an update

Structure and Substrate Binding Properties of cobB, a Sir2 Homolog Protein Deacetylase from Escherichia coli

P304

e0189689

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P31

scholarly article

P356

10.1371/JOURNAL.PONE.0189689

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P407

English

P433

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

P478

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

P50

Teresa de Diego

Manuel Canovas

Julia Gallego-Jara

P577

2017-12-18T00:00:00Z

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P698

29253849

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P932

5734772

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