about
Structure of a Sir2 enzyme bound to an acetylated p53 peptideCrystal Structure of the Eukaryotic Strong Inward-Rectifier K+ Channel Kir2.2 at 3.1 A ResolutionA phylogenetically conserved NAD+-dependent protein deacetylase activity in the Sir2 protein family.Mechanism of sirtuin inhibition by nicotinamide: altering the NAD(+) cosubstrate specificity of a Sir2 enzymeSIR2 family of NAD(+)-dependent protein deacetylases.Compartmentalization of metabolic pathways in yeast mitochondria improves the production of branched-chain alcohols.Traditional and novel tools to probe the mitochondrial metabolism in health and disease.Structural basis for the mechanism and regulation of Sir2 enzymes.Harnessing yeast organelles for metabolic engineering.Uncovering the role of branched-chain amino acid transaminases in Saccharomyces cerevisiae isobutanol biosynthesis.Metabolic engineering: Biosensors get the green light.Insights into the Sirtuin Mechanism from Ternary Complexes Containing NAD+ and Acetylated PeptideThe Structural Basis of Sirtuin Substrate Affinity†,‡Mitochondrial Compartmentalization Confers Specificity to the 2-Ketoacid Recursive Pathway: Increasing Isopentanol Production in Saccharomyces cerevisiaeXylose utilization stimulates mitochondrial production of isobutanol and 2-methyl-1-butanol in Saccharomyces cerevisiaeXylose assimilation enhances the production of isobutanol in engineered Saccharomyces cerevisiaeLight-based control of metabolic flux through assembly of synthetic organelles
P50
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P50
description
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Jose L Avalos
@ast
Jose L Avalos
@en
Jose L Avalos
@es
Jose L Avalos
@nl
type
label
Jose L Avalos
@ast
Jose L Avalos
@en
Jose L Avalos
@es
Jose L Avalos
@nl
prefLabel
Jose L Avalos
@ast
Jose L Avalos
@en
Jose L Avalos
@es
Jose L Avalos
@nl
P106
P1153
7006889248
P21
P31
P496
0000-0002-7209-4208