Widespread and enzyme-independent Nε-acetylation and Nε-succinylation of proteins in the chemical conditions of the mitochondrial matrix

Journal of Biological Chemistry

Volumn 288, Issue 40, 2013, Pages 29036-29045

  Wagner, Gregory R ^a   Payne, R Mark ^a  

^a INDIANA UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACYL-COA; ALKALINE PH; CHEMICAL CONDITIONS; MITOCHONDRIAL MATRIX; NON-ENZYMATIC; NONENZYMATIC PROTEIN; PROTEIN ACYLATION; SUCCINYLATION;

ACETYLATION; ACYLATION; ALKALINITY; AMINO ACIDS; PROTEINS;

MITOCHONDRIA;

ACYL COENZYME A; LYSINE; SIRTUIN 3; SIRTUIN 5;

ACYLATION; ALKALINITY; ANIMAL TISSUE; ARTICLE; BIOINFORMATICS; CONCENTRATION (PARAMETERS); CONCENTRATION RESPONSE; CONTROLLED STUDY; IN VITRO STUDY; MICROENVIRONMENT; MITOCHONDRION; MOUSE; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN ACYLATION; PROTEIN MODIFICATION; PROTEIN SUCCINYLATION;

ACETYL COENZYME A; ACETYLATION; METABOLIC DISEASES; METABOLIC REGULATION; MITOCHONDRIAL METABOLISM; NONENZYMATIC; PH REGULATION; SIRTUINS; SUCCINYL COENZYME A; SUCCINYLATION;

ACETYLATION; AMINO ACID SEQUENCE; ANIMALS; CATALYSIS; COENZYME A; COMPUTATIONAL BIOLOGY; HYDROGEN-ION CONCENTRATION; HYDROXIDES; KINETICS; MICE; MICE, INBRED C57BL; MITOCHONDRIA; MITOCHONDRIAL PROTEINS; MOLECULAR SEQUENCE DATA; SIRTUIN 3; SUCCINATES;

EID: 84885155285     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.486753     Document Type: Article

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