SCOPUS 정보 검색 플랫폼

Volumn 16, Issue 16, 2015, Pages 2337-2347

The ε-Amino Group of Protein Lysine Residues Is Highly Susceptible to Nonenzymatic Acylation by Several Physiological Acyl-CoA Thioesters

(5) Simic, Zeljko a Weiwad, Matthias a Schierhorn, Angelika a Steegborn, Clemens b Schutkowski, Mike a

a MARTIN LUTHER UNIVERSITY HALLE WITTENBERG (Germany)

b UNIVERSITY OF BAYREUTH (Germany)

Author keywords

acetyl coenzyme A; acylation; protein modifications; sirtuin; succinyl coenzyme A

Indexed keywords

ACYL COENZYME A; CARBAMOYL PHOSPHATE SYNTHASE; LYSINE; SUCCINYL COENZYME A; THIOESTER; AMINE; CYCLOPHILIN A; PEPTIDE; RECOMBINANT PROTEIN; SIRT5 PROTEIN, HUMAN; SIRTUIN; SIRTUIN 3;

ARTICLE; DEACYLATION; ENZYME ACTIVITY; METABOLITE; NATIVE POLYACRYLAMIDE GEL ELECTROPHORESIS; PH; PRIORITY JOURNAL; SURFACE CHARGE; TEMPERATURE DEPENDENCE; ACYLATION; BIOSYNTHESIS; CHEMISTRY; CONFORMATION; GENETICS; HUMAN; KINETICS; MASS SPECTROMETRY; METABOLISM; MITOCHONDRION; THERMODYNAMICS; X RAY CRYSTALLOGRAPHY;

ACYL COENZYME A; ACYLATION; AMINES; CRYSTALLOGRAPHY, X-RAY; CYCLOPHILIN A; HUMANS; KINETICS; LYSINE; MITOCHONDRIA; MOLECULAR CONFORMATION; PEPTIDES; RECOMBINANT PROTEINS; SIRTUIN 3; SIRTUINS; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; THERMODYNAMICS;

EID: 84945472675 PISSN: 14394227 EISSN: 14397633 Source Type: Journal
DOI: 10.1002/cbic.201500364 Document Type: Article

Times cited : (44)

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