Proteome analysis reveals phosphorylation of ATP synthase β-subunit in human skeletal muscle and proteins with potential roles in type 2 diabetes

Journal of Biological Chemistry

Volumn 278, Issue 12, 2003, Pages 10436-10442

  Højlund, Kurt ^a   Wrzesinski, Krzysztof ^b   Larsen, Peter Mose ^b   Fey, Stephen J ^b   Roepstorff, Peter ^b   Handberg, Aase ^a   Dela, Flemming ^c   Vinten, Jørgen ^d   McCormack, James G ^e   Reynet, Christine ^e   Beck Nielsen, Henning ^a  

^a ODENSE UNIVERSITY HOSPITAL   (Denmark)

^b UNIVERSITY OF SOUTHERN DENMARK   (Denmark)

^c UNIVERSITY OF COPENHAGEN   (Denmark)

^d UNIVERSITY OF COPENHAGEN   (Denmark)

^e NOVO NORDISK A S   (Denmark)

Author keywords

[No Author keywords available]

Indexed keywords

BIOSYNTHESIS; CATALYSIS; INSULIN; MUSCLE; PROTEINS; STRESSES;

INSULIN RESISTANCE;

BIOCHEMISTRY;

ADENOSINE TRIPHOSPHATE; C PEPTIDE; CREATINE KINASE BB; HEAT SHOCK PROTEIN; HEMOGLOBIN A1C; INSULIN; MUSCLE PROTEIN; PROTEOME; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; BIOLOGICAL MARKER; COLLAGEN TYPE 4; CREATINE KINASE; HEAT SHOCK PROTEIN 90; PROTEIN SUBUNIT; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE;

ADULT; ARTICLE; BETA CHAIN; CLINICAL ARTICLE; CONTROLLED STUDY; DIET RESTRICTION; ENZYME PHOSPHORYLATION; FEMALE; HUMAN; INSULIN RESISTANCE; MALE; MASS SPECTROMETRY; MITOCHONDRIAL RESPIRATION; MUSCLE BIOPSY; NON INSULIN DEPENDENT DIABETES MELLITUS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN PROCESSING; SEQUENCE ANALYSIS; SKELETAL MUSCLE; AMINO ACID SEQUENCE; BIOSYNTHESIS; CHEMISTRY; GLUCOSE BLOOD LEVEL; METABOLISM; MIDDLE AGED; MOLECULAR GENETICS; PHOSPHORYLATION;

ADENOSINE TRIPHOSPHATE; ADULT; AMINO ACID SEQUENCE; BIOLOGICAL MARKERS; BLOOD GLUCOSE; COLLAGEN TYPE IV; CREATINE KINASE; DIABETES MELLITUS, TYPE 2; FASTING; FEMALE; HSP90 HEAT-SHOCK PROTEINS; HUMANS; MALE; MIDDLE AGED; MOLECULAR SEQUENCE DATA; MUSCLE, SKELETAL; PHOSPHORYLATION; PROTEIN SUBUNITS; PROTEOME; PROTON-TRANSLOCATING ATPASES;

EID: 0038576291     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M212881200     Document Type: Article

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