Phosphorylation of hormone-sensitive lipase by protein kinase A in vitro promotes an increase in its hydrophobic surface area

FEBS Journal

Volumn 276, Issue 17, 2009, Pages 4752-4762

  Krintel, Christian ^a,b   Mörgelin, Matthias ^b   Logan, Derek T ^b   Holm, Cecilia ^a  

^a LUND UNIVERSITY   (Sweden)

^b LUND UNIVERSITY   (Sweden)

Author keywords

Cholesterol ester hydrolase; Electron microscopy; Fluorescence spectroscopy; Phospholipid vesicles

Indexed keywords

4,4' DIANILINO 1,1' BINAPHTHYL 5,5' DISULFONIC ACID; CYCLIC AMP DEPENDENT PROTEIN KINASE; FLUORESCENT DYE; HORMONE SENSITIVE LIPASE; TRIOLEIN; UNCLASSIFIED DRUG;

ADIPOCYTE; ANIMAL CELL; ARTICLE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME ACTIVITY; HYDROLYSIS; HYDROPHOBICITY; IN VITRO STUDY; IN VIVO STUDY; NONHUMAN; PHOSPHOLIPID VESICLE; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN INTERACTION; PROTEIN PHOSPHORYLATION; PROTEIN PURIFICATION; TRANSMISSION ELECTRON MICROSCOPY;

ADIPOCYTES; ANILINO NAPHTHALENESULFONATES; ANIMALS; CYCLIC AMP-DEPENDENT PROTEIN KINASES; FLUORESCENT DYES; HUMANS; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MICROSCOPY, ELECTRON; PHOSPHORYLATION; RATS; SERINE; STEROL ESTERASE;

RATTUS;

EID: 68849090290     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2009.07172.x     Document Type: Article

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