Chemical specificity and physical properties of the lipid bilayer in the regulation of protein kinase C by anionic phospholipids: Evidence for the lack of a specific binding site for phosphatidylserine

Proceedings of the National Academy of Sciences of the United States of America

Volumn 93, Issue 5, 1996, Pages 1907-1912

  Mosior, Marian ^a,b   Golini, Erin S ^a   Epand, Richard M ^a  

^a MCMASTER UNIVERSITY   (Canada)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Membrane lateral phase separation; Phospholipid inverted phase propensity; Protein lipid interactions

Indexed keywords

PROTEIN KINASE C;

AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; BINDING SITE; CELLULAR DISTRIBUTION; CHEMICAL COMPOSITION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME REGULATION; ENZYME SPECIFICITY; LIPID BILAYER; LIPID MEMBRANE; NONHUMAN; PHOSPHOLIPID MEMBRANE; PRIORITY JOURNAL; PROTEIN LIPID INTERACTION; RAT;

AMINO ACID SEQUENCE; ANIMALS; ANIONS; BRAIN; CALCIUM; CALORIMETRY, DIFFERENTIAL SCANNING; ENZYME ACTIVATION; LIPID BILAYERS; MEMBRANE PROTEINS; MOLECULAR SEQUENCE DATA; PEPTIDES; PHOSPHOLIPIDS; PROTEIN KINASE C; RATS; THERMODYNAMICS;

EID: 0029921355     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.93.5.1907     Document Type: Article

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