Relevance of Fatty acid covalently bound to Escherichia coli -hemolysin and membrane microdomains in the oligomerization process

Journal of Biological Chemistry

Volumn 284, Issue 37, 2009, Pages 25199-25210

  Herlax, Vanesa ^a   Maté, Sabina ^a   Rimoldi, Omar ^a   Bakás, Laura ^a,b  

^a INSTITUTO DE INVESTIGACIONES BIOQUÍMICAS DE LA PLATA INIBIOLP   (Argentina)

^b FACULTAD DE CIENCIAS EXACTAS   (Argentina)

Author keywords

[No Author keywords available]

Indexed keywords

ACYL CHAIN; COVALENTLY BOUND; CYTOLYTIC ACTIVITIES; CYTOTOXIC ACTIVITIES; DETERGENT-RESISTANT MEMBRANES; ERYTHROCYTE GHOSTS; ERYTHROCYTE MEMBRANE; FLUORESCENCE RESONANCE ENERGY TRANSFER; FLUORESCENCE RESONANCE ENERGY TRANSFER MEASUREMENTS; HEMOLYTIC ACTIVITY; MAMMALIAN CELLS; MEMBRANE MICRODOMAINS; MUTANT PROTEINS; PATHOGENIC STRAINS; PLANAR LIPID MEMBRANES; PORE FORMATION; PROTEIN-PROTEIN INTERACTIONS; WHOLE CELL;

ACYLATION; AMINES; AMINO ACIDS; BLOOD; CELL MEMBRANES; DETERGENTS; ENERGY TRANSFER; ESCHERICHIA COLI; EXPERIMENTS; FATTY ACIDS; FLUORESCENCE; LIPOSOMES; MAMMALS; OLIGOMERIZATION; ORGANIC ACIDS; PHOSPHOLIPIDS; PROTEINS; RESONANCE; SYNTHESIS (CHEMICAL); TOXIC MATERIALS;

MEMBRANES;

ALPHA HEMOLYSIN; CHOLESTEROL; CYSTEINE; FATTY ACID;

ACYLATION; AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; CONTROLLED STUDY; COVALENT BOND; CYTOTOXICITY; ERYTHROCYTE GHOST; ERYTHROCYTE MEMBRANE; ESCHERICHIA COLI; FATTY ACID ANALYSIS; FLUORESCENCE RESONANCE ENERGY TRANSFER; HEMOLYSIS; MEMBRANE BINDING; MEMBRANE STRUCTURE; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION;

ANIMALS; CHOLESTEROL; CYSTEINE; ERYTHROCYTE MEMBRANE; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; FATTY ACIDS; FLUORESCENCE RESONANCE ENERGY TRANSFER; HEMOLYSIN PROTEINS; LYSINE; MEMBRANE MICRODOMAINS; MODELS, BIOLOGICAL; PROTEIN BINDING; PROTEIN INTERACTION MAPPING; PROTEIN STRUCTURE, TERTIARY; SHEEP;

ALEXA; ESCHERICHIA COLI; MAMMALIA; OVIS ARIES;

EID: 69949119994     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.009365     Document Type: Article

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