A pore-forming toxin requires a specific residue for its activity in membranes with particular physicochemical properties

Journal of Biological Chemistry

Volumn 290, Issue 17, 2015, Pages 10850-10861

  Morante, Koldo ^a,b   Caaveiro, Jose M M ^a   Tanaka, Koji ^a   González Mañas, Juan Manuel ^b   Tsumoto, Kouhei ^a  

^a UNIVERSITY OF TOKYO   (Japan)

^b UNIVERSITY OF THE BASQUE COUNTRY UPV EHU   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MEMBRANES; CELL DEATH; CHOLESTEROL; PHOSPHOLIPIDS; PROTEINS;

CONSERVED RESIDUES; CYTOLYTIC ACTIVITIES; LIPID COMPOSITION; MECHANISM OF ACTION; MEMBRANE PROTEINS; PHYSICOCHEMICAL PROPERTY; PORE FORMING TOXINS; PROTEIN-BASED BIOSENSORS;

MEMBRANES;

CHOLESTEROL; CYTOLYSIN; FRAGACEATOXIN C; LIPID; MEMBRANE PROTEIN; PHENYLALANINE; PHENYLALANINE 16; SPHINGOMYELIN; UNCLASSIFIED DRUG; COELENTERATE VENOM; LIPOSOME; MEMBRANE LIPID;

ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; BIOSENSOR; CELL DEATH; CONTROLLED STUDY; ERYTHROCYTE; LIPID COMPOSITION; MOLECULAR MECHANICS; NONHUMAN; PHYSICAL CHEMISTRY; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN PURIFICATION; SEA ANEMONE; SITE DIRECTED MUTAGENESIS; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMAL; BINDING SITE; CELL MEMBRANE; CHEMICAL STRUCTURE; CHEMISTRY; DRUG EFFECTS; GENETICS; HEMOLYSIS; METABOLISM; MOLECULAR GENETICS; PROTEIN CONFORMATION; PROTEIN STABILITY; SEQUENCE HOMOLOGY; THERMODYNAMICS; X RAY CRYSTALLOGRAPHY;

ACTINIARIA;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; BINDING SITES; CELL MEMBRANE; CHOLESTEROL; CNIDARIAN VENOMS; CRYSTALLOGRAPHY, X-RAY; HEMOLYSIS; LIPOSOMES; MEMBRANE LIPIDS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PHYSICOCHEMICAL PHENOMENA; PROTEIN CONFORMATION; PROTEIN STABILITY; SEA ANEMONES; SEQUENCE HOMOLOGY, AMINO ACID; THERMODYNAMICS;

EID: 84928401355     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.615211     Document Type: Article

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