Aromatic residues of Caveolin-1 binding motif of α-hemolysin are essential for membrane penetration

Biochemical and Biophysical Research Communications

Volumn 363, Issue 1, 2007, Pages 197-202

  Pany, Satyabrata ^a   Krishnasastry, M V ^a  

^a NATIONAL CENTRE FOR CELL SCIENCE   (India)

Author keywords

Hemolysin; Caveolin 1 binding motif; Hetero oligomerization; Membrane penetration; Scaffolding domain

Indexed keywords

ALPHA HEMOLYSIN; AROMATIC COMPOUND; BACTERIAL PROTEIN; CAVEOLIN 1; HEMOLYSIN; MUTANT PROTEIN; PROTEIN SUBUNIT; STAPHYLOCOCCUS TOXIN; UNCLASSIFIED DRUG;

ARTICLE; CELL MEMBRANE PERMEABILITY; CONFORMATIONAL TRANSITION; FLUORESCENCE SPECTROSCOPY; HEMOLYSIS; INCUBATION TIME; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN MODIFICATION; PROTEIN MOTIF;

AMINO ACID MOTIFS; AMINO ACIDS, AROMATIC; BACTERIAL TOXINS; BINDING SITES; CAVEOLIN 1; CELLS, CULTURED; ERYTHROCYTE MEMBRANE; HEMOLYSIN PROTEINS; HEMOLYSIS; HUMANS; PROTEIN BINDING;

EID: 34548790062     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.08.132     Document Type: Article

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