Voltage-dependent anion channel 1-based peptides interact with hexokinase to prevent its anti-apoptotic activity

Journal of Biological Chemistry

Volumn 284, Issue 6, 2009, Pages 3946-3955

  Arzoine, Laetitia ^a   Zilberberg, Noam ^a   Ben Romano, Ronit ^a   Shoshan Barmatz, Varda ^a  

^a BEN GURION UNIVERSITY OF THE NEGEV   (Israel)

Author keywords

[No Author keywords available]

Indexed keywords

ANTI-APOPTOTIC EFFECTS; ANTI-APOPTOTIC PROTEIN; ANTIAPOPTOTIC ACTIVITIES; APOPTOTIC CELL DEATH; CELL-PENETRATING PEPTIDE; CHEMOTHERAPEUTIC AGENTS; CYTOCHROME C; HEXOKINASE; IN-CELL; ISOFORMS; N-TERMINAL; OUTER MITOCHONDRIAL MEMBRANES; REAL TIME; SITE DIRECTED MUTAGENESIS; STAUROSPORINE; SYNTHETIC PEPTIDE; TIME-DEPENDENT; TUMOR CELLS; VOLTAGE-DEPENDENT ANION CHANNELS;

CELL DEATH; CELL MEMBRANES; NEGATIVE IONS; PEPTIDES; PLANTS (BOTANY); SURFACE PLASMON RESONANCE; TUMORS;

AMINES;

CELL PENETRATING PEPTIDE; CELL PROTEIN; CYTOCHROME C; HEXOKINASE; HEXOKINASE 1; HEXOKINASE 2; PROTEIN LP4; UNCLASSIFIED DRUG; VOLTAGE DEPENDENT ANION CHANNEL 1; ANTINEOPLASTIC AGENT; ENZYME INHIBITOR; HK1 PROTEIN, HUMAN; HK1 PROTEIN, MOUSE; ISOENZYME; PEPTIDE; STAUROSPORINE; VDAC1 PROTEIN, HUMAN; VDAC1 PROTEIN, MOUSE;

AMINO ACID SEQUENCE; ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL TISSUE; APOPTOSIS; ARTICLE; BINDING SITE; CELL PROTECTION; CELL SURVIVAL; CELL VIABILITY; CONTROLLED STUDY; ENZYME ACTIVITY; HUMAN; HUMAN CELL; MITOCHONDRIAL MEMBRANE; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN SECRETION; PROTEIN SYNTHESIS; RAT; SITE DIRECTED MUTAGENESIS; TUMOR CELL; ANIMAL; ANTIBODY SPECIFICITY; BAGG ALBINO MOUSE; CHEMISTRY; DRUG EFFECT; METABOLISM; TUMOR CELL LINE;

ANIMALS; ANTINEOPLASTIC AGENTS; APOPTOSIS; CELL LINE, TUMOR; CELL SURVIVAL; CYTOCHROMES C; ENZYME INHIBITORS; HEXOKINASE; HUMANS; ISOENZYMES; MICE; MICE, INBRED BALB C; ORGAN SPECIFICITY; PEPTIDES; STAUROSPORINE; VOLTAGE-DEPENDENT ANION CHANNEL 1;

EID: 63649100705     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M803614200     Document Type: Article

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