Caspase-1 promiscuity is counterbalanced by rapid inactivation of processed enzyme

Journal of Biological Chemistry

Volumn 286, Issue 37, 2011, Pages 32513-32524

  Walsh, John G ^a   Logue, Susan E ^a   Lüthi, Alexander U ^a   Martin, Seamus J ^a  

^a TRINITY COLLEGE DUBLIN   (Ireland)

Author keywords

[No Author keywords available]

Indexed keywords

APOPTOTIC; CASPASE-3; CASPASES; CONCENTRATION-DEPENDENT; CYSTEINE PROTEASE; ENDOGENOUS CONCENTRATION; HALF LIVES; IN-VIVO; INTRINSIC DIFFERENCES; PROTEIN SUBSTRATE; RELATIVE ABUNDANCE; SUBSTRATE SPECIFICITY;

AMINO ACIDS; CELL DEATH;

SUBSTRATES;

APOPTOSOME; CASPASE 2; CASPASE 3; CASPASE 4; CASPASE 5; CASPASE 6; CASPASE 7; CASPASE 9; GELSOLIN; INFLAMMASOME; INTERLEUKIN 18; INTERLEUKIN 1BETA; INTERLEUKIN 1BETA CONVERTING ENZYME; P21 ACTIVATED KINASE 2; PROTEIN BID; PROTEIN P17; PROTEIN P23; X LINKED INHIBITOR OF APOPTOSIS;

APOPTOSIS; ARTICLE; CONCENTRATION RESPONSE; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME INACTIVATION; ENZYME SPECIFICITY; ENZYME SUBSTRATE; HUMAN; HUMAN CELL; INFLAMMATION; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; PRIORITY JOURNAL; PROTEIN CLEAVAGE; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN QUATERNARY STRUCTURE;

CASPASE 1; CASPASE 3; CASPASE 7; ENZYME STABILITY; HUMANS; JURKAT CELLS; SUBSTRATE SPECIFICITY;

EID: 80052754179     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.225862     Document Type: Article

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