Multiple species of CPP32 and Mch2 are the major active caspases present in apoptotic cells

EMBO Journal

Volumn 16, Issue 9, 1997, Pages 2271-2281

  Faleiro, Lavina ^a,b   Kobayashi, Ryuji ^a   Fearnhead, Howard ^a   Lazebnik, Yuri ^a  

^a Howard Hughes Medical Institute Cold Spring Harbor Laboratory Cold Spring Harbor   (United States)

^b STONY BROOK UNIVERSITY   (United States)

Author keywords

Affinity labels; Apoptosis; Cancer therapy; Caspases (ICE like proteases); Proteases

Indexed keywords

ANTIBODY; CASPASE; CELL ENZYME; ETOPOSIDE; FAS ANTIBODY; PROTEINASE; STAUROSPORINE; UNCLASSIFIED DRUG;

AFFINITY LABELING; APOPTOSIS; ARTICLE; CANCER CELL; CANCER THERAPY; CELL DEATH; CELL LINE; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME PURIFICATION; HUMAN; HUMAN CELL; LEUKEMIA CELL LINE; PRIORITY JOURNAL; PROTEIN PROCESSING;

AFFINITY LABELS; AMINO ACID SEQUENCE; APOPTOSIS; CASPASE 3; CASPASE 6; CASPASES; CYSTEINE ENDOPEPTIDASES; ELECTROPHORESIS, GEL, TWO-DIMENSIONAL; ENZYME ACTIVATION; ENZYME PRECURSORS; HUMANS; JURKAT CELLS; MOLECULAR SEQUENCE DATA; PROTEIN PROCESSING, POST-TRANSLATIONAL;

MAMMALIA;

EID: 0030973417     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/16.9.2271     Document Type: Article

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