An evolutionarily conserved tripartite tryptophan motif stabilizes the prodomains of cathepsin L-like cysteine proteases

European Journal of Biochemistry

Volumn 267, Issue 10, 2000, Pages 2965-2972

  Kreusch, Stefan ^a   Fehn, Mark ^a   Maubach, Gunter ^a   Nissler, Karl ^a   Rommerskirch, Winfried ^a   Schilling, Klaus ^a   Weber, Ekkehard ^b   Wenz, Ingrid ^a   Wiederanders, Bernd ^a  

^a FRIEDRICH SCHILLER UNIVERSITY JENA   (Germany)

^b MARTIN LUTHER UNIVERSITY HALLE WITTENBERG   (Germany)

Author keywords

ERFNIN motif; Procathepsin S; Propeptide; Protein folding; Tryptophan stack

Indexed keywords

CATHEPSIN S; COMPLEMENTARY DNA; CYSTEINE PROTEINASE; ENZYME PRECURSOR; TRYPTOPHAN;

ARTICLE; CULTURE MEDIUM; DELETION MUTANT; ENDOPLASMIC RETICULUM; ENZYME ACTIVITY; HUMAN; HUMAN CELL; KIDNEY CELL; MASS SPECTROMETRY; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN FOLDING;

EID: 0034117738     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2000.01312.x     Document Type: Article

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