The function of propeptide domains of cysteine proteinases

Advances in Experimental Medicine and Biology

Volumn 477, Issue , 2000, Pages 261-270

  Wiederanders, B ^a  

^a JENA UNIVERSITY HOSPITAL   (Germany)

Author keywords

ERFNIN motif; Inhibitor function; Maturation; Mutagenesis; Procathepsin S; Targeting

Indexed keywords

CATHEPSIN L; CATHEPSIN S INHIBITOR; CYSTEINE PROTEINASE; ENZYME PRECURSOR; PROTEIN PRECURSOR; RECOMBINANT CATHEPSIN S; RECOMBINANT PROTEIN; TRP 28; TRP 31; TRP 52; UNCLASSIFIED DRUG;

CONFERENCE PAPER; DENATURATION; ENZYME ANALYSIS; ENZYME INHIBITOR INTERACTION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; SITE DIRECTED MUTAGENESIS;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BIOLOGICAL TRANSPORT; CATHEPSINS; CELLS, CULTURED; CYSTEINE ENDOPEPTIDASES; CYSTEINE PROTEINASE INHIBITORS; ENZYME PRECURSORS; HUMANS; KIDNEY; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP; TRANSFECTION;

EID: 0034471704     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: None     Document Type: Conference Paper

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