The heavy-light chain loop of human cathepsin-L modulates its activity and stability

Protein and Peptide Letters

Volumn 15, Issue 1, 2008, Pages 47-53

  Fairhead, Michael ^a   Van Der Walle, Christopher F ^a  

^a UNIVERSITY OF STRATHCLYDE   (United Kingdom)

Author keywords

Cathepsin L; Cysteine protease; Protein engineering; Silicatein

Indexed keywords

CATHEPSIN; CATHEPSIN L; CYSTEINE PROTEINASE; MUTANT PROTEIN; SILICATEIN ALPHA; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ANIMAL; ARTICLE; CHEMISTRY; ENZYME SPECIFICITY; ENZYME STABILITY; ENZYMOLOGY; GENETICS; HUMAN; ISOLATION AND PURIFICATION; METABOLISM; MOLECULAR GENETICS; PANDALIDAE; PH; PROTEIN CONFORMATION; PROTEIN TERTIARY STRUCTURE; SEQUENCE ALIGNMENT;

AMINO ACID SEQUENCE; ANIMALS; CATHEPSINS; CYSTEINE ENDOPEPTIDASES; ENZYME STABILITY; HUMANS; HYDROGEN-ION CONCENTRATION; MOLECULAR SEQUENCE DATA; MUTANT PROTEINS; PANDALIDAE; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT; SUBSTRATE SPECIFICITY;

DECAPODA (CRUSTACEA);

EID: 38849091399     PISSN: 09298665     EISSN: None     Source Type: Journal    
DOI: 10.2174/092986608783330468     Document Type: Article

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