A molten globule-to-ordered structure transition of Drosophila melanogaster crammer is required for its ability to inhibit cathepsin

Biochemical Journal

Volumn 442, Issue 3, 2012, Pages 563-572

  Tseng, Tien Sheng ^a   Cheng, Chao Sheng ^a   Chen, Dian Jiun ^a   Shih, Min Fang ^a   Liu, Yu Nan ^a   Hsu, Shang Te Danny ^a,b   Lyu, Ping Chiang ^a,c  

^a NATIONAL TSING HUA UNIVERSITY   (Taiwan)

^b INSTITUTE OF BIOLOGICAL CHEMISTRY   (Taiwan)

^c CHINA MEDICAL UNIVERSITY   (Taiwan)

Author keywords

Cathepsin; Crammer; Long term memory (LTM); Molten globule; Propeptide like protease inhibitor

Indexed keywords

CATHEPSIN L; CYSTEINE; DIMER; MONOMER; SERINE;

ACIDITY; ARTICLE; CRAMMER GENE; DISULFIDE BOND; DROSOPHILA MELANOGASTER; GENE; GENE FUNCTION; GENE STRUCTURE; GENETIC VARIABILITY; LYSOSOME; MOLECULAR RECOGNITION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PH; POINT MUTATION; PRIORITY JOURNAL; PROTEIN FOLDING;

ANIMALS; BINDING SITES; CATHEPSINS; DIMERIZATION; DROSOPHILA MELANOGASTER; DROSOPHILA PROTEINS; HYDROGEN-ION CONCENTRATION; PROTEIN CONFORMATION; PROTEIN FOLDING;

DROSOPHILA MELANOGASTER;

EID: 84863241639     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20111360     Document Type: Article

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