Dissociation of glucocerebrosidase dimer in solution by its co-factor, saposin C

Biochemical and Biophysical Research Communications

Volumn 457, Issue 4, 2015, Pages 561-566

  Gruschus, James M ^a   Jiang, Zhiping ^a   Yap, Thai Leong ^a   Hill, Stephanie A ^a   Grishaev, Alexander ^b   Piszczek, Grzegorz ^a   Sidransky, Ellen ^c   Lee, Jennifer C ^a  

^a NATIONAL INSTITUTES OF HEALTH   (United States)

^b NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

^c NATIONAL HUMAN GENOME RESEARCH INSTITUTE   (United States)

Author keywords

AUC; Gaucher disease; NMR; Parkinson disease; synuclein

Indexed keywords

DIMER; GLUCOSYLCERAMIDASE; MONOMER; SAPOSIN C; SPHINGOLIPID ACTIVATOR PROTEIN; TETRAMER; UNCLASSIFIED DRUG; ALPHA SYNUCLEIN;

AREA UNDER THE CURVE; ARTICLE; BINDING SITE; DISSOCIATION; ENZYME BINDING; ENZYME STRUCTURE; ISOTHERMAL TITRATION CALORIMETRY; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN MULTIMERIZATION; PROTEIN PURIFICATION; STOICHIOMETRY; ULTRACENTRIFUGATION; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME ACTIVE SITE; ENZYMOLOGY; GAUCHER DISEASE; HUMAN; METABOLISM; PARKINSON DISEASE; PROTEIN STABILITY;

ALPHA-SYNUCLEIN; CATALYTIC DOMAIN; GAUCHER DISEASE; GLUCOSYLCERAMIDASE; HUMANS; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PARKINSON DISEASE; PROTEIN MULTIMERIZATION; PROTEIN STABILITY; SAPOSINS;

EID: 84922724492     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2015.01.024     Document Type: Article

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