Domain a of protein disulfide isomerase plays key role in inhibiting α-synuclein fibril formation

Cell Stress and Chaperones

Volumn 15, Issue 4, 2010, Pages 415-421

  Cheng, Han ^a,b   Wang, Lei ^a   Wang, Chih Chen ^a  

^a INSTITUTE OF BIOPHYSICS   (China)

^b UNIVERSITY OF CHINESE ACADEMY OF SCIENCES   (China)

Author keywords

Synuclein; Fibril; Isothermal titration calorimetry; Protein disulfide isomerase

Indexed keywords

ALPHA SYNUCLEIN; DISULFIDE ISOMERASE; HEAT SHOCK PROTEIN; UNCLASSIFIED DRUG; PROTEIN DISULFIDE ISOMERASE; RECOMBINANT PROTEIN; THIAZOLE DERIVATIVE; THIOFLAVINE;

ARTICLE; ENDOPLASMIC RETICULUM; GEL FILTRATION; IN VITRO STUDY; ISOTHERMAL TITRATION CALORIMETRY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN LOCALIZATION; PROTEIN PURIFICATION; CALORIMETRY; CHEMISTRY; GENETICS; HUMAN; METABOLISM; PROTEIN TERTIARY STRUCTURE; ULTRASTRUCTURE;

ALPHA-SYNUCLEIN; CALORIMETRY; HUMANS; PROTEIN DISULFIDE-ISOMERASES; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; THIAZOLES;

EID: 77955653538     PISSN: 13558145     EISSN: 14661268     Source Type: Journal    
DOI: 10.1007/s12192-009-0157-2     Document Type: Article

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