Mechanism of the antichaperone activity of protein disulfide isomerase: Facilitated assembly of large, insoluble aggregates of denatured lysozyme and PDI

Biochemistry

Volumn 39, Issue 5, 2000, Pages 1180-1188

  Sideraki, Vera ^a   Gilbert, Hiram F ^a  

^a BAYLOR COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; PROTEIN DISULFIDE ISOMERASE;

AMYLOIDOSIS; ARTICLE; ENZYME ACTIVITY; ENZYME DENATURATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN FOLDING;

ANIMALS; DOSE-RESPONSE RELATIONSHIP, DRUG; ENZYME ACTIVATION; MOLECULAR CHAPERONES; MOLECULAR WEIGHT; MURAMIDASE; OXIDATION-REDUCTION; PROTEIN DENATURATION; PROTEIN DISULFIDE-ISOMERASE; PROTEIN FOLDING; RATS; SOLUBILITY; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY; TIME FACTORS; ULTRACENTRIFUGATION;

EID: 0034620510     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi992246q     Document Type: Article

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