The effect of (-)-epigallo-catechin-(3)-gallate on amyloidogenic proteins suggests a common mechanism

Advances in Experimental Medicine and Biology

Volumn 863, Issue , 2015, Pages 139-161

  Andrich, Kathrin ^a,b   Bieschke, Jan ^a  

^a WASHINGTON UNIVERSITY IN ST LOUIS   (United States)

^b MAX DELBRÜCK CENTER FOR MOLECULAR MEDICINE   (Germany)

Author keywords

Aggregation; Amyloid polypeptides; Epigallocathechin 3 gallate (EGCG); Fibrils

Indexed keywords

AMYLOID; AMYLOID PROTEIN; EPIGALLOCATECHIN GALLATE; CATECHIN; PROTEIN AGGREGATE;

AMYLOIDOSIS; ANTIGEN BINDING; ARTICLE; BETA SHEET; CONFORMATIONAL TRANSITION; DRUG EFFECT; DRUG MECHANISM; DRUG PROTEIN BINDING; DRUG STRUCTURE; HUMAN; MOLECULAR INTERACTION; MOLECULAR PROBE; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN STABILITY; ANALOGS AND DERIVATIVES; ANIMAL; CHEMISTRY; METABOLISM; PROTEIN MULTIMERIZATION;

AMYLOIDOGENIC PROTEINS; ANIMALS; CATECHIN; HUMANS; PROTEIN AGGREGATES; PROTEIN MULTIMERIZATION;

EID: 84934992570     PISSN: 00652598     EISSN: 22148019     Source Type: Book Series    
DOI: 10.1007/978-3-319-18365-7_7     Document Type: Article

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