Fluphenazine·HCl and Epigallocatechin Gallate Modulate the Rate of Formation and Structural Properties of Apolipoprotein C-II Amyloid Fibrils

Biochemistry

Volumn 54, Issue 24, 2015, Pages 3831-3838

  Zlatic, Courtney O ^a   Mao, Yu ^a   Ryan, Timothy M ^b   Mok, Yee Foong ^a   Roberts, Blaine R ^b   Howlett, Geoffrey J ^a   Griffin, Michael D W ^a  

^a UNIVERSITY OF MELBOURNE   (Australia)

^b UNIVERSITY OF MELBOURNE   (Australia)

Author keywords

[No Author keywords available]

Indexed keywords

AGGREGATES; LIPOPROTEINS; MOLECULES; SIZE DISTRIBUTION;

AMYLOID FIBRIL FORMATION; AMYLOID FORMATION; ANTIPSYCHOTIC DRUG; CONCENTRATION-DEPENDENT; EPIGALLOCATECHIN GALLATE; POTENT ACTIVATORS; PROTEIN MISFOLDING; SMALL-MOLECULE DRUGS;

GLYCOPROTEINS;

AMYLOID; APOLIPOPROTEIN C2; DIHYDREXIDINE; EPIGALLOCATECHIN GALLATE; ESOMEPRAZOLE; FENOLDOPAM MESILATE; FLUPHENAZINE; PANTOPRAZOLE; RIFAMPICIN; CATECHIN; MOLECULAR LIBRARY; NEUROLEPTIC AGENT; NEUROPROTECTIVE AGENT; NEW DRUG; PROTEIN AGGREGATE; RECOMBINANT PROTEIN; THIAZOLE DERIVATIVE; THIOFLAVINE;

ARTICLE; CONTROLLED STUDY; DRUG EFFECT; DRUG POTENCY; DRUG PROTEIN BINDING; DRUG SCREENING; FIBER; HUMAN; KINETICS; MOLECULE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ASSEMBLY; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PURIFICATION; PROTEIN STRUCTURE; PROTEIN UNFOLDING; ANALOGS AND DERIVATIVES; ANTAGONISTS AND INHIBITORS; BINDING COMPETITION; CHEMICALLY INDUCED; CHEMISTRY; DRUG DEVELOPMENT; DRUG EFFECTS; GENETICS; METABOLISM; MOLECULAR LIBRARY; PARTICLE SIZE; PATHOLOGY; PROTEIN CONFORMATION; PROTEOSTASIS DEFICIENCIES; TRANSMISSION ELECTRON MICROSCOPY; ULTRACENTRIFUGATION; ULTRASTRUCTURE;

AMYLOID; ANTIPSYCHOTIC AGENTS; APOLIPOPROTEIN C-II; BINDING, COMPETITIVE; CATECHIN; DRUG DISCOVERY; DRUGS, INVESTIGATIONAL; FLUPHENAZINE; HUMANS; KINETICS; MICROSCOPY, ELECTRON, TRANSMISSION; NEUROPROTECTIVE AGENTS; PARTICLE SIZE; PROTEIN AGGREGATES; PROTEIN CONFORMATION; PROTEOSTASIS DEFICIENCIES; RECOMBINANT PROTEINS; SMALL MOLECULE LIBRARIES; THIAZOLES; ULTRACENTRIFUGATION;

EID: 84935033737     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/acs.biochem.5b00399     Document Type: Article

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