The ability of rodent islet amyloid polypeptide to inhibit amyloid formation by human islet amyloid polypeptide has important implications for the mechanism of amyloid formation and the design of inhibitors

Biochemistry

Volumn 49, Issue 5, 2010, Pages 872-881

  Cao, Ping ^a   Meng, Fanling ^a   Abedini, Andisheh ^b   Raleigh, Daniel P ^a  

^a STONY BROOK UNIVERSITY   (United States)

^b Columbia University ^*  (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID FIBRIL; AMYLOID FORMATION; CIRCULAR DICHROISM; DOSE-DEPENDENT MANNER; HUMAN ISLETS; IN-VITRO; IN-VIVO; INHIBITOR DESIGN; INTERACTION INTERFACE; KINETIC EXPERIMENT; LAG PHASE; N-TERMINALS; POLYPEPTIDE HORMONES; PRIMARY SEQUENCES; THIOFLAVIN; TYPE II; WILD TYPES;

ABILITY TESTING; DICHROISM; MACHINE DESIGN; PEPTIDES; PHASE INTERFACES; TRANSMISSION ELECTRON MICROSCOPY;

GLYCOPROTEINS;

AMYLIN; MUTANT PROTEIN; PROTEIN; RAT AMYLIN; THIOFLAVINE; UNCLASSIFIED DRUG;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; AQUEOUS SOLUTION; ARTICLE; CONCENTRATION RESPONSE; CONTROLLED STUDY; DRUG DESIGN; HUMAN VERSUS ANIMAL COMPARISON; MORPHOLOGY; POINT MUTATION; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; WILD TYPE;

AMINO ACID SEQUENCE; AMYLOID; ANIMALS; ASPARTIC ACID; DRUG DESIGN; HUMANS; MOLECULAR SEQUENCE DATA; PHENYLALANINE; POINT MUTATION; PROTEIN STRUCTURE, SECONDARY; RATS;

RATTUS; RODENTIA;

EID: 75749156581     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi901751b     Document Type: Article

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