Zn(II) ions co-secreted with insulin suppress inherent amyloidogenic properties of monomeric insulin

Biochemical Journal

Volumn 430, Issue 3, 2010, Pages 511-518

  Noormägi, Andra ^a   Gavrilova, Julia ^a   Smirnova, Julia ^a   Tõugu, Vello ^a   Palumaa, Peep ^a  

^a TALLINN UNIVERSITY OF TECHNOLOGY   (Estonia)

Author keywords

Fibrillation; Fluorescence spectroscopy; Insulin; Temperature dependence; Thioflavin T (ThT); Zinc

Indexed keywords

ANTIGENS; FLUORESCENCE; FLUORESCENCE SPECTROSCOPY; INSULIN; IONS; PEPTIDES; PHOSPHATASES; PHYSIOLOGY; TEMPERATURE DISTRIBUTION; ZINC; ZINC COMPOUNDS;

AMYLOID FIBRIL; AMYLOIDOGENIC PEPTIDES; AUTOANTIBODIES; CELL DAMAGE; COMPLEX FORMATIONS; EFFECT OF CO; FIBRILLATION; HEXAMERS; HISTIDINE RESIDUES; IN-VITRO; INHIBITORY EFFECT; OSMOTIC STABILITY; PEPTIDE HORMONES; PH VALUE; PHYSIOLOGICAL PH; SECRETORY GRANULES; TEMPERATURE DEPENDENCE; THIOFLAVIN T; TYPE 1 DIABETES;

PH EFFECTS;

AMYLIN; C PEPTIDE; HISTIDINE; INSULIN; MONOMERIC INSULIN; UNCLASSIFIED DRUG; ZINC ION; AMYLOID; ION; ORGANOMETALLIC COMPOUND; PROTEIN BINDING; ZINC;

ARTICLE; CIRCULATION; COMPLEX FORMATION; IC 50; IN VITRO STUDY; INSULIN RELEASE; PH; PRIORITY JOURNAL; PROTEIN FOLDING; SIGNAL TRANSDUCTION; TRANSMISSION ELECTRON MICROSCOPY; ALGORITHM; CHEMISTRY; ELECTROSPRAY MASS SPECTROMETRY; KINETICS; METABOLISM; PROTEIN MULTIMERIZATION; TEMPERATURE; ULTRASTRUCTURE;

ALGORITHMS; AMYLOID; HYDROGEN-ION CONCENTRATION; INSULIN; IONS; KINETICS; MICROSCOPY, ELECTRON, TRANSMISSION; ORGANOMETALLIC COMPOUNDS; PROTEIN BINDING; PROTEIN MULTIMERIZATION; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; TEMPERATURE; ZINC;

EID: 77956654475     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20100627     Document Type: Article

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