Repeat domains of melanosome matrix protein Pmel17 orthologs form amyloid fibrils at the acidic melanosomal pH

Journal of Biological Chemistry

Volumn 286, Issue 10, 2011, Pages 8385-8393

  McGlinchey, Ryan P ^a   Shewmaker, Frank ^a   Hu, Kan Nian ^a   McPhie, Peter ^a   Tycko, Robert ^a   Wickner, Reed B ^a  

^a NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACIDIC PH; AMYLOID FIBRIL; AMYLOID FORMATION; FILAMENT FORMATION; IN-VITRO; IN-VIVO; MATRIX PROTEINS; MELANIN SYNTHESIS; ORTHOLOGS; PER UNIT LENGTH; PROTEASE DIGESTION; SEQUENCE CONSERVATION; SOLID STATE NMR; SPLICE VARIANTS; ZEBRAFISH;

NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; SOLID STATE PHYSICS;

GLYCOPROTEINS;

AMYLOID; AMYLOID BETA PROTEIN; MEMBRANE PROTEIN; PROTEIN PMEL17; UNCLASSIFIED DRUG;

ACIDITY; AMINO ACID SEQUENCE; ARTICLE; BETA SHEET; MELANOSOME; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN SYNTHESIS; REPEAT DOMAIN; SEQUENCE HOMOLOGY;

AMYLOID; ANIMALS; GP100 MELANOMA ANTIGEN; HUMANS; HYDROGEN-ION CONCENTRATION; MICE; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID; ZEBRAFISH;

DANIO RERIO; VERTEBRATA;

EID: 79953136045     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.197152     Document Type: Article

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