Disulfide bond formation significantly accelerates the assembly of Ure2p fibrils because of the proximity of a potential amyloid stretch

Journal of Biological Chemistry

Volumn 284, Issue 17, 2009, Pages 11134-11141

  Fei, Li ^a,b   Perrett, Sarah ^a  

^a INSTITUTE OF BIOPHYSICS   (China)

^b UNIVERSITY OF CHINESE ACADEMY OF SCIENCES   (China)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID-LIKE FIBRIL; ASSEMBLY KINETICS; ASSEMBLY PROCESS; CHARGED RESIDUES; DISULFIDE BOND FORMATION; FIBRIL FORMATION; FORMING REGION; HYDROPHOBIC RESIDUES; IN-VITRO; IN-VIVO; N-TERMINAL; NATIVE STATE; OXIDIZING CONDITIONS; PEPTIDE FIBRILS; SPECTROSCOPIC METHOD; STRUCTURAL CHANGE; WILD TYPES; YEAST SACCHAROMYCES CEREVISIAE;

AMINES; PEPTIDES;

GLYCOPROTEINS;

AMYLOID; CYSTEINE; MUTANT PROTEIN; OCTAPEPTIDE; PRION PROTEIN; PROTEIN URE2; UNCLASSIFIED DRUG; ARGININE; DISULFIDE; OXIDIZING AGENT; PEPTIDE; SACCHAROMYCES CEREVISIAE PROTEIN; URE2 PROTEIN, S CEREVISIAE;

AMINO ACID SUBSTITUTION; ARTICLE; BETA SHEET; CONTROLLED STUDY; DELETION MUTANT; DISULFIDE BOND; FIBER; HYDROPHOBICITY; NONHUMAN; OXIDATION; PHENOTYPE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ASSEMBLY; PROTEIN POLYMERIZATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; CHEMISTRY; CIRCULAR DICHROISM; ELECTRON MICROSCOPY; GENE DELETION; KINETICS; METABOLISM; MUTATION; PRION; PROTEIN TERTIARY STRUCTURE; SACCHAROMYCES CEREVISIAE;

SACCHAROMYCES CEREVISIAE;

AMYLOID; ARGININE; CIRCULAR DICHROISM; CYSTEINE; DISULFIDES; GENE DELETION; KINETICS; MICROSCOPY, ELECTRON; MUTATION; OXIDANTS; PEPTIDES; PRIONS; PROTEIN STRUCTURE, TERTIARY; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS;

EID: 66449136918     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M809673200     Document Type: Article

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