Low levels of asparagine deamidation can have a dramatic effect on aggregation of amyloidogenic peptides: Implications for the study of amyloid formation

Protein Science

Volumn 11, Issue 2, 2002, Pages 342-349

  Nilsson, Melanie R ^a   Driscoll, Miles ^a   Raleigh, Daniel P ^a  

^a STONY BROOK UNIVERSITY   (United States)

Author keywords

Amylin; Amyloid; Chemical modification; Deamidation; Diabetes mellitus; IAPP; Islet amyloid polypeptide; Protein aggregation

Indexed keywords

AMYLIN; AMYLOID; AMYLOIDOGENIC PEPTIDE; PEPTIDE; POLYPEPTIDE; UNCLASSIFIED DRUG;

ARTICLE; DEAMINATION; DIABETES MELLITUS; DIABETOGENESIS; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; PEPTIDE ANALYSIS; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN MODIFICATION; PROTEIN PURIFICATION; REACTION TIME;

AMIDES; AMYLOID; ASPARAGINE; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CONGO RED; HUMANS; PEPTIDE FRAGMENTS; PROTEIN BINDING; PROTEIN CONFORMATION; SOLUTIONS; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; SPECTROSCOPY, FOURIER TRANSFORM INFRARED;

EID: 0036145439     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.48702     Document Type: Article

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