Tuning the conformational properties of the prion peptide

Proteins: Structure, Function and Bioinformatics

Volumn 76, Issue 1, 2009, Pages 213-225

  Ho, Chai Chi ^a   Lee, Lily Y L ^a   Huang, Kuo Ting ^b   Lin, Chun Cheng ^b,c   Ku, Mei Yun ^a   Yang, Chien Chih ^d   Chan, Sunney I ^b   Hsu, Ruei Lin ^a   Chen, Rita P Y ^a  

^a INSTITUTE OF BIOLOGICAL CHEMISTRY   (Taiwan)

^b INSTITUTE OF CHEMISTRY   (Taiwan)

^c NATIONAL TSING HUA UNIVERSITY   (Taiwan)

^d NATIONAL TAIWAN UNIVERSITY   (Taiwan)

Author keywords

Amyloid; Amyloidogenesis; Fibrillization; Glycosylation; Misfolding; Phosphorylation; Prion

Indexed keywords

ACETYLGLUCOSAMINIDASE; ALPHA N ACETYLGALACTOSAMINIDASE; AMYLOID; ARGININE; BETA N ACETYLGALACTOSAMINIDASE; GLYCINE; N ACETYL BETA GLUCOSAMINIDASE; PRION PROTEIN; PRION PROTEIN[108-144]; SERINE; THIOFLAVINE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ELECTRON MICROSCOPY; INDUCED MUTATION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN GLYCOSYLATION; PROTEIN PHOSPHORYLATION; PROTEIN STRUCTURE;

AMINO ACID SEQUENCE; AMYLOID; GLUCOSAMINE; GLYCOSYLATION; HUMANS; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDES; PRIONS; PROTEIN CONFORMATION; PROTEIN FOLDING;

CRICETINAE;

EID: 66249133010     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22341     Document Type: Article

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