Effects of randomizing the Sup35NM prion domain sequence on formation of amyloid fibrils in vitro

Biochemical and Biophysical Research Communications

Volumn 353, Issue 1, 2007, Pages 139-146

  Liu, Yingxia ^a,d   Wei, Haiyan ^b,d,e   Wang, Jianwei ^c,d   Qu, Jianguo ^d   Zhao, Weiming ^b   Tao, Hung ^a,b,d  

^a INSTITUTE OF BASIC MEDICAL SCIENCES   (China)

^b SHANDONG UNIVERSITY   (China)

^c INSTITUTE OF PATHOGEN BIOLOGY   (China)

^d CHINESE CENTER FOR DISEASE CONTROL AND PREVENTION   (China)

^e Technical Center of Beijing Entry Exit Inspection   (China)

Author keywords

Fibril formation; Prion domain; Sup35NM; Yeast prion

Indexed keywords

AMYLOID; ASPARAGINE; GLUTAMINE; GLYCINE; PRION PROTEIN; PROTEIN SUP35NM;

AMINO ACID COMPOSITION; AMINO ACID SEQUENCE; ARTICLE; NONHUMAN; POLYMERIZATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DOMAIN; PROTEIN FUNCTION; REACTION ANALYSIS; REACTION TIME; SACCHAROMYCES CEREVISIAE; SEQUENCE ANALYSIS;

AMINO ACID SEQUENCE; AMYLOID; BINDING SITES; DIMERIZATION; FUNGAL PROTEINS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PRIONS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; RANDOM ALLOCATION; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 33845624669     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.11.143     Document Type: Article

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