Oligomerization of the proteolytic products is an intrinsic property of prion proteins

Biochemical and Biophysical Research Communications

Volumn 323, Issue 4, 2004, Pages 1278-1286

  Georgieva, Dessislava ^a,b   Koker, Mirjam ^c   Redecke, Lars ^a   Perbandt, Markus ^a   Clos, Joachim ^c   Bredehorst, Reinhard ^d   Genov, Nicolay ^b   Betzel, Christian ^a  

^a UNIVERSITY MEDICAL CENTER HAMBURG EPPENDORF   (Germany)

^b INSTITUTE OF ORGANIC CHEMISTRY   (Bulgaria)

^c BERNHARD NOCHT INSTITUTE FOR TROPICAL MEDICINE   (Germany)

^d UNIVERSITY OF HAMBURG   (Germany)

Author keywords

Chemical chaperones; Prion; Prionase; Proteinase K; Subtilisin DY

Indexed keywords

ALCOHOL; BACTERIAL ENZYME; CHAPERONE; DIMETHYL SULFOXIDE; GLYCEROL; PRION PROTEIN; PROTEIN HYDROLYSATE; PROTEINASE; PROTEINASE K; RECOMBINANT PROTEIN; SUBTILISIN;

ARTICLE; BACTERIAL CELL; CHEMICAL MODIFICATION; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME SUBUNIT; HYDROLYSIS; NONHUMAN; OLIGOMERIZATION; PHYSICAL CHEMISTRY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DEGRADATION; SCRAPIE;

ANIMALS; BINDING SITES; CRICETINAE; DIMERIZATION; ENDOPEPTIDASES; HUMANS; HYDROLYSIS; KINETICS; MESOCRICETUS; MODELS, MOLECULAR; PEPTIDE HYDROLASES; PRIONS; PROTEIN BINDING; PROTEIN CONFORMATION; RATS; RECOMBINANT PROTEINS; SPECIES SPECIFICITY;

BACTERIA (MICROORGANISMS); CRICETINAE; MESOCRICETUS AURATUS;

EID: 4644281709     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.08.230     Document Type: Article

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