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Journal article

Rapid formation of amyloid from alpha-monomeric recombinant human PrP in vitro.

Abstract:

The infectious agent of prion diseases is identified with PrP(Sc), a beta-rich, amyloidogenic and partially protease resistant isoform of the cellular glycoprotein, PrP(C). To understand the process of prion formation in vivo, we and others have studied defined misfolding pathways of recombinant PrP in vitro. The low-level infectivity of the in vitro misfolded murine PrP amyloid has recently been reported. Here we analyze the in vitro kinetics of amyloid formation from recombinant human PrP(9...

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Publication status:
Published

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Publisher copy:
10.1110/ps.041000905

Authors


Journal:
Protein science : a publication of the Protein Society
Volume:
14
Issue:
4
Pages:
942-947
Publication date:
2005-04-05
DOI:
EISSN:
1469-896X
ISSN:
0961-8368
URN:
uuid:28c0baf9-ade2-4979-acd3-49b1f85fc375
Source identifiers:
14326
Local pid:
pubs:14326

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