- 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...
Expand abstract - Publication status:
- Published
- 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
- Language:
- English
- Keywords:
- Copyright date:
- 2005
Journal article
Rapid formation of amyloid from alpha-monomeric recombinant human PrP in vitro.
Actions
Authors
Bibliographic Details
Item Description
Terms of use
Metrics
Altmetrics
Dimensions
If you are the owner of this record, you can report an update to it here: Report update to this record