This title appears in the Scientific Report :
2010
Please use the identifier:
http://dx.doi.org/10.1089/rej.2009.0932 in citations.
Amyloid formation: Age-related mechanism in Creutzfeldt-Jakob disease?
Amyloid formation: Age-related mechanism in Creutzfeldt-Jakob disease?
Protein aggregation occurs in many age-related neurodegenerative diseases, where it can lead to deposits of naturally occurring proteins in the brain. In case of Creutzfeldt-Jakob disease (CJD), these deposits consist of prion protein (PrP). CJD has three etiologies: spontaneous, genetic, or caused...
Saved in:
Personal Name(s): | Lüers, L. |
---|---|
Panza, G. / Henke, F. / Aygenim, T. / Weiß, J. / Willbold, D. / Birkmann, E. | |
Contributing Institute: |
Strukturbiochemie; ISB-3 JARA - HPC; JARA-HPC |
Published in: | Rejuvenation research, 13 (2010) |
Imprint: |
Larchmont, NY
Liebert
2010
|
DOI: |
10.1089/rej.2009.0932 |
PubMed ID: |
20017612 |
Document Type: |
Journal Article |
Research Program: |
BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung Funktion und Dysfunktion des Nervensystems |
Series Title: |
Rejuvenation Research
13 |
Subject (ZB): | |
Publikationsportal JuSER |
Protein aggregation occurs in many age-related neurodegenerative diseases, where it can lead to deposits of naturally occurring proteins in the brain. In case of Creutzfeldt-Jakob disease (CJD), these deposits consist of prion protein (PrP). CJD has three etiologies: spontaneous, genetic, or caused by infection. A polymorphism within the PrP gene is associated with susceptibility of infection. The main event in prion diseases is the conversion of PrP from its naturally occurring isoform to its disease-associated isoform. Here, we present the adaption of a previously reported in vitro conversion system based on hamster recombinant PrP to analyze amyloid fibril formation of human recombinant PrP. We further compare the aggregation characteristics of the human PrP according to the polymorphism variants M129 and V129. |