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Are prions misfolded molecular chaperones?
- Source :
- FEBS Letters. (3):155-157
- Publisher :
- Published by Elsevier B.V.
-
Abstract
- A theory has been developed that could explain prion infection. Prions could be molecular chaperones that are required for their own assembly. The theory has been deduced from an analysis of protein folding and consequences explored by computer simulations. Thermo-kinetic analysis of protein folding shows that a misfolded chaperone gives rise to new misfolded chaperones. Consequently such a protein could behave as a new kind of informative molecule and replicate misfolding according to a process similar to infection. A quantitative model has been derived from this hypothesis that displays the characteristics of prion infections. This hypothesis satisfactorily explains the three manifestations infection, familial and sporadic — that are the characteristics features of all prion diseases.
- Subjects :
- Prions
Protein Conformation
Biophysics
Computational biology
Biology
Biochemistry
Models, Biological
Creutzfeldt-Jakob Syndrome
Prion infection
Structural Biology
Genetics
Animals
Humans
Computer Simulation
Protein folding
Molecular Biology
Structure modification
Thermo-kinetics
A protein
Cell Biology
Virology
Quantitative model
Chaperone (protein)
biology.protein
Prion
Thermodynamics
Scrapie
Subjects
Details
- Language :
- English
- ISSN :
- 00145793
- Issue :
- 3
- Database :
- OpenAIRE
- Journal :
- FEBS Letters
- Accession number :
- edsair.doi.dedup.....4fbb8a3219036baba722336d222e3b41
- Full Text :
- https://doi.org/10.1016/0014-5793(91)80657-O