http://www.cnr.it/ontology/cnr/individuo/prodotto/ID302323
Structural determinants in prion protein folding and stability (Articolo in rivista)
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- Label
- Structural determinants in prion protein folding and stability (Articolo in rivista) (literal)
- Anno
- 2014-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1016/j.jmb.2014.09.017 (literal)
- Alternative label
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Benetti F.; Biarnes X.; Attanasio F.; Giachin G.; Rizzarelli E.; Legname G. (literal)
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- http://www.scopus.com/inward/record.url?eid=2-s2.0-84908192029&partnerID=q2rCbXpz (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
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- Note
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- Department of Neuroscience, Scuola Internazionale Superiore di Studi Avanzati, Via Bonomea 265, Trieste, I-34136, Italy; Italian Institute of Technology, Scuola Internazionale Superiore di Studi Avanzati Unit, Via Bonomea 265, Trieste, I-34136, Italy; Department of Physics, Scuola Internazionale Superiore di Studi Avanzati, Trieste, I-34136, Italy; National Research Council, Institute of Biostructures and Bioimaging, Viale Andrea Doria 6, Catania, I-95125, Italy; Elettra - Sincrotrone Trieste S.C.p.A., AREA Science Park, Basovizza Trieste, I-34149, Italy; European Center for the Sustainable Impact of Nanotechnology, Veneto Nanotech S.C.p.A., Rovigo, I-45100, Italy; Laboratory of Biochemistry, Institut Químic de Sarrià, Universitat Ramon Llull, Via Augusta 390, Barcelona, 08017, Spain (literal)
- Titolo
- Structural determinants in prion protein folding and stability (literal)
- Abstract
- Prions are responsible for a heterogeneous group of fatal neurodegenerative diseases, involving post-translational
modifications of the cellular prion protein. Epidemiological studies on Creutzfeldt-Jakob disease, a
prototype prion disorder, show a majority of cases being sporadic, while the remaining occurrences are either
genetic or iatrogenic. The molecular mechanisms by which PrPC is converted into its pathological isoform have
not yet been established. While point mutations and seeds trigger the protein to cross the energy barriers, thus
causing genetic and infectious transmissible spongiform encephalopathies, respectively, the mechanism
responsible for sporadic forms remains unclear. Since prion diseases are protein-misfolding disorders, we
investigated prion protein folding and stability as functions of different milieus. Using spectroscopic techniques
and atomistic simulations, we dissected the contribution of major structural determinants, also defining the
energy landscape of prion protein. In particular, we elucidated (i) the essential role of the octapeptide region in
prion protein folding and stability, (ii) the presence of a very enthalpically stable intermediate in prion-susceptible
species, and (iii) the role of the disulfide bridge in prion protein folding. (literal)
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