CINECA IRIS Institutional Research Information System
IRIS è la soluzione IT che facilita la raccolta e la gestione dei dati relativi alle attività e ai prodotti della ricerca. Fornisce a ricercatori, amministratori e valutatori gli strumenti per monitorare i risultati della ricerca, aumentarne la visibilità e allocare in modo efficace le risorse disponibili.
EnglishMost proteins fold into their native structure through well defined pathways which involve a limited number of transient intermediates. Intermediates play a relevant role in the folding process; many diseases of genetic nature are in fact coupled with protein misfolding due to formation of stable, inactive intermediate species of the protein. This review deals with a number of diseases associated with protein misfolding and briefly describes the mechanism(s) responsible, at molecular level, for such pathologies. It is also considered the (native ⇆ molten globule) transition, recently observed for some proteins, in which a native protein converts into a stable compact intermediate state able to carry out distinct physiological functions inside the cell. A non-native compact form of cyt c, for example, appears to have a role in the programmed cell death (apoptosis) after that the protein is released from the mitochondrion and non-native forms of the same protein appear involved in some of the disorders attributed to amyloid formation. © 2008 Bentham Science Publishers Ltd.
Santucci R., S.F. (2008). Protein folding, unfolding and misfolding: Role played by intermediate states. MINI-REVIEWS IN MEDICINAL CHEMISTRY, 8(1), 57-62.
| Tipologia: | Articolo su rivista |
| Citazione: | Santucci R., S.F. (2008). Protein folding, unfolding and misfolding: Role played by intermediate states. MINI-REVIEWS IN MEDICINAL CHEMISTRY, 8(1), 57-62. |
| IF: | Con Impact Factor ISI |
| Lingua: | English |
| Settore Scientifico Disciplinare: | Settore BIO/10 |
| Revisione (peer review): | Sì, ma tipo non specificato |
| Tipo: | Articolo |
| Rilevanza: | Rilevanza internazionale |
| Digital Object Identifier (DOI): | http://dx.doi.org/10.2174/138955708783331522 |
| Stato di pubblicazione: | Pubblicato |
| Data di pubblicazione: | 2008 |
| Titolo: | Protein folding, unfolding and misfolding: Role played by intermediate states |
| Autori: | |
| Autori: | Santucci R., Sinibaldi F., Fiorucci L. |
| Appare nelle tipologie: | 01 - Articolo su rivista |
File in questo prodotto:
Copyright © 2020