Most 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 |