Severe bleeding disorders such as Haemophilia B are mainly caused by missense mutations that may affect protein folding, thus leading to the production of structurally-altered proteins associated with low or very low circulating levels. The research activity was aimed at characterizing the mechanism underlying the defective intracellular biosynthesis (misfolding), premature degradation and/or stress of the endoplasmic reticulum in cellular models of sever Haemophilia B and to evaluate the effects of small molecules or drugs acting as chemical/pharmacological chaperones in restoring the molecular defect. Reference: Pignani S, Todaro A, Ferrarese M, Marchi S, Lombardi S, Balestra D, Pinton P, Bernardi F, Pinotti M, Branchini A. The chaperone-like sodium phenylbutyrate improves factor IX intracellular trafficking and activity impaired by the frequent p.R294Q mutation. J Thromb Haemost. 2018 Oct;16(10):2035-2043.
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Autori: | |
Autori: | Branchini, Alessio |
Titolo: | Improved intracellular processing of protein variants as a personalized therapeutic approach for Haemophilia |
Data di pubblicazione: | 2015 |
Data finale: | 2017 |
Tipo: | Coordinatore |
Finanziamenti: | Nessun Finanziamento |
???metadata.dc.type.research???: | Internazionale |
Appare nelle tipologie: | 08.1 Coordinamento Prog.Ricerca Naz. ed Internaz. |