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The structure of N184K amyloidogenic variant of gelsolin highlights the role of the H-bond network for protein stability and aggregation properties
Matteo de Rosa, Alberto Barbiroli, Francesco Bonì +8
Mutations in the gelsolin protein are responsible for a rare conformational disease known as AGel amyloidosis. Four of these mutations are hosted by the second domain of the protei…
High-resolution crystal structure of gelsolin domain 2 in complex with the physiological calcium ion
Michela Bollati, Emanuele Scalone, Francesco Bonì +4
The second domain of gelsolin (G2) hosts mutations responsible for a hereditary form of amyloidosis. The active form of gelsolin is Ca2+-bound; it is also a dynamic protein, hence…
Nanobody interaction unveils structure, dynamics and proteotoxicity of the Finnish-type amyloidogenic gelsolin variant
Toni Giorgino, Davide Mattioni, Amal Hassan +8
AGel amyloidosis, formerly known as familial amyloidosis of the Finnish-type, is caused by pathological aggregation of proteolytic fragments of plasma gelsolin. So far, four mutati…
Exploring the Role of Interdisciplinarity in Physics: Success, Talent and Luck
Alessandro Pluchino, Giulio Burgio, Andrea Rapisarda +4
Although interdisciplinarity is often touted as a necessity for modern research, the evidence on the relative impact of sectorial versus to interdisciplinary science is qualitative…