26 citations · 46 across the 4 of their papers we have counts for
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A novel hotspot of gelsolin instability and aggregation propensity triggers a new mechanism of amyloidosis
Michela Bollati, Luisa Diomede, Toni Giorgino +14
The multidomain protein gelsolin (GSN) is composed of six homologous modules, sequentially named G1 to G6. Single point substitutions in this protein are responsible for AGel amylo…
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…