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Stefano Ricagno
University of Milan
115Publications
20H-index
1,348Citations
Publications 115
Newest
#1Adnane AchourH-Index: 23
Last.R. SunH-Index: 2
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#1Adnane Achour (Karolinska University Hospital)H-Index: 23
#2Luca Broggini (University of Milan)
Last.Stefano Ricagno (University of Milan)H-Index: 20
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#1Martina MaritanH-Index: 3
#2Stefano RicagnoH-Index: 20
Last.L. ObertiH-Index: 1
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#1L. Oberti (University of Milan)H-Index: 1
#2Martina Maritan (University of Milan)H-Index: 3
Last.Stefano Ricagno (University of Milan)H-Index: 20
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#1Martina Maritan (University of Milan)H-Index: 3
#2Arianna Ambrosetti (University of Milan)
Last.Stefano Ricagno (University of Milan)H-Index: 20
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Beta-2 microglobulin (β2m) is a protein responsible for a pathologic condition, known as dialysis-related amyloidosis (DRA), caused by its aggregation and subsequent amyloid formation. A naturally occurring mutation of β2m, D76N, presents a higher amyloidogenic propensity compared to the wild type counterpart. Since the three-dimensional structure of the protein is essentially unaffected by the mutation, the increased aggregation propensity of D76N has been generally ascribed to its lower thermo...
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#1Tanguy Le Marchand (University of Lyon)H-Index: 7
#2Matteo de Rosa (University of Milan)H-Index: 10
Last.Stefano Ricagno (University of Milan)H-Index: 20
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Spontaneous aggregation of folded and soluble native proteins in vivo is still a poorly understood process. A prototypic example is the D76N mutant of beta-2 microglobulin (β2m) that displays an aggressive aggregation propensity. Here we investigate the dynamics of β2m by X-ray crystallography, solid-state NMR, and molecular dynamics simulations to unveil the effects of the D76N mutation. Taken together, our data highlight the presence of minor disordered substates in crystalline β2m. The destab...
10 CitationsSource
#1Paolo Swuec (University of Milan)H-Index: 7
#2Francesca Lavatelli (UNIPV: University of Pavia)H-Index: 24
Last.Martino Bolognesi (University of Milan)H-Index: 58
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Systemic light chain (AL) amyloidosis is a life-threatening disease caused by aggregation and deposition of monoclonal immunoglobulin light chains (LC) in target organs. Severity of heart involvement is the most important factor determining prognosis. Here, we report the 4.0 Angstroem resolution cryo-electron microscopy (cryo-EM) map and structural model of amyloid fibrils extracted from the heart of an AL patient affected by severe amyloid cardiomyopathy. The fibrils are composed of one asymmet...
3 CitationsSource
#1L. ObertiH-Index: 1
#2Paola RognoniH-Index: 10
Last.Stefano RicagnoH-Index: 20
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#1L. ObertiH-Index: 1
#2Paola RognoniH-Index: 10
Last.Stefano RicagnoH-Index: 20
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