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Conformational dynamics in crystals reveal the molecular bases for D76N beta-2 microglobulin aggregation propensity

Autor: Le Marchand, Tanguy, de Rosa, Matteo, Salvi, Nicola, Sala, Benedetta Maria, Andreas, Loren B., Barbet-Massin, Emeline, Sormanni, Pietro, Barbiroli, Alberto, Porcari, Riccardo, Sousa Mota, Cristiano, de Sanctis, Daniele, Bolognesi, Martino, Emsley, Lyndon, Bellotti, Vittorio, Blackledge, Martin, Camilloni, Carlo, Pintacuda, Guido, Ricagno, Stefano

Publikováno v: Nature Communications
Nature Communications, Vol 9, Iss 1, Pp 1-11 (2018)
Nature Communications, Nature Publishing Group, 2018, 9, pp.1658-1-1658-11. ⟨10.1038/s41467-018-04078-y⟩
Nature communications 9 (2018). doi:10.1038/s41467-018-04078-y
info:cnr-pdr/source/autori:Le Marchand T.; De Rosa M.; Salvi N.; Sala B.M.; Andreas L.B.; Barbet-Massin E.; Sormanni P.; Barbiroli A.; Porcari R.; Sousa Mota C.; De Sanctis D.; Bolognesi M.; Emsley L.; Bellotti V.; Blackledge M.; Camilloni C.; Pintacuda G.; Ricagno S./titolo:Conformational dynamics in crystals reveal the molecular bases for D76N beta-2 microglobulin aggregation propensity/doi:10.1038%2Fs41467-018-04078-y/rivista:Nature communications/anno:2018/pagina_da:/pagina_a:/intervallo_pagine:/volume:9
'Nature Communications ', vol: 9, pages: 1658-1-1658-11 (2018)
Nature Communications, 2018, 9, pp.1658-1-1658-11. ⟨10.1038/s41467-018-04078-y⟩

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

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::e53b45c1fb7223fc33f25c6a9fc4c52b

Structure, Folding Dynamics, and Amyloidogenesis of D76N β2-Microglobulin : ROLES OF SHEAR FLOW, HYDROPHOBIC SURFACES, AND α-CRYSTALLIN

Autor: Mangione, P. Patrizia, Esposito, Gennaro, Relini, Annalisa, Raimondi, Sara, Porcari, Riccardo, Giorgetti, Sofia, Corazza, Alessandra, Fogolari, Federico, Penco, Amanda, Goto, Yuji, Lee, Young-Ho, Yagi, Hisashi, Cecconi, Ciro, Naqvi, Mohsin M., Gillmore, Julian D., Hawkins, Philip N., Chiti, Fabrizio, Rolandi, Ranieri, Taylor, Graham W., Pepys, Mark B., Stoppini, Monica, Bellotti, Vittorio

Publikováno v: The Journal of Biological Chemistry
The Journal of biological chemistry
288 (2013): 30917–30930. doi:10.1074/jbc.M113.498857
info:cnr-pdr/source/autori:Mangione, P. Patrizia; Esposito, Gennaro; Relini, Annalisa; Raimondi, Sara; Porcari, Riccardo; Giorgetti, Sofia; Corazza, Alessandra; Fogolari, Federico; Penco, Amanda; Goto, Yuji; Lee, Young-Ho; Yagi, Hisashi; Cecconi, Ciro; Naqvi, Mohsin M.; Gillmore, Julian D.; Hawkins, Philip N.; Chiti, Fabrizio; Rolandi, Ranieri; Taylor, Graham W.; Pepys, Mark B.; Stoppini, Monica; Bellotti, Vittorio/titolo:Structure, Folding Dynamics, and Amyloidogenesis of D76N beta(2)-Microglobulin ROLES OF SHEAR FLOW, HYDROPHOBIC SURFACES, AND alpha-CRYSTALLIN/doi:10.1074%2Fjbc.M113.498857/rivista:The Journal of biological chemistry (Print)/anno:2013/pagina_da:30917/pagina_a:30930/intervallo_pagine:30917–30930/volume:288

Background: We recently discovered the first natural human β2-microglobulin variant, D76N, as an amyloidogenic protein. Results: Fluid flow on hydrophobic surfaces triggers its amyloid fibrillogenesis. The α-crystallin chaperone inhibits variant-me

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::a0c4a87444253fef50ec52d13e6266d7
https://hdl.handle.net/11094/71279

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