Reduction of conformational mobility and aggregation in W60G beta(2)-microglobulin: assessment by N-15 NMR relaxation

Autor: Gumral, D, Fogolari, F, Corazza, A, Viglino, P, Giorgetti, S, Stoppini, M, Esposito, G

The amyloid pathology associated with long-term haemodialysis is due to the deposition of (2)-microglobulin, the non-polymorphic light chain of class I major histocompatibility complex, that accumulates at bone joints into amyloid fibrils. Several li

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od_____10007::9a8d8349a20116e248b3e659f77a450e
https://hdl.handle.net/20.500.11831/6314

Aggregation properties the controlling roles of Trp60 and Trp95 in beta(2)-microglobulin function, folding and amyloid aggregation properties

Autor: Esposito, G, Ricagno, S, Corazza, A, Rennella, E, Gumral, D, Mimmi, MC, Betto, E, Pucillo, CEM, Fogolari, F, Viglino, P, Raimondi, S, Giorgetti, S, Bolognesi, B, Merlini, G, Stoppini, M, Bolognesi, M, Bellotti, V

Publikováno v: Journal of Molecular Biology 378 (2008): 887–897.
info:cnr-pdr/source/autori:Esposito, G; Ricagno, S; Corazza, A; Rennella, E; Gumral, D; Mimmi, MC; Betto, E; Pucillo, CEM; Fogolari, F; Viglino, P; Raimondi, S; Giorgetti, S; Bolognesi, B; Merlini, G; Stoppini, M; Bolognesi, M; Bellotti, V/titolo:Aggregation properties the controlling roles of Trp60 and Trp95 in beta(2)-microglobulin function, folding and amyloid aggregation properties/doi:/rivista:Journal of Molecular Biology/anno:2008/pagina_da:887/pagina_a:897/intervallo_pagine:887–897/volume:378

"Amyloidosis associated to hemodialysis is caused by persistently high beta(2)-microglobulin (beta(2)m) serum levels. beta(2)m is an intrinsically amyloidogenic protein whose capacity to assemble into amyloid fibrils in vitro and in vivo is concentra

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=cnr_________::033cf54d4c90b20704540aa0f2b8765c
https://publications.cnr.it/doc/3327

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