D25V apolipoprotein C-III variant causes dominant hereditary systemic amyloidosis and confers cardiovascular protective lipoprotein profile

Autor: Valleix, S., Guglielmo Verona, Jourde-Chiche, N., Nédelec, B., Mangione, P. P., Bridoux, F., Mangé, A., Dogan, A., Goujon, J. -M, Lhomme, M., Dauteuille, C., Chabert, M., Porcari, R., Waudby, C. A., Relini, A., Talmud, P. J., Kovrov, O., Olivecrona, G., Stoppini, M., Christodoulou, J., Hawkins, P. N., Grateau, G., Delpech, M., Kontush, A., Gillmore, J. D., Kalopissis, A. D., Bellotti, V.

Publikováno v: Nature Communications
Nature Communications, 2016, pp.10353. ⟨10.1038/ncomms10353⟩
Scopus-Elsevier
Nature Communications, Nature Publishing Group, 2016, pp.10353
Nature Communications, Vol 7, Iss 1, Pp 1-14 (2016)
Nature Communications, Nature Publishing Group, 2016, pp.10353. ⟨10.1038/ncomms10353⟩

Apolipoprotein C-III deficiency provides cardiovascular protection, but apolipoprotein C-III is not known to be associated with human amyloidosis. Here we report a form of amyloidosis characterized by renal insufficiency caused by a new apolipoprotei

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::194cade83039b6591442874b6285d900
https://amu.hal.science/hal-01467259/document

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

Fibrillogenesis of ApoA-1 1-93: Identification of an intermediate with a collapsed and partially folded conformation

Autor: Raimondi S., Mangione P., Obici L., Di Gaetano S., Guglielmi F., Pagnozzi D., Giorgetti S., Orru S., Stoppini M., Merlini G., Bellotti V., ARCIELLO, ANGELA, MONTI, MARIA, PUCCI, PIETRO, PICCOLI, RENATA

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______3730::15559ff3a4f3a77752c1b1a99a36fa99
http://hdl.handle.net/11588/356027

Structure, folding dynamics, and amyloidogenesis of D76N β2-microglobulin: roles of shear flow, hydrophobic surfaces, and α-crystallin

Autor: Mangione, P. P., Esposito, Gennaro, Relini, A., Raimondi, S., Porcari, R., Giorgetti, S., Corazza, Alessandra, Fogolari, Federico, Penco, A., Goto, Y., Lee, Y. H., Yagi, H., Cecconi, C., Naqvi, M. M., Gillmore, J. D., Hawkins, P. N., Chiti, F., Rolandi, R., Taylor, G. W., Pepys, M. B., Stoppini, M., Bellotti, V.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______3659::7c2121fd493b0b0c2b2feb75affa359c
http://hdl.handle.net/11390/902141

Reduction of conformational mobility and aggregation in W60G β2-microglobulin: assessment by 15N NMR relaxation

Autor: GUMRAL GOKKAYA, Devrim, Fogolari, Federico, Corazza, Alessandra, Viglino, Paolo, Giorgetti, S., Stoppini, M., Bellotti, V., Esposito, Gennaro

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______3659::8b386e64f3013f9a4a6c9bc0a0796244
http://hdl.handle.net/11390/902143