Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Alessia Andreola"'
Autor:
Giuliana Verdone, Palma Mangione, Vittorio Bellotti, Gennaro Esposito, Fabio Pettirossi, Alessandra Corazza, Monica Stoppini, Sofia Giorgetti, Alessia Andreola, Paolo Viglino
Publikováno v:
Protein Science. 11:487-499
β2-microglobulin (β2-m) is the nonpolymorphic light chain of the class I major histocompatibility complex (MHC-I). It consists of 99 residues with a single disulfide bridge between the two Cys residues of the sequence at positions 25 and 80 and fol
Autor:
Ersilia De Lorenzi, Gabriele Caccialanza, Gabriella Massolini, Sofia Giorgetti, Palma Mangione, Vittorio Bellotti, Fabrizio Chiti, Alessia Andreola, Silvia Grossi
Publikováno v:
ELECTROPHORESIS. 23:918-925
Dialysis-related amyloidosis is a disease in which partial unfolding of beta(2)-microglobulin plays a key pathogenetic role in the formation of the amyloid fibrils. We have recently demonstrated that a partially unfolded conformer of beta(2)-microglo
Autor:
Chiara Galbusera, Alessia Andreola, Palma Mangione, Elena Tabolotti, Gabriele Caccialanza, Vittorio Bellotti, Gabriella Massolini, Ersilia De Lorenzi
Publikováno v:
Electrophoresis. 21:3280-3289
In this work we used affinity capillary electrophoresis (ACE) to investigate the extent of interaction between a pool of drugs and wild-type transthyretin. After qualitative preliminary screening, attention was focused on the most promising molecules
Publikováno v:
Pharmacological research. 50(4)
A process of protein aggregation that causes intracellular or extracellular accumulation of insoluble protein deposits causes many important neurodegenerative diseases associated with the ageing. The recognition that protein aggregation plays a promi
Autor:
Julian Garcia, Alessia Andreola, Sofia Giorgetti, Palma Mangione, Alessandra Corazza, Vittorio Bellotti, Fabrizio Chiti, Paolo Viglino, David R. Booth, Pascal Dumy, Gennaro Esposito, Philip N. Hawkins
Definition of the transition mechanism from the native globular protein into fibrillar polymer was greatly improved by the biochemical and biophysical studies carried out on the two amyloidogenic variants of human lysozyme, I56T and D67H. Here we rep
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::77134fd56656fc57666dcdc91c0cf59b
http://hdl.handle.net/11390/879622
http://hdl.handle.net/11390/879622
Autor:
Enrico Monzani, Monica Stoppini, Jaume Torres, Laura Obici, Sofia Giorgetti, Vittorio Bellotti, Palma Mangione, Alessia Andreola, Giampaolo Merlini, Margaret Sunde
Publikováno v:
The Journal of biological chemistry. 278(4)
The N-terminal portion of apolipoprotein A-I corresponding to the first 93 residues has been identified as the main component of apolipoprotein A-I fibrils in a form of systemic amyloidosis. We have been able to characterize the process of conformati
Autor:
Ersilia, De Lorenzi, Silvia, Grossi, Gabriella, Massolini, Sofia, Giorgetti, Palma, Mangione, Alessia, Andreola, Fabrizio, Chiti, Vittorio, Bellotti, Gabriele, Caccialanza
Publikováno v:
Electrophoresis. 23(6)
Dialysis-related amyloidosis is a disease in which partial unfolding of beta(2)-microglobulin plays a key pathogenetic role in the formation of the amyloid fibrils. We have recently demonstrated that a partially unfolded conformer of beta(2)-microglo
Autor:
Vittorio Bellotti, Lia Asti, Giampaolo Merlini, Alessia Andreola, Sofia Giorgetti, Palma Mangione, Margaret Sunde, Monica Stoppini, Laura Obici, Luca Gianelli, Gennaro Esposito, Paolo Viglino
Publikováno v:
Protein science : a publication of the Protein Society. 10(1)
We recently described a new apolipoprotein A1 variant presenting a Leu174Ser replacement mutation that is associated with a familial form of systemic amyloidosis displaying predominant heart involvement. We have now identified a second unrelated pati
Autor:
Giampaolo Merlini, Vittorio Bellotti, Alessia Andreola, Giovanni Palladini, Laura Obici, Simona Casarini, Vittorio Perfetti
Publikováno v:
Clinical Chemistry and Laboratory Medicine. 39
Protein aggregation occurs in vivo as a result of improper folding or misfolding. Diverse diseases arise from protein misfolding and are now grouped under the term "protein conformational diseases", including most of the neurodegenerative disorders s