benedetta bolognesi
benedetta bolognesi
IBEC, Barcelona
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Citata da
Citata da
ANS binding reveals common features of cytotoxic amyloid species
B Bolognesi, JR Kumita, TP Barros, EK Esbjorner, LM Luheshi, ...
ACS chemical biology 5 (8), 735-740, 2010
The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β1−40 peptide
P Narayan, A Orte, RW Clarke, B Bolognesi, S Hook, KA Ganzinger, ...
Nature structural & molecular biology 19 (1), 79-83, 2012
A concentration-dependent liquid phase separation can cause toxicity upon increased protein expression
B Bolognesi, NL Gotor, R Dhar, D Cirillo, M Baldrighi, GG Tartaglia, ...
Cell reports 16 (1), 222-231, 2016
The mutational landscape of a prion-like domain
B Bolognesi, AJ Faure, M Seuma, JM Schmiedel, GG Tartaglia, B Lehner
Nature communications 10 (1), 4162, 2019
The controlling roles of Trp60 and Trp95 in β2-microglobulin function, folding and amyloid aggregation properties
G Esposito, S Ricagno, A Corazza, E Rennella, D Gmral, MC Mimmi, ...
Journal of molecular biology 378 (4), 887-897, 2008
Detergent-like interaction of Congo red with the amyloid β peptide
C Lendel, B Bolognesi, A Wahlström, CM Dobson, A Graslund
Biochemistry 49 (7), 1358-1360, 2010
The H50Q mutation induces a 10-fold decrease in the solubility of α-synuclein
R Porcari, C Proukakis, CA Waudby, B Bolognesi, PP Mangione, ...
Journal of Biological Chemistry 290 (4), 2395-2404, 2015
Neurodegenerative diseases: quantitative predictions of protein–RNA interactions
D Cirillo, F Agostini, P Klus, D Marchese, S Rodriguez, B Bolognesi, ...
Rna 19 (2), 129-140, 2013
Disulfide bonds reduce the toxicity of the amyloid fibrils formed by an extracellular protein
MF Mossuto, B Bolognesi, B Guixer, A Dhulesia, F Agostini, JR Kumita, ...
Angewandte Chemie 123 (31), 7186-7189, 2011
An integrative study of protein-RNA condensates identifies scaffolding RNAs and reveals players in fragile X-associated tremor/ataxia syndrome
F Cid-Samper, M Gelabert-Baldrich, B Lang, N Lorenzo-Gotor, RD Ponti, ...
Cell reports 25 (12), 3422-3434. e7, 2018
The cleverSuite approach for protein characterization: predictions of structural properties, solubility, chaperone requirements and RNA-binding abilities
P Klus, B Bolognesi, F Agostini, D Marchese, A Zanzoni, GG Tartaglia
Bioinformatics 30 (11), 1601-1608, 2014
Reaching the limit
B Bolognesi, B Lehner
Elife 7, e39804, 2018
Hydrophobicity and conformational change as mechanistic determinants for nonspecific modulators of amyloid β self-assembly
A Abelein, B Bolognesi, CM Dobson, A Graslund, C Lendel
Biochemistry 51 (1), 126-137, 2012
Principles of self-organization in biological pathways: a hypothesis on the autogenous association of alpha-synuclein
A Zanzoni, D Marchese, F Agostini, B Bolognesi, D Cirillo, M Botta-Orfila, ...
Nucleic acids research 41 (22), 9987-9998, 2013
Intrinsic determinants of neurotoxic aggregate formation by the amyloid β peptide
AC Brorsson, B Bolognesi, GG Tartaglia, SL Shammas, G Favrin, I Watson, ...
Biophysical journal 98 (8), 1677-1684, 2010
X-inactivation: quantitative predictions of protein interactions in the Xist network
F Agostini, D Cirillo, B Bolognesi, GG Tartaglia
Nucleic acids research 41 (1), e31-e31, 2013
The genetic landscape for amyloid beta fibril nucleation accurately discriminates familial Alzheimer’s disease mutations
M Seuma, AJ Faure, M Badia, B Lehner, B Bolognesi
elife 10, e63364, 2021
Methods and models in neurodegenerative and systemic protein aggregation diseases
AC Brorsson, JR Kumita, I MacLeod, B Bolognesi, E Speretta, LM Luheshi, ...
Front. Biosci 15 (1), 373-396, 2010
Single Point Mutations Induce a Switch in the Molecular Mechanism of the Aggregation of the Alzheimer’s Disease Associated Aβ42 Peptide
B Bolognesi, SIA Cohen, P Aran Terol, EK Esbjörner, S Giorgetti, ...
ACS Chemical Biology 9 (2), 378-382, 2014
An atlas of amyloid aggregation: the impact of substitutions, insertions, deletions and truncations on amyloid beta fibril nucleation
M Seuma, B Lehner, B Bolognesi
Nature Communications 13 (1), 7084, 2022
Il sistema al momento non pu eseguire l'operazione. Riprova pi tardi.
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