sameAs
The controlling roles of Trp60 and Trp95 in beta2-microglobulin function, folding and amyloid aggregation propertiesThe extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β(1-40) peptideIntrinsic determinants of neurotoxic aggregate formation by the amyloid beta peptideHydrophobicity and conformational change as mechanistic determinants for nonspecific modulators of amyloid β self-assembly.The H50Q mutation induces a 10-fold decrease in the solubility of α-synuclein.Neurodegenerative diseases: quantitative predictions of protein-RNA interactions.X-inactivation: quantitative predictions of protein interactions in the Xist network.Principles of self-organization in biological pathways: a hypothesis on the autogenous association of alpha-synucleinPhysicochemical principles of protein aggregation.Disulfide bonds reduce the toxicity of the amyloid fibrils formed by an extracellular protein.The cleverSuite approach for protein characterization: predictions of structural properties, solubility, chaperone requirements and RNA-binding abilities.A Concentration-Dependent Liquid Phase Separation Can Cause Toxicity upon Increased Protein Expression.ANS binding reveals common features of cytotoxic amyloid species.Single point mutations induce a switch in the molecular mechanism of the aggregation of the Alzheimer's disease associated Aβ42 peptide.Detergent-like interaction of Congo red with the amyloid beta peptide.Selenium-enhanced electron microscopic imaging of different aggregate forms of a segment of the amyloid β peptide in cells.Reaching the limitFibril-induced glutamine-/asparagine-rich prions recruit stress granule proteins in mammalian cells
P50
Q27650266-5231334F-41F3-4CC9-9579-C3B6D6067D23Q28854601-BF829282-9BC2-421A-BBD4-630DC4DA96DEQ33795575-98C0BDD0-5B1A-4D46-ACC1-6E8C26AD3FECQ34088492-BC0860DF-C0B4-44C9-A8B5-6AE26624C568Q35002998-2D06894C-77B2-46C4-86B9-2F8139FB1F9FQ36526561-598FA78E-209E-418B-B86C-7331C4315960Q36668804-3F6E95AC-395C-479F-8AD5-2DBBA5EB3A81Q37528739-952E8361-24A8-47DE-8C9A-2CF238EB5716Q38105684-FACA42FD-AC61-4757-8312-2CEB38A569C5Q38300383-22807AC6-F72F-48E8-9BCE-EEA964956DE7Q39257118-6CB0DBB9-04B0-495D-967B-5A1ECC5ADB19Q42030489-6E804025-0A19-4F5E-9975-C6AC12C275DDQ43021800-10ECCE7D-02EF-4C88-92BA-98B707E8A874Q43523290-AA499480-0950-47FC-B2AA-DE6902B1DDECQ46608976-E28F3B7E-F520-447E-9FD8-F34E836D5AA9Q53159868-6FE3B487-F3B1-4111-92E1-D3FAFB6A162FQ56530016-C437528D-A344-4664-9C1F-38A971171536Q91564012-E836F020-AA4B-418A-907C-A8EF64CD36AB
P50
description
biotecnòloga
@ca
hulumtuese
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Benedetta Bolognesi
@ast
Benedetta Bolognesi
@ca
Benedetta Bolognesi
@en
Benedetta Bolognesi
@es
Benedetta Bolognesi
@nl
type
label
Benedetta Bolognesi
@ast
Benedetta Bolognesi
@ca
Benedetta Bolognesi
@en
Benedetta Bolognesi
@es
Benedetta Bolognesi
@nl
prefLabel
Benedetta Bolognesi
@ast
Benedetta Bolognesi
@ca
Benedetta Bolognesi
@en
Benedetta Bolognesi
@es
Benedetta Bolognesi
@nl
P21
P31
P496
0000-0002-6632-947X