Abstract
Francesco Simone Ruggeri
Abstract
Authors
Institutions
No ROR-resolved institution is linked to this work yet.
Provenance
crossref
Confidence 100%
pubmed
Confidence 98%
europepmc
Confidence 96%
unpaywall
Confidence 95%
datacite
Confidence 0%
No local reference links have been materialized yet.
No local citing links have been materialized yet.
Half a century of amyloids: past, present and future
10.1039/c9cs00199a · 2020
The amyloid state and its association with protein misfolding diseases
10.1038/nrm3810 · 2014
Towards pharmacological prevention of Alzheimer disease
10.1038/s41582-025-01154-y · 2025
Single-molecule techniques in biophysics: a review of the progress in methods and applications
10.1088/1361-6633/aa8a02 · 2018
Nanoscale analysis beyond imaging by atomic force microscopy: molecular perspectives on oncology and neurodegeneration
10.1002/smsc.202500351 · 2025
A current view on Tau protein phosphorylation in Alzheimer's disease
10.1016/j.conb.2021.03.003 · 2021
The Amyloid-β pathway in Alzheimer's disease
10.1038/s41380-021-01249-0 · 2021
Inflammasome assembly in neurodegenerative diseases
10.1016/j.tins.2023.07.009 · 2023
Effects of oligomer toxicity, fibril toxicity and fibril spreading in synucleinopathies Cell
10.1007/s00018-022-04166-9 · 2022
Small soluble α-synuclein aggregates are the toxic species in Parkinson's disease
10.1038/s41467-022-33252-6 · 2022
Different soluble aggregates of Aβ42 can give rise to cellular toxicity through different mechanisms
10.1038/s41467-019-09477-3 · 2019
Formation of amyloid loops in brain tissues is controlled by the flexibility of protofibril chains
10.1073/pnas.2216234120 · 2023
Imaging protein aggregates in the serum and cerebrospinal fluid in Parkinson's disease
10.1093/brain/awab306 · 2022
Molecular pathology of neurodegenerative diseases by cryo-EM of amyloids
10.1038/s41586-023-06437-2 · 2023
The influence of pathogenic mutations in α-Synuclein on biophysical and structural characteristics of amyloid fibrils
10.1021/acsnano.9b09676 · 2020
Quantifying misfolded protein oligomers as drug targets and biomarkers in Alzheimer and Parkinson diseases
10.1038/s41570-021-00254-9 · 2021
Differential diagnostic performance of a panel of plasma biomarkers for different types of dementia
2022
Associating Alzheimer's disease pathology with its cerebrospinal fluid biomarkers
10.1093/brain/awac013 · 2022
Revised criteria for diagnosis and staging of Alzheimer's disease: alzheimer's Association workgroup
10.1002/alz.13859 · 2024
Amyloid fibril inhibition, acceleration, or fragmentation; are nano-based approaches advance in the right direction?
10.1016/j.nantod.2020.100983 · 2020
Amyloid fibril polymorphism: a challenge for molecular imaging and therapy
10.1111/joim.12732 · 2018
SynPull: an advanced method for studying neurodegeneration-related aggregates in synaptosomes using super-resolution microscopy
10.1016/j.chembiol.2025.01.001 · 2025
Nanoscopic tau aggregates are not shared intermediates but disease-specific entities across tauopathies
10.1016/j.celrep.2026.116934 · 2026
Single-molecule characterization and super-resolution imaging of Alzheimer's disease-relevant tau aggregates in human samples
10.1002/anie.202317756 · 2024
Cryo-EM observation of the amyloid key structure of polymorphic TDP-43 amyloid fibrils
10.1038/s41467-023-44489-0 · 2024
Cryo-EM structures of amyloid-β 42 filaments from human brains
10.1126/science.abm7285 · 2022
Unraveling Alzheimer's complexity with a distinct Aβ42 fibril type and specific AV-45 binding
10.1038/s41589-025-01921-4 · 2026
Cryo-EM structures of amyloid-β filaments with the Arctic mutation (E22G) from human and mouse brains
10.1007/s00401-022-02533-1 · 2023
CryoET of β-amyloid and tau within postmortem Alzheimer's disease brain
10.1038/s41586-024-07680-x · 2024
Recent advances and current trends in cryo-electron microscopy
10.1016/j.sbi.2022.102484 · 2022
Single-oligomer characterization of tau phosphorylation and mechanical state
10.1021/acsmeasuresciau.5c00116 · 2025
Maturation-dependent changes in the size, structure and seeding capacity of Aβ42 amyloid fibrils
10.1038/s42003-024-05858-7 · 2024
Unresolved referenced work
2026
The supramolecular architecture of amyloid fibrils formed by a human tau-derived hexapeptide VQIVYK
10.1039/d5nr04317d · 2026
Amyloid-β oligomers, curvilinear and annular assemblies, imaged by cryo-ET, cryo-EM, and AFM
10.1126/sciadv.adx9030 · 2025
Structural identification of individual helical amyloid filaments by integration of cryo-electron microscopy-derived maps in comparative morphometric atomic force microscopy image analysis
10.1016/j.jmb.2022.167466 · 2022
Structural reconstruction of individual filaments in Aβ42 fibril populations assembled in vitro reveal rare species that resemble ex vivo amyloid polymorphs from human brains
10.1038/s42004-025-01741-6 · 2025
Soluble amyloid beta-containing aggregates are present throughout the brain at early stages of Alzheimer's disease
10.1093/braincomms/fcab147 · 2021
Quantification of amyloid fibril polymorphism by nano-morphometry reveals the individuality of filament assembly
10.1038/s42004-020-00372-3 · 2020
A tutorial on optical photothermal infrared (O-PTIR) microscopy
10.1063/5.0219983 · 2024
Effect of RNA on the supramolecular architecture of α-synuclein fibrils
10.1016/j.bpj.2025.04.031 · doi-reference
Intermediate antiparallel fibrils in Aβ40 Dutch mutant aggregation: insights from nanoscale infrared spectroscopy
10.1021/acs.jpcb.3c01869 · doi-reference
Structurally distinct polymorphs of tau aggregates revealed by nanoscale infrared spectroscopy
10.1021/acs.jpclett.1c02660 · doi-reference
The role of phospholipid saturation and composition in α-synuclein aggregation and toxicity: a dual in vitro and in vivo approach
10.1002/pro.70121 · doi-reference
Nanoscale structural characterization of amyloid β 1–42 oligomers and fibrils grown in the presence of fatty acids
10.1021/acschemneuro.4c00275 · doi-reference
From disordered to ordered: nanoscale spectroscopy reveals structural evolution of amyloid beta 40 fibrils
10.1002/cphc.202500818 · doi-reference
Nanoscale infrared spectroscopy identifies structural heterogeneity in individual amyloid fibrils and prefibrillar aggregates
10.1021/acs.jpcb.2c04797 · doi-reference
Structural characterization of individual α-Synuclein oligomers formed at different stages of protein aggregation by atomic force microscopy-infrared spectroscopy
10.1021/acs.analchem.0c00593 · doi-reference
Infrared nanospectroscopy reveals the molecular interaction fingerprint of an aggregation inhibitor with single Aβ42 oligomers
10.1038/s41467-020-20782-0 · doi-reference
FUS phase separation is modulated by a molecular chaperone and methylation of arginine Cation-pi interactions
10.1016/j.cell.2018.03.056 · doi-reference
Aggregation of α-synuclein splice isoforms through a phase separation pathway
10.1126/sciadv.adq5396 · doi-reference
Spontaneous nucleation and fast aggregate-dependent proliferation of α-synuclein aggregates within liquid condensates at neutral pH
10.1073/pnas.2208792120 · doi-reference
Resolving protein condensates and aggregates in vivo by boxcar-enhanced Fluorescence-detected mid-Infrared photothermaL microscopy (FILM)
10.1038/s42004-026-01970-3 · doi-reference
Correlative optical photothermal infrared and X-ray fluorescence for chemical imaging of trace elements and relevant molecular structures directly in neurons
10.1038/s41377-021-00590-x · doi-reference
Mid-infrared chemical imaging of intracellular tau fibrils using fluorescence-guided computational photothermal microscopy
10.1038/s41377-023-01191-6 · doi-reference
Strain-distinct α-Synuclein and tau cross-seeding uncovered by correlative approach with optical photothermal infrared sub-micron imaging
10.1021/jacs.5c02811 · doi-reference
Lipid mediated formation of antiparallel aggregates in cerebral amyloid angiopathy
10.1007/s00401-025-02911-5 · doi-reference
Label-free infrared spectroscopic imaging reveals heterogeneity of β-Sheet aggregates in alzheimer's disease
10.1021/acs.jpclett.1c02306 · doi-reference
Intermediate antiparallel β structure in amyloid β plaques revealed by infrared spectroscopic imaging
10.1021/acschemneuro.3c00400 · doi-reference
Infrared nanospectroscopy characterisation of oligomeric and fibrillar aggregates during amyloid formation
10.1038/ncomms8831 · doi-reference
Colocalization of β-Sheets and carotenoids in Aβ plaques revealed with multimodal spatially resolved vibrational spectroscopy
10.1021/acs.jpcb.3c04782 · doi-reference
Fluorescently guided optical photothermal infrared microspectroscopy for protein-specific bioimaging at subcellular level
10.1021/acs.jmedchem.2c01359 · doi-reference
Single molecule secondary structure determination of proteins through infrared absorption nanospectroscopy
10.1038/s41467-020-16728-1 · doi-reference
Obtaining information about protein secondary structures in aqueous solution using fourier transform IR spectroscopy
10.1038/nprot.2015.024 · doi-reference
Using Fourier transform IR spectroscopy to analyze biological materials
10.1038/nprot.2014.110 · doi-reference
Label-free Aβ plaque detection in Alzheimer's disease brain tissue using infrared microscopy and neural networks
10.1016/j.heliyon.2025.e42111 · doi-reference
Infrared and Raman chemical imaging and spectroscopy at the nanoscale
10.1039/c8cs00916c · doi-reference