Fabrizio Chiti

University of Florence

Italy

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Articles (19)

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2025

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2022

Collaborators (17)

Chiara Donati

ITALY

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Peter M. Tessier

University of Michigan

UNITED STATES

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Valentina Bessi

ITALY

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Giulia Fani

University of Florence

ITALY

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Michele Vendruscolo

Professor

University of Cambridge

UNITED KINGDOM

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Alfonso De Simone

Imperial College London

UNITED KINGDOM

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Caterina Bernacchioni

Associate Professor, Applied Biology

University of Florence

ITALY

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Paolo Matteini

Istituto di fisica applicata Nello Carrara Consiglio Nazionale delle Ricerche

ITALY

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Francesco Bemporad

Associate Professor of Biochemistry

Università degli Studi di Napoli Federico II

ITALY

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Daniel Harries

ISRAEL

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Cristina Cecchi

University of Florence

ITALY

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Martino Calamai

University of Florence

ITALY

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Nunilo Cremades

Universidad de Zaragoza

SPAIN

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Jeffery Kelly

Lita Annenberg Hazen Professor of Chemistry

Scripps Research Institute

UNITED STATES

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Ryan Limbocker

Assistant Professor

United States Military Academy

UNITED STATES

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Assaf Friedler

ISRAEL

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Alessandra Bigi

Assistant Professor (RTD-A)

University of Florence

ITALY

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Fabrizio Chiti

Research Interests

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Articles (19)

Natural aminosterols inhibit <scp>NMDA</scp> receptors with low nanomolar potency

Structural commonalities determined by physicochemical principles in the complex polymorphism of the amyloid state of proteins

Detection of an Intermediate in the Unfolding Process of the N-Terminal Domain of TDP-43

Structure–Toxicity Relationship in Intermediate Fibrils from α-Synuclein Condensates

Harnessing topological machine learning in Raman spectroscopy: Perspectives for Alzheimer’s disease detection via cerebrospinal fluid analysis

Biophysical characterization of the phase separation of TDP-43 devoid of the C-terminal domain

Leveraging Machine Learning-Guided Molecular Simulations Coupled with Experimental Data to Decipher Membrane Binding Mechanisms of Aminosterols

Sphingosine 1‐phosphate attenuates neuronal dysfunction induced by amyloid‐β oligomers through endocytic internalization of NMDA receptors

Characterization of Pairs of Toxic and Nontoxic Misfolded Protein Oligomers Elucidates the Structural Determinants of Oligomer Toxicity in Protein Misfolding Diseases

Amyloid aggregation is potently slowed down by osmolytes due to compaction of partially folded state

Quantitative Attribution of the Protective Effects of Aminosterols against Protein Aggregates to Their Chemical Structures and Ability to Modulate Biological Membranes

Alzheimer Disease Detection from Raman Spectroscopy of the Cerebrospinal Fluid via Topological Machine Learning

Small molecule protein binding to correct cellular folding or stabilize the native state against misfolding and aggregation

Squalamine and trodusquemine: two natural products for neurodegenerative diseases, from physical chemistry to the clinic

Conversion of the Native N-Terminal Domain of TDP-43 into a Monomeric Alternative Fold with Lower Aggregation Propensity

Biophysical characterization of full‐length TAR DNA‐binding protein (TDP‐43) phase separation

Amyloid fibrils act as a reservoir of soluble oligomers, the main culprits in protein deposition diseases

Misfolded protein oligomers induce an increase of intracellular Ca2+ causing an escalation of reactive oxidative species

A quantitative biology approach correlates neuronal toxicity with the largest inclusions of TDP-43

Collaborators (17)

Chiara Donati

Peter M. Tessier

Valentina Bessi

Giulia Fani

Michele Vendruscolo

Alfonso De Simone

Caterina Bernacchioni

Paolo Matteini

Francesco Bemporad

Daniel Harries

Cristina Cecchi

Martino Calamai

Nunilo Cremades

Jeffery Kelly

Ryan Limbocker

Assaf Friedler

Alessandra Bigi

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