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Fabrizio Chiti

Fabrizio Chiti

D-Index & Metrics

Biology and Biochemistry

D-Index
72
Citations
33445
World Ranking
6120
National Ranking
143

Overview

Fabrizio Chiti is affiliated with the University of Florence in Italy, working primarily in the fields of Biochemistry, Genetics and Molecular Biology, and Medicine. Their research focuses extensively on Molecular Biology, Physiology, Neurology, Cell Biology, and Cellular and Molecular Neuroscience.

The scientist's main research topics include:

  • Alzheimer's disease research and treatments
  • Lipid Membrane Structure and Behavior
  • Prion Diseases and Protein Misfolding
  • Amyotrophic Lateral Sclerosis Research
  • Parkinson's Disease Mechanisms and Treatments
  • Protein Structure and Dynamics
  • Cellular transport and secretion

Fabrizio Chiti has contributed to several publications with a notable presence in well-known scientific venues. Frequent publication venues include:

  • ACS Chemical Neuroscience
  • International Journal of Molecular Sciences
  • Alzheimer's & Dementia
  • Current Opinion in Structural Biology
  • Scientific Reports

Selected recent papers by Fabrizio Chiti are:

  • The release of toxic oligomers from α-synuclein fibrils induces dysfunction in neuronal cells, 2021, Nature Communications
  • Misfolded protein oligomers: mechanisms of formation, cytotoxic effects, and pharmacological approaches against protein misfolding diseases, 2024, Molecular Neurodegeneration
  • Transthyretin Inhibits Primary and Secondary Nucleations of Amyloid-β Peptide Aggregation and Reduces the Toxicity of Its Oligomers, 2020, Biomacromolecules
  • Aβ Oligomers Dysregulate Calcium Homeostasis by Mechanosensitive Activation of AMPA and NMDA Receptors, 2021, ACS Chemical Neuroscience
  • Trodusquemine displaces protein misfolded oligomers from cell membranes and abrogates their cytotoxicity through a generic mechanism, 2020, Communications Biology

The scientist frequently collaborates with several co-authors, including:

  • Cristina Cecchi
  • Roberta Cascella
  • Michele Vendruscolo
  • Alessandra Bigi
  • Silvia Errico

Best Publications

  • Protein Misfolding, Functional Amyloid, and Human Disease

    Fabrizio Chiti;Christopher M. Dobson

  • Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases.

    Monica Bucciantini;Elisa Giannoni;Fabrizio Chiti;Fabrizio Chiti;Fabiana Baroni

  • Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade

    Fabrizio Chiti;Christopher M. Dobson

  • Designing conditions for in vitro formation of amyloid protofilaments and fibrils

    Fabrizio Chiti;Paul Webster;Niccolò Taddei;Anne Clark

  • Rationalization of the effects of mutations on peptide and protein aggregation rates.

    Fabrizio Chiti;Massimo Stefani;Niccolò Taddei;Giampietro Ramponi

  • Amyloid formation by globular proteins under native conditions

    Fabrizio Chiti;Christopher M Dobson

  • Prediction of "aggregation-prone" and "aggregation-susceptible" regions in proteins associated with neurodegenerative diseases.

    Amol P. Pawar;Kateri F. DuBay;Jesús Zurdo;Fabrizio Chiti

  • Structural basis of membrane disruption and cellular toxicity by α-synuclein oligomers

    Giuliana Fusco;Giuliana Fusco;Serene W. Chen;Serene W. Chen;Philip T. F. Williamson;Roberta Cascella

  • A causative link between the structure of aberrant protein oligomers and their toxicity

    Silvia Campioni;Benedetta Mannini;Mariagioia Zampagni;Anna Pensalfini;Anna Pensalfini

  • Kinetic partitioning of protein folding and aggregation.

    Fabrizio Chiti;Niccolò Taddei;Fabiana Baroni;Cristina Capanni

  • Prediction of Aggregation-Prone Regions in Structured Proteins

    Gian Gaetano Tartaglia;Amol P. Pawar;Silvia Campioni;Christopher M. Dobson

  • Prefibrillar amyloid protein aggregates share common features of cytotoxicity.

    Monica Bucciantini;Giulia Calloni;Fabrizio Chiti;Lucia Formigli

  • Prediction of the absolute aggregation rates of amyloidogenic polypeptide chains.

    Kateri F. DuBay;Amol P. Pawar;Fabrizio Chiti;Jesús Zurdo

  • Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding.

    Fabrizio Chiti;Niccolò Taddei;Paul M. White;Monica Bucciantini

  • Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases

    Fabrizio Chiti;Martino Calamai;Niccolò Taddei;Massimo Stefani

  • Protein misfolded oligomers: experimental approaches, mechanism of formation, and structure-toxicity relationships.

    Francesco Bemporad;Fabrizio Chiti

  • Prefibrillar amyloid aggregates could be generic toxins in higher organisms

    Serena Baglioni;Fiorella Casamenti;Monica Bucciantini;Leila M. Luheshi

  • Short amino acid stretches can mediate amyloid formation in globular proteins: The Src homology 3 (SH3) case

    Salvador Ventura;Jesús Zurdo;Saravanakumar Narayanan;Matilde Parreño

  • Mutational analysis of the propensity for amyloid formation by a globular protein.

    Fabrizio Chiti;Niccolò Taddei;Monica Bucciantini;Paul White

  • Prevention of amyloid‐like aggregation as a driving force of protein evolution

    Elodie Monsellier;Fabrizio Chiti

Frequent Co-Authors

Christopher M. Dobson
Christopher M. Dobson University of Cambridge
Niccolò Taddei
Niccolò Taddei University of Florence
Massimo Stefani
Massimo Stefani University of Florence
Michele Vendruscolo
Michele Vendruscolo University of Cambridge
Giampietro Ramponi
Giampietro Ramponi University of Florence
Tuomas P. J. Knowles
Tuomas P. J. Knowles University of Cambridge
Vittorio Bellotti
Vittorio Bellotti University College London
Alberto Diaspro
Alberto Diaspro Italian Institute of Technology
Martino Bolognesi
Martino Bolognesi University of Milan
Fiorella Casamenti
Fiorella Casamenti University of Florence

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