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Fabrizio Chiti

Showing results (1-10 of 182) with videos related to

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EMBO Reports|August 2, 2007
Prevention of amyloid-like aggregation as a driving force of protein evolutionElodie Monsellier, Fabrizio Chiti
Chemistry & Biology|March 27, 2012
Protein misfolded oligomers: experimental approaches, mechanism of formation, and structure-toxicity relationshipsFrancesco Bemporad, Fabrizio Chiti
Genome Biology|January 30, 2026
Understanding liquid-liquid phase separation through TDP-43: fundamental principles, subcellular compartmentalisation, and role of solid inclusion formationAlessandra Bigi, Fabrizio Chiti
Neural Regeneration Research|November 16, 2021
Mechanosensitivity of N-methyl-D-aspartate receptors (NMDAR) is the key through which amyloid beta oligomers activate themGiulia Fani, Fabrizio Chiti
FEBS Letters|July 15, 2009
"Native-like aggregation" of the acylphosphatase from Sulfolobus solfataricus and its biological implicationsFrancesco Bemporad, Fabrizio Chiti
Frontiers in Molecular Neuroscience|April 21, 2017
Chaperones as Suppressors of Protein Misfolded Oligomer ToxicityBenedetta Mannini, Fabrizio Chiti
Current Opinion in Structural Biology|October 28, 2008
Amyloidogenesis in its biological environment: challenging a fundamental issue in protein misfolding diseasesVittorio Bellotti, Fabrizio Chiti
Current Opinion in Structural Biology|March 29, 2022
Editorial overview: Folding and bindingFabrizio Chiti, Anna Sablina
Annual Review of Biochemistry|June 8, 2006
Protein misfolding, functional amyloid, and human diseaseFabrizio Chiti, Christopher M Dobson
Annual Review of Biochemistry|May 13, 2017
Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last DecadeFabrizio Chiti, Christopher M Dobson
Pageof 19

Showing results (1-10 of 182) with videos related to

Sort By:
Pageof 19
EMBO Reports|August 2, 2007
Prevention of amyloid-like aggregation as a driving force of protein evolutionElodie Monsellier, Fabrizio Chiti
Chemistry & Biology|March 27, 2012
Protein misfolded oligomers: experimental approaches, mechanism of formation, and structure-toxicity relationshipsFrancesco Bemporad, Fabrizio Chiti
Genome Biology|January 30, 2026
Understanding liquid-liquid phase separation through TDP-43: fundamental principles, subcellular compartmentalisation, and role of solid inclusion formationAlessandra Bigi, Fabrizio Chiti
Neural Regeneration Research|November 16, 2021
Mechanosensitivity of N-methyl-D-aspartate receptors (NMDAR) is the key through which amyloid beta oligomers activate themGiulia Fani, Fabrizio Chiti
FEBS Letters|July 15, 2009
"Native-like aggregation" of the acylphosphatase from Sulfolobus solfataricus and its biological implicationsFrancesco Bemporad, Fabrizio Chiti
Frontiers in Molecular Neuroscience|April 21, 2017
Chaperones as Suppressors of Protein Misfolded Oligomer ToxicityBenedetta Mannini, Fabrizio Chiti
Current Opinion in Structural Biology|October 28, 2008
Amyloidogenesis in its biological environment: challenging a fundamental issue in protein misfolding diseasesVittorio Bellotti, Fabrizio Chiti
Current Opinion in Structural Biology|March 29, 2022
Editorial overview: Folding and bindingFabrizio Chiti, Anna Sablina
Annual Review of Biochemistry|June 8, 2006
Protein misfolding, functional amyloid, and human diseaseFabrizio Chiti, Christopher M Dobson
Annual Review of Biochemistry|May 13, 2017
Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last DecadeFabrizio Chiti, Christopher M Dobson
Pageof 19