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Fabrizio Chiti

Showing results (11-20 of 182) with videos related to

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Nature Chemical Biology|December 18, 2008
Amyloid formation by globular proteins under native conditionsFabrizio Chiti, Christopher M Dobson
Current Opinion in Structural Biology|January 9, 2022
Small molecule protein binding to correct cellular folding or stabilize the native state against misfolding and aggregationFabrizio Chiti, Jeffery W Kelly
EMBO Reports|June 18, 2011
Prediction of amyloid aggregation in vivoMattia Belli, Matteo Ramazzotti, Fabrizio Chiti
Plos One|March 19, 2013
The N-terminal helix controls the transition between the soluble and amyloid states of an FF domainVirginia Castillo, Fabrizio Chiti, Salvador Ventura
The Journal of Biological Chemistry|February 3, 2019
Capturing Aβ42 aggregation in the cellFrancesco Bemporad, Cristina Cecchi, Fabrizio Chiti
Journal of the American Chemical Society|March 14, 2008
The degree of structural protection at the edge beta-strands determines the pathway of amyloid formation in globular proteinsGemma Soldi, Francesco Bemporad, Fabrizio Chiti
Methods in Enzymology|October 19, 2006
Protein aggregation starting from the native globular stateGiordana Marcon, Georgia Plakoutsi, Fabrizio Chiti
Scientific Reports|August 1, 2015
The Folding process of Human Profilin-1, a novel protein associated with familial amyotrophic lateral sclerosisEdoardo Del Poggetto, Fabrizio Chiti, Francesco Bemporad
Journal of Biochemistry|August 14, 2009
Amyloid formation by the model protein muscle acylphosphatase is accelerated by heparin and heparan sulphate through a scaffolding-based mechanismNeda Motamedi-Shad, Elodie Monsellier, Fabrizio Chiti
Biophysical Journal|September 20, 2005
Amyloid fibril formation can proceed from different conformations of a partially unfolded proteinMartino Calamai, Fabrizio Chiti, Christopher M Dobson
Pageof 19

Showing results (11-20 of 182) with videos related to

Sort By:
Pageof 19
Nature Chemical Biology|December 18, 2008
Amyloid formation by globular proteins under native conditionsFabrizio Chiti, Christopher M Dobson
Current Opinion in Structural Biology|January 9, 2022
Small molecule protein binding to correct cellular folding or stabilize the native state against misfolding and aggregationFabrizio Chiti, Jeffery W Kelly
EMBO Reports|June 18, 2011
Prediction of amyloid aggregation in vivoMattia Belli, Matteo Ramazzotti, Fabrizio Chiti
Plos One|March 19, 2013
The N-terminal helix controls the transition between the soluble and amyloid states of an FF domainVirginia Castillo, Fabrizio Chiti, Salvador Ventura
The Journal of Biological Chemistry|February 3, 2019
Capturing Aβ42 aggregation in the cellFrancesco Bemporad, Cristina Cecchi, Fabrizio Chiti
Journal of the American Chemical Society|March 14, 2008
The degree of structural protection at the edge beta-strands determines the pathway of amyloid formation in globular proteinsGemma Soldi, Francesco Bemporad, Fabrizio Chiti
Methods in Enzymology|October 19, 2006
Protein aggregation starting from the native globular stateGiordana Marcon, Georgia Plakoutsi, Fabrizio Chiti
Scientific Reports|August 1, 2015
The Folding process of Human Profilin-1, a novel protein associated with familial amyotrophic lateral sclerosisEdoardo Del Poggetto, Fabrizio Chiti, Francesco Bemporad
Journal of Biochemistry|August 14, 2009
Amyloid formation by the model protein muscle acylphosphatase is accelerated by heparin and heparan sulphate through a scaffolding-based mechanismNeda Motamedi-Shad, Elodie Monsellier, Fabrizio Chiti
Biophysical Journal|September 20, 2005
Amyloid fibril formation can proceed from different conformations of a partially unfolded proteinMartino Calamai, Fabrizio Chiti, Christopher M Dobson
Pageof 19