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Physical Review Letters|November 22, 2002
Lack of self-averaging in neutral evolution of proteinsUgo Bastolla, Markus Porto, H Eduardo Roman, et al.
Frontiers in Neuroscience|March 15, 2021
Rationally Designed Bicyclic Peptides Prevent the Conversion of Aβ42 Assemblies Into Fibrillar StructuresTatsuya Ikenoue, Francesco A Aprile, Pietro Sormanni, et al.
Proceedings of the National Academy of Sciences of the United States of America|December 6, 2003
Structures and relative free energies of partially folded states of proteinsMichele Vendruscolo, Emanuele Paci, Martin Karplus, et al.
Journal of the American Chemical Society|July 5, 2011
The A53T mutation is key in defining the differences in the aggregation kinetics of human and mouse α-synucleinLijuan Kang, Kuen-Phon Wu, Michele Vendruscolo, et al.
The Journal of Physical Chemistry. B|January 22, 2009
Factors that affect the degree of twist in beta-sheet structures: a molecular dynamics simulation study of a cross-beta filament of the GNNQQNY peptideXavier Periole, Aldo Rampioni, Michele Vendruscolo, et al.
Cold Spring Harbor Perspectives in Biology|April 3, 2019
The Amyloid Phenomenon and Its Significance in Biology and MedicineChristopher M Dobson, Tuomas P J Knowles, Michele Vendruscolo
Proceedings of the National Academy of Sciences of the United States of America|July 14, 2025
Amyloid-β modulates the phase separation and aggregation of α-synucleinAlexander Röntgen, Zenon Toprakcioglu, Owen M Morris, et al.
ACS Chemical Neuroscience|July 9, 2024
Preparation and Characterization of Zn(II)-Stabilized Aβ42 OligomersAlicia González Díaz, Rodrigo Cataldi, Benedetta Mannini, et al.
Proceedings of the National Academy of Sciences of the United States of America|February 7, 2024
Modulation of α-synuclein in vitro aggregation kinetics by its alternative splice isoformsAlexander Röntgen, Zenon Toprakcioglu, James E Tomkins, et al.
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