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Plos One|July 18, 2013
Wildtype and A30P mutant alpha-synuclein form different fibril structuresSøren Bang Nielsen, Francesca Macchi, Samuele Raccosta, et al.Iucrj|December 9, 2014
Investigating increasingly complex macromolecular systems with small-angle X-ray scatteringBente Vestergaard, Zehra SayersAdvances in Experimental Medicine and Biology|December 9, 2017
SAS-Based Studies of Protein FibrillationCarlotta Marasini, Bente VestergaardCurrent Opinion in Structural Biology|October 27, 2015
Protein-protein interactions: a supra-structural phenomenon demanding trans-disciplinary biophysical approachesOlwyn Byron, Bente VestergaardFEBS Letters|August 23, 2015
Cholesterol facilitates interactions between α-synuclein oligomers and charge-neutral membranesAndreas van Maarschalkerweerd, Valeria Vetri, Bente VestergaardJournal of Translational Medicine|May 13, 2022
Recommendations for addressing the translational gap between experimental and clinical research on amyloid diseasesMiriam Solomon, Vito Foderà, Annette Eva Langkilde, et al.Proceedings of the National Academy of Sciences of the United States of America|February 9, 2011
Low-resolution structure of a vesicle disrupting α-synuclein oligomer that accumulates during fibrillationLise Giehm, Dmitri I Svergun, Daniel E Otzen, et al.Scientific Reports|February 12, 2019
Early Stage Alpha-Synuclein Amyloid Fibrils are Reservoirs of Membrane-Binding SpeciesThomas Skamris, Carlotta Marasini, Kenneth L Madsen, et al.Scientific Reports|June 26, 2015
Considerably Unfolded Transthyretin Monomers Preceed and Exchange with Dynamically Structured Amyloid ProtofibrilsMinna Groenning, Raul I Campos, Daniel Hirschberg, et al.Journal of Applied Crystallography|September 23, 2014
In situ microfluidic dialysis for biological small-angle X-ray scatteringMagda Skou, Søren Skou, Thomas G Jensen, et al.Pageof 7