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Soft Matter|September 2, 2025
On the self-assembly of αB-crystallinEwelina Lindbladh, Marija Dubackic, Dev Thacker, et al.Proceedings of the National Academy of Sciences of the United States of America|November 24, 2021
Amyloid β 42 fibril structure based on small-angle scatteringVeronica Lattanzi, Ingemar André, Urs Gasser, et al.Physical Chemistry Chemical Physics : PCCP|May 1, 2026
The chaperone DNAJB6b halts amyloid formation through association with transient Aβ oligomersJosef Getachew, Andreas Carlsson, Emil Axell, et al.Communications Chemistry|August 3, 2026
Human chaperone DNAJB6b suppresses tau fibril formation through co-aggregationAndreas Carlsson, Emil Axell, Johan Wallerstein, et al.ACS Chemical Neuroscience|April 30, 2025
The Role of α-Synuclein-DNAJB6b Coaggregation in Amyloid SuppressionTinna Pálmadóttir, Josef Getachew, Dev Thacker, et al.Soft Matter|January 13, 2025
α-Synuclein interaction with POPC/POPS vesiclesMarija Dubackic, Veronica Lattanzi, Yun Liu, et al.Biophysical Chemistry|February 12, 2025
On the thermal and chemical stability of DNAJB6b and its globular domainsCelia Fricke, Jelica Milošević, Andreas Carlsson, et al.Langmuir : the ACS Journal of Surfaces and Colloids|August 11, 2022
α-Synuclein Interaction with Lipid Bilayer DiscsMarija Dubackic, Yun Liu, Elizabeth G Kelley, et al.QRB Discovery|December 25, 2025
The low complexity linker of DNAJB6b is key to its anti-amyloid functionTimas Merkelis, Ulf Olsson, Sara LinseBiophysical Journal|November 8, 2025
Does amyloid fibril nucleation occur at surfaces only?Jon Pallbo, Sara Linse, Ulf OlssonPageof 42