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Biochemistry|August 4, 2012
Calcium-dependent interaction of calmodulin with human 80S ribosomes and polyribosomesPetra Behnen, Elizabeth Davis, Erin Delaney, et al.Biophysics Reviews|February 20, 2025
On the reversibility of amyloid fibril formationTinna Pálmadóttir, Josef Getachew, Lei Ortigosa-Pascual, et al.Proceedings of the National Academy of Sciences of the United States of America|July 13, 2017
Monomeric and fibrillar α-synuclein exert opposite effects on the catalytic cycle that promotes the proliferation of Aβ42 aggregatesSean Chia, Patrick Flagmeier, Johnny Habchi, et al.Frontiers in Immunology|June 20, 2019
The Molecular Basis of Human IgG-Mediated Enhancement of C4b-Binding Protein Recruitment to Group A StreptococcusDavid Ermert, Maisem Laabei, Antonin Weckel, et al.ACS Chemical Neuroscience|February 26, 2024
Extracellular Vesicles Slow Down Aβ(1-42) Aggregation by Interfering with the Amyloid Fibril Elongation StepVesa Halipi, Nima Sasanian, Julia Feng, et al.FEBS Letters|November 6, 2004
Islet amyloid polypeptide-induced membrane leakage involves uptake of lipids by forming amyloid fibersEmma Sparr, Maarten F M Engel, Dmitri V Sakharov, et al.Nanotoxicology|May 17, 2016
Translocation of 40 nm diameter nanowires through the intestinal epithelium of Daphnia magnaKarin Mattsson, Karl Adolfsson, Mikael T Ekvall, et al.Nanotoxicology|July 29, 2018
Disaggregation of gold nanoparticles by Daphnia magnaKarin Mattsson, Ruben Aguilar, Oscar Torstensson, et al.The FEBS Journal|April 5, 2013
Förster resonance energy transfer studies of calmodulin produced by native protein ligation reveal inter-domain electrostatic repulsionErik Hellstrand, Stephanie Kukora, Cynthia F Shuman, et al.Journal of the American Chemical Society|September 28, 2021
Mechanism of Secondary Nucleation at the Single Fibril Level from Direct Observations of Aβ42 AggregationManuela R Zimmermann, Subhas C Bera, Georg Meisl, et al.Pageof 35