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The Biochemical Journal|September 15, 2005
Recombinant prion protein does not possess SOD-1 activitySamantha Jones, Mark Batchelor, Daljit Bhelt, et al.Proceedings of the National Academy of Sciences of the United States of America|August 3, 2019
Desmin forms toxic, seeding-competent amyloid aggregates that persist in muscle fibersNiraja Kedia, Khalid Arhzaouy, Sara K Pittman, et al.Scientific Reports|March 5, 2021
Bank vole prion protein extends the use of RT-QuIC assays to detect prions in a range of inherited prion diseasesTze How Mok, Akin Nihat, Connie Luk, et al.Elife|August 7, 2024
Syntaxin-6 delays prion protein fibril formation and prolongs the presence of toxic aggregation intermediatesDaljit Sangar, Elizabeth Hill, Kezia Jack, et al.The Journal of General Virology|July 19, 2006
Codon 129 polymorphism of the human prion protein influences the kinetics of amyloid formationPatrick A Lewis, M Howard Tattum, Samantha Jones, et al.Journal of Molecular Biology|May 27, 2023
Loss of Residues 119-136, Including the First β-strand of Human Prion Protein, Generates an Aggregation-competent Partially "Open" FormLaszlo L P Hosszu, Daljit Sangar, Mark Batchelor, et al.The Journal of Biological Chemistry|May 15, 2026
Prion propagation is controlled by discrete structural regions of PrP rather than overall stabilitySavroop K Bhamra, Parineeta Arora, May Liew, et al.The Journal of Biological Chemistry|April 17, 2009
Conformational properties of beta-PrPLaszlo L P Hosszu, Clare R Trevitt, Samantha Jones, et al.Biochemistry|December 14, 2005
Definable equilibrium states in the folding of human prion proteinLaszlo L P Hosszu, Mark A Wells, Graham S Jackson, et al.The Journal of Biological Chemistry|May 5, 2004
The residue 129 polymorphism in human prion protein does not confer susceptibility to Creutzfeldt-Jakob disease by altering the structure or global stability of PrPCLaszlo L P Hosszu, Graham S Jackson, Clare R Trevitt, et al.Pageof 2