Associated Papers
Human prion protein: exploring the thermodynamic stability and structural dynamics of its pathogenic mutants.
Halder P et al.
Journal of Biomolecular Structure & Dynamics, 2022
In silico analysis of prion protein mutants: a comparative study by molecular dynamics approach.
Doss CG et al.
Cell Biochemistry and Biophysics, 2013
The landscape of the prion protein's structural response to mutation revealed by principal component analysis of multiple NMR ensembles.
Gendoo DM et al.
Plos Computational Biology, 2012
Molecular dynamics as an approach to study prion protein misfolding and the effect of pathogenic mutations.
van der Kamp MW et al.
Topics in Current Chemistry, 2011
Solution structure and dynamics of the I214V mutant of the rabbit prion protein.
Wen Y et al.
Plos One, 2010
NMR structure of the human prion protein with the pathological Q212P mutation reveals unique structural features.
Ilc G et al.
Plos One, 2010
Changing the solvent accessibility of the prion protein disulfide bond markedly influences its trafficking and effect on cell function.
Tabrett CA et al.
The Biochemical Journal, 2010
Helix H1 of the prion protein is rather stable against environmental perturbations: molecular dynamics of mutation and deletion variants of PrP(90-231).
Santini S et al.
Cellular and Molecular Life Sciences : Cmls, 2004
Impact of the tail and mutations G131V and M129V on prion protein flexibility.
Santini S et al.
Proteins, 2003
Analysis of the prion protein in primates reveals a new polymorphism in codon 226 (Y226F).
Glatzel M et al.
Biological Chemistry, 2002
NMR structures of three single-residue variants of the human prion protein.
Calzolai L et al.
Proceedings of the National Academy of Sciences of the United States of America, 2000
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