Associated Papers
Intrinsic determinants of prion protein neurotoxicity in Drosophila: from sequence to (dys)function.
Cembran A et al.
Frontiers in Molecular Neuroscience, 2023
Structural consequences of sequence variation in mammalian prion β2α2 loop segments.
Glynn C et al.
Frontiers in Neuroscience, 2022
Cervid Prion Protein Polymorphisms: Role in Chronic Wasting Disease Pathogenesis.
Arifin MI et al.
International Journal of Molecular Sciences, 2021
Protease resistance of infectious prions is suppressed by removal of a single atom in the cellular prion protein.
Leske H et al.
Plos One, 2017
Human prion protein sequence elements impede cross-species chronic wasting disease transmission.
Kurt TD et al.
The Journal of Clinical Investigation, 2015
A proposed mechanism for the promotion of prion conversion involving a strictly conserved tyrosine residue in the β2-α2 loop of PrPC.
Kurt TD et al.
The Journal of Biological Chemistry, 2014
De novo prion aggregates trigger autophagy in skeletal muscle.
Joshi-Barr S et al.
Journal of Virology, 2014
The effect of β2-α2 loop mutation on amyloidogenic properties of the prion protein.
Dutta A et al.
Febs Letters, 2013
Probing early misfolding events in prion protein mutants by NMR spectroscopy.
Giachin G et al.
Molecules (basel, Switzerland), 2013
Structural definition is important for the propagation of the yeast [PSI+] prion.
Marchante R et al.
Molecular Cell, 2013
N-terminal helix-cap in α-helix 2 modulates β-state misfolding in rabbit and hamster prion proteins.
Sweeting B et al.
Plos One, 2013
In silico analysis of prion protein mutants: a comparative study by molecular dynamics approach.
Doss CG et al.
Cell Biochemistry and Biophysics, 2013
Disruption of the X-loop turn of the prion protein linked to scrapie resistance.
Scouras AD et al.
Protein Engineering, Design & Selection : Peds, 2012
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
Introduction of glutamines into the B2-H2 loop promotes prion protein conversion.
Avbelj M et al.
Biochemical and Biophysical Research Communications, 2011
Toward the molecular basis of inherited prion diseases: NMR structure of the human prion protein with V210I mutation.
Biljan I et al.
Journal of Molecular Biology, 2011
Spongiform encephalopathy in transgenic mice expressing a point mutation in the β2-α2 loop of the prion protein.
Sigurdson CJ et al.
The Journal of Neuroscience : the Official Journal of the Society for Neuroscience, 2011
Strain specific resistance to murine scrapie associated with a naturally occurring human prion protein polymorphism at residue 171.
Striebel JF et al.
Plos Pathogens, 2011
Solution structure and dynamics of the I214V mutant of the rabbit prion protein.
Wen Y et al.
Plos One, 2010
Horse prion protein NMR structure and comparisons with related variants of the mouse prion protein.
Pérez DR et al.
Journal of Molecular Biology, 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
Conformational diversity in prion protein variants influences intermolecular beta-sheet formation.
Lee S et al.
The Embo Journal, 2010
Prion protein NMR structure from tammar wallaby (Macropus eugenii) shows that the beta2-alpha2 loop is modulated by long-range sequence effects.
Christen B et al.
Journal of Molecular Biology, 2009
NMR structure of the bank vole prion protein at 20 degrees C contains a structured loop of residues 165-171.
Christen B et al.
Journal of Molecular Biology, 2008
Searching for factors that distinguish disease-prone and disease-resistant prions via sequence analysis.
Kedarisetti KD et al.
Bioinformatics and Biology Insights, 2008
Prion protein NMR structures of elk and of mouse/elk hybrids.
Gossert AD et al.
Proceedings of the National Academy of Sciences of the United States of America, 2005
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
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
Identifying critical sites of PrP(c)-PrP(Sc) interaction in prion-infected cells by dominant-negative inhibition.
Taguchi Y et al.
Prion, 0