Published in J Biol Chem on February 02, 2004
Molecular architecture of human prion protein amyloid: a parallel, in-register beta-structure. Proc Natl Acad Sci U S A (2007) 2.55
Folding versus aggregation: polypeptide conformations on competing pathways. Arch Biochem Biophys (2007) 1.97
Prion diseases and their biochemical mechanisms. Biochemistry (2009) 1.65
Spontaneous generation of prion infectivity in fatal familial insomnia knockin mice. Neuron (2009) 1.49
The expanding universe of prion diseases. PLoS Pathog (2006) 1.45
Prion disease susceptibility is affected by beta-structure folding propensity and local side-chain interactions in PrP. Proc Natl Acad Sci U S A (2010) 1.16
Neurotoxic mutants of the prion protein induce spontaneous ionic currents in cultured cells. J Biol Chem (2010) 1.12
Early intermediate in human prion protein folding as evidenced by ultrarapid mixing experiments. J Am Chem Soc (2006) 1.09
Pathogenic mutations in the hydrophobic core of the human prion protein can promote structural instability and misfolding. J Mol Biol (2010) 1.08
An N-terminal polybasic domain and cell surface localization are required for mutant prion protein toxicity. J Biol Chem (2011) 1.03
Prion protein amyloid formation under native-like conditions involves refolding of the C-terminal alpha-helical domain. J Biol Chem (2008) 1.02
Selective vulnerability to neurodegenerative disease: the curious case of Prion Protein. Dis Model Mech (2014) 0.98
The consequences of pathogenic mutations to the human prion protein. Protein Eng Des Sel (2009) 0.98
Dynamic diagnosis of familial prion diseases supports the β2-α2 loop as a universal interference target. PLoS One (2011) 0.98
Prion protein with an octapeptide insertion has impaired neuroprotective activity in transgenic mice. EMBO J (2007) 0.98
Expression of mutant or cytosolic PrP in transgenic mice and cells is not associated with endoplasmic reticulum stress or proteasome dysfunction. PLoS One (2011) 0.96
Profoundly different prion diseases in knock-in mice carrying single PrP codon substitutions associated with human diseases. Proc Natl Acad Sci U S A (2013) 0.94
Folding kinetics of the human prion protein probed by temperature jump. Proc Natl Acad Sci U S A (2009) 0.94
The role of the 132-160 region in prion protein conformational transitions. Protein Sci (2005) 0.94
Intraspecies prion transmission results in selection of sheep scrapie strains. PLoS One (2010) 0.93
NMR structure of the human prion protein with the pathological Q212P mutation reveals unique structural features. PLoS One (2010) 0.92
Differential stability of the bovine prion protein upon urea unfolding. Protein Sci (2009) 0.88
Protein folding and misfolding on surfaces. Int J Mol Sci (2008) 0.88
Energy landscape of the prion protein helix 1 probed by metadynamics and NMR. Biophys J (2012) 0.86
Introducing a rigid loop structure from deer into mouse prion protein increases its propensity for misfolding in vitro. PLoS One (2013) 0.85
Refinement of under-determined loops of Human Prion Protein by database-derived distance constraints. Int J Data Min Bioinform (2009) 0.83
Microsecond unfolding kinetics of sheep prion protein reveals an intermediate that correlates with susceptibility to classical scrapie. Biophys J (2011) 0.82
Prion protein misfolding, strains, and neurotoxicity: an update from studies on Mammalian prions. Int J Cell Biol (2013) 0.82
Loss of anti-Bax function in Gerstmann-Sträussler-Scheinker syndrome-associated prion protein mutants. PLoS One (2009) 0.81
PrP charge structure encodes interdomain interactions. Sci Rep (2015) 0.80
Global analysis of protein folding thermodynamics for disease state characterization. J Proteome Res (2015) 0.79
The effect of β2-α2 loop mutation on amyloidogenic properties of the prion protein. FEBS Lett (2013) 0.79
Failure of prion protein oxidative folding guides the formation of toxic transmembrane forms. J Biol Chem (2012) 0.78
Pathogenic mutations within the hydrophobic domain of the prion protein lead to the formation of protease-sensitive prion species with increased lethality. J Virol (2013) 0.78
A Native-like Intermediate Serves as a Branching Point between the Folding and Aggregation Pathways of the Mouse Prion Protein. Structure (2015) 0.78
Comparing the folding and misfolding energy landscapes of phosphoglycerate kinase. Biophys J (2012) 0.76
Effect of hydrophobic mutations in the H2-H3 subdomain of prion protein on stability and conversion in vitro and in vivo. PLoS One (2011) 0.76
Real value prediction of protein folding rate change upon point mutation. J Comput Aided Mol Des (2012) 0.76
Disease-associated mutations in the prion protein impair laminin-induced process outgrowth and survival. J Biol Chem (2012) 0.76
Prion protein self-peptides modulate prion interactions and conversion. BMC Biochem (2009) 0.76
Rapid folding of the prion protein captured by pressure-jump. Eur Biophys J (2009) 0.76
Discovery of Age-Related Protein Folding Stability Differences in the Mouse Brain Proteome. J Proteome Res (2016) 0.75
Potential approaches for heterologous prion protein treatment of prion diseases. Prion (2016) 0.75
Mammalian prions generated from bacterially expressed prion protein in the absence of any mammalian cofactors. J Biol Chem (2010) 2.57
Molecular architecture of human prion protein amyloid: a parallel, in-register beta-structure. Proc Natl Acad Sci U S A (2007) 2.55
Molecular basis of barriers for interspecies transmissibility of mammalian prions. Mol Cell (2004) 2.39
Beta-sheet core of human prion protein amyloid fibrils as determined by hydrogen/deuterium exchange. Proc Natl Acad Sci U S A (2007) 2.14
Fibril conformation as the basis of species- and strain-dependent seeding specificity of mammalian prion amyloids. Cell (2005) 2.06
Structural organization of brain-derived mammalian prions examined by hydrogen-deuterium exchange. Nat Struct Mol Biol (2011) 1.90
Interaction between human prion protein and amyloid-beta (Abeta) oligomers: role OF N-terminal residues. J Biol Chem (2010) 1.88
Molecular conformation and dynamics of the Y145Stop variant of human prion protein in amyloid fibrils. Proc Natl Acad Sci U S A (2008) 1.86
Prion diseases and their biochemical mechanisms. Biochemistry (2009) 1.65
PrP conformational transitions alter species preference of a PrP-specific antibody. J Biol Chem (2010) 1.62
Conformational flexibility of Y145Stop human prion protein amyloid fibrils probed by solid-state nuclear magnetic resonance spectroscopy. J Am Chem Soc (2010) 1.55
Distinct structures of scrapie prion protein (PrPSc)-seeded versus spontaneous recombinant prion protein fibrils revealed by hydrogen/deuterium exchange. J Biol Chem (2009) 1.27
Polymorphism at residue 129 modulates the conformational conversion of the D178N variant of human prion protein 90-231. Biochemistry (2005) 1.21
Nucleation-dependent conformational conversion of the Y145Stop variant of human prion protein: structural clues for prion propagation. Proc Natl Acad Sci U S A (2003) 1.14
Kinetic intermediate in the folding of human prion protein. J Biol Chem (2002) 1.13
Intermolecular alignment in Y145Stop human prion protein amyloid fibrils probed by solid-state NMR spectroscopy. J Am Chem Soc (2011) 1.10
Early intermediate in human prion protein folding as evidenced by ultrarapid mixing experiments. J Am Chem Soc (2006) 1.09
Disease-associated F198S mutation increases the propensity of the recombinant prion protein for conformational conversion to scrapie-like form. J Biol Chem (2002) 1.08
Small protease sensitive oligomers of PrPSc in distinct human prions determine conversion rate of PrP(C). PLoS Pathog (2012) 1.07
Conformational diversity in prion protein variants influences intermolecular beta-sheet formation. EMBO J (2009) 1.07
Molecular biology and pathology of prion strains in sporadic human prion diseases. Acta Neuropathol (2010) 1.06
The role of glycophosphatidylinositol anchor in the amplification of the scrapie isoform of prion protein in vitro. FEBS Lett (2009) 1.04
Atypical effect of salts on the thermodynamic stability of human prion protein. J Biol Chem (2003) 1.03
Prion protein amyloid formation under native-like conditions involves refolding of the C-terminal alpha-helical domain. J Biol Chem (2008) 1.02
Soluble prion protein inhibits amyloid-β (Aβ) fibrillization and toxicity. J Biol Chem (2012) 0.96
Crystal structure of a human prion protein fragment reveals a motif for oligomer formation. J Am Chem Soc (2013) 0.94
Role of N-terminal familial mutations in prion protein fibrillization and prion amyloid propagation in vitro. J Biol Chem (2006) 0.93
Functional interactions of nucleocapsid protein of feline immunodeficiency virus and cellular prion protein with the viral RNA. J Mol Biol (2002) 0.93
Conformational stability of mammalian prion protein amyloid fibrils is dictated by a packing polymorphism within the core region. J Biol Chem (2013) 0.92
Antimicrobial activity of human prion protein is mediated by its N-terminal region. PLoS One (2009) 0.90
Structural polymorphism in amyloids: new insights from studies with Y145Stop prion protein fibrils. J Biol Chem (2011) 0.89
Cellular prion protein regulates its own α-cleavage through ADAM8 in skeletal muscle. J Biol Chem (2012) 0.88
Cellular oxidant stress and advanced glycation endproducts of albumin: caveats of the dichlorofluorescein assay. Arch Biochem Biophys (2002) 0.87
Mechanism of stabilization of Bacillus circulans xylanase upon the introduction of disulfide bonds. Biophys Chem (2006) 0.84
Nanomechanical properties of human prion protein amyloid as probed by force spectroscopy. Biophys J (2008) 0.82
Recombinant human prion protein inhibits prion propagation in vitro. Sci Rep (2013) 0.82
The effect of β2-α2 loop mutation on amyloidogenic properties of the prion protein. FEBS Lett (2013) 0.79
Interaction between prion protein and Aβ amyloid fibrils revisited. ACS Chem Neurosci (2014) 0.78
Prion strains under the magnifying glass. Nat Struct Mol Biol (2007) 0.77
Thermodynamic stabilization of the folded domain of prion protein inhibits prion infection in vivo. Cell Rep (2013) 0.77
Structural underpinnings of prion protein conversion. J Biol Chem (2011) 0.75
Protein science: discriminating taste of prions. Nature (2007) 0.75