Published in J Biol Chem on December 12, 2013
Strain-dependent profile of misfolded prion protein aggregates. Sci Rep (2016) 0.78
Scrapie prions aggregate to form amyloid-like birefringent rods. Cell (1983) 7.92
A general model of prion strains and their pathogenicity. Science (2007) 6.94
In vitro generation of infectious scrapie prions. Cell (2005) 6.86
A protease-resistant protein is a structural component of the scrapie prion. Cell (1983) 6.72
Generating a prion with bacterially expressed recombinant prion protein. Science (2010) 6.26
Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding. Nature (2001) 6.20
Formation of native prions from minimal components in vitro. Proc Natl Acad Sci U S A (2007) 5.94
The most infectious prion protein particles. Nature (2005) 5.37
RNA molecules stimulate prion protein conversion. Nature (2003) 4.06
N-terminal truncation of the scrapie-associated form of PrP by lysosomal protease(s): implications regarding the site of conversion of PrP to the protease-resistant state. J Virol (1991) 3.55
Ultra-efficient replication of infectious prions by automated protein misfolding cyclic amplification. J Biol Chem (2006) 2.98
Getting a grip on prions: oligomers, amyloids, and pathological membrane interactions. Annu Rev Biochem (2009) 2.80
Pathologic conformations of prion proteins. Annu Rev Biochem (1998) 2.50
Cell-free propagation of prion strains. EMBO J (2008) 2.20
Protease-sensitive synthetic prions. PLoS Pathog (2010) 2.14
Isolation and characterization of a proteinase K-sensitive PrPSc fraction. Biochemistry (2006) 1.86
Thermal stability and conformational transitions of scrapie amyloid (prion) protein correlate with infectivity. Protein Sci (1993) 1.59
The physical relationship between infectivity and prion protein aggregates is strain-dependent. PLoS Pathog (2010) 1.59
Partial unfolding and refolding of scrapie-associated prion protein: evidence for a critical 16-kDa C-terminal domain. Biochemistry (1996) 1.40
Protease-sensitive conformers in broad spectrum of distinct PrPSc structures in sporadic Creutzfeldt-Jakob disease are indicator of progression rate. PLoS Pathog (2011) 1.11
Protein misfolding cyclic amplification of infectious prions. Nat Protoc (2012) 1.10
High-resolution structure of infectious prion protein: the final frontier. Nat Struct Mol Biol (2012) 1.09
PK-sensitive PrP is infectious and shares basic structural features with PK-resistant PrP. PLoS Pathog (2012) 1.06
The enzymatic activity of proteinase K is controlled by calcium. Eur J Biochem (1988) 1.04
Strain-specific role of RNAs in prion replication. J Virol (2012) 1.04
Physiological role of the cellular prion protein. Vet Res (2007) 1.03
Changes in prion replication environment cause prion strain mutation. FASEB J (2013) 0.99
Ionic strength and transition metals control PrPSc protease resistance and conversion-inducing activity. J Biol Chem (2004) 0.91
Generation of prions in vitro and the protein-only hypothesis. Prion (2010) 0.88
On the biology of prions. Acta Neuropathol (1987) 0.87
Alcoholic fixation of blood to surgical instruments-a possible factor in the surgical transmission of CJD? J Hosp Infect (2004) 0.81
Prions: disease propagation and disease therapy by conformational transmission. Trends Mol Med (2001) 0.81
Kosmotropic anions promote conversion of recombinant prion protein into a PrPSc-like misfolded form. PLoS One (2012) 0.81
Prions, proteinase K and infectivity. Prion (2012) 0.78
In vitro generation of infectious scrapie prions. Cell (2005) 6.86
Ultra-efficient replication of infectious prions by automated protein misfolding cyclic amplification. J Biol Chem (2006) 2.98
A novel human disease with abnormal prion protein sensitive to protease. Ann Neurol (2008) 2.95
Prion strain mutation determined by prion protein conformational compatibility and primary structure. Science (2010) 2.71
Detection of prions in blood. Nat Med (2005) 2.66
Caspase-12 and endoplasmic reticulum stress mediate neurotoxicity of pathological prion protein. EMBO J (2003) 2.34
Cell-free propagation of prion strains. EMBO J (2008) 2.20
Presymptomatic detection of prions in blood. Science (2006) 2.14
Crossing the species barrier by PrP(Sc) replication in vitro generates unique infectious prions. Cell (2008) 2.09
Protein misfolding cyclic amplification for diagnosis and prion propagation studies. Methods Enzymol (2006) 2.04
Converting a peptide into a drug: strategies to improve stability and bioavailability. Curr Med Chem (2002) 2.02
Accelerated high fidelity prion amplification within and across prion species barriers. PLoS Pathog (2008) 1.89
Isolation and characterization of a proteinase K-sensitive PrPSc fraction. Biochemistry (2006) 1.86
Detection of infectious prions in urine. FEBS Lett (2008) 1.85
De novo generation of infectious prions in vitro produces a new disease phenotype. PLoS Pathog (2009) 1.83
Prions in the urine of patients with variant Creutzfeldt-Jakob disease. N Engl J Med (2014) 1.74
The disulfide isomerase Grp58 is a protective factor against prion neurotoxicity. J Neurosci (2005) 1.74
Production of cattle lacking prion protein. Nat Biotechnol (2006) 1.63
Unfolded protein response transcription factor XBP-1 does not influence prion replication or pathogenesis. Proc Natl Acad Sci U S A (2008) 1.60
Stressing out the ER: a role of the unfolded protein response in prion-related disorders. Curr Mol Med (2006) 1.49
Cyclic amplification of protein misfolding and aggregation. Methods Mol Biol (2005) 1.48
Estimating prion concentration in fluids and tissues by quantitative PMCA. Nat Methods (2010) 1.40
The prion strain phenomenon: molecular basis and unprecedented features. Biochim Biophys Acta (2006) 1.39
Pharmacological profiles of peptide drug candidates for the treatment of Alzheimer's disease. J Biol Chem (2003) 1.34
Molecular cross talk between misfolded proteins in animal models of Alzheimer's and prion diseases. J Neurosci (2010) 1.33
Prion protein glycosylation is not required for strain-specific neurotropism. J Virol (2009) 1.31
In vivo generation of neurotoxic prion protein: role for hsp70 in accumulation of misfolded isoforms. PLoS Genet (2009) 1.29
Amyloid formation modulates the biological activity of a bacterial protein. J Biol Chem (2005) 1.27
Misfolded protein aggregates: mechanisms, structures and potential for disease transmission. Semin Cell Dev Biol (2011) 1.25
Perturbation of endoplasmic reticulum homeostasis facilitates prion replication. J Biol Chem (2007) 1.13
Generation of a new form of human PrP(Sc) in vitro by interspecies transmission from cervid prions. J Biol Chem (2011) 1.12
Prion protein misfolding affects calcium homeostasis and sensitizes cells to endoplasmic reticulum stress. PLoS One (2010) 1.11
Reduction of amyloid load and cerebral damage in a transgenic mouse model of Alzheimer's disease by treatment with a beta-sheet breaker peptide. FASEB J (2002) 1.11
Cross-seeding of misfolded proteins: implications for etiology and pathogenesis of protein misfolding diseases. PLoS Pathog (2013) 1.10
Protein misfolding cyclic amplification of infectious prions. Nat Protoc (2012) 1.10
Is loss of function of the prion protein the cause of prion disorders? Trends Mol Med (2003) 1.10
High-resolution structure of infectious prion protein: the final frontier. Nat Struct Mol Biol (2012) 1.09
Cellular factors implicated in prion replication. FEBS Lett (2010) 1.07
Prion replication alters the distribution of synaptophysin and caveolin 1 in neuronal lipid rafts. Am J Pathol (2004) 1.04
Cross currents in protein misfolding disorders: interactions and therapy. CNS Neurol Disord Drug Targets (2009) 0.98
Bactericidal activity of both secreted and nonsecreted microcin E492 requires the mannose permease. J Bacteriol (2006) 0.96
Passage of murine scrapie prion protein across the mouse vascular blood-brain barrier. Biochem Biophys Res Commun (2004) 0.92
Microcin amyloid fibrils A are reservoir of toxic oligomeric species. J Biol Chem (2012) 0.91
Smoking exacerbates amyloid pathology in a mouse model of Alzheimer's disease. Nat Commun (2013) 0.90
A homogeneous 384-well high-throughput binding assay for a TNF receptor using alphascreen technology. J Biomol Screen (2003) 0.89
Changes in the glycosylation pattern of prion protein in murine scrapie. Implications for the mechanism of neurodegeneration in prion diseases. J Biol Chem (2002) 0.89
Calcineurin inhibition at the clinical phase of prion disease reduces neurodegeneration, improves behavioral alterations and increases animal survival. PLoS Pathog (2010) 0.88
Generation of prions in vitro and the protein-only hypothesis. Prion (2010) 0.88
Role of calcineurin in neurodegeneration produced by misfolded proteins and endoplasmic reticulum stress. Curr Opin Cell Biol (2011) 0.88
Recent US Case of Variant Creutzfeldt-Jakob Disease-Global Implications. Emerg Infect Dis (2015) 0.86
Molecular mechanisms of neurotoxicity of pathological prion protein. Curr Mol Med (2004) 0.86
Computational selection of inhibitors of Abeta aggregation and neuronal toxicity. Bioorg Med Chem (2009) 0.85
Cyclic amplification of prion protein misfolding. Methods Mol Biol (2012) 0.84
Kosmotropic anions promote conversion of recombinant prion protein into a PrPSc-like misfolded form. PLoS One (2012) 0.81
Natural animal models of neurodegenerative protein misfolding diseases. Curr Pharm Des (2012) 0.81
Maturation of human tripeptidyl-peptidase I in vitro. J Biol Chem (2004) 0.79
Initial fate of prions upon peripheral infection: half-life, distribution, clearance, and tissue uptake. FASEB J (2011) 0.79
Emerging roles of the unfolded protein response signaling in physiology and disease. Curr Mol Med (2006) 0.79
HIV/AIDS: modified stem cells in the spotlight. Cell Mol Life Sci (2014) 0.79
Protein misfolding disorders and rational design of antimisfolding agents. Methods Mol Biol (2006) 0.78
Reversibility of prion-induced neurodegeneration. Lancet Neurol (2007) 0.76
Animal models for neurodegenerative diseases associated to accumulation of misfolded protein aggregates. Curr Pharm Des (2012) 0.75