|Fatal familial insomnia: a second kindred with mutation of prion protein gene at codon 178.
|Deletion in the prion protein gene in a demented patient.
|Mutant prion proteins in Gerstmann-Straussler-Scheinker disease with neurofibrillary tangles.
|Fatal familial insomnia and familial Creutzfeldt-Jakob disease: disease phenotype determined by a DNA polymorphism.
|New mutation in scrapie amyloid precursor gene (at codon 178) in Finnish Creutzfeldt-Jakob kindred.
|Amyloid protein of Gerstmann-Straussler-Scheinker disease (Indiana kindred) is an 11 kd fragment of prion protein with an N-terminal glycine at codon 58.
|Genomic structure of the human prion protein gene.
|Transmissible familial Creutzfeldt-Jakob disease associated with five, seven, and eight extra octapeptide coding repeats in the PRNP gene.
|Mutation in codon 200 of scrapie amyloid protein gene in two clusters of Creutzfeldt-Jakob disease in Slovakia.
|Linkage of a prion protein missense variant to Gerstmann-Straussler syndrome.
|Pro-->Leu change at position 102 of prion protein is the most common but not the sole mutation related to Gerstmann-Straussler syndrome.
|Human prion protein cDNA: molecular cloning, chromosomal mapping, and biological implications.
|Molecular cloning of a human prion protein cDNA.
|SSCP analysis and sequencing of the human prion protein gene (PRNP) detects two different 24 bp deletions in an atypical Alzheimer's disease family.
|A variant of Gerstmann-Straussler-Scheinker disease carrying codon 105 mutation with codon 129 polymorphism of the prion protein gene: a clinicopathological study.
|Gerstmann-Straussler-Scheinker disease with mutation at codon 102 and methionine at codon 129 of PRNP in previously unreported patients.
|A new point mutation of the prion protein gene in Creutzfeldt-Jakob disease.
|A missense mutation at codon 105 with codon 129 polymorphism of the prion protein gene in a new variant of Gerstmann-Straussler-Scheinker disease.
|Japanese family with Creutzfeldt-Jakob disease with codon 200 point mutation of the prion protein gene.
|Mutation in codon 200 and polymorphism in codon 129 of the prion protein gene in Libyan Jews with Creutzfeldt-Jakob disease.
|Genetic and infectious prion diseases.
|Mutations and polymorphisms in the prion protein gene.
|Novel missense variants of prion protein in Creutzfeldt-Jakob disease or Gerstmann-Straussler syndrome.
|Polymorphism at codon 129 or codon 219 of PRNP and clinical heterogeneity in a previously unreported family with Gerstmann-Straussler-Scheinker disease (PrP-P102L mutation).
|Mutation of the prion protein gene at codon 208 in familial Creutzfeldt-Jakob disease.
|Familial spongiform encephalopathy associated with a novel prion protein gene mutation.
|A prion-linked psychiatric disorder.
|Protective prion protein polymorphisms against sporadic Creutzfeldt-Jakob disease.
|Phenotypic variability of Gerstmann-Straussler-Scheinker disease is associated with prion protein heterogeneity.
|A Huntington disease-like neurodegenerative disorder maps to chromosome 20p.
|Complete genomic sequence and analysis of the prion protein gene region from three mammalian species.
|Novel PRNP sequence variant associated with familial encephalopathy.
|NMR solution structure of the human prion protein.
|High prevalence of pathogenic mutations in patients with early-onset dementia detected by sequence analyses of four different genes.
|Identification of three novel mutations (E196K, V203I, E211Q) in the prion protein gene (PRNP) in inherited prion diseases with Creutzfeldt-Jakob disease phenotype.
|NMR structures of three single-residue variants of the human prion protein.
|Solution structure of the E200K variant of human prion protein. Implications for the mechanism of pathogenesis in familial prion diseases.
|Molecular genetics of human prion diseases in Germany.
|Crystal structure of the human prion protein reveals a mechanism for oligomerization.
|A new PRNP mutation (G131V) associated with Gerstmann-Straussler-Scheinker disease.
|The DNA sequence and comparative analysis of human chromosome 20.
|Molecular features of the copper binding sites in the octarepeat domain of the prion protein.
|The Thr183Ala mutation, not the loss of the first glycosylation site, alters the physical properties of the prion protein.
|Balancing selection at the prion protein gene consistent with prehistoric kurulike epidemics.
|Prion, amyloid beta-derived Cu(II) ions, or free Zn(II) ions support S-nitroso-dependent autocleavage of glypican-1 heparan sulfate.
|The octapeptide repeats in mammalian prion protein constitute a pH-dependent folding and aggregation site.
|The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
|The octarepeat domain of the prion protein binds Cu(II) with three distinct coordination modes at pH 7.4.
|Atomic structures of amyloid cross-beta spines reveal varied steric zippers.
|The prion protein is a combined zinc and copper binding protein: Zn2+ alters the distribution of Cu2+ coordination modes.
|Biosynthesis of prion protein nucleocytoplasmic isoforms by alternative initiation of translation.
|Crystal structure of human prion protein bound to a therapeutic antibody.
|Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.
|Early onset prion disease from octarepeat expansion correlates with copper or zinc binding properties.
|A novel protective prion protein variant that colocalizes with kuru exposure.
|Conformational diversity in prion protein variants influences intermolecular beta-sheet formation.
|Glypican-1 mediates both prion protein lipid raft association and disease isoform formation.
|Prion fibrillization is mediated by a native structural element that comprises helices H2 and H3.
|Copper (II) promotes the formation of soluble neurotoxic PrP oligomers in acidic environment.
|Characterizing the novel protein p33MONOX.
|An overlapping reading frame in the PRNP gene encodes a novel polypeptide distinct from the prion protein.
|A naturally occurring variant of the human prion protein completely prevents prion disease.