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Antibody binding defines a structure for an epitope that participates in the PrPC-->PrPSc conformational change

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Antibody binding defines a structure for an epitope that participates in the PrPC-->PrPSc conformational change (English)

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1 reference

5

S B Prusiner

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Fred E Cohen

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7

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F E Cohen

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author name string

Z F Kanyo

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1

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K M Pan

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2

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R A Williamson

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3

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D R Burton

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4

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R J Fletterick

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6

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language of work or name

English

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publication date

5 November 1999

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published in

Journal of Molecular Biology

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volume

293

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issue

4

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page(s)

855-63

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cites work

Circumventing tolerance to generate autologous monoclonal antibodies to the prion protein

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Synthetic peptides homologous to prion protein residues 106-147 form amyloid-like fibrils in vitro

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Generation of a large combinatorial library of the immunoglobulin repertoire in phage lambda

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AMoRe: an automated package for molecular replacement

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Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons

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Prion protein selectively binds copper(II) ions

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Copper binding to the prion protein: structural implications of four identical cooperative binding sites

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NMR structure of the mouse prion protein domain PrP(121-231)

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Loops in globular proteins: a novel category of secondary structure

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Pro----leu change at position 102 of prion protein is the most common but not the sole mutation related to Gerstmann-Sträussler syndrome

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Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins

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Assembly of combinatorial antibody libraries on phage surfaces: the gene III site

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Molecular characteristics of a protease-resistant, amyloidogenic and neurotoxic peptide homologous to residues 106-126 of the prion protein

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Characterization of the bovine prion protein gene: the expression requires interaction between the promoter and intron

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B lymphocytes and neuroinvasion

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A transmembrane form of the prion protein in neurodegenerative disease

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Crystallographic R factor refinement by molecular dynamics

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Pathologic conformations of prion proteins

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A conformational transition at the N terminus of the prion protein features in formation of the scrapie isoform

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Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform

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Structure of the recombinant full-length hamster prion protein PrP(29-231): the N terminus is highly flexible

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Neurotoxicity of a prion protein fragment

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26-10 Fab-digoxin complex: affinity and specificity due to surface complementarity

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Improved methods for building protein models in electron density maps and the location of errors in these models

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Analytical molecular surface calculation

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Channel formation by a neurotoxic prion protein fragment

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Raster3D Version 2.0. A program for photorealistic molecular graphics

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Copper binding to the N-terminal tandem repeat region of mammalian and avian prion protein: structural studies using synthetic peptides

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Taxonomy and conformational analysis of loops in proteins.

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Distinct prion proteins in short and long scrapie incubation period mice

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MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

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Eight prion strains have PrP(Sc) molecules with different conformations

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Mice with gene targetted prion protein alterations show that Prnp, Sinc and Prni are congruent

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A variant of Gerstmann-Sträussler-Scheinker disease carrying codon 105 mutation with codon 129 polymorphism of the prion protein gene: a clinicopathological study

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DOI

10.1006/JMBI.1999.3193

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PubMed publication ID

10543972

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(Q27620158)

Antibody binding defines a structure for an epitope that participates in the PrPC-->PrPSc conformational change

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