Predicted alpha-helical regions of the prion protein when synthesized as peptides form amyloid. - Wikidata - awgldk - TriplyDB

Predicted alpha-helical regions of the prion protein when synthesized as peptides form amyloid.

Predicted alpha-helical regions of the prion protein when synthesized as peptides form amyloid.

http://www.wikidata.org/entity/Q37302673

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β-hairpin-mediated formation of structurally distinct multimers of neurotoxic prion peptides Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins Prions α-Cleavage of cellular prion protein Probing the role of structural features of mouse PrP in yeast by expression as Sup35-PrP fusions Sheep prion protein synthetic peptide spanning helix 1 and beta-strand 2 (residues 142-166) shows beta-hairpin structure in solution Strain-specified relative conformational stability of the scrapie prion protein Immobilized prion protein undergoes spontaneous rearrangement to a conformation having features in common with the infectious form.Solvent microenvironments and copper binding alters the conformation and toxicity of a prion fragment Distinct PrP properties suggest the molecular basis of strain variation in transmissible mink encephalopathy.Selenomethionine incorporation into amyloid sequences regulates fibrillogenesis and toxicity Structural instability of the prion protein upon M205S/R mutations revealed by molecular dynamics simulations Determination of solution conformations of PrP106-126, a neurotoxic fragment of prion protein, by 1H NMR and restrained molecular dynamics.Solid-state NMR studies of the secondary structure of a mutant prion protein fragment of 55 residues that induces neurodegeneration.Methionine sulfoxides on prion protein Helix-3 switch on the alpha-fold destabilization required for conversion.Sporadic Creutzfeldt-Jakob disease--a review.Neurodegeneration in humans caused by prions A receptor for infectious and cellular prion protein.Interactions of the chaperone Hsp104 with yeast Sup35 and mammalian PrP.Prion protein (PrP) synthetic peptides induce cellular PrP to acquire properties of the scrapie isoform Amphotericin B inhibits the generation of the scrapie isoform of the prion protein in infected cultures.Affinity-tagged miniprion derivatives spontaneously adopt protease-resistant conformations Theoretical model of prion propagation: a misfolded protein induces misfolding.Dynamic diagnosis of familial prion diseases supports the β2-α2 loop as a universal interference target.Intersheet rearrangement of polypeptides during nucleation of {beta}-sheet aggregates.Overexpression of nonconvertible PrPc delta114-121 in scrapie-infected mouse neuroblastoma cells leads to trans-dominant inhibition of wild-type PrP(Sc) accumulation.Characterization of the prion protein in human urine.Is there a risk of prion-like disease transmission by Alzheimer- or Parkinson-associated protein particles?The stability and dynamics of the human calcitonin amyloid peptide DFNKF Genetic organization, length conservation, and evolution of RNA polymerase II carboxyl-terminal domain.Stabilities and conformations of Alzheimer's beta -amyloid peptide oligomers (Abeta 16-22, Abeta 16-35, and Abeta 10-35): Sequence effects.The dark side of lysosome-related organelles: specialization of the endocytic pathway for melanosome biogenesis.Influence of pH on the human prion protein: insights into the early steps of misfolding.Prion protein misfolding.Secondary structure provides a template for the folding of nearby polypeptides.Structural polymorphism in amyloids: new insights from studies with Y145Stop prion protein fibrils.Proposed three-dimensional structure for the cellular prion protein Endogenous proteolytic cleavage of normal and disease-associated isoforms of the human prion protein in neural and non-neural tissues.Etiology and pathogenesis of prion diseases.Cellular prion protein regulates its own α-cleavage through ADAM8 in skeletal muscle.

P2860

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P2860

Predicted alpha-helical regions of the prion protein when synthesized as peptides form amyloid.

http://www.wikidata.org/entity/Q37302673

description

1992 nî lūn-bûn

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1992年の論文

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1992年学术文章

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1992年学术文章

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1992年学术文章

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1992年学术文章

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1992年学术文章

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1992年學術文章

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1992年學術文章

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1992年學術文章

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name

Predicted alpha-helical region ...... ized as peptides form amyloid.

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Predicted alpha-helical region ...... ized as peptides form amyloid.

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type

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Predicted alpha-helical region ...... ized as peptides form amyloid.

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Predicted alpha-helical region ...... ized as peptides form amyloid.

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prefLabel

Predicted alpha-helical region ...... ized as peptides form amyloid.

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Predicted alpha-helical region ...... ized as peptides form amyloid.

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Proceedings of the National Academy of Sciences of the United States of America

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Predicted alpha-helical region ...... ized as peptides form amyloid.

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Baldwin MA

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Cohen F

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Fletterick R

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Gabriel JM

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Lloyd DH

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P2860

Structure of a protein superfiber: spider dragline silk

Structural comparison of two serine proteinase-protein inhibitor complexes: eglin-c-subtilisin Carlsberg and CI-2-subtilisin Novo

Interdomain motion in liver alcohol dehydrogenase. Structural and energetic analysis of the hinge bending mode

Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins

Human alpha 2(VI) collagen gene. Heterogeneity at the 5'-untranslated region generated by an alternate exon

The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor

pH-dependent structural transitions of Alzheimer amyloid peptides.

Structure and X-ray amino acid sequence of a bacteriochlorophyll A protein from Prosthecochloris aestuarii refined at 1.9 A resolution.

Molecular biology of prion diseases.

Mutant prion proteins in Gerstmann-Sträussler-Scheinker disease with neurofibrillary tangles.

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10940-10944

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scholarly article

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22

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89

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Stanley B. Prusiner

David M. Holtzman

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1992-11-01T00:00:00Z

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21718018

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1438300

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Prion protein family

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50458

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