Distinct structures of scrapie prion protein (PrPSc)-seeded versus spontaneous recombinant prion protein fibrils revealed by hydrogen/deuterium exchange.
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Techniques to elucidate the conformation of prionsDefining the conformational features of anchorless, poorly neuroinvasive prionsThe effect of β2-α2 loop mutation on amyloidogenic properties of the prion proteinCritical significance of the region between Helix 1 and 2 for efficient dominant-negative inhibition by conversion-incompetent prion proteinParallel in-register intermolecular β-sheet architectures for prion-seeded prion protein (PrP) amyloids.Charge neutralization of the central lysine cluster in prion protein (PrP) promotes PrP(Sc)-like folding of recombinant PrP amyloids.Progress towards structural understanding of infectious sheep PrP-amyloid.Prion Protein Prolines 102 and 105 and the Surrounding Lysine Cluster Impede Amyloid Formation.Post-translational modifications in PrP expand the conformational diversity of prions in vivoSolution structure, conformational dynamics, and CD4-induced activation in full-length, glycosylated, monomeric HIV gp120The role of glycophosphatidylinositol anchor in the amplification of the scrapie isoform of prion protein in vitro.Mammalian prions generated from bacterially expressed prion protein in the absence of any mammalian cofactorsNa+/K+-ATPase is present in scrapie-associated fibrils, modulates PrP misfolding in vitro and links PrP function and dysfunction.Amyloid structure: conformational diversity and consequences.Probing the conformation of a prion protein fibril with hydrogen exchange.Identifying critical sites of PrP(c)-PrP(Sc) interaction in prion-infected cells by dominant-negative inhibition.Influence of pH on the human prion protein: insights into the early steps of misfolding.QUDeX-MS: hydrogen/deuterium exchange calculation for mass spectra with resolved isotopic fine structure.Elongation of mouse prion protein amyloid-like fibrils: effect of temperature and denaturant concentration.Structural determinants of phenotypic diversity and replication rate of human prions.How does domain replacement affect fibril formation of the rabbit/human prion proteinsA Structural and Functional Comparison Between Infectious and Non-Infectious Autocatalytic Recombinant PrP Conformers.Molecular pathogenesis of sporadic prion diseases in man.On-tissue Direct Monitoring of Global Hydrogen/Deuterium Exchange by MALDI Mass Spectrometry: Tissue Deuterium Exchange Mass Spectrometry (TDXMS).Prions and the potential transmissibility of protein misfolding diseasesConformational stability of mammalian prion protein amyloid fibrils is dictated by a packing polymorphism within the core region.Proteomics applications in prion biology and structure.Treatment with a non-toxic, self-replicating anti-prion delays or prevents prion disease in vivo.Evaluation of infective property of recombinant prion protein amyloids in cultured cells overexpressing cellular prion protein.Role of the central lysine cluster and scrapie templating in the transmissibility of synthetic prion protein aggregates.Epigallocatechin Gallate Remodels Overexpressed Functional Amyloids in Pseudomonas aeruginosa and Increases Biofilm Susceptibility to Antibiotic Treatment.C-Terminal Threonine Reduces Aβ43 Amyloidogenicity Compared with Aβ42.Polymorphism of amyloid-like fibrils can be defined by the concentration of seeds.Rapid α-oligomer formation mediated by the Aβ C terminus initiates an amyloid assembly pathway.Cofactor molecules induce structural transformation during infectious prion formation.Conserved amyloid core structure of stop mutants of the human prion protein.Conformational properties of prion strains can be transmitted to recombinant prion protein fibrils in real-time quaking-induced conversion.Applying the tools of chemistry (mass spectrometry and covalent modification by small molecule reagents) to the detection of prions and the study of their structure.Recombinant PrPSc shares structural features with brain-derived PrPSc: Insights from limited proteolysis.Artificial strain of human prions created in vitro.
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Distinct structures of scrapie prion protein (PrPSc)-seeded versus spontaneous recombinant prion protein fibrils revealed by hydrogen/deuterium exchange.
description
article científic
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article scientifique
@fr
articolo scientifico
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artigo científico
@pt
bilimsel makale
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scientific article published on 13 July 2009
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Distinct structures of scrapie ...... y hydrogen/deuterium exchange.
@en
Distinct structures of scrapie prion protein
@nl
type
label
Distinct structures of scrapie ...... y hydrogen/deuterium exchange.
@en
Distinct structures of scrapie prion protein
@nl
prefLabel
Distinct structures of scrapie ...... y hydrogen/deuterium exchange.
@en
Distinct structures of scrapie prion protein
@nl
P2093
P2860
P50
P356
P1476
Distinct structures of scrapie ...... by hydrogen/deuterium exchange
@en
P2093
Jae-Il Kim
Ryuichiro Atarashi
Witold K Surewicz
P2860
P304
24233-24241
P356
10.1074/JBC.M109.036558
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P577
2009-07-13T00:00:00Z