Correlation of structural elements and infectivity of the HET-s prion. - Wikidata - wikimedia - TriplyDB

Correlation of structural elements and infectivity of the HET-s prion.

Correlation of structural elements and infectivity of the HET-s prion.

http://www.wikidata.org/entity/Q35031685

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A scientific revolution? The prion anomaly may challenge the central dogma of molecular biology The mechanism of prion inhibition by HET-S Amyloid of Rnq1p, the basis of the [PIN+] prion, has a parallel in-register beta-sheet structure Amyloid of the prion domain of Sup35p has an in-register parallel beta-sheet structure Mechanisms of amyloid formation revealed by solution NMR The yeast prions [PSI+] and [URE3] are molecular degenerative diseases Potential roles for prions and protein-only inheritance in cancer As a toxin dies a prion comes to life: A tentative natural history of the [Het-s] prion Yeast prions: structure, biology, and prion-handling systems Development and application of STEM for the biological sciences Dipole tensor-based atomic-resolution structure determination of a nanocrystalline protein by solid-state NMR Paramagnetic shifts in solid-state NMR of proteins to elicit structural information High-Resolution Solid-State NMR Structure of a 17.6 kDa Protein The amyloid-Congo red interface at atomic resolution Structural basis for recognition of synaptic vesicle protein 2C by botulinum neurotoxin A Structural basis for the recognition and cross-linking of amyloid fibrils by human apolipoprotein E Experimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrils Screening for toxic amyloid in yeast exemplifies the role of alternative pathway responsible for cytotoxicity Unlike twins: an NMR comparison of two α-synuclein polymorphs featuring different toxicity 3D structure of Alzheimer's amyloid-beta(1-42) fibrils Intermolecular structure determination of amyloid fibrils with magic-angle spinning and dynamic nuclear polarization NMR.Effect of the amyloid β hairpin's structure on the handedness of helices formed by its aggregates.Structural analysis and mapping of individual protein complexes by infrared nanospectroscopy.Two-dimensional solid-state NMR applied to a chimeric potassium channel.β-Helical architecture of cytoskeletal bactofilin filaments revealed by solid-state NMR.Prion amyloid structure explains templating: how proteins can be genes.Getting a grip on prions: oligomers, amyloids, and pathological membrane interactions.Mechanistic and environmental control of the prevalence and lifetime of amyloid oligomers Quantitative analysis of the water occupancy around the selectivity filter of a K+ channel in different gating modes.Synthesis and structural investigations of N-alkylated beta-peptidosulfonamide-peptide hybrids of the amyloidogenic amylin(20-29) sequence: Implications of supramolecular folding for the design of peptide-based bionanomaterials.Polymorphic fibril formation by residues 10-40 of the Alzheimer's beta-amyloid peptide.Solid-state NMR spectroscopy reveals that water is nonessential to the core structure of alpha-synuclein fibrils Insight into the structure of amyloid fibrils from the analysis of globular proteins.AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides.Metal ion-dependent, reversible, protein filament formation by designed beta-roll polypeptides.Bacterial inclusion bodies contain amyloid-like structure Exploring beta-sheet structure and interactions with chemical model systems.Solid-state NMR evidence for inequivalent GvpA subunits in gas vesicles Molecular dynamics simulations to gain insights into the stability and morphologies of K3 oligomers from beta2-microglobulin.BETASCAN: probable beta-amyloids identified by pairwise probabilistic analysis.

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Correlation of structural elements and infectivity of the HET-s prion.

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2005年の論文

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Correlation of structural elements and infectivity of the HET-s prion.

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Correlation of structural elements and infectivity of the HET-s prion.

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Correlation of structural elements and infectivity of the HET-s prion.

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Correlation of structural elements and infectivity of the HET-s prion.

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Correlation of structural elements and infectivity of the HET-s prion.

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Correlation of structural elements and infectivity of the HET-s prion.

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Correlation of structural elements and infectivity of the HET-s prion.

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Ansgar B Siemer

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Christiane Ritter

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Marie-Lise Maddelein

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Matthias Ernst

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Roland Riek

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Thorsten Lührs

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P2860

Amyloid aggregates of the HET-s prion protein are infectious.

The protein product of the het-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog

The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data

Novel proteinaceous infectious particles cause scrapie

Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils

Solid-state NMR studies of the secondary structure of a mutant prion protein fragment of 55 residues that induces neurodegeneration.

The sequences appended to the amyloid core region of the HET-s prion protein determine higher-order aggregate organization in vivo.

Molecular genetics of heterokaryon incompatibility in filamentous ascomycetes.

Does the agent of scrapie replicate without nucleic acid?

Synthetic mammalian prions.

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Prion protein family

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