Amyloid of Rnq1p, the basis of the [PIN+] prion, has a parallel in-register beta-sheet structure - Test2 - elhamkhani - TriplyDB

Amyloid of Rnq1p, the basis of the [PIN+] prion, has a parallel in-register beta-sheet structure

Amyloid of Rnq1p, the basis of the [PIN+] prion, has a parallel in-register beta-sheet structure

http://www.wikidata.org/entity/Q24653587

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Modulation and elimination of yeast prions by protein chaperones and co-chaperones Yeast prions: structure, biology, and prion-handling systems The [RNQ+] prion: a model of both functional and pathological amyloid Intermolecular structure determination of amyloid fibrils with magic-angle spinning and dynamic nuclear polarization NMR.Parallel in-register intermolecular β-sheet architectures for prion-seeded prion protein (PrP) amyloids.Prion amyloid structure explains templating: how proteins can be genes.Synchrotron infrared microspectroscopy detecting the evolution of Huntington's disease neuropathology and suggesting unique correlates of dysfunction in white versus gray brain matter.Implications of protein structure instability: from physiological to pathological secondary structure.Getting a grip on prions: oligomers, amyloids, and pathological membrane interactions.Utilizing NMR and EPR spectroscopy to probe the role of copper in prion diseases.BETASCAN: probable beta-amyloids identified by pairwise probabilistic analysis.Measurement of amyloid fibril mass-per-length by tilted-beam transmission electron microscopy.Distinct type of transmission barrier revealed by study of multiple prion determinants of Rnq1.Amyloid structure and assembly: insights from scanning transmission electron microscopy.Use of yeast as a system to study amyloid toxicity Analyzing the birth and propagation of two distinct prions, [PSI+] and [Het-s](y), in yeast.The core of Ure2p prion fibrils is formed by the N-terminal segment in a parallel cross-β structure: evidence from solid-state NMR.Characterization of prion-like conformational changes of the neuronal isoform of Aplysia CPEB Seeding specificity and ultrastructural characteristics of infectious recombinant prions.Viruses and prions of Saccharomyces cerevisiae Prions: En route from structural models to structures.Amyloid structure: conformational diversity and consequences.Sporadic distribution of prion-forming ability of Sup35p from yeasts and fungi.The α-helical C-terminal domain of full-length recombinant PrP converts to an in-register parallel β-sheet structure in PrP fibrils: evidence from solid state nuclear magnetic resonance.Structural characterization of GNNQQNY amyloid fibrils by magic angle spinning NMR Physical and structural basis for polymorphism in amyloid fibrils The [PSI+] prion exists as a dynamic cloud of variants The relationship of prions and translation Repeat domains of melanosome matrix protein Pmel17 orthologs form amyloid fibrils at the acidic melanosomal pH.Structural evolution of Iowa mutant β-amyloid fibrils from polymorphic to homogeneous states under repeated seeded growth Heteronuclear proton assisted recoupling Protein inheritance (prions) based on parallel in-register beta-sheet amyloid structures.Structural insights into functional and pathological amyloid.Prion diseases of yeast: amyloid structure and biology.Amyloid of the Candida albicans Ure2p prion domain is infectious and has an in-register parallel β-sheet structure.A small, glutamine-free domain propagates the [SWI(+)] prion in budding yeast.Comparison of β-sheets of capped polyalanine with those of the tau-amyloid structures VQIVYK and VQIINK. A density functional theory study.Amyloid-like fibrils from a domain-swapping protein feature a parallel, in-register conformation without native-like interactions.Hierarchical organization in the amyloid core of yeast prion protein Ure2.Solid-state NMR studies of amyloid fibril structure

P2860

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P2860

Amyloid of Rnq1p, the basis of the [PIN+] prion, has a parallel in-register beta-sheet structure

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2008 nî lūn-bûn

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Genetic and environmental factors affecting the de novo appearance of the [PSI+] prion in Saccharomyces cerevisiae

Structure of the cross-beta spine of amyloid-like fibrils

Amyloid of the prion domain of Sup35p has an in-register parallel beta-sheet structure

High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy

Atomic structures of amyloid cross-beta spines reveal varied steric zippers

Prions affect the appearance of other prions: the story of [PIN(+)].

[URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae

A structural model for Alzheimer's beta -amyloid fibrils based on experimental constraints from solid state NMR

Experimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrils

Multiple quantum solid-state NMR indicates a parallel, not antiparallel, organization of beta-sheets in Alzheimer's beta-amyloid fibrils

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