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. - Wikidata - awgldk - TriplyDB

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.

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.

http://www.wikidata.org/entity/Q34512151

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Multifaceted Role of Sialylation in Prion Diseases Yeast prions: structure, biology, and prion-handling systems Antiparallel -sheet architecture in Iowa-mutant -amyloid fibrils Crystal Structure of a Human Prion Protein Fragment Reveals a Motif for Oligomer Formation Critical significance of the region between Helix 1 and 2 for efficient dominant-negative inhibition by conversion-incompetent prion protein A general Monte Carlo/simulated annealing algorithm for resonance assignment in NMR of uniformly labeled biopolymers Parallel in-register intermolecular β-sheet architectures for prion-seeded prion protein (PrP) amyloids.Progress towards structural understanding of infectious sheep PrP-amyloid.Globular domain of the prion protein needs to be unlocked by domain swapping to support prion protein conversion Dynamic diagnosis of familial prion diseases supports the β2-α2 loop as a universal interference target.Molecular structure of amyloid fibrils controls the relationship between fibrillar size and toxicity.Structure-based drug design identifies polythiophenes as antiprion compounds.Physical and structural basis for polymorphism in amyloid fibrils Structural evolution of Iowa mutant β-amyloid fibrils from polymorphic to homogeneous states under repeated seeded growth Structural insights into functional and pathological amyloid.Elongation of mouse prion protein amyloid-like fibrils: effect of temperature and denaturant concentration.Intermolecular alignment in Y145Stop human prion protein amyloid fibrils probed by solid-state NMR spectroscopy PrP assemblies: spotting the responsible regions in prion propagation.On the problem of resonance assignments in solid state NMR of uniformly ¹⁵N,¹³C-labeled proteins.Fibril formation of the rabbit/human/bovine prion proteins Interaction of prion protein with acetylcholinesterase: potential pathobiological implications in prion diseases.Protein folding activity of the ribosome (PFAR) -- a target for antiprion compounds How does domain replacement affect fibril formation of the rabbit/human prion proteins Segmental polymorphism in a functional amyloid.Amyloid polymorphism: structural basis and neurobiological relevance.Structural polymorphism in amyloids: new insights from studies with Y145Stop prion protein fibrils.Non-reducing alkaline solubilization and rapid on-column refolding of recombinant prion protein.Integrity of helix 2-helix 3 domain of the PrP protein is not mandatory for prion replication.PrP charge structure encodes interdomain interactions Enhanced sensitivity by nonuniform sampling enables multidimensional MAS NMR spectroscopy of protein assemblies.Secondary-structure prediction revisited: Theoretical β-sheet propensity and coil propensity represent structures of amyloids and aid in elucidating phenomena involved in interspecies transmission of prions.Dissecting structure of prion amyloid fibrils by hydrogen-deuterium exchange ultraviolet Raman spectroscopy.Parallel β-sheet vibrational couplings revealed by 2D IR spectroscopy of an isotopically labeled macrocycle: quantitative benchmark for the interpretation of amyloid and protein infrared spectra.Helices 2 and 3 are the initiation sites in the PrP(C) → PrP(SC) transition Prions and the potential transmissibility of protein misfolding diseases Decrypting Prion Protein Conversion into a β-Rich Conformer by Molecular Dynamics Intrinsically semi-disordered state and its role in induced folding and protein aggregation Prion nucleation site unmasked by transient interaction with phospholipid cofactor.The role of RNA in mammalian prion protein conversion.Prion protein oligomer and its neurotoxicity.

P2860

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P2860

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.

http://www.wikidata.org/entity/Q34512151

description

2010 nî lūn-bûn

@nan

2010 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

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2010 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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The α-helical C-terminal domai ...... te nuclear magnetic resonance.

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The α-helical C-terminal domai ...... te nuclear magnetic resonance.

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The α-helical C-terminal domai ...... te nuclear magnetic resonance.

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The α-helical C-terminal domai ...... te nuclear magnetic resonance.

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The α-helical C-terminal domai ...... te nuclear magnetic resonance.

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Ilia V Baskakov

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Natallia Makarava

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Regina Savtchenko

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Valeriy G Ostapchenko

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P2860

Generating a prion with bacterially expressed recombinant prion protein.

Recombinant prion protein induces a new transmissible prion disease in wild-type animals.

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

Molecular structural basis for polymorphism in Alzheimer's -amyloid fibrils

1H, 13C and 15N chemical shift referencing in biomolecular NMR

NMRPipe: a multidimensional spectral processing system based on UNIX pipes

Supramolecular structure in full-length Alzheimer's beta-amyloid fibrils: evidence for a parallel beta-sheet organization from solid-state nuclear magnetic resonance.

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

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9488-9497

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scholarly article

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10.1021/BI1013134

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20925423

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3025268

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