Domain organization and structure-function relationship of the HET-s prion protein of Podospora anserina. - Wikidata - wikimedia - TriplyDB

Domain organization and structure-function relationship of the HET-s prion protein of Podospora anserina.

Domain organization and structure-function relationship of the HET-s prion protein of Podospora anserina.

http://www.wikidata.org/entity/Q39756452

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The mechanism of prion inhibition by HET-S Characterization of the native and fibrillar conformation of the human Nalpha-acetyltransferase ARD1 Comparative analysis of programmed cell death pathways in filamentous fungi As a toxin dies a prion comes to life: A tentative natural history of the [Het-s] prion The prion gene is associated with human long-term memory Screening for toxic amyloid in yeast exemplifies the role of alternative pathway responsible for cytotoxicity Line-Broadening in Low-Temperature Solid-State NMR Spectra of Fibrils.Insight into the structure of amyloid fibrils from the analysis of globular proteins.Contribution of specific residues of the β-solenoid fold to HET-s prion function, amyloid structure and stability.Analyzing the birth and propagation of two distinct prions, [PSI+] and [Het-s](y), in yeast.Origins and evolution of the HET-s prion-forming protein: searching for other amyloid-forming solenoids.Prions: En route from structural models to structures.Amyloid structure: conformational diversity and consequences.Genomic clustering and homology between HET-S and the NWD2 STAND protein in various fungal genomes The [Het-s] prion, an amyloid fold as a cell death activation trigger Heterogeneous seeding of HET-s(218-289) and the mutability of prion structures.Sporadic distribution of prion-forming ability of Sup35p from yeasts and fungi.Structure-based drug design identifies polythiophenes as antiprion compounds.The mechanism of toxicity in HET-S/HET-s prion incompatibility.The [URE3] prion is not conserved among Saccharomyces species Structural dependence of HET-s amyloid fibril infectivity assessed by cryoelectron microscopy Towards revealing the structure of bacterial inclusion bodies.Lysophospholipid-containing membranes modulate the fibril formation of the repeat domain of a human functional amyloid, pmel17.Protein inheritance (prions) based on parallel in-register beta-sheet amyloid structures.Correlation of structural elements and infectivity of the HET-s prion.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.Signal transduction by a fungal NOD-like receptor based on propagation of a prion amyloid fold Dual conformation of H2H3 domain of prion protein in mammalian cells.Probing fibril dissolution of the repeat domain of a functional amyloid, Pmel17, on the microscopic and residue level Localization of HET-S to the cell periphery, not to [Het-s] aggregates, is associated with [Het-s]-HET-S toxicity.Amyloid fibril formation by the glaucoma-associated olfactomedin domain of myocilin.Identification of a novel cell death-inducing domain reveals that fungal amyloid-controlled programmed cell death is related to necroptosis.Degradation of fungal prion HET-s(218-289) induces formation of a generic amyloid fold A non-Q/N-rich prion domain of a foreign prion, [Het-s], can propagate as a prion in yeast.Role of Hsp104 in the propagation and inheritance of the [Het-s] prion.Nucleation-dependent conformational conversion of the Y145Stop variant of human prion protein: structural clues for prion propagation.Prions of fungi: inherited structures and biological roles Structural basis of infectious and non-infectious amyloids The yeast Sup35NM domain propagates as a prion in mammalian cells.

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Domain organization and structure-function relationship of the HET-s prion protein of Podospora anserina.

http://www.wikidata.org/entity/Q39756452

description

2003 nî lūn-bûn

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2003年の論文

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年學術文章

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2003年學術文章

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2003年學術文章

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Domain organization and struct ...... protein of Podospora anserina.

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Domain organization and struct ...... protein of Podospora anserina.

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Domain organization and struct ...... protein of Podospora anserina.

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Domain organization and struct ...... protein of Podospora anserina.

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Domain organization and struct ...... protein of Podospora anserina.

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Domain organization and struct ...... protein of Podospora anserina.

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The EMBO Journal

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Domain organization and struct ...... protein of Podospora anserina.

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P2093

Axelle Balguerie

http://www.w3.org/2001/XMLSchema#string

Bénédicte Coulary-Salin

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Christiane Ritter

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Ioan Lascu

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Jean-Marie Schmitter

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Katell Bathany

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Roland Riek

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Stéphane Chaignepain

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Suzana Dos Reis

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Sven J Saupe

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P2860

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

Extent of N-terminal methionine excision from Escherichia coli proteins is governed by the side-chain length of the penultimate amino acid

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

Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution

Protein misfolding, evolution and disease

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

Proposal for a common nomenclature for sequence ions in mass spectra of peptides

Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S. cerevisiae.

Molecular genetics of heterokaryon incompatibility in filamentous ascomycetes.

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2071-2081

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10.1093/EMBOJ/CDG213

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9

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22

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2003-05-01T00:00:00Z

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232797574

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12727874

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Prion protein family

protein structure

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156085

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