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The role of the N-terminal oligopeptide repeats of the yeast Sup35 prion protein in propagation and transmission of prion variantsMutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALSIs tau ready for admission to the prion club?Appearance and propagation of polyglutamine-based amyloids in yeast: tyrosine residues enable polymer fragmentationA systematic survey identifies prions and illuminates sequence features of prionogenic proteinsAmyloid of the prion domain of Sup35p has an in-register parallel beta-sheet structurePrion-like domains as epigenetic regulators, scaffolds for subcellular organization, and drivers of neurodegenerative diseaseFuzzy complexes: Specific binding without complete foldingThe yeast prions [PSI+] and [URE3] are molecular degenerative diseasesYeast prions and human prion-like proteins: sequence features and prediction methodsYeast prions: structure, biology, and prion-handling systemsThe complexity and implications of yeast prion domainsStrategies for identifying new prions in yeastDeterminants of Amyloid Formation for the Yeast Termination Factor Nab3Prion amyloid structure explains templating: how proteins can be genes.Prions, amyloids, and RNA: Pieces of a puzzle.Compositional determinants of prion formation in yeastYeast prions assembly and propagation: contributions of the prion and non-prion moieties and the nature of assemblies.The clustering and spatial arrangement of beta-sheet sequence, but not order, govern alpha-synuclein fibrillogenesisContribution of specific residues of the β-solenoid fold to HET-s prion function, amyloid structure and stability.Effect of domestication on the spread of the [PIN+] prion in Saccharomyces cerevisiae.[PSI+] maintenance is dependent on the composition, not primary sequence, of the oligopeptide repeat domain.PrionHome: a database of prions and other sequences relevant to prion phenomena.The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease.The prion hypothesis: from biological anomaly to basic regulatory mechanism.The effects of amino acid composition of glutamine-rich domains on amyloid formation and fragmentation.Prion domain of yeast Ure2 protein adopts a completely disordered structure: a solid-support EPR studyRepeat domains of melanosome matrix protein Pmel17 orthologs form amyloid fibrils at the acidic melanosomal pH.Discovering putative prion sequences in complete proteomes using probabilistic representations of Q/N-rich domains.Chromatin condensing functions of the linker histone C-terminal domain are mediated by specific amino acid composition and intrinsic protein disorder.Protein inheritance (prions) based on parallel in-register beta-sheet amyloid structures.Polycation-π interactions are a driving force for molecular recognition by an intrinsically disordered oncoprotein family.Prion diseases of yeast: amyloid structure and biology.Prion-forming ability of Ure2 of yeasts is not evolutionarily conserved.Distinct amino acid compositional requirements for formation and maintenance of the [PSI⁺] prion in yeast.Opposing effects of glutamine and asparagine govern prion formation by intrinsically disordered proteins.Increasing prion propensity by hydrophobic insertion.Amyloid of the Candida albicans Ure2p prion domain is infectious and has an in-register parallel β-sheet structure.Interaction networks of prion, prionogenic and prion-like proteins in budding yeast, and their role in gene regulationSolid-state NMR studies of amyloid fibril structure
P2860
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P2860
description
2005 nî lūn-bûn
@nan
2005 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Primary sequence independence for prion formation
@ast
Primary sequence independence for prion formation
@en
type
label
Primary sequence independence for prion formation
@ast
Primary sequence independence for prion formation
@en
prefLabel
Primary sequence independence for prion formation
@ast
Primary sequence independence for prion formation
@en
P2093
P2860
P356
P1476
Primary sequence independence for prion formation
@en
P2093
Eric D Ross
Herman K Edskes
Michael J Terry
P2860
P304
12825-12830
P356
10.1073/PNAS.0506136102
P407
P50
P577
2005-08-25T00:00:00Z