Filaments of the Ure2p prion protein have a cross-beta core structure.
about
Fibrillogenesis of huntingtin and other glutamine containing proteinsYeast prions: structure, biology, and prion-handling systemsThe structure of a polyQ-anti-polyQ complex reveals binding according to a linear lattice modelPrion amyloid structure explains templating: how proteins can be genes.Parallel beta-sheets and polar zippers in amyloid fibrils formed by residues 10-39 of the yeast prion protein Ure2p.Structure of the prion Ure2p in protein fibrils assembled in vitro.Molecular structures of quiescently grown and brain-derived polymorphic fibrils of the Alzheimer amyloid abeta9-40 peptide: a comparison to agitated fibrils.Yeast prions assembly and propagation: contributions of the prion and non-prion moieties and the nature of assemblies.Amyloid structure and assembly: insights from scanning transmission electron microscopy.New insights into the molecular mechanism of amyloid formation from cysteine scanning.The core of Ure2p prion fibrils is formed by the N-terminal segment in a parallel cross-β structure: evidence from solid-state NMR.Beta arcades: recurring motifs in naturally occurring and disease-related amyloid fibrilsPrion generation in vitro: amyloid of Ure2p is infectious.Viruses and prions of Saccharomyces cerevisiaePrions: En route from structural models to structures.Physical and structural basis for polymorphism in amyloid fibrilsThe relationship of prions and translationPrion-forming ability of Ure2 of yeasts is not evolutionarily conserved.Self-Assembly of Amyloid Fibrils That Display Active Enzymes.Prions in yeast.Insights into the architecture of the Ure2p yeast protein assemblies from helical twisted fibrilsNanoimaging for protein misfolding and related diseases.The structural biology of protein aggregation diseases: Fundamental questions and some answersStructural basis of infectious and non-infectious amyloidsThe functional curli amyloid is not based on in-register parallel beta-sheet structureFunctional amyloids signal their arrival.The yeast prion protein Ure2: insights into the mechanism of amyloid formation.Molecular interactions of amyloid nanofibrils with biological aggregation modifiers: implications for cytotoxicity mechanisms and biomaterial design.Resveratrol selectively remodels soluble oligomers and fibrils of amyloid Abeta into off-pathway conformersIn vitro analysis of SpUre2p, a prion-related protein, exemplifies the relationship between amyloid and prion.
P2860
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P2860
Filaments of the Ure2p prion protein have a cross-beta core structure.
description
2005 nî lūn-bûn
@nan
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
2005年论文
@zh
2005年论文
@zh-cn
name
Filaments of the Ure2p prion protein have a cross-beta core structure.
@en
type
label
Filaments of the Ure2p prion protein have a cross-beta core structure.
@en
prefLabel
Filaments of the Ure2p prion protein have a cross-beta core structure.
@en
P2093
P1476
Filaments of the Ure2p prion protein have a cross-beta core structure
@en
P2093
Alasdair C Steven
David R Davies
Deepak Sharma
Hideyo Inouye
Naiqian Cheng
Reed B Wickner
Thang K Chiu
Ulrich Baxa
P304
P356
10.1016/J.JSB.2005.02.007
P577
2005-05-01T00:00:00Z