Unraveling infectious structures, strain variants and species barriers for the yeast prion [PSI+].
about
Prions, protein homeostasis, and phenotypic diversityMechanisms of amyloid formation revealed by solution NMRSup35 methionine oxidation is a trigger for de novo [PSI(+)] prion formationHigh-throughput analysis of concentration-dependent antibody self-association.Optical trapping with high forces reveals unexpected behaviors of prion fibrils.A synergistic small-molecule combination directly eradicates diverse prion strain structuresAmyloid fibers provide structural integrity to Bacillus subtilis biofilms.Ribosome-associated peroxiredoxins suppress oxidative stress-induced de novo formation of the [PSI+] prion in yeast.Principles governing oligomer formation in amyloidogenic peptides.[PSI+] maintenance is dependent on the composition, not primary sequence, of the oligopeptide repeat domain.The prion hypothesis: from biological anomaly to basic regulatory mechanism.Relationship between prion propensity and the rates of individual molecular steps of fibril assembly.Looked at life from both sides nowOpposing effects of glutamine and asparagine govern prion formation by intrinsically disordered proteins.Role of water in protein aggregation and amyloid polymorphism.Structural polymorphism in amyloids: new insights from studies with Y145Stop prion protein fibrils.Differences in prion strain conformations result from non-native interactions in a nucleus.Prions in yeast.Distinct Prion Domain Sequences Ensure Efficient Amyloid Propagation by Promoting Chaperone Binding or Processing In Vivo.Computer simulation study of amyloid fibril formation by palindromic sequences in prion peptidesStrain conformation, primary structure and the propagation of the yeast prion [PSI+].Hsp104 drives "protein-only" positive selection of Sup35 prion strains encoding strong [PSI(+)].Cellular strategies for regulating functional and nonfunctional protein aggregation.A Decentralized Approach to the Formulation of Hypotheses: A Hierarchical Structural Model for a Prion Self-Assembled SystemIon-specific effects on prion nucleation and strain formation.Interaction of human laminin receptor with Sup35, the [PSI⁺] prion-forming protein from S. cerevisiae: a yeast model for studies of LamR interactions with amyloidogenic proteinsAggregation of scaffolding protein DISC1 dysregulates phosphodiesterase 4 in Huntington's diseaseEmergence and natural selection of drug-resistant prions.The elusive middle domain of Hsp104 and ClpB: location and function.Self-propagating amyloid as a critical regulator for diverse cellular functions.RepA-WH1 prionoid: a synthetic amyloid proteinopathy in a minimalist hostMechanistic and Structural Insights into the Prion-Disaggregase Activity of Hsp104.Prion-like proteins and their computational identification in proteomes.Expanding the yeast prion world: Active prion conversion of non-glutamine/asparagine-rich Mod5 for cell survival.Site-specific structural analysis of a yeast prion strain with species-specific seeding activity.Engineered bacterial hydrophobic oligopeptide repeats in a synthetic yeast prion, [REP-PSI (+)].Countering amyloid polymorphism and drug resistance with minimal drug cocktails.Enabling stop codon read-through translation in bacteria as a probe for amyloid aggregation.Visualization of transient protein-protein interactions that promote or inhibit amyloid assembly.Conformational features of tau fibrils from Alzheimer's disease brain are faithfully propagated by unmodified recombinant protein.
P2860
Q24610666-1F2F445A-F157-473F-AFF4-008A3775FBA6Q26797492-4EEC0F65-E80C-4435-A7EE-7A72C6120486Q26798417-376D4E00-F9E7-4E82-AF3B-9305360287DCQ30462680-F172468D-9CEF-4D4B-BE99-7B7F6C394011Q30504869-97F0C965-9024-4C42-903C-B51CDD036273Q30885765-5098F268-57F2-45C4-B2F3-B8EBA1DE72ECQ33719842-2F00963C-9459-4B32-98F7-1E778E63C56CQ33778624-A7E28D7D-552B-4FAE-A014-9A938C7914E3Q33787635-C24254B0-499E-4E12-AB16-32EB8A9A1B48Q33961634-6EB0F90C-4930-4FD2-8EB9-FD7CD9A113DDQ34412881-67096BFB-4A77-4182-99DA-162F05C1B827Q34752080-8C88B020-9ECA-4A7B-83C1-55E06E8D0411Q34829539-086CD8BE-8EEC-48AE-B2F8-D776E42EA182Q35094005-B729DCD7-7309-4A2D-88C3-086695F44E12Q35556010-1A014CF3-C443-4B74-AC28-038DB28CB2B5Q35604887-8C719B1F-5310-420F-8EF8-B9B6E88C80CDQ35751972-808B4BD4-E0BD-4AA9-A329-BC92903238BDQ36154362-E7848DDA-B18A-45BF-906E-DF2F4F951EA3Q36182814-3D7E7244-BC06-4E1B-B470-B8339DE88140Q36251051-95690821-0117-43D9-A0D9-6BDA8B49CF6CQ36375495-3F721D98-D811-40F9-870B-840950E2306FQ36429359-7246B3F3-006B-43F3-A1EB-07FA5BC10DB0Q36713371-B8ABA96F-0069-4060-A195-0025EE21EE9FQ37134269-E9B70E8B-E46A-4EDD-B901-6C17CE73E3C2Q37234018-2DB05F3D-C021-4DBC-8544-B9FF1F4BEA16Q37453424-2F734057-F05C-43C9-BCB1-85B2D3EBFA98Q37730673-F2E5D87C-2913-4268-86E0-870697FE2673Q37737577-E3813240-8D6D-41C5-94CE-77BA48BAC144Q37917880-B5AACB91-A311-4363-9D68-B52626931511Q38202935-8654501E-C2A2-4348-8873-8F4301CB12C1Q38297136-AE5D02A0-41D1-4674-89D6-78DB093B4493Q38648239-0263AA01-3F7E-4B17-A20A-72CB0ED8CE42Q39167900-6EC5989D-428B-4014-ADF6-A5DBA1F87AC8Q39332640-3D631AA1-DE49-4048-A64F-DA942E330C40Q39440212-AA99CB20-9716-44D1-8FA8-984E297E58A4Q39835239-FD59BF80-82C8-4375-9559-1FBDC45D9843Q40749941-6B12FFA4-60F6-4F25-A3B7-E50B16AFABA1Q41703556-E175B129-A147-426F-8D8F-8E22A4965508Q42062269-AB63E9F1-9310-465C-8211-D4FBF9D73BF3Q42082255-48642952-156A-4DF0-95B6-6C886A181C8E
P2860
Unraveling infectious structures, strain variants and species barriers for the yeast prion [PSI+].
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
2009年论文
@zh
2009年论文
@zh-cn
name
Unraveling infectious structur ...... rs for the yeast prion [PSI+].
@ast
Unraveling infectious structur ...... rs for the yeast prion [PSI+].
@en
type
label
Unraveling infectious structur ...... rs for the yeast prion [PSI+].
@ast
Unraveling infectious structur ...... rs for the yeast prion [PSI+].
@en
prefLabel
Unraveling infectious structur ...... rs for the yeast prion [PSI+].
@ast
Unraveling infectious structur ...... rs for the yeast prion [PSI+].
@en
P2860
P356
P1476
Unraveling infectious structur ...... rs for the yeast prion [PSI+].
@en
P2860
P2888
P304
P356
10.1038/NSMB.1617
P577
2009-06-01T00:00:00Z