Prion protein repeat expansion results in increased aggregation and reveals phenotypic variability.
about
Curli functional amyloid systems are phylogenetically widespread and display large diversity in operon and protein structureComplex adaptations can drive the evolution of the capacitor [PSI], even with realistic rates of yeast sexThe spontaneous appearance rate of the yeast prion [PSI+] and its implications for the evolution of the evolvability properties of the [PSI+] systemPrions, protein homeostasis, and phenotypic diversityThe strength of selection against the yeast prion [PSI+]Epigenetic principles and mechanisms underlying nervous system functions in health and diseaseThe [RNQ+] prion: a model of both functional and pathological amyloidThe complexity and implications of yeast prion domainsProbing the role of structural features of mouse PrP in yeast by expression as Sup35-PrP fusionsPrion protein insertional mutations increase aggregation propensity but not fiber stability.Parallels between pathogens and gluten peptides in celiac sprueDisease-associated mutant ubiquitin causes proteasomal impairment and enhances the toxicity of protein aggregates.The number and transmission of [PSI] prion seeds (Propagons) in the yeast Saccharomyces cerevisiae.Heterologous prion interactions are altered by mutations in the prion protein Rnq1p.Compositional determinants of prion formation in yeast[PSI+] maintenance is dependent on the composition, not primary sequence, of the oligopeptide repeat domain.Conserved roles of the prion protein domains on subcellular localization and cell-cell adhesionEvolutionary insight into the functional amyloids of the pseudomonads.Generating new prions by targeted mutation or segment duplication.De novo design of synthetic prion domains.Prions in yeast.Distinct Prion Domain Sequences Ensure Efficient Amyloid Propagation by Promoting Chaperone Binding or Processing In Vivo.Mutants of the Paf1 complex alter phenotypic expression of the yeast prion [PSI+]Screening for amyloid aggregation by Semi-Denaturing Detergent-Agarose Gel ElectrophoresisInsights into intragenic and extragenic effectors of prion propagation using chimeric prion proteins.Prion formation by a yeast GLFG nucleoporin.Engineered bacterial hydrophobic oligopeptide repeats in a synthetic yeast prion, [REP-PSI (+)].Heterologous prion-forming proteins interact to cross-seed aggregation in Saccharomyces cerevisiae.Expression of human FUS/TLS in yeast leads to protein aggregation and cytotoxicity, recapitulating key features of FUS proteinopathy.Yeast models for amyloid disease.Prion protein modulates glucose homeostasis by altering intracellular iron.
P2860
Q21090831-2BF72599-8F07-4711-9AB7-AC87429D20AEQ21563345-6386E646-DE41-42A6-B815-515A12B940E9Q22065131-7E4E60D1-BFE9-436C-94D8-FA941E8B8325Q24610666-5AB64732-F709-471B-934F-6B0A5584D37CQ24645062-C6B40EBC-74CF-4D1B-9F46-BA37B6864634Q24657549-7E087DEC-88D9-4D4C-8ED8-5B0EEC0A09DEQ27008442-6E2E0D45-09DF-4EC1-BBB3-124CBE27A083Q27015164-C7828867-1576-429E-8A29-21848CD43D93Q27022544-CDA41FE0-E877-41F6-A171-04CC985DE0B0Q33325657-3C843ED5-DADA-49CF-BED1-C67741C287EDQ33329537-8C1479CB-768A-4086-9CEC-6280E3498994Q33408783-19A5B5EE-B47F-464E-8072-383AB3FB854DQ33415032-EFAA3ABA-D123-4CD0-B428-3260C1512DD2Q33422679-DEE24661-82CD-41FA-93D1-27FFCBC7C9A4Q33558139-295B0B8D-DC06-4B34-9897-CA995D654234Q33961634-7742CDF5-2874-4B97-9CC2-965B09CC7106Q34922583-EB92512C-1128-4317-96D3-AD28EED97530Q35014769-0C1CE3AB-E8B0-4B56-B17E-EA2E4112B944Q35865739-2A1AFDB0-E89B-4D83-AC62-1114384F02A5Q35921831-C01787CC-84F4-4236-9260-7FEB70535AD3Q36154362-08D54F50-0983-47B7-AE33-47E338866591Q36182814-D035DAF9-1B22-4446-99B3-B3BC3ADB1154Q37158405-1F2C598F-2969-4324-A571-4AC1813AF020Q37296945-4E1C4D8B-5BEA-4263-8D3B-E3697DCF044DQ37355539-9F137020-25DE-4CCE-BE06-BA7A2B5DCA05Q39331113-BD76FF01-F4E9-4A06-849E-78C29A6904DEQ39835239-87D70C13-E9D6-49CE-8117-2C39895B94E4Q41062902-4AE7C059-4533-4C6F-80E9-5FE53E75F517Q42732668-03260431-BEAE-4C75-9E9C-9314F056CC89Q43452372-7328B2B1-C4C1-411F-8E05-43FF0ADC37A9Q55285231-021F2F9C-B692-48AF-AEFC-18D313E7C238
P2860
Prion protein repeat expansion results in increased aggregation and reveals phenotypic variability.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
Prion protein repeat expansion ...... eveals phenotypic variability.
@ast
Prion protein repeat expansion ...... eveals phenotypic variability.
@en
type
label
Prion protein repeat expansion ...... eveals phenotypic variability.
@ast
Prion protein repeat expansion ...... eveals phenotypic variability.
@en
prefLabel
Prion protein repeat expansion ...... eveals phenotypic variability.
@ast
Prion protein repeat expansion ...... eveals phenotypic variability.
@en
P2093
P2860
P356
P1476
Prion protein repeat expansion ...... reveals phenotypic variability
@en
P2093
Amar A Desai
Elizabeth M H Tank
Heather L True
P2860
P304
P356
10.1128/MCB.02127-06
P407
P577
2007-06-04T00:00:00Z