about
Prions, protein homeostasis, and phenotypic diversityAppearance and propagation of polyglutamine-based amyloids in yeast: tyrosine residues enable polymer fragmentationAmyloid of Rnq1p, the basis of the [PIN+] prion, has a parallel in-register beta-sheet structureA systematic survey identifies prions and illuminates sequence features of prionogenic proteinsMore than just trash bins? Potential roles for extracellular vesicles in the vertical and horizontal transmission of yeast prionsActin, Membrane Trafficking and the Control of Prion Induction, Propagation and Transmission in YeastAssessing the causes and consequences of co-polymerization in amyloid formationPrion strains and amyloid polymorphism influence phenotypic variationYeast prions: structure, biology, and prion-handling systemsThe [RNQ+] prion: a model of both functional and pathological amyloidCuring of the [URE3] prion by Btn2p, a Batten disease-related protein.Spontaneous variants of the [RNQ+] prion in yeast demonstrate the extensive conformational diversity possible with prion proteinsHeterologous cross-seeding mimics cross-species prion conversion in a yeast model.Prion amyloid structure explains templating: how proteins can be genes.De novo [PSI +] prion formation involves multiple pathways to form infectious oligomers.Heterologous prion interactions are altered by mutations in the prion protein Rnq1p.Distinct type of transmission barrier revealed by study of multiple prion determinants of Rnq1.Influence of prion variant and yeast strain variation on prion-molecular chaperone requirementsRequirements of Hsp104p activity and Sis1p binding for propagation of the [RNQ(+)] prionInvestigating the interactions of yeast prions: [SWI+], [PSI+], and [PIN+].Analyzing the birth and propagation of two distinct prions, [PSI+] and [Het-s](y), in yeast.[SWI], the prion formed by the chromatin remodeling factor Swi1, is highly sensitive to alterations in Hsp70 chaperone system activity.Prion formation and polyglutamine aggregation are controlled by two classes of genes.Myopathy-causing mutations in an HSP40 chaperone disrupt processing of specific client conformers.Analysis of the [RNQ+] prion reveals stability of amyloid fibers as the key determinant of yeast prion variant propagation.Low activity of select Hsp104 mutants is sufficient to propagate unstable prion variantsPolymorphism in Alzheimer Abeta amyloid organization reflects conformational selection in a rugged energy landscape.Prion-promoted phosphorylation of heterologous amyloid is coupled with ubiquitin-proteasome system inhibition and toxicity.Amyloid structure: conformational diversity and consequences.Sporadic distribution of prion-forming ability of Sup35p from yeasts and fungi.Hsp40s specify functions of Hsp104 and Hsp90 protein chaperone machines.The prion hypothesis: from biological anomaly to basic regulatory mechanism.Structural insights into a yeast prion illuminate nucleation and strain diversityConservation of a portion of the S. cerevisiae Ure2p prion domain that interacts with the full-length protein.Heterologous gln/asn-rich proteins impede the propagation of yeast prions by altering chaperone availabilityThe [URE3] prion is not conserved among Saccharomyces speciesDe novo appearance and "strain" formation of yeast prion [PSI+] are regulated by the heat-shock transcription factor.Destabilizing interactions among [PSI(+)] and [PIN(+)] yeast prion variants.Specificity of class II Hsp40 Sis1 in maintenance of yeast prion [RNQ+].Protein inheritance (prions) based on parallel in-register beta-sheet amyloid structures.
P2860
Q24610666-DBBD6F78-75B4-4C67-BF11-D379722F1327Q24648915-E4ECFD5E-34F7-4D40-89A8-CFEFCAA8B7B5Q24653587-7CA28334-D035-4ED6-BDE1-3905088664D4Q24658451-4D85755E-2497-4EC7-A973-0C650EFCF013Q26778300-1389C82F-49C9-4F32-A236-CCF3850AD00EQ26778771-31572F34-8EAF-4171-921A-CE25786C06A9Q26824195-A7A0D01E-BB30-4313-8704-CD36B6A1E77AQ26827209-B7862C86-9F61-4196-9DA7-10CE4B5EEE36Q27007482-6D3E9843-8263-4EBF-8954-E1B818F18C52Q27008442-3DA0F454-E4B2-4901-BD9D-EDCB0E7E8086Q27930078-BD03DF1E-CA9A-409D-9E07-038B788EDB11Q28534632-5E81BA78-635A-42EB-9D4C-BB1BFBF61E97Q30377551-673142BE-B21D-4542-8683-F959A4569A99Q30392820-CFD6931C-CDE8-4368-880D-F985A029C3F1Q30849388-382BD617-B1D7-4967-954F-A76E2779F9ACQ33422679-7470600F-F287-4069-A3F7-C344F0F38FC8Q33527001-281CC680-4470-4123-B3DA-975C5C6C1F90Q33575503-508DD5FB-1245-45A7-8271-0CEB37FB0318Q33576052-4650723E-A070-4746-813D-EA6A21B32BDFQ33779615-71E010FB-C2EC-4935-A807-6C80C9A91D81Q33818444-1773FF23-75B0-415B-A671-E429EB9E284FQ33838230-29507B17-860F-4F0D-981F-B3348352A89BQ33916796-DA27507F-31BB-4D98-9F53-C6C253282195Q33947263-EBE47AE2-A045-4B05-BE57-676FDBA3B8F4Q33966829-EA02ABB2-2447-4AFC-A6D9-EB68577150B2Q34051189-C6DB50B5-B35B-4E16-9091-FF28AA61D97AQ34059772-82B47D2F-FCFE-444F-965C-FC1B52611A0FQ34115717-9F3A86E3-F672-4E8D-97B0-83D9231EAF63Q34175001-5BB42D49-40F4-40DA-8859-1010D31B476DQ34336671-E5791FFA-3155-4986-8C02-14956A6F37D0Q34350913-BDE59F28-60CA-474E-9555-54B903D7AFE6Q34412881-740DBA41-6895-46F6-97FB-AFE475971984Q34425023-ADB5AE92-71C5-45B5-87F9-C8FF5D6FBA3EQ34443813-73DCF510-D755-4849-9027-D68FB4D8D714Q34566018-AB016339-3BB8-41D4-9124-93E33987FD1CQ34589020-54FAB55C-1B8E-4BF5-8783-D22EC5A6931FQ34611525-9CF38569-F89D-4C40-9C5A-63A613310075Q34619382-FE96FD9C-BA46-4061-BB0A-40A9C570A429Q34813968-72FBC3D2-129A-4E90-A285-74D6C7ACC5F3Q34911325-7739FFFC-081E-4376-B08F-11CD86F44D2A
P2860
description
2002 nî lūn-bûn
@nan
2002 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年学术文章
@wuu
2002年学术文章
@zh-cn
2002年学术文章
@zh-hans
2002年学术文章
@zh-my
2002年学术文章
@zh-sg
2002年學術文章
@yue
name
Interactions among prions and prion "strains" in yeast.
@ast
Interactions among prions and prion "strains" in yeast.
@en
Interactions among prions and prion "strains" in yeast.
@nl
type
label
Interactions among prions and prion "strains" in yeast.
@ast
Interactions among prions and prion "strains" in yeast.
@en
Interactions among prions and prion "strains" in yeast.
@nl
prefLabel
Interactions among prions and prion "strains" in yeast.
@ast
Interactions among prions and prion "strains" in yeast.
@en
Interactions among prions and prion "strains" in yeast.
@nl
P2093
P2860
P356
P1476
Interactions among prions and prion "strains" in yeast.
@en
P2093
Herman K Edskes
Joo Y Hong
Michael E Bradley
P2860
P304
16392-16399
P356
10.1073/PNAS.152330699
P407
P478
99 Suppl 4
P577
2002-07-30T00:00:00Z