[URE3] prion propagation in Saccharomyces cerevisiae: requirement for chaperone Hsp104 and curing by overexpressed chaperone Ydj1p.
about
Amyloids: friend or foe?A heritable switch in carbon source utilization driven by an unusual yeast prionMolecular chaperones: guardians of the proteome in normal and disease statesDisaggregases, molecular chaperones that resolubilize protein aggregatesYeast prions and human prion-like proteins: sequence features and prediction methodsModulation and elimination of yeast prions by protein chaperones and co-chaperonesThe [RNQ+] prion: a model of both functional and pathological amyloidDifferences in the curing of [PSI+] prion by various methods of Hsp104 inactivationHsp104-dependent remodeling of prion complexes mediates protein-only inheritanceSpiral architecture of the Hsp104 disaggregase reveals the basis for polypeptide translocationCuring of the [URE3] prion by Btn2p, a Batten disease-related protein.Analysis of the AAA sensor-2 motif in the C-terminal ATPase domain of Hsp104 with a site-specific fluorescent probe of nucleotide binding.Increased expression of Hsp40 chaperones, transcriptional factors, and ribosomal protein Rpp0 can cure yeast prions.A novel Rtg2p activity regulates nitrogen catabolism in yeast.Yeast prions are useful for studying protein chaperones and protein quality controlCooperative kinetics of both Hsp104 ATPase domains and interdomain communication revealed by AAA sensor-1 mutants.Aggregation of human S100A8 and S100A9 amyloidogenic proteins perturbs proteostasis in a yeast modelHeterologous cross-seeding mimics cross-species prion conversion in a yeast model.Conformational stability of PrP amyloid fibrils controls their smallest possible fragment size.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.Function of SSA subfamily of Hsp70 within and across species varies widely in complementing Saccharomyces cerevisiae cell growth and prion propagation.The Schizosaccharomyces pombe Hsp104 disaggregase is unable to propagate the [PSI] prion.Structure and assembly properties of the N-terminal domain of the prion Ure2p in isolation and in its natural contextYeast prions assembly and propagation: contributions of the prion and non-prion moieties and the nature of assemblies.Requirements of Hsp104p activity and Sis1p binding for propagation of the [RNQ(+)] prionDominant gain-of-function mutations in Hsp104p reveal crucial roles for the middle region.A region within the C-terminal domain of Ure2p is shown to interact with the molecular chaperone Ssa1p by the use of cross-linkers and mass spectrometry.Hsp104 overexpression cures Saccharomyces cerevisiae [PSI+] by causing dissolution of the prion seedsRole for Hsp70 chaperone in Saccharomyces cerevisiae prion seed replication.Prion formation and polyglutamine aggregation are controlled by two classes of genes.Curing of yeast [PSI+] prion by guanidine inactivation of Hsp104 does not require cell division.Sti1 regulation of Hsp70 and Hsp90 is critical for curing of Saccharomyces cerevisiae [PSI+] prions by Hsp104.Induction of distinct [URE3] yeast prion strains.Hsp104 interacts with Hsp90 cochaperones in respiring yeastViruses and prions of Saccharomyces cerevisiaeYeast prion protein derivative defective in aggregate shearing and production of new 'seeds'Amino acid residue 184 of yeast Hsp104 chaperone is critical for prion-curing by guanidine, prion propagation, and thermotoleranceInternal initiation drives the synthesis of Ure2 protein lacking the prion domain and affects [URE3] propagation in yeast cells.Antagonistic interactions between yeast [PSI(+)] and [URE3] prions and curing of [URE3] by Hsp70 protein chaperone Ssa1p but not by Ssa2p.
P2860
Q24653554-303DE542-0F5B-419E-8227-608971FC16E9Q24655783-8440D6AD-F211-405A-9904-5A0A2A6E5A88Q26766168-F1D07EE0-D186-421E-82D3-F9A013840D69Q26796603-2A33F521-D805-4556-A69C-1A24810FC4E1Q26863334-E5113242-B5EB-47C1-B6C9-528E70AFB66BQ26999322-28AAFA99-006B-44FE-AB8E-C047E6132D08Q27008442-9BD5713A-98DC-46D9-B85F-D9CCB68B86C6Q27302269-960ABCCC-0969-4ADE-9064-EECCC4C04183Q27334853-F4BA1945-00BD-4D44-9A08-4E4313F00BD4Q27723476-CB4F12E9-7FBF-465D-94C8-37A77B8E806DQ27930078-9091B164-FA56-4C92-86DD-E20585E13A54Q27931784-E965CA42-B10D-430C-A8B3-E601DF66DAFCQ27933549-010B8E63-D169-4C47-A253-90E6C8020387Q27937973-7EE130A0-7386-4AA2-B779-06A1B6ECFC73Q28081556-22C4987B-A32E-4012-9FF1-B23747D89662Q28344719-D19592F6-D192-4ADF-B61E-E4D5FF45F82FQ28487681-94748CFA-B756-4E50-BD1B-605710933465Q30377551-37F445CD-3F6B-4AE4-9CA3-E71819B4ECCDQ30491031-6A2957F9-4D69-445A-9292-FEA8472593B7Q33415032-3B5ACD2E-EF82-452A-BA2E-840658022387Q33422679-2DE9AC19-A992-46BA-9EDD-57FD2F6AF130Q33493419-62EEAF38-50CD-4CE1-95E6-08F1BB932FB7Q33504161-150F614D-C29F-40BB-B97F-BF59B96B333CQ33546404-D92CBFEF-BEC8-4AD0-8FA9-03836F559C24Q33575482-F79B669D-08A4-4F06-B338-980B59A87183Q33576052-85C34109-2506-40EA-9F73-B4B558996B8DQ33692013-2ED8392E-ED8E-4080-AA4E-0DD83B0424ADQ33746945-2C69D9DC-0CC2-48B6-97CA-BB9DD0788E83Q33766780-B92063D3-D9C9-4A47-B80E-0B6ADB0710B9Q33860269-F1A05281-BCA0-4493-AE50-633CAD71C6A9Q33916796-5DF5D9CB-697C-41A6-82A9-E116BA1A4FA4Q33929074-D0B06CCD-CF86-4806-964F-95980C88F031Q33963759-0EA95179-A11D-45E1-9118-ADB786BDCDD8Q34012527-ABBE5820-C1DA-4F00-A900-013D5591E95CQ34012698-40A23710-4485-46DD-9675-6CBF64B038C9Q34077960-F0CACDEB-E11F-4309-ADAC-0074517B2816Q34085020-9F9F06B6-AB96-4998-A6F1-95B7DB5E4F91Q34098129-B8311786-B6D0-42FF-8E61-4E275F3457E1Q34179953-B5D259B3-0BB4-4BC0-9941-819BD9CE72B7Q34280090-6052A648-5B34-44E5-AF2E-7497F4258091
P2860
[URE3] prion propagation in Saccharomyces cerevisiae: requirement for chaperone Hsp104 and curing by overexpressed chaperone Ydj1p.
description
2000 nî lūn-bûn
@nan
2000 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
[URE3] prion propagation in Sa ...... overexpressed chaperone Ydj1p.
@ast
[URE3] prion propagation in Sa ...... overexpressed chaperone Ydj1p.
@en
type
label
[URE3] prion propagation in Sa ...... overexpressed chaperone Ydj1p.
@ast
[URE3] prion propagation in Sa ...... overexpressed chaperone Ydj1p.
@en
prefLabel
[URE3] prion propagation in Sa ...... overexpressed chaperone Ydj1p.
@ast
[URE3] prion propagation in Sa ...... overexpressed chaperone Ydj1p.
@en
P2860
P921
P1476
[URE3] prion propagation in Sa ...... overexpressed chaperone Ydj1p.
@en
P2093
H K Edskes
H Moriyama
P2860
P304
P356
10.1128/MCB.20.23.8916-8922.2000
P407
P50
P577
2000-12-01T00:00:00Z