Hsp70 chaperones as modulators of prion life cycle: novel effects of Ssa and Ssb on the Saccharomyces cerevisiae prion [PSI+] - Wikidata - awgldk - TriplyDB

Hsp70 chaperones as modulators of prion life cycle: novel effects of Ssa and Ssb on the Saccharomyces cerevisiae prion [PSI+]

Hsp70 chaperones as modulators of prion life cycle: novel effects of Ssa and Ssb on the Saccharomyces cerevisiae prion [PSI+]

http://www.wikidata.org/entity/Q34572502

about

Disaggregases, molecular chaperones that resolubilize protein aggregates Modulation and elimination of yeast prions by protein chaperones and co-chaperones Yeast prions: structure, biology, and prion-handling systems Amyloid cannot resist identification Molecular chaperones and stress-inducible protein-sorting factors coordinate the spatiotemporal distribution of protein aggregates.Hsp104, Hsp70 and Hsp40 interplay regulates formation, growth and elimination of Sup35 prions.Yeast prions are useful for studying protein chaperones and protein quality control The Hofmeister effect on amyloid formation using yeast prion protein Sensitivity-enhanced NMR reveals alterations in protein structure by cellular milieus Heritable yeast prions have a highly organized three-dimensional architecture with interfiber structures.De novo [PSI +] prion formation involves multiple pathways to form infectious oligomers.Modulation of Abeta42 low-n oligomerization using a novel yeast reporter system Hsp110 chaperones regulate prion formation and propagation in S. cerevisiae by two discrete activities.Extra N-terminal residues have a profound effect on the aggregation properties of the potential yeast prion protein Mca1 Requirements of Hsp104p activity and Sis1p binding for propagation of the [RNQ(+)] prion Prion dynamics and the quest for the genetic determinant in protein-only inheritance [SWI], the prion formed by the chromatin remodeling factor Swi1, is highly sensitive to alterations in Hsp70 chaperone system activity.Role for Hsp70 chaperone in Saccharomyces cerevisiae prion seed replication.In vivo monitoring of the prion replication cycle reveals a critical role for Sis1 in delivering substrates to Hsp104 Sti1 regulation of Hsp70 and Hsp90 is critical for curing of Saccharomyces cerevisiae [PSI+] prions by Hsp104.Polyglutamine toxicity is controlled by prion composition and gene dosage in yeast.Molecular chaperones and the assembly of the prion Sup35p, an in vitro study.De novo appearance and "strain" formation of yeast prion [PSI+] are regulated by the heat-shock transcription factor.Trans-species activity of a nonself recognition domain.Protein inheritance (prions) based on parallel in-register beta-sheet amyloid structures.Molecular chaperones antagonize proteotoxicity by differentially modulating protein aggregation pathways.Destabilization and recovery of a yeast prion after mild heat shock.Molecular chaperone Hsp104 can promote yeast prion generation Insights into prion biology: integrating a protein misfolding pathway with its cellular environment.Heterologous aggregates promote de novo prion appearance via more than one mechanism.Importance of the Hsp70 ATPase domain in yeast prion propagation Insight into molecular basis of curing of [PSI+] prion by overexpression of 104-kDa heat shock protein (Hsp104).Prion species barrier between the closely related yeast proteins is detected despite coaggregation.Stoichiometry and Affinity of Thioflavin T Binding to Sup35p Amyloid Fibrils.The ribosome-associated complex antagonizes prion formation in yeast.Prion aggregate structure in yeast cells is determined by the Hsp104-Hsp110 disaggregase machinery.Prions in yeast.Prion-Associated Toxicity is Rescued by Elimination of Cotranslational Chaperones.The role of Sse1 in the de novo formation and variant determination of the [PSI+] prion.Contributions of the Prion Protein Sequence, Strain, and Environment to the Species Barrier.

P2860

Q26796603-EEB75288-03C9-486A-AB56-D0F28C074828 Q26999322-CA92AC56-63D2-45CA-8A33-8BCBFD8380F9 Q27007482-73EFCAF0-504F-4F44-A54A-FD15C3FD623F Q27012702-23B3EFFC-96B7-4B2A-B109-8E8FB32BE685 Q27929853-7B70FA82-71C3-4A47-8F00-786C6C043371 Q27930409-05B0D827-B2A4-49FF-9041-6940F046903A Q28081556-C9A30B61-BEF1-4BC6-8667-F478EBBA937F Q28263695-3EE728CF-904D-4226-A9E3-A0478A0B3AA2 Q30380175-B599471E-68A9-4309-907D-6811D0E08632 Q30524959-2CD3EC57-FE79-4566-BEE3-546C68039063 Q30849388-FAC29546-291A-4EFB-AAEE-3D7E0CF35EE4 Q33258510-F7509919-0CE6-4A4C-A642-546CD4C41EA4 Q33323369-14CA6971-2B2E-4C77-9595-700443F9A477 Q33548706-95701B43-3BA6-44A5-93EA-3B47BA44250E Q33576052-B61ACA37-B637-4FB0-A79C-D3259E3EA75C Q33757606-89399769-7D05-4AF9-AE75-E7B5EA2DC8FE Q33838230-2C412AE1-CDAA-427A-B2B4-D20E8EDE1730 Q33860269-83E8AF3E-D73B-40B1-BA36-95790C838EC6 Q33874246-92790AFD-B059-4071-848D-0C990AC98B8D Q33963759-66513023-C565-4FD0-A653-849BDEC94BE8 Q34246922-DB8D174D-C423-432F-A751-28C891CF0FCB Q34411039-20CD76FD-5205-4390-AD25-391DF1E453EC Q34611525-577C42D0-752F-47FA-BC2D-E8F18B17742F Q34630831-026615B7-0A18-4973-BE2C-0D7393E295D7 Q34911325-74C8A127-B268-4974-A8AE-CED1374624A7 Q34979557-BB818FC4-C6AE-4080-A4C8-CB8E0FC9195C Q34985224-EEC13482-B4BC-439A-AFEE-9696ED7F5859 Q35065489-6A858B9B-9436-4610-AFC0-702A0AF7CEA2 Q35194908-901066F0-9FA2-4255-A04B-A73C96915478 Q35539781-B569F845-3088-451F-A3F1-05A1FFDBC14A Q35641429-42B82834-31FB-41D2-9720-1281556EDDED Q35643775-2753A04A-B332-45CD-8175-5C1A9A14B9C2 Q35669744-78B47C88-09B3-4217-B64B-3EECAAD842A3 Q36030781-7248C4F2-52D4-4DAD-AFC8-D4B05C1D9A59 Q36147694-D94A905A-7825-41CA-BB63-049ABC90EB6E Q36149376-004691CF-0275-4716-B595-E843BA220CCE Q36154362-265B0130-9CF8-4EB1-99D3-B97ABB61829A Q36187230-C4C9DAD3-43E6-440B-BE24-1329E018339B Q36287669-401E70AD-0F51-4326-AFAC-F9C136284C9B Q36466180-C4A5B6AB-25D5-48F1-8742-96357D7DAC83

P2860

Hsp70 chaperones as modulators of prion life cycle: novel effects of Ssa and Ssb on the Saccharomyces cerevisiae prion [PSI+]

http://www.wikidata.org/entity/Q34572502

description

2004 nî lūn-bûn

@nan

2004 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2004 թվականի նոյեմբերին հրատարակված գիտական հոդված

@hy

2004年の論文

@ja

2004年論文

@yue

2004年論文

@zh-hant

2004年論文

@zh-hk

2004年論文

@zh-mo

2004年論文

@zh-tw

2004年论文

@wuu

name

Hsp70 chaperones as modulators ...... omyces cerevisiae prion [PSI+]

@ast

Hsp70 chaperones as modulators ...... omyces cerevisiae prion [PSI+]

@en

Hsp70 chaperones as modulators ...... omyces cerevisiae prion [PSI+]

@nl

type

label

Hsp70 chaperones as modulators ...... omyces cerevisiae prion [PSI+]

@ast

Hsp70 chaperones as modulators ...... omyces cerevisiae prion [PSI+]

@en

Hsp70 chaperones as modulators ...... omyces cerevisiae prion [PSI+]

@nl

prefLabel

Hsp70 chaperones as modulators ...... omyces cerevisiae prion [PSI+]

@ast

Hsp70 chaperones as modulators ...... omyces cerevisiae prion [PSI+]

@en

Hsp70 chaperones as modulators ...... omyces cerevisiae prion [PSI+]

@nl

P1433

Q34572502-00769F7B-9172-44BC-86A3-3FB89DD9C673

P1476

Q34572502-A111E324-CE2C-4F89-94AB-9E03BD30CBC6

P2093

Q34572502-2BED9BDC-209B-418A-BB46-84AE4941DEA3

Q34572502-499A4489-E4D0-454D-AFAF-1576CF56000C

Q34572502-5CDC87E2-48F7-4599-9606-4B5F289D22FA

Q34572502-6AF620A7-500A-4EF7-A880-2CA477149816

Q34572502-76931FEC-1DFF-4372-A0D0-9824CB72044E

Q34572502-7C29623A-B49C-474F-8BFB-DB6E6F8E88DC

Q34572502-97EBF70F-8237-4954-8EB7-23D0670CB687

Q34572502-B966EB5B-F25E-4AB8-991D-A7805AB61C88

Q34572502-BF10E4CE-EBBD-41FD-AABB-DE5696F3DDB2

P2860

Q34572502-04FD6641-4D2E-4432-AFAF-9611ACFA6AA9

Q34572502-077FCEEF-CD9E-4D1F-947E-7979E007DEE3

Q34572502-08A8B3F3-9ED9-493E-8E2B-80C9EDFECF69

Q34572502-12F0046C-8FDA-4D62-BF13-F3BA8A631ADC

Q34572502-1AA4AAD4-AFED-4F3E-A92E-AF0EAE2172F1

Q34572502-1D4DCFB3-8D7C-4381-82A2-06C575ACC274

Q34572502-1F67173F-E06A-42E0-A8BA-3F4D5527332E

Q34572502-1FB58EC9-B62F-4503-90FD-CFA58536DB51

Q34572502-21C674A4-7835-43FC-965B-E0B7056719F0

Q34572502-22AE848A-B61D-4645-AA2E-DD3DE14C72B5

P304

Q34572502-FCA858D0-C975-4281-8A1D-3BD945DA8D4C

P31

Q34572502-1D462798-4C23-471C-AAD4-6451D0B24D4D

P356

Q34572502-DACE2140-79F6-437E-B4D1-F9847D0E6A3E

P407

Q34572502-355EC009-DB2C-4327-B8CA-839A1C2AA78C

P433

Q34572502-FCAA41A9-58BF-469B-A27D-028FD7F77873

P478

Q34572502-8A1212D2-D592-4357-B860-129CEBC1DC52

P577

Q34572502-81E0E807-0CF4-4544-9EB8-E72E6EA4A938

P5875

Q34572502-D3517B2E-D5F4-43C0-8037-7EFE6CC88B70

P698

Q34572502-2759EF36-7940-4FE8-AC8B-07D8D67A3DA9

P921

Q34572502-25442992-5E96-4C1C-839F-23602ED10832

Q34572502-2DE6F6C0-76EA-4963-93C3-BEC173FB46AA

Q34572502-C181B5F5-E594-4AE2-8C26-8B08A478054D

P932

Q34572502-CEB92C01-E25B-4878-A049-567799015A4A

P356

GENETICS.104.037168

P1433

P1476

Hsp70 chaperones as modulators ...... omyces cerevisiae prion [PSI+]

@en

P2093

Gary P Newnam

http://www.w3.org/2001/XMLSchema#string

Keith D Wilkinson

http://www.w3.org/2001/XMLSchema#string

Kim D Allen

http://www.w3.org/2001/XMLSchema#string

Kristin B Wittich

http://www.w3.org/2001/XMLSchema#string

Peggy A Winslett

http://www.w3.org/2001/XMLSchema#string

Renee D Wegrzyn

http://www.w3.org/2001/XMLSchema#string

Susanne Müller

http://www.w3.org/2001/XMLSchema#string

Tatiana A Chernova

http://www.w3.org/2001/XMLSchema#string

Yury O Chernoff

http://www.w3.org/2001/XMLSchema#string

P2860

Prion Protein Biology

Genetic and environmental factors affecting the de novo appearance of the [PSI+] prion in Saccharomyces cerevisiae

Propagation of the yeast prion-like [psi+] determinant is mediated by oligomerization of the SUP35-encoded polypeptide chain release factor

Non-Mendelian mutation allowing ureidosuccinic acid uptake in yeast

A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae

Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins.

The translation machinery and 70 kd heat shock protein cooperate in protein synthesis.

Increased expression of Hsp40 chaperones, transcriptional factors, and ribosomal protein Rpp0 can cure yeast prions.

The molecular chaperone Ssb from Saccharomyces cerevisiae is a component of the ribosome-nascent chain complex.

Prions affect the appearance of other prions: the story of [PIN(+)].

P304

1227-1242

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1534/GENETICS.104.037168

http://www.w3.org/2001/XMLSchema#string

P407

P433

3

http://www.w3.org/2001/XMLSchema#string

P478

169

http://www.w3.org/2001/XMLSchema#string

P577

2004-11-15T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

8180715

http://www.w3.org/2001/XMLSchema#string

P698

15545639

http://www.w3.org/2001/XMLSchema#string

P921

Prion protein family

molecular chaperones

Saccharomyces cerevisiae

P932

1449557

http://www.w3.org/2001/XMLSchema#string