The role of Sse1 in the de novo formation and variant determination of the [PSI+] prion. - Wikidata - awgldk - TriplyDB

The role of Sse1 in the de novo formation and variant determination of the [PSI+] prion.

The role of Sse1 in the de novo formation and variant determination of the [PSI+] prion.

http://www.wikidata.org/entity/Q36287669

about

Modulation and elimination of yeast prions by protein chaperones and co-chaperones Yeast prions: structure, biology, and prion-handling systems Curing of the [URE3] prion by Btn2p, a Batten disease-related protein.Prion-impairing mutations in Hsp70 chaperone Ssa1: effects on ATPase and chaperone activities.Yeast prions are useful for studying protein chaperones and protein quality control The NatA acetyltransferase couples Sup35 prion complexes to the [PSI+] phenotype De novo [PSI +] prion formation involves multiple pathways to form infectious oligomers.Hsp110 chaperones regulate prion formation and propagation in S. cerevisiae by two discrete activities.Function of SSA subfamily of Hsp70 within and across species varies widely in complementing Saccharomyces cerevisiae cell growth and prion propagation.Influence of prion variant and yeast strain variation on prion-molecular chaperone requirements Hierarchical functional specificity of cytosolic heat shock protein 70 (Hsp70) nucleotide exchange factors in yeast.Coordinated Hsp110 and Hsp104 Activities Power Protein Disaggregation in Saccharomyces cerevisiae.Investigating the interactions of yeast prions: [SWI+], [PSI+], and [PIN+].[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.Sti1 regulation of Hsp70 and Hsp90 is critical for curing of Saccharomyces cerevisiae [PSI+] prions by Hsp104.The mammalian disaggregase machinery: Hsp110 synergizes with Hsp70 and Hsp40 to catalyze protein disaggregation and reactivation in a cell-free system Assessment of inactivating stop codon mutations in forty Saccharomyces cerevisiae strains: implications for [PSI] prion- mediated phenotypes.Distinct subregions of Swi1 manifest striking differences in prion transmission and SWI/SNF function Hsp40s specify functions of Hsp104 and Hsp90 protein chaperone machines.Heterologous gln/asn-rich proteins impede the propagation of yeast prions by altering chaperone availability Molecular chaperone Hsp104 can promote yeast prion generation Functional diversification of hsp40: distinct j-protein functional requirements for two prions allow for chaperone-dependent prion selection Hsp90-Associated Immunophilin Homolog Cpr7 Is Required for the Mitotic Stability of [URE3] Prion in Saccharomyces cerevisiae.Prion aggregate structure in yeast cells is determined by the Hsp104-Hsp110 disaggregase machinery.Prions in yeast.The Yeast Prion [SWI(+)] Abolishes Multicellular Growth by Triggering Conformational Changes of Multiple Regulators Required for Flocculin Gene Expression.Structural variants of yeast prions show conformer-specific requirements for chaperone activity.Prions are affected by evolution at two levels Variant-specific [PSI+] infection is transmitted by Sup35 polymers within [PSI+] aggregates with heterogeneous protein composition Schizosaccharomyces pombe disaggregation machinery chaperones support Saccharomyces cerevisiae growth and prion propagation.Cytoplasmic expression of mouse prion protein causes severe toxicity in Caenorhabditis elegans The yeast Sup35NM domain propagates as a prion in mammalian cells.Mutational analysis of Sse1 (Hsp110) suggests an integral role for this chaperone in yeast prion propagation in vivo.Multiple hsp70 isoforms in the eukaryotic cytosol: mere redundancy or functional specificity?Influence of Hsp70s and their regulators on yeast prion propagation Physiological and environmental control of yeast prions.The BAG homology domain of Snl1 cures yeast prion [URE3] through regulation of Hsp70 chaperones A toxic imbalance of Hsp70s in Saccharomyces cerevisiae is caused by competition for cofactors.Prions, Chaperones, and Proteostasis in Yeast.

P2860

Q26999322-BF667D2C-25CC-42A1-B33F-8E8E11E6A752 Q27007482-231B8AE7-EB8D-441F-A2DF-1035A44CAAB0 Q27930078-8711F077-AEA1-45D3-A3AC-20B7118A6143 Q27934126-5C57572B-BFA2-4429-BFF0-EC6991480FA1 Q28081556-12DF6129-3B8B-4392-A558-FA4FE4B40104 Q28303621-56AF8E67-510E-4355-9054-FECAB0C546BA Q30849388-1FB72DCF-6AD8-4F5F-ABEF-35A9D4CA6416 Q33323369-EE9F1CB5-96B8-4B4D-BF65-CB171D6EE842 Q33493419-B32FB67A-A617-4F65-A96B-0AC5F6C7B811 Q33575503-AE2C7149-ADAD-449E-99C9-2332D12505B7 Q33676604-B9631142-7CAA-48A9-B282-EE9007B4C603 Q33715895-3F3A6615-5FFE-450F-AA4D-D468F54154FC Q33779615-3B848FB3-9817-446D-BD78-819F56F487C8 Q33838230-CDB14829-B8CA-4F94-B034-22DBCE8E85E5 Q33916796-851C4904-51D5-4FCC-8B7E-EAC0DA0B449D Q33963759-DF355F0B-DEA5-45E9-A6FF-2FA02DE6941A Q34056277-02D3CE32-C6E3-4D5E-B9B3-53AF730496B9 Q34110267-A191734F-D8FE-455F-9CDA-30463862B4D9 Q34177997-C0F33A7E-502D-4A80-AD37-DCF86EC7FD04 Q34350913-F9110927-1731-4513-B3A5-3BA2A93B40B9 Q34566018-165F48E2-3FC9-460B-ADA5-1B72631625A5 Q35065489-57E36CF1-A341-4D6D-ABF3-0290D6D1C579 Q35212560-4212839A-5431-48A8-AF48-61DD61ED3EAD Q35810283-CF82421B-E683-45AF-BD9F-0D80D0829EF8 Q36149376-F1EA8EDD-A109-4A30-A7FF-14C34E7C7A7F Q36154362-AFE1E468-A50D-4F2F-AD3E-9B0616CFACFF Q36440715-0CDA3FEB-A662-4CC1-A3E7-1DB7BC727531 Q36498591-CCC86962-D931-4001-87F2-C20844082070 Q36604678-88332FB3-B59F-4AB0-9A3E-E19A49870B52 Q36678054-D405CF35-C951-4E4A-923F-F78A3B902CCC Q36826419-AE105CCA-CEC9-4D02-81B7-5AA6B75D563B Q36983264-04D713A5-0CEC-49A2-AB8C-91BB653FCB8F Q37062021-C06E4F01-495A-4FAE-86B4-2E58210C6BC2 Q37079553-0BC16E61-46E2-43CF-BF8E-768311943E74 Q37200825-0F7AA917-BBFE-48C4-8088-574020B29250 Q37266700-0CD2A1F1-C47F-4621-B25F-A72877896EDD Q37633376-E7474D16-979B-4672-B1D6-038B1FBCA86F Q37655701-F3E97DF9-5289-4F88-B4F8-953B768F46D7 Q38664570-417A5004-5CD3-4346-ADF0-8F7AE4A45A04 Q38999127-3C5F19C2-F7A1-435E-911D-400A8BA87CAD

P2860

The role of Sse1 in the de novo formation and variant determination of the [PSI+] prion.

http://www.wikidata.org/entity/Q36287669

description

2007 nî lūn-bûn

@nan

2007年の論文

@ja

2007年学术文章

@wuu

2007年学术文章

@zh-cn

2007年学术文章

@zh-hans

2007年学术文章

@zh-my

2007年学术文章

@zh-sg

2007年學術文章

@yue

2007年學術文章

@zh

2007年學術文章

@zh-hant

name

The role of Sse1 in the de novo formation and variant determination of the [PSI+] prion.

@ast

The role of Sse1 in the de novo formation and variant determination of the [PSI+] prion.

@en

type

label

The role of Sse1 in the de novo formation and variant determination of the [PSI+] prion.

@ast

The role of Sse1 in the de novo formation and variant determination of the [PSI+] prion.

@en

prefLabel

The role of Sse1 in the de novo formation and variant determination of the [PSI+] prion.

@ast

The role of Sse1 in the de novo formation and variant determination of the [PSI+] prion.

@en

P1433

Q36287669-6B0BF2D6-BB36-4D84-8407-F4DE4EACB90D

P1476

Q36287669-055C5D6B-6AC9-47D9-AF28-B6FDD2924ECA

P2093

Q36287669-2F551449-52EE-4CC1-8472-39DE271C5369

Q36287669-4F4ECFB3-D03E-4B0E-853F-223AF9FE581A

Q36287669-620A204A-AA1C-47FF-A14B-97F244E7B221

Q36287669-A251E357-2830-4A54-9CA7-D3BD8EC9436A

Q36287669-D27AE630-6786-499A-8FAE-462464CD71C8

P2860

Q36287669-044BA4F5-1B91-4D5E-96A7-CD7810D4DB48

Q36287669-046F44DA-47C7-4069-AA33-D8E4307C8407

Q36287669-0C306FA8-09E2-4B0F-AC9E-2A2AD22D16AA

Q36287669-113C3CD2-82A9-4B50-B088-B58792A04FB0

Q36287669-15B2C06E-D122-4A4A-9DB4-7D5F8ADDE175

Q36287669-1E82D3AF-2F9E-456D-8CD2-D2013E36A829

Q36287669-25A76229-6323-4369-97AD-471E33C572B2

Q36287669-25B9FDA6-5249-4FC8-8D7D-FFD69EB87B0B

Q36287669-2D87F795-6264-4FB9-841E-C815E338E76D

Q36287669-34FB63D5-ADEC-43D7-8D97-4A5BE309563F

P304

Q36287669-58265C22-CB8E-4789-9967-391B977E3DF8

P31

Q36287669-75EF0A9A-D787-419D-817B-C7155AFC5491

P356

Q36287669-38C7EFEF-0307-4950-A111-A5BC2B7DED07

P407

Q36287669-DAC2FFF7-1E01-42A2-83CF-0EC808907AFF

P433

Q36287669-7EE549A2-5E08-40BD-94C9-F501C365F99C

P478

Q36287669-E4B67662-F5AB-42A6-9F60-EEC3CBE599E6

P577

Q36287669-AD0B54B5-8DA6-44F1-96B4-DE45A6C31B1B

P5875

Q36287669-A6AE501D-A0AC-43AE-B7FB-74F4E69ABDF8

P698

Q36287669-DC989B2A-4A66-4D37-80AE-5133BFC24209

P921

Q36287669-5EAFD222-65E5-45C5-80FF-D06E4460CE4B

P932

Q36287669-DB063148-C11F-45C4-B5E1-FCCCB9B89EA5

P356

GENETICS.107.077982

P1433

P1476

The role of Sse1 in the de novo formation and variant determination of the [PSI+] prion.

@en

P2093

Kevin A Morano

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

Kyung-Won Park

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

Liming Li

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

Qing Fan

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

Zhiqiang Du

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

P2860

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

The products of the SUP45 (eRF1) and SUP35 genes interact to mediate translation termination in Saccharomyces cerevisiae

Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s.

Isolation and characterization of SSE1 and SSE2, new members of the yeast HSP70 multigene family.

Characterization of Hsp70 binding and nucleotide exchange by the yeast Hsp110 chaperone Sse1.

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

The yeast Hsp110 family member, Sse1, is an Hsp90 cochaperone.

Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor.

[URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae

P304

1583-1593

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

P31

scholarly article

P356

10.1534/GENETICS.107.077982

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

P407

P433

3

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

P478

177

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

P577

2007-11-01T00:00:00Z

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

P5875

5807703

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

P698

18039878

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

P921

Prion protein family

P932

2147939

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