HSP90 interacts with RAR1 and SGT1 and is essential for RPS2-mediated disease resistance in Arabidopsis. - Wikidata - wikimedia - TriplyDB

HSP90 interacts with RAR1 and SGT1 and is essential for RPS2-mediated disease resistance in Arabidopsis.

HSP90 interacts with RAR1 and SGT1 and is essential for RPS2-mediated disease resistance in Arabidopsis.

http://www.wikidata.org/entity/Q36161654

about

Structural and functional coupling of Hsp90- and Sgt1-centred multi-protein complexes Sgt1 is required for human kinetochore assembly TPR Proteins in Plant Hormone Signaling SGT1 is essential for Nod1 activation Mechanisms of Hsp90 regulation Heat Shock Proteins: A Review of the Molecular Chaperones for Plant Immunity The double face of Morgana in tumorigenesis The 'active life' of Hsp90 complexes For security and stability: SGT1 in plant defense and development Human Sgt1 binds HSP90 through the CHORD-Sgt1 domain and not the tetratricopeptide repeat domain Structure and Functional Studies of the CS Domain of the Essential H/ACA Ribonucleoparticle Assembly Protein SHQ1 The Box H/ACA snoRNP Assembly Factor Shq1p is a Chaperone Protein Homologous to Hsp90 Cochaperones that Binds to the Cbf5p Enzyme Structural Basis for Assembly of Hsp90-Sgt1-CHORD Protein Complexes: Implications for Chaperoning of NLR Innate Immunity Receptors Sgt1p is a unique co-chaperone that acts as a client adaptor to link Hsp90 to Skp1p.The heat shock protein/chaperone network and multiple stress resistance Recessive Resistance to Plant Viruses: Potential Resistance Genes Beyond Translation Initiation Factors Dynamic nucleotide-dependent interactions of cysteine- and histidine-rich domain (CHORD)-containing Hsp90 cochaperones Chp-1 and melusin with cochaperones PP5 and Sgt1 Phenotypic diversity and altered environmental plasticity in Arabidopsis thaliana with reduced Hsp90 levels The Hsp90 co-chaperone Sgt1 governs Candida albicans morphogenesis and drug resistance The mammalian CHORD-containing protein melusin is a stress response protein interacting with Hsp90 and Sgt1 Transcript dynamics at early stages of molecular interactions of MYMIV with resistant and susceptible genotypes of the leguminous host, Vigna mungo Tudor domain containing 12 (TDRD12) is essential for secondary PIWI interacting RNA biogenesis in mice Role of type III effector secretion during bacterial pathogenesis in another kingdom Allosteric regulation of the Hsp90 dynamics and stability by client recruiter cochaperones: protein structure network modeling Low-resolution structure of the full-length barley (Hordeum vulgare) SGT1 protein in solution, obtained using small-angle X-ray scattering.Comparative analysis of protein-protein interactions in the defense response of rice and wheat High throughput virus-induced gene silencing implicates heat shock protein 90 in plant disease resistance.Regulation of Nod1 by Hsp90 chaperone complex.Mammalian CHORD-containing protein 1 is a novel heat shock protein 90-interacting protein.Sgt1, but not Rar1, is essential for the RB-mediated broad-spectrum resistance to potato late blight Evolutionary diversification of plant shikimate kinase gene duplicates Ubiquitin, hormones and biotic stress in plants SRFR1 negatively regulates plant NB-LRR resistance protein accumulation to prevent autoimmunity.The Soybean Rhg1 locus for resistance to the soybean cyst nematode Heterodera glycines regulates the expression of a large number of stress- and defense-related genes in degenerating feeding cells.Putative resistance gene markers associated with quantitative trait loci for fire blight resistance in Malus 'Robusta 5' accessions An elm EST database for identifying leaf beetle egg-induced defense genes.The small heat shock protein 20 RSI2 interacts with and is required for stability and function of tomato resistance protein I-2.Plant immune responses against viruses: how does a virus cause disease?Mechanisms of plant resistance to viruses.Specific missense alleles of the arabidopsis jasmonic acid co-receptor COI1 regulate innate immune receptor accumulation and function.

P2860

Q24316241-4D7522DE-3F8C-4BB8-991D-6B56F4F6A829 Q24537151-090C30C0-B00B-41C1-8D7C-96E71AD7DF38 Q24641869-45C9B094-0C18-4EBE-903E-D68A27B21609 Q24683802-67F4E208-B33A-4C6D-B627-7D7A47FC026F Q26741834-279DBC6C-6CFF-4A26-8CA7-D8F39794FD71 Q26775227-D5522A8E-0694-48F2-A870-2D4D16EA80E2 Q26783788-7A59107A-291B-4CEA-A659-DE7982BE3B40 Q26829003-FC05665F-C2BB-41BB-A134-6374A8AE1C35 Q27022509-A476F522-D1D7-4C05-BDA7-C654C34FD748 Q27643082-7EC6C8C6-13F4-466F-AACA-D501CA2246B8 Q27652939-B90836D9-317D-4D04-A296-DCF2E78E7B23 Q27655418-71604C47-766C-4441-B12C-628C2724F6C8 Q27663674-064E7CCB-521C-46CB-987A-68DF69580698 Q27931036-85C899BD-933F-4A9B-A1E3-462349CADDE2 Q28070209-614A5EF5-4117-4470-B27E-EB30178EFCA2 Q28079696-2432EE9D-3619-48D2-886D-6FE947F0B76B Q28118520-5C5DC45B-962E-47CE-AA33-751E3E5F84C6 Q28469256-0052BA26-8D0A-4838-9D14-B96EF68EB18B Q28483590-CADF54AD-1FA5-4757-9A17-B9B81B7DF014 Q28506605-3B082987-34C5-44CF-93C2-484E197EE68B Q28546501-BC2B2AB7-08C2-46E2-BDBF-9054BB4C7187 Q28593136-2EE484CD-4891-4A1F-B44F-119320A7F680 Q28775800-D1B1D8DB-CCF0-4077-8C5E-6C459E96C869 Q30358343-45D99CA7-170F-4243-B2E7-118384BE078B Q30361188-CFF45407-22B9-4993-B775-666D78F5CFFA Q30537813-21B49CC2-DD22-4D41-9860-9D8243E6A41E Q31021171-286B3628-D36C-411B-B4E0-6BD76D6B50D4 Q33289338-F9B22B56-83A6-463C-800A-9BA73FA84CA3 Q33289380-20A229D4-C0AC-4C71-9281-BA10C4A863DB Q33316230-79DD7129-13BB-4D68-B815-A9CBEF051F72 Q33389861-0E323B87-921C-4BB7-84C3-960053791FE8 Q33576532-9CFA2136-8785-4F4A-865E-92D49C7A0D31 Q33700582-2A672A61-4516-4C32-9E0F-04CF65DE4193 Q33824880-231CC53F-350F-4F3D-A14A-020517D11869 Q34218487-AA193803-C9E8-4233-9518-BD9994AF57F0 Q34306119-AE215468-4B9E-4498-88A5-7D9311A6015E Q34333943-BF85B693-B5EC-4665-937D-A497D7B83176 Q34346888-6753AFC6-D8F8-4C60-82CF-EA271E716C8F Q34446982-9D4F9C99-B6A9-48C0-980D-BBC767EDE705 Q34456103-4D912538-1925-4C31-8F9B-AC1CFCCBF8C9

P2860

HSP90 interacts with RAR1 and SGT1 and is essential for RPS2-mediated disease resistance in Arabidopsis.

http://www.wikidata.org/entity/Q36161654

description

2003 nî lūn-bûn

@nan

2003年の論文

@ja

2003年論文

@yue

2003年論文

@zh-hant

2003年論文

@zh-hk

2003年論文

@zh-mo

2003年論文

@zh-tw

2003年论文

@wuu

2003年论文

@zh

2003年论文

@zh-cn

name

HSP90 interacts with RAR1 and ...... ase resistance in Arabidopsis.

@ast

HSP90 interacts with RAR1 and ...... ase resistance in Arabidopsis.

@en

type

label

HSP90 interacts with RAR1 and ...... ase resistance in Arabidopsis.

@ast

HSP90 interacts with RAR1 and ...... ase resistance in Arabidopsis.

@en

prefLabel

HSP90 interacts with RAR1 and ...... ase resistance in Arabidopsis.

@ast

HSP90 interacts with RAR1 and ...... ase resistance in Arabidopsis.

@en

P1433

Q36161654-C9643FEE-8E9C-4F80-B10A-715791165E60

P1476

Q36161654-BB135534-7B70-4B05-8649-E504D393C2FE

P2093

Q36161654-06854743-59F0-4BE2-83B3-444E3657AE08

Q36161654-2115615C-4C7D-49CE-BD9B-FE75C6BF1A8F

Q36161654-36998987-2FDC-4774-A34F-42A24AAE8206

Q36161654-E9155307-8653-416A-951D-41F4B67FF039

P2860

Q36161654-018AA876-EB07-4BE1-B7D6-DFB2DDE270AD

Q36161654-076C1BA7-6781-46F5-9C69-9E77BAD7C9A4

Q36161654-10F2309F-FFB7-4E9D-AD19-355BD3C6ED09

Q36161654-13108769-BB41-4C75-BA34-BE543248561F

Q36161654-1D1DCB48-6718-4EB3-B938-B6A5334001A2

Q36161654-23CC25F2-F57C-43AE-BC21-EFCCA1127795

Q36161654-2FD573B8-4ABF-4B4D-8394-6A4365785BF8

Q36161654-396995D8-57C5-42C0-8426-CCFE486FCB57

Q36161654-3B768AAE-DA12-4E59-A742-6052B802DC73

Q36161654-3BEFC607-12DF-4928-84C5-2500F7E8E3FC

P304

Q36161654-2627ECC6-FBB8-4827-80C4-CD03A2C15485

P31

Q36161654-FF9B1D8C-57EB-4192-920C-D1AC07FFB63C

P356

Q36161654-4319F0BF-C2EA-478D-928A-ED84C31FD6F7

P407

Q36161654-C48A86C8-9CFD-4577-97CE-AFF2FDC4546A

P433

Q36161654-829C1EFF-6606-4E24-9B5E-A7FE6816C3E7

P478

Q36161654-86EEEFA6-25FD-4E24-92C8-AAE64629CE36

P577

Q36161654-8A24353A-EE62-487A-BB1C-ECE01D8CC6D3

P5875

Q36161654-162A48B2-1AD6-4F7C-954F-A176F6611647

P698

Q36161654-E84A00C4-F5FC-4CF4-A41C-D602155F7756

P932

Q36161654-0295BB0F-C122-4A73-A355-75B4EE11FC9E

P356

PNAS.2033934100

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

HSP90 interacts with RAR1 and ...... ase resistance in Arabidopsis.

@en

P2093

Akira Takahashi

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

Catarina Casais

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

Kazuya Ichimura

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

Ken Shirasu

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

P2860

SGT1 encodes an essential component of the yeast kinetochore assembly pathway and a novel subunit of the SCF ubiquitin ligase complex

Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine

Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions

Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent

Hsp90 enables Ctf13p/Skp1p to nucleate the budding yeast kinetochore.

Sgt1p contributes to cyclic AMP pathway activity and physically interacts with the adenylyl cyclase Cyr1p/Cdc35p in budding yeast

Promotion of NEDD-CUL1 conjugate cleavage by COP9 signalosome

Plant pathogens and integrated defence responses to infection

Interaction of Hsp90 with 20S proteasome: thermodynamic and kinetic characterization

The Hsp90 family of proteins in Arabidopsis thaliana

P304

11777-11782

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

P31

scholarly article

P356

10.1073/PNAS.2033934100

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

P407

P433

20

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

P478

100

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

P577

2003-09-22T00:00:00Z

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

P5875

9085579

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

P698

14504384

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

P932

208834

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