Isolation and characterization of STI1, a stress-inducible gene from Saccharomyces cerevisiae.
about
The 58,000-dalton cellular inhibitor of the interferon-induced double-stranded RNA-activated protein kinase (PKR) is a member of the tetratricopeptide repeat family of proteinsA novel human protein serine/threonine phosphatase, which possesses four tetratricopeptide repeat motifs and localizes to the nucleusCharacterization of a novel 23-kilodalton protein of unactive progesterone receptor complexesIdentification of a novel cellular TPR-containing protein, SGT, that interacts with the nonstructural protein NS1 of parvovirus H-1.Hsp70 chaperones: cellular functions and molecular mechanismMutational analysis of the hsp70-interacting protein HipSBA1 encodes a yeast hsp90 cochaperone that is homologous to vertebrate p23 proteinsCNS1 encodes an essential p60/Sti1 homolog in Saccharomyces cerevisiae that suppresses cyclophilin 40 mutations and interacts with Hsp90.Sgt1p is a unique co-chaperone that acts as a client adaptor to link Hsp90 to Skp1p.Cns1 is an essential protein associated with the hsp90 chaperone complex in Saccharomyces cerevisiae that can restore cyclophilin 40-dependent functions in cpr7Delta cellsSYM1 is the stress-induced Saccharomyces cerevisiae ortholog of the mammalian kidney disease gene Mpv17 and is required for ethanol metabolism and tolerance during heat shock.The Hsp70/90 cochaperone, Sti1, suppresses proteotoxicity by regulating spatial quality control of amyloid-like proteins.Increased expression of Hsp40 chaperones, transcriptional factors, and ribosomal protein Rpp0 can cure yeast prions.Distinct roles for the Hsp40 and Hsp90 molecular chaperones during cystic fibrosis transmembrane conductance regulator degradation in yeast.In vivo analysis of the Hsp90 cochaperone Sti1 (p60)The sequence of a 30 kb fragment on the left arm of chromosome XV from Saccharomyces cerevisiae reveals 15 open reading frames, five of which correspond to previously identified genes.Identification of Saccharomyces cerevisiae genes conferring resistance to quinoline ring-containing antimalarial drugsCns1 is an activator of the Ssa1 ATPase activity.The yeast Hsp110 family member, Sse1, is an Hsp90 cochaperone.Plasmodium falciparum Hop (PfHop) Interacts with the Hsp70 Chaperone in a Nucleotide-Dependent Fashion and Exhibits Ligand SelectivityThe Hsp organizer protein hop enhances the rate of but is not essential for glucocorticoid receptor folding by the multiprotein Hsp90-based chaperone systemHop modulates Hsp70/Hsp90 interactions in protein foldingAntifungal activities of antineoplastic agents: Saccharomyces cerevisiae as a model system to study drug actionThe carboxy-terminal domain of Hsc70 provides binding sites for a distinct set of chaperone cofactorsCharacterization of functional domains of the eukaryotic co-chaperone HipThe tetratricopeptide repeat: a structural motif mediating protein-protein interactionsCharacterisation of the Plasmodium falciparum Hsp70-Hsp90 organising protein (PfHop)p62cdc23 of Saccharomyces cerevisiae: a nuclear tetratricopeptide repeat protein with two mutable domains.Bacterial lipopolysaccharide induces expression of the stress response genes hop and H411.Analysis of cell wall proteins regulated in stem of susceptible and resistant tomato species after inoculation with Ralstonia solanacearum: a proteomic approach.The Hsp70/Hsp90 Chaperone Machinery in Neurodegenerative DiseasesSuppression of an Hsp70 mutant phenotype in Saccharomyces cerevisiae through loss of function of the chromatin component Sin1p/Spt2p.Hsp90 binds and regulates Gcn2, the ligand-inducible kinase of the alpha subunit of eukaryotic translation initiation factor 2 [corrected]Hsp104 interacts with Hsp90 cochaperones in respiring yeastRegulation of vascular endothelial cell polarization and migration by Hsp70/Hsp90-organizing proteinFolding of the glucocorticoid receptor by the reconstituted Hsp90-based chaperone machinery. The initial hsp90.p60.hsp70-dependent step is sufficient for creating the steroid binding conformation.Folding of the glucocorticoid receptor by the heat shock protein (hsp) 90-based chaperone machinery. The role of p23 is to stabilize receptor.hsp90 heterocomplexes formed by hsp90.p60.hsp70.Effect of mutation of the tetratricopeptide repeat and asparatate-proline 2 domains of Sti1 on Hsp90 signaling and interaction in Saccharomyces cerevisiaesti35, a stress-responsive gene in Fusarium spp.The tgl gene: social motility and stimulation in Myxococcus xanthus.
P2860
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P2860
Isolation and characterization of STI1, a stress-inducible gene from Saccharomyces cerevisiae.
description
1989 nî lūn-bûn
@nan
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
1989年论文
@zh
1989年论文
@zh-cn
name
Isolation and characterization ...... from Saccharomyces cerevisiae.
@ast
Isolation and characterization ...... from Saccharomyces cerevisiae.
@en
type
label
Isolation and characterization ...... from Saccharomyces cerevisiae.
@ast
Isolation and characterization ...... from Saccharomyces cerevisiae.
@en
prefLabel
Isolation and characterization ...... from Saccharomyces cerevisiae.
@ast
Isolation and characterization ...... from Saccharomyces cerevisiae.
@en
P2860
P356
P1476
Isolation and characterization ...... from Saccharomyces cerevisiae.
@en
P2093
C M Nicolet
P2860
P304
P356
10.1128/MCB.9.9.3638
P407
P577
1989-09-01T00:00:00Z