The specific interaction of the Rous sarcoma virus transforming protein, pp60src, with two cellular proteins.
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Chaperoning checkpoint kinase 1 (Chk1), an Hsp90 client, with purified chaperonesAkt forms an intracellular complex with heat shock protein 90 (Hsp90) and Cdc37 and is destabilized by inhibitors of Hsp90 functionSequence and regulation of a gene encoding a human 89-kilodalton heat shock proteinThe carboxy-terminal region of mammalian HSP90 is required for its dimerization and function in vivoThe common 90-kd protein component of non-transformed '8S' steroid receptors is a heat-shock proteinInhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation.Conformational activation of a basic helix-loop-helix protein (MyoD1) by the C-terminal region of murine HSP90 (HSP84)A noncatalytic domain conserved among cytoplasmic protein-tyrosine kinases modifies the kinase function and transforming activity of Fujinami sarcoma virus P130gag-fpsPhosphorylation of the immunosuppressant FK506-binding protein FKBP52 by casein kinase II: regulation of HSP90-binding activity of FKBP52CDC37 is required for p60v-src activity in yeastParalog Specific Hsp90 Inhibitors - A Brief History and a Bright Futurehsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures.The phosphatase Ppt1 is a dedicated regulator of the molecular chaperone Hsp90Mechanism of dimer formation of the 90-kDa heat-shock proteinAn RNA aptamer perturbs heat shock transcription factor activity in Drosophila melanogasterSubstrate-binding characteristics of proteins in the 90 kDa heat shock protein familyDegradation and biosynthesis of the glucose transporter protein in chicken embryo fibroblasts transformed by the src oncogene.Amino acid alterations within a highly conserved region of the Rous sarcoma virus src gene product pp60src inactivate tyrosine protein kinase activity.Transformation by the src oncogene alters glucose transport into rat and chicken cells by different mechanisms.Deletions and insertions within an amino-terminal domain of pp60v-src inactivate transformation and modulate membrane stabilityRous sarcoma virus variants that encode src proteins with an altered carboxy terminus are defective for cellular transformation.Monoclonal antibodies to Rous sarcoma virus pp60src react with enzymatically active cellular pp60src of avian and mammalian origin.Estradiol-induced phosphorylation of ERK1/2 in explants of the mouse cerebral cortex: the roles of heat shock protein 90 (Hsp90) and MEK2.The v-rel oncogene product is complexed to a 40-kDa phosphoprotein in transformed lymphoid cells.Inositol phospholipid-specific phospholipase C: complete cDNA and protein sequences and sequence homology to tyrosine kinase-related oncogene productsHSP90 interacts with and regulates the activity of heat shock factor 1 in Xenopus oocytes.Hepadnavirus assembly and reverse transcription require a multi-component chaperone complex which is incorporated into nucleocapsids.Double-stranded DNA induces the phosphorylation of several proteins including the 90 000 mol. wt. heat-shock protein in animal cell extractsSpontaneous high expression of heat-shock proteins in mouse embryonal carcinoma cells and ectoderm from day 8 mouse embryo.Cdc37 promotes the stability of protein kinases Cdc28 and Cak1.The oncoprotein kinase chaperone CDC37 functions as an oncogene in mice and collaborates with both c-myc and cyclin D1 in transformation of multiple tissuesCdc37 engages in stable, S14A mutation-reinforced association with the most atypical member of the yeast kinome, Cdk-activating kinase (Cak1).Hsp90: chaperoning signal transduction.Proposal for a role of the Hsp90/Hsp70-based chaperone machinery in making triage decisions when proteins undergo oxidative and toxic damage.Maturation of the tyrosine kinase c-src as a kinase and as a substrate depends on the molecular chaperone Hsp90.Emerging role of heat shock proteins in biology and medicine.Immune responses of leishmaniasis patients to heat shock proteins of Leishmania species and humans.Heat-shock protein 83 of Leishmania mexicana amazonensis is an abundant cytoplasmic protein with a tandemly repeated genomic arrangement.Relationship of heat shock proteins and induced thermal resistance.The Chemical Biology of Molecular Chaperones--Implications for Modulation of Proteostasis
P2860
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P2860
The specific interaction of the Rous sarcoma virus transforming protein, pp60src, with two cellular proteins.
description
1981 nî lūn-bûn
@nan
1981年の論文
@ja
1981年学术文章
@wuu
1981年学术文章
@zh
1981年学术文章
@zh-cn
1981年学术文章
@zh-hans
1981年学术文章
@zh-my
1981年学术文章
@zh-sg
1981年學術文章
@yue
1981年學術文章
@zh-hant
name
The specific interaction of th ...... c, with two cellular proteins.
@en
The specific interaction of th ...... c, with two cellular proteins.
@nl
type
label
The specific interaction of th ...... c, with two cellular proteins.
@en
The specific interaction of th ...... c, with two cellular proteins.
@nl
prefLabel
The specific interaction of th ...... c, with two cellular proteins.
@en
The specific interaction of th ...... c, with two cellular proteins.
@nl
P2093
P1433
P1476
The specific interaction of th ...... c, with two cellular proteins.
@en
P2093
P304
P356
10.1016/0092-8674(81)90055-6
P407
P577
1981-08-01T00:00:00Z