about
Hsp90 regulates p50(cdc37) function during the biogenesis of the activeconformation of the heme-regulated eIF2 alpha kinaseHsp90: a specialized but essential protein-folding toolHeat-shock protein 90 and Cdc37 interact with LKB1 and regulate its stabilityp50(cdc37) acting in concert with Hsp90 is required for Raf-1 functionRegulation of CDK4 activity by a novel CDK4-binding protein, p34(SEI-1)Gene expression profile of HIV-1 Tat expressing cells: a close interplay between proliferative and differentiation signalsChaperone ligand-discrimination by the TPR-domain protein Tah1.Cdc37p is required for stress-induced high-osmolarity glycerol and protein kinase C mitogen-activated protein kinase pathway functionality by interaction with Hog1p and Slt2p (Mpk1p)Gankyrin is an ankyrin-repeat oncoprotein that interacts with CDK4 kinase and the S6 ATPase of the 26 S proteasomeCalmodulin is essential for cyclin-dependent kinase 4 (Cdk4) activity and nuclear accumulation of cyclin D1-Cdk4 during G1Hsc70 regulates accumulation of cyclin D1 and cyclin D1-dependent protein kinaseATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo.Transforming activity of Fbxo7 is mediated specifically through regulation of cyclin D/cdk6.Hsp90 binds and regulates Gcn2, the ligand-inducible kinase of the alpha subunit of eukaryotic translation initiation factor 2 [corrected]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 tissuesC/EBPalpha triggers proteasome-dependent degradation of cdk4 during growth arrestStructure of an Hsp90-Cdc37-Cdk4 complex.Cdc37 interacts with the glycine-rich loop of Hsp90 client kinasesCdc37 goes beyond Hsp90 and kinasesCdk4 deficiency inhibits skin tumor development but does not affect normal keratinocyte proliferation.The cyclin D1-CDK4 oncogenic interactome enables identification of potential novel oncogenes and clinical prognosisDifferential in vivo regulation of steroid hormone receptor activation by Cdc37pInduction of angiogenesis by heat shock protein 90 mediated by protein kinase Akt and endothelial nitric oxide synthaseHsp90 inhibitor 17-DMAG decreases expression of conserved herpesvirus protein kinases and reduces virus production in Epstein-Barr virus-infected cellsEffects of HIV protease inhibitor ritonavir on Akt-regulated cell proliferation in breast cancerComparative proteomics analysis of chronic atrophic gastritis: changes of protein expression in chronic atrophic gastritis without Helicobacter pylori infection.Hsp90 and client protein maturation.Oncogenic activity of amplified miniature chromosome maintenance 8 in human malignancies.Cyclin D-CDK subunit arrangement is dependent on the availability of competing INK4 and p21 class inhibitors.Induced expression of p16(INK4a) inhibits both CDK4- and CDK2-associated kinase activity by reassortment of cyclin-CDK-inhibitor complexes.Cdc37 is essential for chromosome segregation and cytokinesis in higher eukaryotes.Identification of Cdc37 as a novel regulator of the stress-responsive mitogen-activated protein kinaseKaposi's sarcoma-associated herpesvirus encodes a functional cyclin.Regulation of stability of cyclin-dependent kinase CDK11p110 and a caspase-processed form, CDK11p46, by Hsp90.Hsp90/p50cdc37 is required for mixed-lineage kinase (MLK) 3 signaling.Identification of a conserved sequence motif that promotes Cdc37 and cyclin D1 binding to Cdk4.CK2 controls multiple protein kinases by phosphorylating a kinase-targeting molecular chaperone, Cdc37.Calmodulin binds to p21(Cip1) and is involved in the regulation of its nuclear localization.The p21(Cip1) and p27(Kip1) CDK 'inhibitors' are essential activators of cyclin D-dependent kinases in murine fibroblasts
P2860
Q24290421-E7531D17-E452-445D-ABFE-A0E6C9F31AEBQ24291482-3A075097-118B-426E-A9B1-FD7F375983ACQ24535623-7A1FEED5-B5D4-4035-9281-066D6A3B89E9Q24554532-A1A9FD1F-417E-49DC-A4DF-55CFF92FABEFQ24597148-87F8C029-808C-4117-9B45-5256C08CF611Q24795458-8133D184-9561-4512-8DD2-147E426829E1Q27929748-291CD1BB-FD36-427D-900F-07AA133E7D9BQ27934813-77F4E811-E934-4F31-BCD3-2D748CC8402DQ28214769-67D0E5AB-3E5B-4D1C-A00F-345D8A1D8A37Q28290353-792F7AE7-AB6B-4977-B76B-FB0DF6999373Q28585533-AEB2798F-E72C-4E23-9604-50296F40CF4EQ33889333-CF016DE2-FB51-45FD-A0D2-8F0A83AC2F0AQ33947132-94FBEA8C-AF15-4877-8595-E98A6AE7833CQ33960774-0A24CBE2-EC8D-4E26-BB26-981C5ADCE2ADQ33961686-8597FAAE-27CA-4E92-938D-1C19BC47155BQ33964019-74EC159A-381E-4B4F-AFFA-EB1E9894123EQ34086004-31DD8C06-17A2-4BB8-AED2-03230152B589Q34562863-AD44E8B6-4723-4F5E-9DA8-FF7DF18831B8Q34564806-E113D3AC-89DA-4FD0-BF2E-CF5265291120Q35588824-5A02DDF3-5CBD-4D06-BA01-4D9D551B77F4Q35747628-A77EE850-35DA-4C71-8C9C-54110FFCCC61Q36186374-905BEFCA-3DE4-4233-A350-211B8D12C7E4Q36947406-7DCC8606-8D5E-4813-B625-ADE0107B7DC0Q37079164-91AA953F-1D1E-4661-8AE7-74E35868BED5Q37123188-5A89F57B-134B-4C04-A4BB-2987A2B57F8FQ37307182-A8214EE0-50AB-422C-9441-F2CDE86B12F4Q37370901-C61783AE-4E3F-4754-AC25-294309A42521Q37928519-716A9CBE-1E67-4642-B487-C1B99FAF1AE9Q38704336-C2B4BCBA-73E4-400B-8B14-414312ECC9CFQ39444740-C1F01E08-CD0E-4E4A-B2F5-E02A5D137443Q39444837-E9674785-61D5-4D26-B993-F13EB1F9A455Q39659016-4E13042D-D4D7-481D-8B1D-2AA1525C45EAQ39791249-E787B4E0-D3D3-4E35-9819-FB9F0B2BE550Q39878517-AF5759F6-1CE2-4CF4-BB87-F31C50387538Q40519604-34D0A321-AB9A-4D35-8828-E2CC3D41720AQ40582216-8B221004-70CC-4624-8A3C-3CC0FDF8FB63Q40602791-1D1761C0-0497-425C-84D7-41C4D5351250Q40763457-C68839EC-220A-4CD6-BE91-A9E39C0389C5Q40934326-47F7974F-167D-4FE4-A409-BF773068BF6FQ40967344-DA288209-74D8-4808-8302-A5582D576FA8
P2860
description
1996 nî lūn-bûn
@nan
1996 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年学术文章
@wuu
1996年学术文章
@zh-cn
1996年学术文章
@zh-hans
1996年学术文章
@zh-my
1996年学术文章
@zh-sg
1996年學術文章
@yue
name
Physical interaction of mammalian CDC37 with CDK4
@ast
Physical interaction of mammalian CDC37 with CDK4
@en
Physical interaction of mammalian CDC37 with CDK4
@nl
type
label
Physical interaction of mammalian CDC37 with CDK4
@ast
Physical interaction of mammalian CDC37 with CDK4
@en
Physical interaction of mammalian CDC37 with CDK4
@nl
prefLabel
Physical interaction of mammalian CDC37 with CDK4
@ast
Physical interaction of mammalian CDC37 with CDK4
@en
Physical interaction of mammalian CDC37 with CDK4
@nl
P2093
P2860
P356
P1476
Physical interaction of mammalian CDC37 with CDK4
@en
P2093
P2860
P304
P356
10.1074/JBC.271.36.22030
P407
P577
1996-09-06T00:00:00Z