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Volumn 29, Issue 24, 2010, Pages 3532-3544

Hsp90 and Hsp40/Erdj3 are required for the expression and anti-apoptotic function of KSHV K1

Author keywords

Heat shock proteins; Hsp40; Hsp90; K1; KSHV; Lytic replication

Indexed keywords

17 DEMETHOXY 17 (2 DIMETHYLAMINOETHYLAMINO)GELDANAMYCIN; CHAPERONE; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 90; HEAT SHOCK PROTEIN 90BETA; K1 PROTEIN; SMALL INTERFERING RNA; TANESPIMYCIN; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 77953784609     PISSN: 09509232     EISSN: 14765594     Source Type: Journal    
DOI: 10.1038/onc.2010.124     Document Type: Article
Times cited : (56)

References (54)
  • 1
  • 2
    • 0036892534 scopus 로고    scopus 로고
    • Transcriptional regulation of the K1 gene product of Kaposi's sarcoma-associated herpesvirus
    • Bowser BS, DeWire SM, Damania B. (2002). Transcriptional regulation of the K1 gene product of Kaposi's sarcoma-associated herpesvirus. J Virol 76: 12574-12583.
    • (2002) J Virol , vol.76 , pp. 12574-12583
    • Bowser, B.S.1    Dewire, S.M.2    Damania, B.3
  • 3
    • 23244444185 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 DNA polymerase requires the mammalian chaperone hsp90 for proper localization to the nucleus
    • Burch AD, Weller SK. (2005). Herpes simplex virus type 1 DNA polymerase requires the mammalian chaperone hsp90 for proper localization to the nucleus. J Virol 79: 10740-10749.
    • (2005) J Virol , vol.79 , pp. 10740-10749
    • Burch, A.D.1    Weller, S.K.2
  • 4
    • 0029069445 scopus 로고
    • Kaposi's sarcoma-associated herpesvirus-like DNA sequences in AIDS-related body-cavity-based lymphomas
    • Cesarman E, Chang Y, Moore PS, Said JW, Knowles DM. (1995). Kaposi's sarcoma-associated herpesvirus-like DNA sequences in AIDS-related body-cavity-based lymphomas. N Engl J Med 332: 1186-1191.
    • (1995) N Engl J Med , vol.332 , pp. 1186-1191
    • Cesarman, E.1    Chang, Y.2    Moore, P.S.3    Said, J.W.4    Knowles, D.M.5
  • 5
    • 77953751745 scopus 로고    scopus 로고
    • Array-based transcript profiling and limiting-dilution RT-PCR analysis identify additional latent genes in KSHV
    • (e-pub ahead of print)
    • Chandriani S, Ganem D. (2010). Array-based transcript profiling and limiting-dilution RT-PCR analysis identify additional latent genes in KSHV. J Virol Mar (e-pub ahead of print).
    • (2010) J Virol Mar
    • Chandriani, S.1    Ganem, D.2
  • 6
    • 0028588064 scopus 로고
    • Identification of herpesvirus-like DNA sequences in AIDS-associated Kaposi's sarcoma
    • Chang Y, Cesarman E, Pessin MS, Lee F, Culpepper J, Knowles DM et al. (1994). Identification of herpesvirus-like DNA sequences in AIDS-associated Kaposi's sarcoma. Science 266: 1865-1869.
    • (1994) Science , vol.266 , pp. 1865-1869
    • Chang, Y.1    Cesarman, E.2    Pessin, M.S.3    Lee, F.4    Culpepper, J.5    Knowles, D.M.6
  • 7
    • 0034048277 scopus 로고    scopus 로고
    • Activation of lymphocyte signaling by the R1 protein of rhesus monkey rhadinovirus
    • Damania B, DeMaria M, Jung JU, Desrosiers RC. (2000). Activation of lymphocyte signaling by the R1 protein of rhesus monkey rhadinovirus. J Virol 74: 2721-2730.
    • (2000) J Virol , vol.74 , pp. 2721-2730
    • Damania, B.1    Demaria, M.2    Jung, J.U.3    Desrosiers, R.C.4
  • 8
    • 0033065430 scopus 로고    scopus 로고
    • Identification of the R1 oncogene and its protein product from the rhadinovirus of rhesus monkeys
    • Damania B, Li M, Choi JK, Alexander L, Jung JU, Desrosiers RC. (1999). Identification of the R1 oncogene and its protein product from the rhadinovirus of rhesus monkeys. J Virol 73: 5123-5131.
    • (1999) J Virol , vol.73 , pp. 5123-5131
    • Damania, B.1    Li, M.2    Choi, J.K.3    Alexander, L.4    Jung, J.U.5    Desrosiers, R.C.6
  • 9
    • 2942716692 scopus 로고    scopus 로고
    • Functional proteomic screens reveal an essential extracellular role for hsp90 alpha in cancer cell invasive-ness
    • Eustace BK, Sakurai T, Stewart JK, Yimlamai D, Unger C, Zehetmeier C et al. (2004). Functional proteomic screens reveal an essential extracellular role for hsp90 alpha in cancer cell invasive-ness. Nat Cell Biol 6: 507-514.
    • (2004) Nat Cell Biol , vol.6 , pp. 507-514
    • Eustace, B.K.1    Sakurai, T.2    Stewart, J.K.3    Yimlamai, D.4    Unger, C.5    Zehetmeier, C.6
  • 11
    • 0037155901 scopus 로고    scopus 로고
    • Involvement of Hsp90 in signaling and stability of 3-phosphoinositide- dependent kinase-1
    • Fujita N, Sato S, Ishida A, Tsuruo T. (2002). Involvement of Hsp90 in signaling and stability of 3-phosphoinositide-dependent kinase-1. J Biol Chem 277: 10346-10353.
    • (2002) J Biol Chem , vol.277 , pp. 10346-10353
    • Fujita, N.1    Sato, S.2    Ishida, A.3    Tsuruo, T.4
  • 12
    • 0037200043 scopus 로고    scopus 로고
    • The turn motif is a phosphorylation switch that regulates the binding of Hsp70 to protein kinase C
    • Gao T, Newton AC. (2002). The turn motif is a phosphorylation switch that regulates the binding of Hsp70 to protein kinase C. J Biol Chem 277: 31585-31592.
    • (2002) J Biol Chem , vol.277 , pp. 31585-31592
    • Gao, T.1    Newton, A.C.2
  • 13
    • 0030031807 scopus 로고    scopus 로고
    • Kaposi sarcoma-associated herpes-like virus (human her-pesvirus type 8 DNA sequences in multicentric Castleman's disease: Is there any relevant association in non-human immunodeficiency virus-infected patients?
    • Gessain A, Sudaka A, Briere J, Fouchard N, Nicola MA, Rio B et al. (1996). Kaposi sarcoma-associated herpes-like virus (human her-pesvirus type 8) DNA sequences in multicentric Castleman's disease: is there any relevant association in non-human immunodeficiency virus-infected patients? Blood 87: 414-416.
    • (1996) Blood , vol.87 , pp. 414-416
    • Gessain, A.1    Sudaka, A.2    Briere, J.3    Fouchard, N.4    Nicola, M.A.5    Rio, B.6
  • 15
    • 21244462689 scopus 로고    scopus 로고
    • In vivo antitumor efficacy of 17-DMAG (17-dimethylaminoethylamino-17- demethoxygeldanamycin hydrochloride), a water-soluble geldanamycin derivative
    • Hollingshead M, Alley M, Burger AM, Borgel S, Pacula-Cox C, Fiebig HH et al. (2005). in vivo antitumor efficacy of 17-DMAG (17-dimethylaminoethylamino- 17-demethoxygeldanamycin hydrochloride), a water-soluble geldanamycin derivative. Cancer Chemother Pharmacol 56: 115-125.
    • (2005) Cancer Chemother Pharmacol , vol.56 , pp. 115-125
    • Hollingshead, M.1    Alley, M.2    Burger, A.M.3    Borgel, S.4    Pacula-Cox, C.5    Fiebig, H.H.6
  • 16
    • 14344265077 scopus 로고    scopus 로고
    • Clinical trials referral resource. Current clinical trials of 17-AG and 17-DMAG
    • 619-620
    • Ivy PS, Schoenfeldt M. (2004). Clinical trials referral resource. Current clinical trials of 17-AG and 17-DMAG. Oncology (Williston Park) 18: 610-615 619-620.
    • (2004) Oncology (Williston Park) , vol.18 , pp. 610-615
    • Ivy, P.S.1    Schoenfeldt, M.2
  • 17
    • 0031572167 scopus 로고    scopus 로고
    • The structure and coding organization of the genomic termini of Kaposi's sarcoma-associated herpesvirus
    • Lagunoff M, Ganem D. (1997). The structure and coding organization of the genomic termini of Kaposi's sarcoma-associated herpesvirus. Virology 236: 147-154.
    • (1997) Virology , vol.236 , pp. 147-154
    • Lagunoff, M.1    Ganem, D.2
  • 18
    • 0033545865 scopus 로고    scopus 로고
    • Deregulated signal transduction by the K1 gene product of Kaposi's sarcoma-associated herpesvirus
    • Lagunoff M, Majeti R, Weiss A, Ganem D. (1999). Deregulated signal transduction by the K1 gene product of Kaposi's sarcoma-associated herpesvirus. Proc Natl Acad Sci USA 96: 5704-5709.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 5704-5709
    • Lagunoff, M.1    Majeti, R.2    Weiss, A.3    Ganem, D.4
  • 19
    • 4644301879 scopus 로고    scopus 로고
    • Regulation of vascular endothelial growth factor receptor 2-mediated phosphorylation of focal adhesion kinase by heat shock protein 90 and Src kinase activities
    • Le Boeuf F, Houle F, Huot J. (2004). Regulation of vascular endothelial growth factor receptor 2-mediated phosphorylation of focal adhesion kinase by heat shock protein 90 and Src kinase activities. J Biol Chem 279: 39175-39185.
    • (2004) J Biol Chem , vol.279 , pp. 39175-39185
    • Le Boeuf, F.1    Houle, F.2    Huot, J.3
  • 20
    • 0034600890 scopus 로고    scopus 로고
    • Inhibition of intracellular transport of B cell antigen receptor complexes by Kaposi's sarcoma-associated herpesvirus K1
    • Lee BS, Alvarez X, Ishido S, Lackner AA, Jung JU. (2000). Inhibition of intracellular transport of B cell antigen receptor complexes by Kaposi's sarcoma-associated herpesvirus K1. J Exp Med 192: 11-21.
    • (2000) J Exp Med , vol.192 , pp. 11-21
    • Lee, B.S.1    Alvarez, X.2    Ishido, S.3    Lackner, A.A.4    Jung, J.U.5
  • 21
    • 0037744675 scopus 로고    scopus 로고
    • Structural analysis of the Kaposi's sarcoma-associated herpesvirus K1 protein
    • Lee BS, Connole M, Tang Z, Harris NL, Jung JU. (2003). Structural analysis of the Kaposi's sarcoma-associated herpesvirus K1 protein. J Virol 77: 8072-8086.
    • (2003) J Virol , vol.77 , pp. 8072-8086
    • Lee, B.S.1    Connole, M.2    Tang, Z.3    Harris, N.L.4    Jung, J.U.5
  • 22
    • 25144462103 scopus 로고    scopus 로고
    • Characterization of the Kaposi's sarcoma-associated herpesvirus K1 signalosome
    • DOI 10.1128/JVI.79.19.12173-12184.2005
    • Lee BS, Lee SH, Feng P, Chang H, Cho NH, Jung JU. (2005). Characterization of the Kaposi's sarcoma-associated herpesvirus K1 signalosome. J Virol 79: 12173-12184. (Pubitemid 41346079)
    • (2005) Journal of Virology , vol.79 , Issue.19 , pp. 12173-12184
    • Lee, B.-S.1    Lee, S.-H.2    Feng, P.3    Chang, H.4    Cho, N.-H.5    Jung, J.U.6
  • 23
    • 0031813291 scopus 로고    scopus 로고
    • Identification of an immunoreceptor tyrosine-based activation motif of K1 transforming protein of Kaposi's sarcoma-associated herpesvirus
    • Lee H, Guo J, Li M, Choi JK, DeMaria M, Rosenzweig M et al. (1998a). Identification of an immunoreceptor tyrosine-based activation motif of K1 transforming protein of Kaposi's sarcoma-associated herpesvirus. Mol Cell Biol 18: 5219-5228.
    • (1998) Mol Cell Biol , vol.18 , pp. 5219-5228
    • Lee, H.1    Guo, J.2    Li, M.3    Choi, J.K.4    Demaria, M.5    Rosenzweig, M.6
  • 24
    • 17344385795 scopus 로고    scopus 로고
    • Deregulation of cell growth by the K1 gene of Kaposi's sarcoma-associated herpesvirus
    • Lee H, Veazey R, Williams K, Li M, Guo J, Neipel F et al. (1998b). Deregulation of cell growth by the K1 gene of Kaposi's sarcoma-associated herpesvirus. Nat Med 4: 435-440.
    • (1998) Nat Med , vol.4 , pp. 435-440
    • Lee, H.1    Veazey, R.2    Williams, K.3    Li, M.4    Guo, J.5    Neipel, F.6
  • 25
    • 0034615701 scopus 로고    scopus 로고
    • Disruption of hsp90 function results in degradation of the death domain kinase, receptor-interacting protein (RIP), and blockage of tumor necrosis factor-induced nuclear factor-kappaB activation
    • Lewis J, Devin A, Miller A, Lin Y, Rodriguez Y, Neckers L et al. (2000). Disruption of hsp90 function results in degradation of the death domain kinase, receptor-interacting protein (RIP), and blockage of tumor necrosis factor-induced nuclear factor-kappaB activation. J Biol Chem 275: 10519-10526.
    • (2000) J Biol Chem , vol.275 , pp. 10519-10526
    • Lewis, J.1    Devin, A.2    Miller, A.3    Lin, Y.4    Rodriguez, Y.5    Neckers, L.6
  • 26
    • 33947117494 scopus 로고    scopus 로고
    • Extracellular heat shock protein-90alpha: Linking hypoxia to skin cell motility and wound healing
    • Li W, Li Y, Guan S, Fan J, Cheng CF, Bright AM et al. (2007). Extracellular heat shock protein-90alpha: linking hypoxia to skin cell motility and wound healing. EMBO J 26: 1221-1233.
    • (2007) EMBO J , vol.26 , pp. 1221-1233
    • Li, W.1    Li, Y.2    Guan, S.3    Fan, J.4    Cheng, C.F.5    Bright, A.M.6
  • 27
    • 45749083004 scopus 로고    scopus 로고
    • Oligomerization of ICP4 and rearrangement of heat shock proteins may be important for herpes simplex virus type 1 prereplicative site formation
    • Livingston CM, DeLuca NA, Wilkinson DE, Weller SK. (2008). Oligomerization of ICP4 and rearrangement of heat shock proteins may be important for herpes simplex virus type 1 prereplicative site formation. J Virol 82: 6324-6336.
    • (2008) J Virol , vol.82 , pp. 6324-6336
    • Livingston, C.M.1    Deluca, N.A.2    Wilkinson, D.E.3    Weller, S.K.4
  • 28
    • 0029037110 scopus 로고
    • Mutational analysis of Hsp90 function: Interactions with a steroid receptor and a protein kinase
    • Nathan DF, Lindquist S. (1995). Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase. Mol Cell Biol 15: 3917-3925.
    • (1995) Mol Cell Biol , vol.15 , pp. 3917-3925
    • Nathan, D.F.1    Lindquist, S.2
  • 29
    • 32944461766 scopus 로고    scopus 로고
    • Suppression of the mTOR-raptor signaling pathway by the inhibitor of heat shock protein 90 geldanamycin
    • Ohji G, Hidayat S, Nakashima A, Tokunaga C, Oshiro N, Yoshino K et al. (2006). Suppression of the mTOR-raptor signaling pathway by the inhibitor of heat shock protein 90 geldanamycin. J Biochem 139: 129-135.
    • (2006) J Biochem , vol.139 , pp. 129-135
    • Ohji, G.1    Hidayat, S.2    Nakashima, A.3    Tokunaga, C.4    Oshiro, N.5    Yoshino, K.6
  • 30
    • 0035881864 scopus 로고    scopus 로고
    • FANCC interacts with Hsp70 to protect hematopoietic cells from IFN-gamma/TNF-alpha-mediated cytotoxicity
    • Pang Q, Keeble W, Christianson TA, Faulkner GR, Bagby GC. (2001). FANCC interacts with Hsp70 to protect hematopoietic cells from IFN-gamma/TNF-alpha- mediated cytotoxicity. EMBO J 20: 4478-4489.
    • (2001) EMBO J , vol.20 , pp. 4478-4489
    • Pang, Q.1    Keeble, W.2    Christianson, T.A.3    Faulkner, G.R.4    Bagby, G.C.5
  • 31
    • 33746364784 scopus 로고    scopus 로고
    • Structure and mechanism of the Hsp90 molecular chaperone machinery
    • Pearl LH, Prodromou C. (2006). Structure and mechanism of the Hsp90 molecular chaperone machinery. Annu Rev Biochem 75: 271-294.
    • (2006) Annu Rev Biochem , vol.75 , pp. 271-294
    • Pearl, L.H.1    Prodromou, C.2
  • 32
    • 0347481388 scopus 로고    scopus 로고
    • Misfolding, degradation, and aggregation of variant proteins. The molecular pathogenesis of short chain acyl-CoA dehydrogenase (SCAD) deficiency
    • Pedersen CB, Bross P, Winter VS, Corydon TJ, Bolund L, Bartlett K et al. (2003). Misfolding, degradation, and aggregation of variant proteins. The molecular pathogenesis of short chain acyl-CoA dehydrogenase (SCAD) deficiency. J Biol Chem 278: 47449-47458.
    • (2003) J Biol Chem , vol.278 , pp. 47449-47458
    • Pedersen, C.B.1    Bross, P.2    Winter, V.S.3    Corydon, T.J.4    Bolund, L.5    Bartlett, K.6
  • 33
    • 2942731290 scopus 로고    scopus 로고
    • Hsp90 invades the outside
    • Picard D. (2004). Hsp90 invades the outside. Nat Cell Biol 6: 479-480.
    • (2004) Nat Cell Biol , vol.6 , pp. 479-480
    • Picard, D.1
  • 35
    • 20844453394 scopus 로고    scopus 로고
    • Activation of Src kinase Lyn by the Kaposi sarcoma-associated herpesvirus K1 protein: Implications for lymphomagen-esis
    • Prakash O, Swamy OR, Peng X, Tang ZY, Li L, Larson JE et al. (2005). Activation of Src kinase Lyn by the Kaposi sarcoma-associated herpesvirus K1 protein: implications for lymphomagen-esis. Blood 105: 3987-3994.
    • (2005) Blood , vol.105 , pp. 3987-3994
    • Prakash, O.1    Swamy, O.R.2    Peng, X.3    Tang, Z.Y.4    Li, L.5    Larson, J.E.6
  • 36
    • 0037134705 scopus 로고    scopus 로고
    • Tumorigenesis and aberrant signaling in transgenic mice expressing the human herpesvirus-8 K1 gene
    • Prakash O, Tang ZY, Peng X, Coleman R, Gill J, Farr G et al. (2002). Tumorigenesis and aberrant signaling in transgenic mice expressing the human herpesvirus-8 K1 gene. J Natl Cancer Inst 94: 926-935.
    • (2002) J Natl Cancer Inst , vol.94 , pp. 926-935
    • Prakash, O.1    Tang, Z.Y.2    Peng, X.3    Coleman, R.4    Gill, J.5    Farr, G.6
  • 37
    • 0032828715 scopus 로고    scopus 로고
    • A generic protein purification method for protein complex characterization and proteome exploration
    • Rigaut G, Shevchenko A, Rutz B, Wilm M, Mann M, Seraphin B. (1999). A generic protein purification method for protein complex characterization and proteome exploration. Nat Biotechnol 17: 1030-1032.
    • (1999) Nat Biotechnol , vol.17 , pp. 1030-1032
    • Rigaut, G.1    Shevchenko, A.2    Rutz, B.3    Wilm, M.4    Mann, M.5    Seraphin, B.6
  • 38
    • 0003064250 scopus 로고    scopus 로고
    • Human herpesvirus 8 K1-associated nuclear factor-kappa B-dependent promoter activity: Role in Kaposi's sarcoma inflammation?
    • Samaniego F, Pati S, Karp JE, Prakash O, Bose D. (2001). Human herpesvirus 8 K1-associated nuclear factor-kappa B-dependent promoter activity: role in Kaposi's sarcoma inflammation? J Natl Cancer Inst Monogr 28: 15-23.
    • (2001) J Natl Cancer Inst Monogr , vol.28 , pp. 15-23
    • Samaniego, F.1    Pati, S.2    Karp, J.E.3    Prakash, O.4    Bose, D.5
  • 39
    • 0034718540 scopus 로고    scopus 로고
    • Modulation of Akt kinase activity by binding to Hsp90
    • Sato S, Fujita N, Tsuruo T. (2000). Modulation of Akt kinase activity by binding to Hsp90. Proc Natl Acad Sci USA 97: 10832-10837.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 10832-10837
    • Sato, S.1    Fujita, N.2    Tsuruo, T.3
  • 40
    • 33845913216 scopus 로고    scopus 로고
    • Intracellular and extracellular functions of heat shock proteins: Repercussions in cancer therapy
    • DOI 10.1189/jlb.0306167
    • Schmitt E, Gehrmann M, Brunet M, Multhoff G, Garrido C. (2007). Intracellular and extracellular functions of heat shock proteins: repercussions in cancer therapy. J Leukoc Biol 81: 15-27. (Pubitemid 46021247)
    • (2007) Journal of Leukocyte Biology , vol.81 , Issue.1 , pp. 15-27
    • Schmitt, E.1    Gehrmann, M.2    Brunet, M.3    Multhoff, G.4    Garrido, C.5
  • 41
    • 11144249887 scopus 로고    scopus 로고
    • ERdj3, a stress-inducible endoplas-mic reticulum DnaJ homologue, serves as a cofactor for BiP's interactions with unfolded substrates
    • Shen Y, Hendershot LM. (2005). ERdj3, a stress-inducible endoplas-mic reticulum DnaJ homologue, serves as a cofactor for BiP's interactions with unfolded substrates. Mol Biol Cell 16: 40-50.
    • (2005) Mol Biol Cell , vol.16 , pp. 40-50
    • Shen, Y.1    Hendershot, L.M.2
  • 42
    • 33745197774 scopus 로고    scopus 로고
    • Depletion of hsp90beta induces multiple defects in B cell receptor signaling
    • Shinozaki F, Minami M, Chiba T, Suzuki M, Yoshimatsu K, Ichikawa Y et al. (2006). Depletion of hsp90beta induces multiple defects in B cell receptor signaling. J Biol Chem 281: 16361-16369.
    • (2006) J Biol Chem , vol.281 , pp. 16361-16369
    • Shinozaki, F.1    Minami, M.2    Chiba, T.3    Suzuki, M.4    Yoshimatsu, K.5    Ichikawa, Y.6
  • 43
    • 8544274533 scopus 로고    scopus 로고
    • Involvement of cell surface HSP90 in cell migration reveals a novel role in the developing nervous system
    • Sidera K, Samiotaki M, Yfanti E, Panayotou G, Patsavoudi E. (2004). Involvement of cell surface HSP90 in cell migration reveals a novel role in the developing nervous system. J Biol Chem 279: 45379-45388.
    • (2004) J Biol Chem , vol.279 , pp. 45379-45388
    • Sidera, K.1    Samiotaki, M.2    Yfanti, E.3    Panayotou, G.4    Patsavoudi, E.5
  • 44
    • 0028828273 scopus 로고
    • Progesterone receptor structure and function altered by geldanamycin, an hsp90-binding agent
    • Smith DF, Whitesell L, Nair SC, Chen S, Prapapanich V, Rimerman RA. (1995). Progesterone receptor structure and function altered by geldanamycin, an hsp90-binding agent. Mol Cell Biol 15: 6804-6812.
    • (1995) Mol Cell Biol , vol.15 , pp. 6804-6812
    • Smith, D.F.1    Whitesell, L.2    Nair, S.C.3    Chen, S.4    Prapapanich, V.5    Rimerman, R.A.6
  • 45
    • 0029166033 scopus 로고
    • Kaposi's sarcoma-associated herpesvirus-like DNA sequences in multicentric Castleman's disease
    • Soulier J, Grollet L, Oksenhendler E, Cacoub P, Cazals-Hatem D, Babinet P et al. (1995). Kaposi's sarcoma-associated herpesvirus-like DNA sequences in multicentric Castleman's disease. Blood 86: 1276-1280.
    • (1995) Blood , vol.86 , pp. 1276-1280
    • Soulier, J.1    Grollet, L.2    Oksenhendler, E.3    Cacoub, P.4    Cazals-Hatem, D.5    Babinet, P.6
  • 46
    • 0842304506 scopus 로고    scopus 로고
    • The K1 Protein of Kaposi's Sarcoma-Associated Herpesvirus Activates the Akt Signaling Pathway
    • DOI 10.1128/JVI.78.4.1918-1927.2004
    • Tomlinson CC, Damania B. (2004). The K1 protein of Kaposi's sarcoma-associated herpesvirus activates the Akt signaling pathway. J Virol 78: 1918-1927. (Pubitemid 38176723)
    • (2004) Journal of Virology , vol.78 , Issue.4 , pp. 1918-1927
    • Tomlinson, C.C.1    Damania, B.2
  • 47
    • 45749104086 scopus 로고    scopus 로고
    • Critical role for endocytosis in the regulation of signaling by the Kaposi's sarcoma-associated herpes-virus K1 protein
    • Tomlinson CC, Damania B. (2008). Critical role for endocytosis in the regulation of signaling by the Kaposi's sarcoma-associated herpes-virus K1 protein. J Virol 82: 6514-6523.
    • (2008) J Virol , vol.82 , pp. 6514-6523
    • Tomlinson, C.C.1    Damania, B.2
  • 48
    • 58149399472 scopus 로고    scopus 로고
    • Geldanamycin-induced Lyn dissociation from aberrant Hsp90-stabilized cytosolic complex is an early event in apoptotic mechanisms in B-chronic lymphocytic leukemia
    • Trentin L, Frasson M, Donella-Deana A, Frezzato F, Pagano MA, Tibaldi E et al. (2008). Geldanamycin-induced Lyn dissociation from aberrant Hsp90-stabilized cytosolic complex is an early event in apoptotic mechanisms in B-chronic lymphocytic leukemia. Blood 112: 4665-4674.
    • (2008) Blood , vol.112 , pp. 4665-4674
    • Trentin, L.1    Frasson, M.2    Donella-Deana, A.3    Frezzato, F.4    Pagano, M.A.5    Tibaldi, E.6
  • 49
    • 33645741486 scopus 로고    scopus 로고
    • Immortalization of primary endothelial cells by the K1 protein of Kaposi's sarcoma-associated herpesvirus
    • Wang L, Dittmer DP, Tomlinson CC, Fakhari FD, Damania B. (2006). Immortalization of primary endothelial cells by the K1 protein of Kaposi's sarcoma-associated herpesvirus. Cancer Res 66: 3658-3666.
    • (2006) Cancer Res , vol.66 , pp. 3658-3666
    • Wang, L.1    Dittmer, D.P.2    Tomlinson, C.C.3    Fakhari, F.D.4    Damania, B.5
  • 50
    • 2442692617 scopus 로고    scopus 로고
    • The Kaposi's sarcoma-associated herpesvirus (KSHV/HHV-8) K1 protein induces expression of angiogenic and invasion factors
    • Wang L, Wakisaka N, Tomlinson CC, DeWire SM, Krall S, Pagano JS et al. (2004). The Kaposi's sarcoma-associated herpesvirus (KSHV/HHV-8) K1 protein induces expression of angiogenic and invasion factors. Cancer Res 64: 2774-2781.
    • (2004) Cancer Res , vol.64 , pp. 2774-2781
    • Wang, L.1    Wakisaka, N.2    Tomlinson, C.C.3    Dewire, S.M.4    Krall, S.5    Pagano, J.S.6
  • 51
    • 33847369549 scopus 로고    scopus 로고
    • K1 protein of human herpesvirus 8 suppresses lymphoma cell Fas-mediated apoptosis
    • Wang S, Wang S, Maeng H, Young DP, Prakash O, Fayad LE et al. (2007). K1 protein of human herpesvirus 8 suppresses lymphoma cell Fas-mediated apoptosis. Blood 109: 2174-2182.
    • (2007) Blood , vol.109 , pp. 2174-2182
    • Wang, S.1    Wang, S.2    Maeng, H.3    Young, D.P.4    Prakash, O.5    Fayad, L.E.6
  • 52
    • 0030878952 scopus 로고    scopus 로고
    • Geldanamycin-stimulated destabilization of mutated p53 is mediated by the proteasome in vivo
    • Whitesell L, Sutphin P, An WG, Schulte T, Blagosklonny MV, Neckers L. (1997). Geldanamycin-stimulated destabilization of mutated p53 is mediated by the proteasome in vivo. Oncogene 14: 2809-2816.
    • (1997) Oncogene , vol.14 , pp. 2809-2816
    • Whitesell, L.1    Sutphin, P.2    An, W.G.3    Schulte, T.4    Blagosklonny, M.V.5    Neckers, L.6
  • 53
    • 0345707575 scopus 로고    scopus 로고
    • The heat shock protein 90 inhibitor geldanamycin and the ErbB inhibitor ZD1839 promote rapid PP1 phosphatase-dependent inactivation of AKT in ErbB2 overexpressing breast cancer cells
    • Xu W, Yuan X, Jung YJ, Yang Y, Basso A, Rosen N et al. (2003). The heat shock protein 90 inhibitor geldanamycin and the ErbB inhibitor ZD1839 promote rapid PP1 phosphatase-dependent inactivation of AKT in ErbB2 overexpressing breast cancer cells. Cancer Res 63: 7777-7784.
    • (2003) Cancer Res , vol.63 , pp. 7777-7784
    • Xu, W.1    Yuan, X.2    Jung, Y.J.3    Yang, Y.4    Basso, A.5    Rosen, N.6
  • 54
    • 14744292998 scopus 로고    scopus 로고
    • Co-immunoprecipitation of Hsp101 with cytosolic Hsc70
    • Zhang C, Guy CL. (2005). Co-immunoprecipitation of Hsp101 with cytosolic Hsc70. Plant Physiol Biochem 43: 13-18.
    • (2005) Plant Physiol Biochem , vol.43 , pp. 13-18
    • Zhang, C.1    Guy, C.L.2


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