메뉴 건너뛰기




Volumn 122, Issue 1, 2012, Pages 174-189

Preclinical validation of AR42, a novel histone deacetylase inhibitor, as treatment for vestibular schwannomas

Author keywords

AKT; apoptosis; AR42; cell cycle arrest; histone deacetylase; histone deacetylase inhibitors; merlin; Neurofibromatosis type 2; vestibular schwannoma

Indexed keywords

AR 42; HISTONE DEACETYLASE INHIBITOR; PROTEIN KINASE B; UNCLASSIFIED DRUG;

EID: 84355161485     PISSN: 0023852X     EISSN: 15314995     Source Type: Journal    
DOI: 10.1002/lary.22392     Document Type: Article
Times cited : (37)

References (104)
  • 4
    • 33645790968 scopus 로고    scopus 로고
    • Malignant transformation and new primary tumours after therapeutic radiation for benign disease: Substantial risks in certain tumour prone syndromes
    • Evans DG, Birch JM, Ramsden RT, Sharif S, Baser ME,. Malignant transformation and new primary tumours after therapeutic radiation for benign disease: substantial risks in certain tumour prone syndromes. J Med Genet 2006; 43: 289-294.
    • (2006) J Med Genet , vol.43 , pp. 289-294
    • Evans, D.G.1    Birch, J.M.2    Ramsden, R.T.3    Sharif, S.4    Baser, M.E.5
  • 5
    • 38449089257 scopus 로고    scopus 로고
    • Glioblastoma multiforme after stereotactic radiotherapy for acoustic neuroma: Case report and review of the literature
    • Balasubramaniam A, Shannon P, Hodaie M, Laperriere N, Michaels H, Guha A,. Glioblastoma multiforme after stereotactic radiotherapy for acoustic neuroma: case report and review of the literature. Neuro Oncol 2007; 9: 447-453.
    • (2007) Neuro Oncol , vol.9 , pp. 447-453
    • Balasubramaniam, A.1    Shannon, P.2    Hodaie, M.3    Laperriere, N.4    Michaels, H.5    Guha, A.6
  • 6
    • 0035656226 scopus 로고    scopus 로고
    • Vestibular schwannoma with malignant transformation: A case report
    • Son EI, Kim IM, Kim SP,. Vestibular schwannoma with malignant transformation: a case report. J Korean Med Sci 2001; 16: 817-821.
    • (2001) J Korean Med Sci , vol.16 , pp. 817-821
    • Son, E.I.1    Kim, I.M.2    Kim, S.P.3
  • 7
    • 0001376559 scopus 로고
    • Contact inhibition, macromolecular synthesis, and polyribosomes in cultured human diploid fibroblasts
    • Levine EM, Becker Y, Boone CW, Eagle H,. Contact inhibition, macromolecular synthesis, and polyribosomes in cultured human diploid fibroblasts. Proc Natl Acad Sci U S A 1965; 53: 350-356.
    • (1965) Proc Natl Acad Sci U S A , vol.53 , pp. 350-356
    • Levine, E.M.1    Becker, Y.2    Boone, C.W.3    Eagle, H.4
  • 8
    • 78651195291 scopus 로고
    • Studies on delayed hypersensitivity. I. Inferences on the comparative binding affinities of antibodies mediating delayed and immediate hypersensitivity reactions in the guinea pig
    • Levine BB,. Studies on delayed hypersensitivity. I. Inferences on the comparative binding affinities of antibodies mediating delayed and immediate hypersensitivity reactions in the guinea pig. J Exp Med 1965; 121: 873-888.
    • (1965) J Exp Med , vol.121 , pp. 873-888
    • Levine, B.B.1
  • 9
    • 37049251927 scopus 로고
    • Cellular growth, contact inhibition, and macromolecular synthesis
    • Eagle H, Levine EM, Boone CW,. Cellular growth, contact inhibition, and macromolecular synthesis. Science 1965; 148: 665.
    • (1965) Science , vol.148 , pp. 665
    • Eagle, H.1    Levine, E.M.2    Boone, C.W.3
  • 10
    • 68149150655 scopus 로고    scopus 로고
    • Neurofibromatosis type 2 (NF2): A clinical and molecular review
    • Evans DG,. Neurofibromatosis type 2 (NF2): a clinical and molecular review. Orphanet J Rare Dis 2009; 4: 16.
    • (2009) Orphanet J Rare Dis , vol.4 , pp. 16
    • Evans, D.G.1
  • 11
    • 0019761388 scopus 로고
    • Central neurofibromatosis with bilateral acoustic neuroma
    • Eldridge R,. Central neurofibromatosis with bilateral acoustic neuroma. Adv Neurol 1981; 29: 57-65.
    • (1981) Adv Neurol , vol.29 , pp. 57-65
    • Eldridge, R.1
  • 12
    • 38549112079 scopus 로고    scopus 로고
    • Nf2/Merlin: A coordinator of receptor signalling and intercellular contact
    • DOI 10.1038/sj.bjc.6604002, PII 6604002
    • Curto M, McClatchey AI,. Nf2/Merlin: a coordinator of receptor signalling and intercellular contact. Br J Cancer 2008; 98: 256-262. (Pubitemid 351161230)
    • (2008) British Journal of Cancer , vol.98 , Issue.2 , pp. 256-262
    • Curto, M.1    McClatchey, A.I.2
  • 13
    • 33645868635 scopus 로고    scopus 로고
    • The tumor suppressors Merlin and expanded function cooperatively to modulate receptor endocytosis and signaling
    • Maitra S, Kulikauskas RM, Gavilan H, Fehon RG,. The tumor suppressors Merlin and expanded function cooperatively to modulate receptor endocytosis and signaling. Curr Biol 2006; 16: 702-709.
    • (2006) Curr Biol , vol.16 , pp. 702-709
    • Maitra, S.1    Kulikauskas, R.M.2    Gavilan, H.3    Fehon, R.G.4
  • 15
    • 4344609072 scopus 로고    scopus 로고
    • A NHERF binding site links the βPDGFR to the cytoskeleton and regulates cell spreading and migration
    • DOI 10.1242/jcs.01156
    • James MF, Beauchamp RL, Manchanda N, Kazlauskas A, Ramesh V,. A NHERF binding site links the betaPDGFR to the cytoskeleton and regulates cell spreading and migration. J Cell Sci 2004; 117: 2951-2961. (Pubitemid 39117670)
    • (2004) Journal of Cell Science , vol.117 , Issue.14 , pp. 2951-2961
    • James, M.F.1    Beauchamp, R.L.2    Manchanda, N.3    Kazlauskas, A.4    Ramesh, V.5
  • 16
    • 65149104670 scopus 로고    scopus 로고
    • Merlin and the ERM proteins-regulators of receptor distribution and signaling at the cell cortex
    • McClatchey AI, Fehon RG,. Merlin and the ERM proteins-regulators of receptor distribution and signaling at the cell cortex. Trends Cell Biol 2009; 19: 198-206.
    • (2009) Trends Cell Biol , vol.19 , pp. 198-206
    • McClatchey, A.I.1    Fehon, R.G.2
  • 17
    • 27844445642 scopus 로고    scopus 로고
    • Perturbations of the AKT signaling pathway in human cancer
    • DOI 10.1038/sj.onc.1209085, PII 1209085
    • Altomare DA, Testa JR,. Perturbations of the AKT signaling pathway in human cancer. Oncogene 2005; 24: 7455-7464. (Pubitemid 41637985)
    • (2005) Oncogene , vol.24 , Issue.50 , pp. 7455-7464
    • Altomare, D.A.1    Testa, J.R.2
  • 18
    • 38349042449 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase/AKT pathway activation in human vestibular schwannoma
    • Jacob A, Lee TX, Neff BA, Miller S, Welling B, Chang LS,. Phosphatidylinositol 3-kinase/AKT pathway activation in human vestibular schwannoma. Otol Neurotol 2008; 29: 58-68.
    • (2008) Otol Neurotol , vol.29 , pp. 58-68
    • Jacob, A.1    Lee, T.X.2    Neff, B.A.3    Miller, S.4    Welling, B.5    Chang, L.S.6
  • 19
    • 65849446043 scopus 로고    scopus 로고
    • Growth inhibitory and anti-tumour activities of OSU-03012, a novel PDK-1 inhibitor, on vestibular schwannoma and malignant schwannoma cells
    • Lee TX, Packer MD, Huang J, et al. Growth inhibitory and anti-tumour activities of OSU-03012, a novel PDK-1 inhibitor, on vestibular schwannoma and malignant schwannoma cells. Eur J Cancer 2009; 45: 1709-1720.
    • (2009) Eur J Cancer , vol.45 , pp. 1709-1720
    • Lee, T.X.1    Packer, M.D.2    Huang, J.3
  • 20
    • 70849088929 scopus 로고    scopus 로고
    • Activation of ERK, AKT and JNK signalling pathways in human schwannomas in situ
    • Hilton DA, Ristic N, Hanemann CO,. Activation of ERK, AKT and JNK signalling pathways in human schwannomas in situ. Histopathology 2009; 55: 744-749.
    • (2009) Histopathology , vol.55 , pp. 744-749
    • Hilton, D.A.1    Ristic, N.2    Hanemann, C.O.3
  • 21
    • 1842578986 scopus 로고    scopus 로고
    • Molecular evolution of the histone deacetylase family: Functional implications of phylogenetic analysis
    • DOI 10.1016/j.jmb.2004.02.006, PII S0022283604001408
    • Gregoretti IV, Lee YM, Goodson HV,. Molecular evolution of the histone deacetylase family: functional implications of phylogenetic analysis. J Mol Biol 2004; 338: 17-31. (Pubitemid 38429783)
    • (2004) Journal of Molecular Biology , vol.338 , Issue.1 , pp. 17-31
    • Gregoretti, I.V.1    Lee, Y.-M.2    Goodson, H.V.3
  • 22
    • 30344477367 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer
    • DOI 10.1038/nrc1779
    • Minucci S, Pelicci PG,. Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer. Nat Rev Cancer 2006; 6: 38-51. (Pubitemid 43054973)
    • (2006) Nature Reviews Cancer , vol.6 , Issue.1 , pp. 38-51
    • Minucci, S.1    Pelicci, P.G.2
  • 23
    • 33644663872 scopus 로고    scopus 로고
    • Histone acetylation-independent effect of histone deacetylase inhibitors on Akt through the reshuffling of protein phosphatase 1 complexes
    • Chen CS,. Histone acetylation-independent effect of histone deacetylase inhibitors on Akt through the reshuffling of protein phosphatase 1 complexes. J Biol Chem 2005; 280: 38879-38887.
    • (2005) J Biol Chem , vol.280 , pp. 38879-38887
    • Chen, C.S.1
  • 24
    • 80052766987 scopus 로고    scopus 로고
    • AR42, a novel histone deacetylase inhibitor, as a potential therapy for vestibular schwannomas and meningiomas
    • Bush ML, Oblinger J, Brendel V, et al. AR42, a novel histone deacetylase inhibitor, as a potential therapy for vestibular schwannomas and meningiomas. Neuro Oncol 2011; 13: 983-999.
    • (2011) Neuro Oncol , vol.13 , pp. 983-999
    • Bush, M.L.1    Oblinger, J.2    Brendel, V.3
  • 26
    • 18244373706 scopus 로고    scopus 로고
    • Enhanced pharmacodynamic and antitumor properties of a histone deacetylase inhibitor encapsulated in liposomes or ErbB2-targeted immunoliposomes
    • DOI 10.1158/1078-0432.CCR-04-2445
    • Drummond DC, Marx C, Guo Z, et al. Enhanced pharmacodynamic and antitumor properties of a histone deacetylase inhibitor encapsulated in liposomes or ErbB2-targeted immunoliposomes. Clin Cancer Res 2005; 11: 3392-3401. (Pubitemid 40627892)
    • (2005) Clinical Cancer Research , vol.11 , Issue.9 , pp. 3392-3401
    • Drummond, D.C.1    Marx, C.2    Guo, Z.3    Scott, G.4    Noble, C.5    Wang, D.6    Pallavicini, M.7    Kirpotin, D.B.8    Benz, C.C.9
  • 28
    • 36048958965 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Overview and perspectives
    • DOI 10.1158/1541-7786.MCR-07-0324
    • Dokmanovic M, Clarke C, Marks PA,. Histone deacetylase inhibitors: overview and perspectives. Mol Cancer Res 2007; 5: 981-989. (Pubitemid 350080267)
    • (2007) Molecular Cancer Research , vol.5 , Issue.10 , pp. 981-989
    • Dokmanovic, M.1    Clarke, C.2    Marks, P.A.3
  • 29
    • 26444439216 scopus 로고    scopus 로고
    • Prospects: Histone deacetylase inhibitors
    • DOI 10.1002/jcb.20532
    • Dokmanovic M, Marks PA,. Prospects: histone deacetylase inhibitors. J Cell Biochem 2005; 96: 293-304. (Pubitemid 41437862)
    • (2005) Journal of Cellular Biochemistry , vol.96 , Issue.2 , pp. 293-304
    • Dokmanovic, M.1    Marks, P.A.2
  • 30
    • 20444479514 scopus 로고    scopus 로고
    • Drug insight: Histone deacetylase inhibitors - Development of the new targeted anticancer agent suberoylanilide hydroxamic acid
    • DOI 10.1038/ncponc0106
    • Kelly WK, Marks PA,. Drug insight: Histone deacetylase inhibitors-development of the new targeted anticancer agent suberoylanilide hydroxamic acid. Nat Clin Pract Oncol 2005; 2: 150-157. (Pubitemid 40823166)
    • (2005) Nature Clinical Practice Oncology , vol.2 , Issue.3 , pp. 150-157
    • Kelly, W.K.1    Marks, P.A.2
  • 31
    • 34547864236 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Molecular mechanisms of action
    • DOI 10.1038/sj.onc.1210620, PII 1210620
    • Xu WS, Parmigiani RB, Marks PA,. Histone deacetylase inhibitors: molecular mechanisms of action. Oncogene 2007; 26: 5541-5552. (Pubitemid 47255934)
    • (2007) Oncogene , vol.26 , Issue.37 , pp. 5541-5552
    • Xu, W.S.1    Parmigiani, R.B.2    Marks, P.A.3
  • 32
    • 0038060250 scopus 로고    scopus 로고
    • Effects of FK228, a novel histone deacetylase inhibitor, on tumor growth and expression of p21 and c-myc genes in vivo
    • DOI 10.1016/S0304-3835(03)00184-8
    • Sasakawa Y, Naoe Y, Inoue T, et al. Effects of FK228, a novel histone deacetylase inhibitor, on tumor growth and expression of p21 and c-myc genes in vivo. Cancer Lett 2003; 195: 161-168. (Pubitemid 36588965)
    • (2003) Cancer Letters , vol.195 , Issue.2 , pp. 161-168
    • Sasakawa, Y.1    Naoe, Y.2    Inoue, T.3    Sasakawa, T.4    Matsuo, M.5    Manda, T.6    Mutoh, S.7
  • 33
    • 0036775301 scopus 로고    scopus 로고
    • Effects of FK228, a novel histone deacetylase inhibitor, on human lymphoma U-937 cells in vitro and in vivo
    • DOI 10.1016/S0006-2952(02)01261-3, PII S0006295202012613
    • Sasakawa Y, Naoe Y, Inoue T, et al. Effects of FK228, a novel histone deacetylase inhibitor, on human lymphoma U-937 cells in vitro and in vivo. Biochem Pharmacol 2002; 64: 1079-1090. (Pubitemid 35247815)
    • (2002) Biochemical Pharmacology , vol.64 , Issue.7 , pp. 1079-1090
    • Sasakawa, Y.1    Naoe, Y.2    Inoue, T.3    Sasakawa, T.4    Matsuo, M.5    Manda, T.6    Mutoh, S.7
  • 34
    • 0038620379 scopus 로고    scopus 로고
    • Cotreatment with the histone deacetylase inhibitor suberoylanilide hydroxamic acid (SAHA) enhances imatinib-induced apoptosis of Bcr-Abl-positive human acute leukemia cells
    • DOI 10.1182/blood-2002-08-2675
    • Nimmanapalli R, Fuino L, Stobaugh C, Richon V, Bhalla K,. Cotreatment with the histone deacetylase inhibitor suberoylanilide hydroxamic acid (SAHA) enhances imatinib-induced apoptosis of Bcr-Abl-positive human acute leukemia cells. Blood 2003; 101: 3236-3239. (Pubitemid 36858020)
    • (2003) Blood , vol.101 , Issue.8 , pp. 3236-3239
    • Nimmanapalli, R.1    Fuino, L.2    Stobaugh, C.3    Richon, V.4    Bhalla, K.5
  • 35
    • 33746338907 scopus 로고    scopus 로고
    • 1/S arrest induced by histone deacetylase inhibitor sodium butyrate in E1A + Ras-transformed cells is mediated through down-regulation of E2F activity and stabilization of β-catenin
    • DOI 10.1074/jbc.M511059200
    • Abramova MV, Pospelova TV, Nikulenkov FP, Hollander CM, Fornace AJ Jr, Pospelov VA,. G1/S arrest induced by histone deacetylase inhibitor sodium butyrate in E1A + Ras-transformed cells is mediated through down-regulation of E2F activity and stabilization of beta-catenin. J Biol Chem 2006; 281: 21040-21051. (Pubitemid 44115445)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.30 , pp. 21040-21051
    • Abramova, M.V.1    Pospelova, T.V.2    Nikulenkov, F.P.3    Hollander, C.M.4    Fornace Jr., A.J.5    Pospelov, V.A.6
  • 36
    • 25444472340 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor butyrate downregulates cyclin B1 gene expression via a p21/WAF-1-dependent mechanism in human colon cancer cells
    • Archer SY, Johnson J, Kim HJ, et al. The histone deacetylase inhibitor butyrate downregulates cyclin B1 gene expression via a p21/WAF-1-dependent mechanism in human colon cancer cells. Am J Physiol Gastrointest Liver Physiol 2005; 289: 696-703.
    • (2005) Am J Physiol Gastrointest Liver Physiol , vol.289 , pp. 696-703
    • Archer, S.Y.1    Johnson, J.2    Kim, H.J.3
  • 38
    • 0035834786 scopus 로고    scopus 로고
    • Activation of p21(WAF1/Cip1) transcription through Sp1 sites by histone deacetylase inhibitor apicidin: Involvement of protein kinase C
    • Han JW, Ahn SH, Kim YK, et al. Activation of p21(WAF1/Cip1) transcription through Sp1 sites by histone deacetylase inhibitor apicidin: involvement of protein kinase C. J Biol Chem 2001; 276: 42084-42090.
    • (2001) J Biol Chem , vol.276 , pp. 42084-42090
    • Han, J.W.1    Ahn, S.H.2    Kim, Y.K.3
  • 39
    • 0034326799 scopus 로고    scopus 로고
    • Apicidin, a histone deacetylase inhibitor, inhibits proliferation of tumor cells via induction of p21WAF1/Cip1 and gelsolin
    • Han JW, Ahn SH, Park SH, et al. Apicidin, a histone deacetylase inhibitor, inhibits proliferation of tumor cells via induction of p21WAF1/Cip1 and gelsolin. Cancer Res 2000; 60: 6068-6074.
    • (2000) Cancer Res , vol.60 , pp. 6068-6074
    • Han, J.W.1    Ahn, S.H.2    Park, S.H.3
  • 40
    • 77954541388 scopus 로고    scopus 로고
    • P21 Downregulation is an important component of PAX3/FKHR oncogenicity and its reactivation by HDAC inhibitors enhances combination treatment
    • Hecker RM, Amstutz RA, Wachtel M, Walter D, Niggli FK, Schafer BW,. p21 Downregulation is an important component of PAX3/FKHR oncogenicity and its reactivation by HDAC inhibitors enhances combination treatment. Oncogene 2010; 29: 3942-3952.
    • (2010) Oncogene , vol.29 , pp. 3942-3952
    • Hecker, R.M.1    Amstutz, R.A.2    Wachtel, M.3    Walter, D.4    Niggli, F.K.5    Schafer, B.W.6
  • 42
    • 58849160500 scopus 로고    scopus 로고
    • Heat shock protein 90 as a drug target: Some like it hot
    • Banerji U,. Heat shock protein 90 as a drug target: some like it hot. Clin Cancer Res 2009; 15: 9-14.
    • (2009) Clin Cancer Res , vol.15 , pp. 9-14
    • Banerji, U.1
  • 43
    • 34547122494 scopus 로고    scopus 로고
    • HDAC inhibitors: Clinical update and mechanism-based potential
    • DOI 10.1016/j.bcp.2007.04.007, PII S0006295207002262
    • Glaser KB,. HDAC inhibitors: clinical update and mechanism-based potential. Biochem Pharmacol 2007; 74: 659-671. (Pubitemid 47096639)
    • (2007) Biochemical Pharmacology , vol.74 , Issue.5 , pp. 659-671
    • Glaser, K.B.1
  • 44
    • 33746417580 scopus 로고    scopus 로고
    • Hsp90: A novel target for cancer therapy
    • DOI 10.2174/156802606777812068
    • Solit DB, Rosen N,. Hsp90: a novel target for cancer therapy. Curr Top Med Chem 2006; 6: 1205-1214. (Pubitemid 44120915)
    • (2006) Current Topics in Medicinal Chemistry , vol.6 , Issue.11 , pp. 1205-1214
    • Solit, D.B.1    Rosen, N.2
  • 45
    • 0346020435 scopus 로고    scopus 로고
    • The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress
    • DOI 10.1016/S0092-8674(03)00939-5
    • Kawaguchi Y, Kovacs JJ, McLaurin A, Vance JM, Ito A, Yao TP,. The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress. Cell 2003; 115: 727-738. (Pubitemid 38030301)
    • (2003) Cell , vol.115 , Issue.6 , pp. 727-738
    • Kawaguchi, Y.1    Kovacs, J.J.2    McLaurin, A.3    Vance, J.M.4    Ito, A.5    Yao, T.-P.6
  • 46
    • 43749109171 scopus 로고    scopus 로고
    • A novel histone deacetylase 8 (HDAC8)-specific inhibitor PCI-34051 induces apoptosis in T-cell lymphomas
    • DOI 10.1038/leu.2008.9, PII LEU20089
    • Balasubramanian S, Ramos J, Luo W, Sirisawad M, Verner E, Buggy JJ,. A novel histone deacetylase 8 (HDAC8)-specific inhibitor PCI-34051 induces apoptosis in T-cell lymphomas. Leukemia 2008; 22: 1026-1034. (Pubitemid 351689885)
    • (2008) Leukemia , vol.22 , Issue.5 , pp. 1026-1034
    • Balasubramanian, S.1    Ramos, J.2    Luo, W.3    Sirisawad, M.4    Verner, E.5    Buggy, J.J.6
  • 51
    • 37349061341 scopus 로고    scopus 로고
    • A natural histone deacetylase inhibitor, Psammaplin A, induces cell cycle arrest and apoptosis in human endometrial cancer cells
    • DOI 10.1016/j.ygyno.2007.08.098, PII S0090825807007135
    • Ahn MY, Jung JH, Na YJ, Kim HS,. A natural histone deacetylase inhibitor, Psammaplin A, induces cell cycle arrest and apoptosis in human endometrial cancer cells. Gynecol Oncol 2008; 108: 27-33. (Pubitemid 350299431)
    • (2008) Gynecologic Oncology , vol.108 , Issue.1 , pp. 27-33
    • Ahn, M.Y.1    Jung, J.H.2    Na, Y.J.3    Kim, H.S.4
  • 52
    • 77951034685 scopus 로고    scopus 로고
    • LGP1, A histone deacetylase inhibitor analogue of FR235222, sensitizes promyelocytic leukaemia U937 cells to TRAIL-mediated apoptosis
    • D'Acunto CW, Carratu A, Rodriquez M, Taddei M, Parente L, Petrella A,. LGP1, A histone deacetylase inhibitor analogue of FR235222, sensitizes promyelocytic leukaemia U937 cells to TRAIL-mediated apoptosis. Anticancer Res 2010; 30: 887-894.
    • (2010) Anticancer Res , vol.30 , pp. 887-894
    • D'Acunto, C.W.1    Carratu, A.2    Rodriquez, M.3    Taddei, M.4    Parente, L.5    Petrella, A.6
  • 54
    • 33749029926 scopus 로고    scopus 로고
    • Antitumor effects of a novel phenylbutyrate-based histone deacetylase inhibitor, (S)-HDAC-42, in prostate cancer
    • DOI 10.1158/1078-0432.CCR-06-0429
    • Kulp SK, Chen CS, Wang DS, Chen CY,. Antitumor effects of a novel phenylbutyrate-based histone deacetylase inhibitor, (S)-HDAC-42, in prostate cancer. Clin Cancer Res 2006; 12: 5199-5206. (Pubitemid 44453349)
    • (2006) Clinical Cancer Research , vol.12 , Issue.17 , pp. 5199-5206
    • Kulp, S.K.1    Chen, C.-S.2    Wang, D.-S.3    Chen, C.-Y.4    Chen, C.-S.5
  • 55
    • 43249120953 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Mechanisms and clinical significance in cancer: HDAC inhibitor-induced apoptosis
    • Shankar S, Srivastava RK,. Histone deacetylase inhibitors: mechanisms and clinical significance in cancer: HDAC inhibitor-induced apoptosis. Adv Exp Med Biol 2008; 615: 261-298.
    • (2008) Adv Exp Med Biol , vol.615 , pp. 261-298
    • Shankar, S.1    Srivastava, R.K.2
  • 56
    • 77957752356 scopus 로고    scopus 로고
    • HDAC-mediated control of ERK- and PI3K-dependent TGF-beta-induced extracellular matrix-regulating genes
    • Barter MJ, Pybus L, Litherland GJ, et al. HDAC-mediated control of ERK- and PI3K-dependent TGF-beta-induced extracellular matrix-regulating genes. Matrix Biol 2010; 29: 602-612.
    • (2010) Matrix Biol , vol.29 , pp. 602-612
    • Barter, M.J.1    Pybus, L.2    Litherland, G.J.3
  • 57
    • 33746380872 scopus 로고    scopus 로고
    • Involvement of HDAC1 and the PI3K/PKC signaling pathways in NF-κB activation by the HDAC inhibitor apicidin
    • DOI 10.1016/j.bbrc.2006.06.196, PII S0006291X06015506
    • Kim YK, Seo DW, Kang DW, Lee HY, Han JW, Kim SN,. Involvement of HDAC1 and the PI3K/PKC signaling pathways in NF-kappaB activation by the HDAC inhibitor apicidin. Biochem Biophys Res Commun 2006; 347: 1088-1093. (Pubitemid 44118225)
    • (2006) Biochemical and Biophysical Research Communications , vol.347 , Issue.4 , pp. 1088-1093
    • Kim, Y.K.1    Seo, D.-W.2    Kang, D.-W.3    Lee, H.Y.4    Han, J.-W.5    Kim, S.-N.6
  • 59
    • 74449089863 scopus 로고    scopus 로고
    • Blockade of the ERK or PI3K-Akt signaling pathway enhances the cytotoxicity of histone deacetylase inhibitors in tumor cells resistant to gefitinib or imatinib
    • Ozaki K, Kosugi M, Baba N, et al. Blockade of the ERK or PI3K-Akt signaling pathway enhances the cytotoxicity of histone deacetylase inhibitors in tumor cells resistant to gefitinib or imatinib. Biochem Biophys Res Commun 2010; 391: 1610-1615.
    • (2010) Biochem Biophys Res Commun , vol.391 , pp. 1610-1615
    • Ozaki, K.1    Kosugi, M.2    Baba, N.3
  • 65
    • 56649111200 scopus 로고    scopus 로고
    • HDAC inhibition upregulates the expression of angiostatic ADAMTS1
    • Chou CW, Chen CC,. HDAC inhibition upregulates the expression of angiostatic ADAMTS1. FEBS Lett 2008; 582: 4059-4065.
    • (2008) FEBS Lett , vol.582 , pp. 4059-4065
    • Chou, C.W.1    Chen, C.C.2
  • 68
    • 0037225763 scopus 로고    scopus 로고
    • Inhibition of hypoxia-induced angiogenesis by FK228, a specific histone deacetylase inhibitor, via suppression of HIF-1alpha activity
    • Mie Lee Y, Kim SH, Kim HS, et al. Inhibition of hypoxia-induced angiogenesis by FK228, a specific histone deacetylase inhibitor, via suppression of HIF-1alpha activity. Biochem Biophys Res Commun 2003; 300: 241-246.
    • (2003) Biochem Biophys Res Commun , vol.300 , pp. 241-246
    • Mie Lee, Y.1    Kim, S.H.2    Kim, H.S.3
  • 70
    • 0034899511 scopus 로고    scopus 로고
    • Trichostatin A, an inhibitor of histone deacetylase, inhibits hypoxia-induced angiogenesis
    • DOI 10.1517/13543784.10.8.1571
    • Williams RJ,. Trichostatin A, an inhibitor of histone deacetylase, inhibits hypoxia-induced angiogenesis. Expert Opin Investig Drugs 2001; 10: 1571-1573. (Pubitemid 32717337)
    • (2001) Expert Opinion on Investigational Drugs , vol.10 , Issue.8 , pp. 1571-1573
    • Williams, R.J.1
  • 71
    • 0037131187 scopus 로고    scopus 로고
    • Akt forms an intracellular complex with heat shock protein 90 (Hsp90) and Cdc37 and is destabilized by inhibitors of Hsp90 function
    • DOI 10.1074/jbc.M206322200
    • Basso AD, Solit DB, Chiosis G, Giri B, Tsichlis P, Rosen N,. Akt forms an intracellular complex with heat shock protein 90 (Hsp90) and Cdc37 and is destabilized by inhibitors of Hsp90 function. J Biol Chem 2002; 277: 39858-39866. (Pubitemid 35190971)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.42 , pp. 39858-39866
    • Basso, A.D.1    Solit, D.B.2    Chiosis, G.3    Giri, B.4    Tsichlis, P.5    Rosen, N.6
  • 72
    • 0037155901 scopus 로고    scopus 로고
    • Involvement of Hsp90 in signaling and stability of 3-phosphoinositide- dependent kinase-1
    • DOI 10.1074/jbc.M106736200
    • Fujita N, Sato S, Ishida A, Tsuruo T,. Involvement of Hsp90 in signaling and stability of 3-phosphoinositide-dependent kinase-1. J Biol Chem 2002; 277: 10346-10353. (Pubitemid 34968152)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.12 , pp. 10346-10353
    • Fujita, N.1    Sato, S.2    Ishida, A.3    Tsuruo, T.4
  • 74
    • 52649133274 scopus 로고    scopus 로고
    • HDAC6 inhibition enhances 17-AAG-mediated abrogation of hsp90 chaperone function in human leukemia cells
    • Rao R, Fiskus W, Yang Y, et al. HDAC6 inhibition enhances 17-AAG-mediated abrogation of hsp90 chaperone function in human leukemia cells. Blood 2008; 112: 1886-1893.
    • (2008) Blood , vol.112 , pp. 1886-1893
    • Rao, R.1    Fiskus, W.2    Yang, Y.3
  • 75
    • 0034718540 scopus 로고    scopus 로고
    • Modulation of Akt kinase activity by binding to Hsp90
    • Sato S, Fujita N, Tsuruo T,. Modulation of Akt kinase activity by binding to Hsp90. Proc Natl Acad Sci U S A 2000; 97: 10832-10837.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 10832-10837
    • Sato, S.1    Fujita, N.2    Tsuruo, T.3
  • 76
    • 48549095272 scopus 로고    scopus 로고
    • Dissecting and targeting the growth factor-dependent and growth factor-independent extracellular signal-regulated kinase pathway in human schwannoma
    • Ammoun S, Flaiz C, Ristic N, Schuldt J, Hanemann CO,. Dissecting and targeting the growth factor-dependent and growth factor-independent extracellular signal-regulated kinase pathway in human schwannoma. Cancer Res 2008; 68: 5236-5245.
    • (2008) Cancer Res , vol.68 , pp. 5236-5245
    • Ammoun, S.1    Flaiz, C.2    Ristic, N.3    Schuldt, J.4    Hanemann, C.O.5
  • 77
    • 78149474027 scopus 로고    scopus 로고
    • ErbB/HER receptor activation and preclinical efficacy of lapatinib in vestibular schwannoma
    • Ammoun S, Cunliffe CH, Allen JC, et al. ErbB/HER receptor activation and preclinical efficacy of lapatinib in vestibular schwannoma. Neuro Oncol 2010; 12: 834-843.
    • (2010) Neuro Oncol , vol.12 , pp. 834-843
    • Ammoun, S.1    Cunliffe, C.H.2    Allen, J.C.3
  • 80
    • 77953408308 scopus 로고    scopus 로고
    • Physiological regulation of Akt activity and stability
    • Liao Y, Hung MC,. Physiological regulation of Akt activity and stability. Am J Transl Res 2010; 2: 19-42.
    • (2010) Am J Transl Res , vol.2 , pp. 19-42
    • Liao, Y.1    Hung, M.C.2
  • 81
    • 65949108039 scopus 로고    scopus 로고
    • Akt phosphorylation of merlin enhances its binding to phosphatidylinositols and inhibits the tumor-suppressive activities of merlin
    • Okada M, Wang Y, Jang SW, Tang X, Neri LM, Ye K,. Akt phosphorylation of merlin enhances its binding to phosphatidylinositols and inhibits the tumor-suppressive activities of merlin. Cancer Res 2009; 69: 4043-4051.
    • (2009) Cancer Res , vol.69 , pp. 4043-4051
    • Okada, M.1    Wang, Y.2    Jang, S.W.3    Tang, X.4    Neri, L.M.5    Ye, K.6
  • 82
    • 66549126222 scopus 로고    scopus 로고
    • Phosphorylation of merlin regulates its stability and tumor suppressive activity
    • Ye K,. Phosphorylation of merlin regulates its stability and tumor suppressive activity. Cell Adh Migr 2007; 1: 196-198.
    • (2007) Cell Adh Migr , vol.1 , pp. 196-198
    • Ye, K.1
  • 84
    • 0031566693 scopus 로고    scopus 로고
    • A Bad kinase makes good
    • DOI 10.1038/36442
    • Franke TF, Cantley LC,. Apoptosis. A Bad kinase makes good. Nature 1997; 390: 116-117. (Pubitemid 27507959)
    • (1997) Nature , vol.390 , Issue.6656 , pp. 116-117
    • Franke, T.F.1    Cantley, L.C.2
  • 85
    • 0034462121 scopus 로고    scopus 로고
    • Forkhead transcription factors are critical effectors of cell death and cell cycle arrest downstream of PTEN
    • DOI 10.1128/MCB.20.23.8969-8982.2000
    • Nakamura N, Ramaswamy S, Vazquez F, Signoretti S, Loda M, Sellers WR,. Forkhead transcription factors are critical effectors of cell death and cell cycle arrest downstream of PTEN. Mol Cell Biol 2000; 20: 8969-8982. (Pubitemid 32245927)
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.23 , pp. 8969-8982
    • Nakamura, N.1    Ramaswamy, S.2    Vazquez, F.3    Signoretti, S.4    Loda, M.5    Sellers, W.R.6
  • 87
  • 88
    • 0029587224 scopus 로고
    • Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
    • DOI 10.1038/378785a0
    • Cross DA, Alessi DR, Cohen P, Andjelkovich M, Hemmings BA,. Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B. Nature 1995; 378: 785-789. (Pubitemid 26004411)
    • (1995) Nature , vol.378 , Issue.6559 , pp. 785-789
    • Cross, D.A.E.1    Alessi, D.R.2    Cohen, P.3    Andjelkovich, M.4    Hemmings, B.A.5
  • 89
    • 0036714127 scopus 로고    scopus 로고
    • Akt regulates growth by directly phosphorylating Tsc2
    • DOI 10.1038/ncb840
    • Potter CJ, Pedraza LG, Xu T,. Akt regulates growth by directly phosphorylating Tsc2. Nat Cell Biol 2002; 4: 658-665. (Pubitemid 34993701)
    • (2002) Nature Cell Biology , vol.4 , Issue.9 , pp. 658-665
    • Potter, C.J.1    Pedraza, L.G.2    Xu, T.3
  • 91
    • 0036342294 scopus 로고    scopus 로고
    • Identification of the tuberous sclerosis complex-2 tumor suppressor gene product tuberin as a target of the phosphoinositide 3-kinase/Akt pathway
    • DOI 10.1016/S1097-2765(02)00568-3
    • Manning BD, Tee AR, Logsdon MN, Blenis J, Cantley LC,. Identification of the tuberous sclerosis complex-2 tumor suppressor gene product tuberin as a target of the phosphoinositide 3-kinase/akt pathway. Mol Cell 2002; 10: 151-162. (Pubitemid 34876569)
    • (2002) Molecular Cell , vol.10 , Issue.1 , pp. 151-162
    • Manning, B.D.1    Tee, A.R.2    Logsdon M.Nicole3    Blenis, J.4    Cantley, L.C.5
  • 92
    • 0032533225 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3β regulates cyclin D1 proteolysis and subcellular localization
    • Diehl JA, Cheng M, Roussel MF, Sherr CJ,. Glycogen synthase kinase-3beta regulates cyclin D1 proteolysis and subcellular localization. Genes Dev 1998; 12: 3499-3511. (Pubitemid 28553242)
    • (1998) Genes and Development , vol.12 , Issue.22 , pp. 3499-3511
    • Diehl, J.A.1    Cheng, M.2    Roussel, M.F.3    Sherr, C.J.4
  • 93
    • 0038003956 scopus 로고    scopus 로고
    • Decisions on life and death: FOXO Forkhead transcription factors are in command when PKB/Akt is off duty
    • DOI 10.1189/jlb.1202629
    • Burgering BM, Medema RH,. Decisions on life and death: FOXO Forkhead transcription factors are in command when PKB/Akt is off duty. J Leukoc Biol 2003; 73: 689-701. (Pubitemid 38040447)
    • (2003) Journal of Leukocyte Biology , vol.73 , Issue.6 , pp. 689-701
    • Burgering, B.M.T.1    Medema, R.H.2
  • 94
    • 0036799377 scopus 로고    scopus 로고
    • Kip1 at threonine 157 and modulation of its cellular localization
    • DOI 10.1038/nm759
    • Shin I, Yakes FM, Rojo F, et al. PKB/Akt mediates cell-cycle progression by phosphorylation of p27(Kip1) at threonine 157 and modulation of its cellular localization. Nat Med 2002; 8: 1145-1152. (Pubitemid 35175970)
    • (2002) Nature Medicine , vol.8 , Issue.10 , pp. 1145-1152
    • Shin, I.1    Yakes, F.M.2    Rojo, F.3    Shin, N.-Y.4    Bakin, A.V.5    Baselga, J.6    Arteaga, C.L.7
  • 98
    • 0035736487 scopus 로고    scopus 로고
    • HER-2/neu induces p53 ubiquitination via Akt-mediated MDM2 phosphorylation
    • DOI 10.1038/ncb1101-973
    • Zhou BP, Liao Y, Xia W, Zou Y, Spohn B, Hung MC,. HER-2/neu induces p53 ubiquitination via Akt-mediated MDM2 phosphorylation. Nat Cell Biol 2001; 3: 973-982. (Pubitemid 34428742)
    • (2001) Nature Cell Biology , vol.3 , Issue.11 , pp. 973-982
    • Zhou, B.P.1    Liao, Y.2    Xia, W.3    Zou, Y.4    Spohn, B.5    Hung, M.-C.6
  • 99
    • 0034745353 scopus 로고    scopus 로고
    • CIP1/WAF1 by Akt-induced phosphorylation in HER-2/neu-overexpressing cells
    • DOI 10.1038/35060032
    • Zhou BP, Liao Y, Xia W, Spohn B, Lee MH, Hung MC,. Cytoplasmic localization of p21Cip1/WAF1 by Akt-induced phosphorylation in HER-2/neu-overexpressing cells. Nat Cell Biol 2001; 3: 245-252. (Pubitemid 32201319)
    • (2001) Nature Cell Biology , vol.3 , Issue.3 , pp. 245-252
    • Zhou, B.P.1    Liao, Y.2    Xia, W.3    Spohn, B.4    Lee, M.-H.5    Hung, M.-C.6
  • 101
    • 0033527577 scopus 로고    scopus 로고
    • Heregulin induces phosphorylation of BRCA1 through phosphatidylinositol 3-Kinase/AKT in breast cancer cells
    • Altiok S, Batt D, Altiok N, et al. Heregulin induces phosphorylation of BRCA1 through phosphatidylinositol 3-Kinase/AKT in breast cancer cells. J Biol Chem 1999; 274: 32274-32278.
    • (1999) J Biol Chem , vol.274 , pp. 32274-32278
    • Altiok, S.1    Batt, D.2    Altiok, N.3
  • 102
    • 0037018847 scopus 로고    scopus 로고
    • A role for PI 3-kinase and PKB activity in the G2/M phase of the cell cycle
    • DOI 10.1016/S0960-9822(02)00843-6, PII S0960982202008436
    • Shtivelman E, Sussman J, Stokoe D,. A role for PI 3-kinase and PKB activity in the G2/M phase of the cell cycle. Curr Biol 2002; 12: 919-924. (Pubitemid 34689227)
    • (2002) Current Biology , vol.12 , Issue.11 , pp. 919-924
    • Shtivelman, E.1    Sussman, J.2    Stokoe, D.3
  • 103
    • 23644434852 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: Insights into mechanisms of lethality
    • DOI 10.1517/14728222.9.4.809
    • Rosato RR, Grant S,. Histone deacetylase inhibitors: insights into mechanisms of lethality. Expert Opin Ther Targets 2005; 9: 809-824. (Pubitemid 41131680)
    • (2005) Expert Opinion on Therapeutic Targets , vol.9 , Issue.4 , pp. 809-824
    • Rosato, R.R.1    Grant, S.2
  • 104
    • 45549091261 scopus 로고    scopus 로고
    • OSU-HDAC42, a Histone Deacetylase Inhibitor, Blocks Prostate Tumor Progression in the Transgenic Adenocarcinoma of the Mouse Prostate Model
    • Sargeant AM, Rengel RC, Kulp SK, et al. OSU-HDAC42, a Histone Deacetylase Inhibitor, Blocks Prostate Tumor Progression in the Transgenic Adenocarcinoma of the Mouse Prostate Model. Cancer Res 2008; 68: 3999-4009.
    • (2008) Cancer Res , vol.68 , pp. 3999-4009
    • Sargeant, A.M.1    Rengel, R.C.2    Kulp, S.K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.