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Volumn 8, Issue 1, 2015, Pages

The synergic effect of vincristine and vorinostat in leukemia in vitro and in vivo

Author keywords

HDAC6; Leukemia; SAHA; Vincristine

Indexed keywords

ALPHA TUBULIN; CASPASE; HISTONE DEACETYLASE 6; VINCRISTINE; VORINOSTAT; ANTINEOPLASTIC AGENT; HYDROXAMIC ACID;

EID: 84938879952     PISSN: None     EISSN: 17568722     Source Type: Journal    
DOI: 10.1186/s13045-015-0176-7     Document Type: Article
Times cited : (76)

References (38)
  • 1
    • 20044379059 scopus 로고    scopus 로고
    • Review: Tubulin function, action of antitubulin drugs, and new drug development
    • 1:CAS:528:DC%2BD2MXkslyhu74%3D 15948296
    • Pellegrini F, Budman DR. Review: tubulin function, action of antitubulin drugs, and new drug development. Cancer Invest. 2005;23(3):264-73.
    • (2005) Cancer Invest , vol.23 , Issue.3 , pp. 264-273
    • Pellegrini, F.1    Budman, D.R.2
  • 2
    • 29344471072 scopus 로고    scopus 로고
    • Understanding microtubule dynamics for improved cancer therapy
    • 1:CAS:528:DC%2BD28Xms1Grug%3D%3D 16314924
    • Honore S, Pasquier E, Braguer D. Understanding microtubule dynamics for improved cancer therapy. Cell Mol Life Sci. 2005;62(24):3039-56. doi: 10.1007/s00018-005-5330-x.
    • (2005) Cell Mol Life Sci , vol.62 , Issue.24 , pp. 3039-3056
    • Honore, S.1    Pasquier, E.2    Braguer, D.3
  • 3
    • 64049097460 scopus 로고    scopus 로고
    • Microtubule dynamics as a target in oncology
    • 1:CAS:528:DC%2BD1MXksVantrg%3D 2778221 19117686
    • Risinger AL, Giles FJ, Mooberry SL. Microtubule dynamics as a target in oncology. Cancer Treat Rev. 2009;35(3):255-61. doi: 10.1016/j.ctrv.2008.11.001.
    • (2009) Cancer Treat Rev , vol.35 , Issue.3 , pp. 255-261
    • Risinger, A.L.1    Giles, F.J.2    Mooberry, S.L.3
  • 4
    • 77957374075 scopus 로고    scopus 로고
    • Microtubule-binding agents: A dynamic field of cancer therapeutics
    • 1:CAS:528:DC%2BC3cXht1akur%2FI 3194401 20885410
    • Dumontet C, Jordan MA. Microtubule-binding agents: a dynamic field of cancer therapeutics. Nat Rev Drug Discov. 2010;9(10):790-803. doi: 10.1038/nrd3253.
    • (2010) Nat Rev Drug Discov , vol.9 , Issue.10 , pp. 790-803
    • Dumontet, C.1    Jordan, M.A.2
  • 5
    • 0033044418 scopus 로고    scopus 로고
    • Microtubules and signal transduction
    • 1:CAS:528:DyaK1MXhsFSnur0%3D 10047525
    • Gundersen GG, Cook TA. Microtubules and signal transduction. Curr Opin Cell Biol. 1999;11(1):81-94.
    • (1999) Curr Opin Cell Biol , vol.11 , Issue.1 , pp. 81-94
    • Gundersen, G.G.1    Cook, T.A.2
  • 6
    • 68849087436 scopus 로고    scopus 로고
    • Microtubule inhibitors: Differentiating tubulin-inhibiting agents based on mechanisms of action, clinical activity, and resistance
    • 1:CAS:528:DC%2BD1MXpvFCnurw%3D 19671735
    • Perez EA. Microtubule inhibitors: differentiating tubulin-inhibiting agents based on mechanisms of action, clinical activity, and resistance. Mol Cancer Ther. 2009;8(8):2086-95. doi: 10.1158/1535-7163.mct-09-0366.
    • (2009) Mol Cancer Ther , vol.8 , Issue.8 , pp. 2086-2095
    • Perez, E.A.1
  • 7
    • 0037444803 scopus 로고    scopus 로고
    • Histone deacetylases (HDACs): Characterization of the classical HDAC family
    • 1223209 12429021
    • De Ruijter AJ, Van Gennip AH, Caron HN, Kemp S, Van Kuilenburg AB. Histone deacetylases (HDACs): characterization of the classical HDAC family. Biochem J. 2003;370(Pt 3):737-49. doi: 10.1042/bj20021321.
    • (2003) Biochem J , vol.370 , pp. 737-749
    • De Ruijter, A.J.1    Van Gennip, A.H.2    Caron, H.N.3    Kemp, S.4    Van Kuilenburg, A.B.5
  • 8
    • 0037406061 scopus 로고    scopus 로고
    • Class II histone deacetylases: Versatile regulators
    • 1:CAS:528:DC%2BD3sXjtFeqt7o%3D 12711221
    • Verdin E, Dequiedt F, Kasler HG. Class II histone deacetylases: versatile regulators. Trends Genet. 2003;19(5):286-93. doi: 10.1016/s0168-9525(03)00073-8.
    • (2003) Trends Genet , vol.19 , Issue.5 , pp. 286-293
    • Verdin, E.1    Dequiedt, F.2    Kasler, H.G.3
  • 9
    • 34547684065 scopus 로고    scopus 로고
    • HDAC6, at the crossroads between cytoskeleton and cell signaling by acetylation and ubiquitination
    • 1:CAS:528:DC%2BD2sXovFersrw%3D 17694087
    • Boyault C, Sadoul K, Pabion M, Khochbin S. HDAC6, at the crossroads between cytoskeleton and cell signaling by acetylation and ubiquitination. Oncogene. 2007;26(37):5468-76. doi: 10.1038/sj.onc.1210614.
    • (2007) Oncogene , vol.26 , Issue.37 , pp. 5468-5476
    • Boyault, C.1    Sadoul, K.2    Pabion, M.3    Khochbin, S.4
  • 10
    • 0037161744 scopus 로고    scopus 로고
    • HDAC6 is a microtubule-associated deacetylase
    • 1:CAS:528:DC%2BD38XjvVersr4%3D 12024216
    • Hubbert C, Guardiola A, Shao R, Kawaguchi Y, Ito A, Nixon A, et al. HDAC6 is a microtubule-associated deacetylase. Nature. 2002;417(6887):455-8. doi: 10.1038/417455a.
    • (2002) Nature , vol.417 , Issue.6887 , pp. 455-458
    • Hubbert, C.1    Guardiola, A.2    Shao, R.3    Kawaguchi, Y.4    Ito, A.5    Nixon, A.6
  • 11
    • 12244295468 scopus 로고    scopus 로고
    • In vivo destabilization of dynamic microtubules by HDAC6-mediated deacetylation
    • 1:CAS:528:DC%2BD38XpslOgsrc%3D 139102 12486003
    • Matsuyama A, Shimazu T, Sumida Y, Saito A, Yoshimatsu Y, Seigneurin-Berny D, et al. In vivo destabilization of dynamic microtubules by HDAC6-mediated deacetylation. EMBO J. 2002;21(24):6820-31.
    • (2002) EMBO J , vol.21 , Issue.24 , pp. 6820-6831
    • Matsuyama, A.1    Shimazu, T.2    Sumida, Y.3    Saito, A.4    Yoshimatsu, Y.5    Seigneurin-Berny, D.6
  • 12
    • 0037416151 scopus 로고    scopus 로고
    • HDAC-6 interacts with and deacetylates tubulin and microtubules in vivo
    • 1:CAS:528:DC%2BD3sXit1yls7c%3D 150348 12606581
    • Zhang Y, Li N, Caron C, Matthias G, Hess D, Khochbin S, et al. HDAC-6 interacts with and deacetylates tubulin and microtubules in vivo. EMBO J. 2003;22(5):1168-79. doi: 10.1093/emboj/cdg115.
    • (2003) EMBO J , vol.22 , Issue.5 , pp. 1168-1179
    • Zhang, Y.1    Li, N.2    Caron, C.3    Matthias, G.4    Hess, D.5    Khochbin, S.6
  • 13
    • 1842631408 scopus 로고    scopus 로고
    • Upregulation and nuclear recruitment of HDAC1 in hormone refractory prostate cancer
    • 1:CAS:528:DC%2BD2cXktl2lsLo%3D 15042618
    • Halkidou K, Gaughan L, Cook S, Leung HY, Neal DE, Robson CN. Upregulation and nuclear recruitment of HDAC1 in hormone refractory prostate cancer. Prostate. 2004;59(2):177-89. doi: 10.1002/pros.20022.
    • (2004) Prostate , vol.59 , Issue.2 , pp. 177-189
    • Halkidou, K.1    Gaughan, L.2    Cook, S.3    Leung, H.Y.4    Neal, D.E.5    Robson, C.N.6
  • 14
    • 33744956666 scopus 로고    scopus 로고
    • Histone deacetylase 3 (HDAC3) and other class i HDACs regulate colon cell maturation and p21 expression and are deregulated in human colon cancer
    • 1:CAS:528:DC%2BD28Xkt1ymt7Y%3D 16533812
    • Wilson AJ, Byun DS, Popova N, Murray LB, L'Italien K, Sowa Y, et al. Histone deacetylase 3 (HDAC3) and other class I HDACs regulate colon cell maturation and p21 expression and are deregulated in human colon cancer. J Biol Chem. 2006;281(19):13548-58. doi: 10.1074/jbc.M510023200.
    • (2006) J Biol Chem , vol.281 , Issue.19 , pp. 13548-13558
    • Wilson, A.J.1    Byun, D.S.2    Popova, N.3    Murray, L.B.4    L'Italien, K.5    Sowa, Y.6
  • 15
    • 2342603414 scopus 로고    scopus 로고
    • Induction of HDAC2 expression upon loss of APC in colorectal tumorigenesis
    • 1:CAS:528:DC%2BD2cXksFCmt7c%3D 15144953
    • Zhu P, Martin E, Mengwasser J, Schlag P, Janssen KP, Gottlicher M. Induction of HDAC2 expression upon loss of APC in colorectal tumorigenesis. Cancer Cell. 2004;5(5):455-63.
    • (2004) Cancer Cell , vol.5 , Issue.5 , pp. 455-463
    • Zhu, P.1    Martin, E.2    Mengwasser, J.3    Schlag, P.4    Janssen, K.P.5    Gottlicher, M.6
  • 16
    • 34248193440 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors in cancer therapy
    • 1:CAS:528:DC%2BD2sXks1aht78%3D 17461739
    • Rasheed WK, Johnstone RW, Prince HM. Histone deacetylase inhibitors in cancer therapy. Expert Opin Investig Drugs. 2007;16(5):659-78. doi: 10.1517/13543784.16.5.659.
    • (2007) Expert Opin Investig Drugs , vol.16 , Issue.5 , pp. 659-678
    • Rasheed, W.K.1    Johnstone, R.W.2    Prince, H.M.3
  • 17
    • 33748451151 scopus 로고    scopus 로고
    • Anticancer activities of histone deacetylase inhibitors
    • 1:CAS:528:DC%2BD28XptVCltrY%3D 16955068
    • Bolden JE, Peart MJ, Johnstone RW. Anticancer activities of histone deacetylase inhibitors. Nat Rev Drug Discov. 2006;5(9):769-84. doi: 10.1038/nrd2133.
    • (2006) Nat Rev Drug Discov , vol.5 , Issue.9 , pp. 769-784
    • Bolden, J.E.1    Peart, M.J.2    Johnstone, R.W.3
  • 18
    • 0035979737 scopus 로고    scopus 로고
    • Duration of nuclear NF-kappaB action regulated by reversible acetylation
    • 1:CAS:528:DC%2BD3MXms1Chsb4%3D
    • Chen L, Fischle W, Verdin E, Greene WC. Duration of nuclear NF-kappaB action regulated by reversible acetylation. Science. 2001;293(5535):1653-7. doi: 10.1126/science.1062374.
    • (2001) Science , vol.293 , Issue.5535 , pp. 1653-1657
    • Chen, L.1    Fischle, W.2    Verdin, E.3    Greene, W.C.4
  • 19
    • 0034676439 scopus 로고    scopus 로고
    • Deacetylation of p53 modulates its effect on cell growth and apoptosis
    • 1:CAS:528:DC%2BD3cXosVertbg%3D 11099047
    • Luo J, Su F, Chen D, Shiloh A, Gu W. Deacetylation of p53 modulates its effect on cell growth and apoptosis. Nature. 2000;408(6810):377-81. doi: 10.1038/35042612.
    • (2000) Nature , vol.408 , Issue.6810 , pp. 377-381
    • Luo, J.1    Su, F.2    Chen, D.3    Shiloh, A.4    Gu, W.5
  • 20
    • 0343484254 scopus 로고    scopus 로고
    • Regulation of E2F1 activity by acetylation
    • 1:CAS:528:DC%2BD3cXhsFKms7s%3D 305604 10675335
    • Martinez-Balbas MA, Bauer UM, Nielsen SJ, Brehm A, Kouzarides T. Regulation of E2F1 activity by acetylation. EMBO J. 2000;19(4):662-71. doi: 10.1093/emboj/19.4.662.
    • (2000) EMBO J , vol.19 , Issue.4 , pp. 662-671
    • Martinez-Balbas, M.A.1    Bauer, U.M.2    Nielsen, S.J.3    Brehm, A.4    Kouzarides, T.5
  • 22
    • 33749331568 scopus 로고    scopus 로고
    • Antitumor activity of suberoylanilide hydroxamic acid against thyroid cancer cell lines in vitro and in vivo
    • 1:CAS:528:DC%2BD28XpvFShtrk%3D 17000694
    • Luong QT, O'Kelly J, Braunstein GD, Hershman JM, Koeffler HP. Antitumor activity of suberoylanilide hydroxamic acid against thyroid cancer cell lines in vitro and in vivo. Clin Cancer Res. 2006;12(18):5570-7. doi: 10.1158/1078-0432.ccr-06-0367.
    • (2006) Clin Cancer Res , vol.12 , Issue.18 , pp. 5570-5577
    • Luong, Q.T.1    O'Kelly, J.2    Braunstein, G.D.3    Hershman, J.M.4    Koeffler, H.P.5
  • 23
    • 67349095775 scopus 로고    scopus 로고
    • Development of vorinostat: Current applications and future perspectives for cancer therapy
    • 1:CAS:528:DC%2BD1MXmsF2jt7k%3D 19181442
    • Richon VM, Garcia-Vargas J, Hardwick JS. Development of vorinostat: current applications and future perspectives for cancer therapy. Cancer Lett. 2009;280(2):201-10. doi: 10.1016/j.canlet.2009.01.002.
    • (2009) Cancer Lett , vol.280 , Issue.2 , pp. 201-210
    • Richon, V.M.1    Garcia-Vargas, J.2    Hardwick, J.S.3
  • 24
    • 25144440127 scopus 로고    scopus 로고
    • Rational development of histone deacetylase inhibitors as anticancer agents: A review
    • 1:CAS:528:DC%2BD2MXhtVyhu7jF 15955865
    • Acharya MR, Sparreboom A, Venitz J, Figg WD. Rational development of histone deacetylase inhibitors as anticancer agents: a review. Mol Pharmacol. 2005;68(4):917-32. doi: 10.1124/mol.105.014167.
    • (2005) Mol Pharmacol , vol.68 , Issue.4 , pp. 917-932
    • Acharya, M.R.1    Sparreboom, A.2    Venitz, J.3    Figg, W.D.4
  • 25
    • 33748794547 scopus 로고    scopus 로고
    • Theoretical basis, experimental design, and computerized simulation of synergism and antagonism in drug combination studies
    • 1:CAS:528:DC%2BD28XhtVOhtLfL 16968952
    • Chou TC. Theoretical basis, experimental design, and computerized simulation of synergism and antagonism in drug combination studies. Pharmacol Rev. 2006;58(3):621-81. doi: 10.1124/pr.58.3.10.
    • (2006) Pharmacol Rev , vol.58 , Issue.3 , pp. 621-681
    • Chou, T.C.1
  • 26
    • 0026643589 scopus 로고
    • Effects of vinblastine, podophyllotoxin and nocodazole on mitotic spindles. Implications for the role of microtubule dynamics in mitosis
    • 1:CAS:528:DyaK38Xls1entb8%3D 1506423
    • Jordan MA, Thrower D, Wilson L. Effects of vinblastine, podophyllotoxin and nocodazole on mitotic spindles. Implications for the role of microtubule dynamics in mitosis. J Cell Sci. 1992;102(Pt 3):401-16.
    • (1992) J Cell Sci , vol.102 , pp. 401-416
    • Jordan, M.A.1    Thrower, D.2    Wilson, L.3
  • 27
    • 0023947838 scopus 로고
    • Posttranslational modifications of alpha tubulin: Detyrosination and acetylation differentiate populations of interphase microtubules in cultured cells
    • 1:CAS:528:DyaL1cXitF2gtLo%3D 3283150
    • Bulinski JC, Richards JE, Piperno G. Posttranslational modifications of alpha tubulin: detyrosination and acetylation differentiate populations of interphase microtubules in cultured cells. J Cell Biol. 1988;106(4):1213-20.
    • (1988) J Cell Biol , vol.106 , Issue.4 , pp. 1213-1220
    • Bulinski, J.C.1    Richards, J.E.2    Piperno, G.3
  • 28
    • 0036731055 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors all induce p21 but differentially cause tubulin acetylation, mitotic arrest, and cytotoxicity
    • 1:CAS:528:DC%2BD3sXmvFOntg%3D%3D 12481415
    • Blagosklonny MV, Robey R, Sackett DL, Du L, Traganos F, Darzynkiewicz Z, et al. Histone deacetylase inhibitors all induce p21 but differentially cause tubulin acetylation, mitotic arrest, and cytotoxicity. Mol Cancer Ther. 2002;1(11):937-41.
    • (2002) Mol Cancer Ther , vol.1 , Issue.11 , pp. 937-941
    • Blagosklonny, M.V.1    Robey, R.2    Sackett, D.L.3    Du, L.4    Traganos, F.5    Darzynkiewicz, Z.6
  • 29
    • 34447115130 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors induce premature sister chromatid separation and override the mitotic spindle assembly checkpoint
    • 1:CAS:528:DC%2BD2sXnsVyqtLs%3D 17616695
    • Magnaghi-Jaulin L, Eot-Houllier G, Fulcrand G, Jaulin C. Histone deacetylase inhibitors induce premature sister chromatid separation and override the mitotic spindle assembly checkpoint. Cancer Res. 2007;67(13):6360-7. doi: 10.1158/0008-5472.can-06-3012.
    • (2007) Cancer Res , vol.67 , Issue.13 , pp. 6360-6367
    • Magnaghi-Jaulin, L.1    Eot-Houllier, G.2    Fulcrand, G.3    Jaulin, C.4
  • 30
    • 24744434639 scopus 로고    scopus 로고
    • Induction of polyploidy by histone deacetylase inhibitor: A pathway for antitumor effects
    • 1:CAS:528:DC%2BD2MXpslaiu7s%3D 16140952
    • Xu WS, Perez G, Ngo L, Gui CY, Marks PA. Induction of polyploidy by histone deacetylase inhibitor: a pathway for antitumor effects. Cancer Res. 2005;65(17):7832-9. doi: 10.1158/0008-5472.can-04-4608.
    • (2005) Cancer Res , vol.65 , Issue.17 , pp. 7832-7839
    • Xu, W.S.1    Perez, G.2    Ngo, L.3    Gui, C.Y.4    Marks, P.A.5
  • 31
    • 0141570734 scopus 로고    scopus 로고
    • Functional interplay between modulation of histone deacetylase activity and its regulatory role in G2-M transition
    • 1:CAS:528:DC%2BD3sXns1Kktbk%3D 14521905
    • Noh EJ, Lee JS. Functional interplay between modulation of histone deacetylase activity and its regulatory role in G2-M transition. Biochem Biophys Res Commun. 2003;310(2):267-73.
    • (2003) Biochem Biophys Res Commun , vol.310 , Issue.2 , pp. 267-273
    • Noh, E.J.1    Lee, J.S.2
  • 32
    • 0033822112 scopus 로고    scopus 로고
    • P21-dependent g(1)arrest with downregulation of cyclin D1 and upregulation of cyclin e by the histone deacetylase inhibitor FR901228
    • 1:CAS:528:DC%2BD3cXntFOhsLo%3D 2363539 10952788
    • Sandor V, Senderowicz A, Mertins S, Sackett D, Sausville E, Blagosklonny MV, et al. P21-dependent g(1)arrest with downregulation of cyclin D1 and upregulation of cyclin E by the histone deacetylase inhibitor FR901228. Br J Cancer. 2000;83(6):817-25. doi: 10.1054/bjoc.2000.1327.
    • (2000) Br J Cancer , vol.83 , Issue.6 , pp. 817-825
    • Sandor, V.1    Senderowicz, A.2    Mertins, S.3    Sackett, D.4    Sausville, E.5    Blagosklonny, M.V.6
  • 33
    • 41549120312 scopus 로고    scopus 로고
    • Vincristine and lomustine induce apoptosis and p21(WAF1) up-regulation in medulloblastoma and normal human epithelial and fibroblast cells
    • 1:CAS:528:DC%2BD1cXmt1ejsbw%3D
    • Shinwari Z, Manogaran PS, Alrokayan SA, Al-Hussein KA, Aboussekhra A. Vincristine and lomustine induce apoptosis and p21(WAF1) up-regulation in medulloblastoma and normal human epithelial and fibroblast cells. J Neuro-Oncol. 2008;87(2):123-32. doi: 10.1007/s11060-007-9502-4.
    • (2008) J Neuro-Oncol , vol.87 , Issue.2 , pp. 123-132
    • Shinwari, Z.1    Manogaran, P.S.2    Alrokayan, S.A.3    Al-Hussein, K.A.4    Aboussekhra, A.5
  • 34
    • 2342635919 scopus 로고    scopus 로고
    • Cell death by mitotic catastrophe: A molecular definition
    • 1:CAS:528:DC%2BD2cXivFKmsLo%3D 15077146
    • Castedo M, Perfettini JL, Roumier T, Andreau K, Medema R, Kroemer G. Cell death by mitotic catastrophe: a molecular definition. Oncogene. 2004;23(16):2825-37. doi: 10.1038/sj.onc.1207528.
    • (2004) Oncogene , vol.23 , Issue.16 , pp. 2825-2837
    • Castedo, M.1    Perfettini, J.L.2    Roumier, T.3    Andreau, K.4    Medema, R.5    Kroemer, G.6
  • 35
    • 1642326716 scopus 로고    scopus 로고
    • Phosphorylation of histone H3: A balancing act between chromosome condensation and transcriptional activation
    • 1:CAS:528:DC%2BD2cXisVGitbs%3D 15041176
    • Nowak SJ, Corces VG. Phosphorylation of histone H3: a balancing act between chromosome condensation and transcriptional activation. Trends Genet. 2004;20(4):214-20. doi: 10.1016/j.tig.2004.02.007.
    • (2004) Trends Genet , vol.20 , Issue.4 , pp. 214-220
    • Nowak, S.J.1    Corces, V.G.2
  • 36
    • 69549120405 scopus 로고    scopus 로고
    • How do anti-mitotic drugs kill cancer cells?
    • 1:CAS:528:DC%2BD1MXhtVGhsL7F 19625502
    • Gascoigne KE, Taylor SS. How do anti-mitotic drugs kill cancer cells? J Cell Sci. 2009;122(Pt 15):2579-85. doi: 10.1242/jcs.039719.
    • (2009) J Cell Sci , vol.122 , pp. 2579-2585
    • Gascoigne, K.E.1    Taylor, S.S.2
  • 37
    • 25144513926 scopus 로고    scopus 로고
    • Mitotic spindle checkpoint inactivation by trichostatin a defines a mechanism for increasing cancer cell killing by microtubule-disrupting agents
    • 1:CAS:528:DC%2BD28XhvFKgsLs%3D 15753652
    • Dowling M, Voong KR, Kim M, Keutmann MK, Harris E, Kao GD. Mitotic spindle checkpoint inactivation by trichostatin a defines a mechanism for increasing cancer cell killing by microtubule-disrupting agents. Cancer Biol Ther. 2005;4(2):197-206.
    • (2005) Cancer Biol Ther , vol.4 , Issue.2 , pp. 197-206
    • Dowling, M.1    Voong, K.R.2    Kim, M.3    Keutmann, M.K.4    Harris, E.5    Kao, G.D.6
  • 38
    • 53549121428 scopus 로고    scopus 로고
    • Histone deacetylase 3 is required for centromeric H3K4 deacetylation and sister chromatid cohesion
    • 1:CAS:528:DC%2BD1cXht1ClsbvN 2559902 18832068
    • Eot-Houllier G, Fulcrand G, Watanabe Y, Magnaghi-Jaulin L, Jaulin C. Histone deacetylase 3 is required for centromeric H3K4 deacetylation and sister chromatid cohesion. Genes Dev. 2008;22(19):2639-44. doi: 10.1101/gad.484108.
    • (2008) Genes Dev , vol.22 , Issue.19 , pp. 2639-2644
    • Eot-Houllier, G.1    Fulcrand, G.2    Watanabe, Y.3    Magnaghi-Jaulin, L.4    Jaulin, C.5


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