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Volumn 86, Issue 2, 2013, Pages 97-103

Histone lysine demethylases in breast cancer

Author keywords

Breast cancer; Histone lysine demethylase; KDM3B; KDM5A; KDM6A; Polycomb

Indexed keywords

HISTONE DEMETHYLASE; HISTONE LYSINE DEMETHYLASE 3B; HISTONE LYSINE DEMETHYLASE 5A; HISTONE LYSINE DEMETHYLASE 6A; POLYCOMB GROUP PROTEIN; UNCLASSIFIED DRUG;

EID: 84876072945     PISSN: 10408428     EISSN: 18790461     Source Type: Journal    
DOI: 10.1016/j.critrevonc.2012.11.008     Document Type: Review
Times cited : (53)

References (26)
  • 2
    • 84856230241 scopus 로고    scopus 로고
    • Inhibitors of histone demethylation and histone deacetylation cooperate in regulating gene expression and inhibiting growth in human breast cancer cells
    • Huang Y., Vasilatos S.N., Boric L., Shaw P.G., Davidson N.E. Inhibitors of histone demethylation and histone deacetylation cooperate in regulating gene expression and inhibiting growth in human breast cancer cells. Breast Cancer Research and Treatment 2012, 131(3):777-789.
    • (2012) Breast Cancer Research and Treatment , vol.131 , Issue.3 , pp. 777-789
    • Huang, Y.1    Vasilatos, S.N.2    Boric, L.3    Shaw, P.G.4    Davidson, N.E.5
  • 3
    • 80054787805 scopus 로고    scopus 로고
    • Targeting histone demethylases: a new avenue for the fight against cancer
    • Rotili D., Mai A. Targeting histone demethylases: a new avenue for the fight against cancer. Genes Cancer 2011, 2(6):663-679.
    • (2011) Genes Cancer , vol.2 , Issue.6 , pp. 663-679
    • Rotili, D.1    Mai, A.2
  • 4
    • 77950868547 scopus 로고    scopus 로고
    • Lysine-specific demethylase 1 (LSD1) is highly expressed in ER-negative breast cancers and a biomarker predicting aggressive biology
    • Lim S., Janzer A., Becker A., et al. Lysine-specific demethylase 1 (LSD1) is highly expressed in ER-negative breast cancers and a biomarker predicting aggressive biology. Carcinogenesis 2010, 31(3):512-520.
    • (2010) Carcinogenesis , vol.31 , Issue.3 , pp. 512-520
    • Lim, S.1    Janzer, A.2    Becker, A.3
  • 5
    • 67650522886 scopus 로고    scopus 로고
    • A novel mammalian flavin-dependent histone demethylase
    • Karytinos A., Forneris F., Profumo A., et al. A novel mammalian flavin-dependent histone demethylase. Journal of Biological Chemistry 2009, 284(26):17775-17782.
    • (2009) Journal of Biological Chemistry , vol.284 , Issue.26 , pp. 17775-17782
    • Karytinos, A.1    Forneris, F.2    Profumo, A.3
  • 6
    • 35148819644 scopus 로고    scopus 로고
    • Carcinogen-induced histone alteration in normal human mammary epithelial cells
    • Bradley C., van der Meer R., Roodi N., et al. Carcinogen-induced histone alteration in normal human mammary epithelial cells. Carcinogenesis 2007, 28(10):2184-2192.
    • (2007) Carcinogenesis , vol.28 , Issue.10 , pp. 2184-2192
    • Bradley, C.1    van der Meer, R.2    Roodi, N.3
  • 7
    • 78649664485 scopus 로고    scopus 로고
    • Structural insights into histone lysine demethylation
    • Hou H., Yu H. Structural insights into histone lysine demethylation. Current Opinion in Structural Biology 2010, 20(6):739-748.
    • (2010) Current Opinion in Structural Biology , vol.20 , Issue.6 , pp. 739-748
    • Hou, H.1    Yu, H.2
  • 8
    • 77449127237 scopus 로고    scopus 로고
    • Enzymatic and structural insights for substrate specificity of a family of jumonji histone lysine demethylases
    • Horton J.R., Upadhyay A.K., Qi H.H., Zhang X., Shi Y., Cheng X. Enzymatic and structural insights for substrate specificity of a family of jumonji histone lysine demethylases. Nature Structural & Molecular Biology 2010, 17(1):38-43.
    • (2010) Nature Structural & Molecular Biology , vol.17 , Issue.1 , pp. 38-43
    • Horton, J.R.1    Upadhyay, A.K.2    Qi, H.H.3    Zhang, X.4    Shi, Y.5    Cheng, X.6
  • 9
    • 32844454603 scopus 로고    scopus 로고
    • Histone demethylation by a family of JmjC domain-containing proteins
    • Tsukada Y., Fang J., Erdjument-Bromage H., et al. Histone demethylation by a family of JmjC domain-containing proteins. Nature 2006, 439(7078):811-816.
    • (2006) Nature , vol.439 , Issue.7078 , pp. 811-816
    • Tsukada, Y.1    Fang, J.2    Erdjument-Bromage, H.3
  • 10
    • 33947608608 scopus 로고    scopus 로고
    • A novel variant of the putative demethylase gene, s-JMJD1C, is a coactivator of the AR
    • Wolf S.S., Patchev V.K., Obendorf M. A novel variant of the putative demethylase gene, s-JMJD1C, is a coactivator of the AR. Archives of Biochemistry and Biophysics 2007, 460(1):56-66.
    • (2007) Archives of Biochemistry and Biophysics , vol.460 , Issue.1 , pp. 56-66
    • Wolf, S.S.1    Patchev, V.K.2    Obendorf, M.3
  • 11
    • 80053441658 scopus 로고    scopus 로고
    • Effects of RNA interference-mediated gene silencing of JMJD2A on human breast cancer cell line MDA-MB-231 in vitro
    • Li B.X., Zhang M.C., Luo C.L., et al. Effects of RNA interference-mediated gene silencing of JMJD2A on human breast cancer cell line MDA-MB-231 in vitro. Journal of Experimental and Clinical Cancer Research 2011, 30:90.
    • (2011) Journal of Experimental and Clinical Cancer Research , vol.30 , pp. 90
    • Li, B.X.1    Zhang, M.C.2    Luo, C.L.3
  • 12
    • 79952800100 scopus 로고    scopus 로고
    • Histone demethylase JMJD2B functions as a co-factor of estrogen receptor in breast cancer proliferation and mammary gland development
    • Kawazu M., Saso K., Tong K.I., et al. Histone demethylase JMJD2B functions as a co-factor of estrogen receptor in breast cancer proliferation and mammary gland development. PLoS ONE 2011, 6(3):e17830.
    • (2011) PLoS ONE , vol.6 , Issue.3
    • Kawazu, M.1    Saso, K.2    Tong, K.I.3
  • 13
    • 79955019522 scopus 로고    scopus 로고
    • PLU-1/JARID1B/KDM5B is required for embryonic survival and contributes to cell proliferation in the mammary gland and in ER+ breast cancer cells
    • Catchpole S., Spencer-Dene B., Hall D., et al. PLU-1/JARID1B/KDM5B is required for embryonic survival and contributes to cell proliferation in the mammary gland and in ER+ breast cancer cells. International Journal of Oncology 2011, 38(5):1267-1277.
    • (2011) International Journal of Oncology , vol.38 , Issue.5 , pp. 1267-1277
    • Catchpole, S.1    Spencer-Dene, B.2    Hall, D.3
  • 14
    • 1642377561 scopus 로고    scopus 로고
    • ONCOMINE: a cancer microarray database and integrated data-mining platform
    • Rhodes D.R., Yu J., Shanker K., et al. ONCOMINE: a cancer microarray database and integrated data-mining platform. AM Neoplasia 2004, 6(1):1-6.
    • (2004) AM Neoplasia , vol.6 , Issue.1 , pp. 1-6
    • Rhodes, D.R.1    Yu, J.2    Shanker, K.3
  • 15
  • 16
    • 0035909531 scopus 로고    scopus 로고
    • A novel nuclear protein, 5qNCA (LOC51780) is a candidate for the myeloid leukemia tumor suppressor gene on chromosome 5 band q31
    • Hu Z., Gomes I., Horrigan S.K., et al. A novel nuclear protein, 5qNCA (LOC51780) is a candidate for the myeloid leukemia tumor suppressor gene on chromosome 5 band q31. Oncogene 2001, 20(47):6946-6954.
    • (2001) Oncogene , vol.20 , Issue.47 , pp. 6946-6954
    • Hu, Z.1    Gomes, I.2    Horrigan, S.K.3
  • 18
    • 43249116995 scopus 로고    scopus 로고
    • Coordinated regulation of transcriptional repression by the RBP2 H3K4 demethylase and Polycomb-Repressive Complex 2
    • Pasini D., Hansen K.H., Christensen J., Agger K., Cloos P.A., Helin K. Coordinated regulation of transcriptional repression by the RBP2 H3K4 demethylase and Polycomb-Repressive Complex 2. Genes and Development 2008, 22(10):1345-1355.
    • (2008) Genes and Development , vol.22 , Issue.10 , pp. 1345-1355
    • Pasini, D.1    Hansen, K.H.2    Christensen, J.3    Agger, K.4    Cloos, P.A.5    Helin, K.6
  • 19
    • 34547687916 scopus 로고    scopus 로고
    • The function and regulation of the JARID1 family of histone H3 lysine 4 demethylases: the Myc connection
    • Secombe J., Eisenman R.N. The function and regulation of the JARID1 family of histone H3 lysine 4 demethylases: the Myc connection. Cell Cycle 2007, 6(11):1324-1328.
    • (2007) Cell Cycle , vol.6 , Issue.11 , pp. 1324-1328
    • Secombe, J.1    Eisenman, R.N.2
  • 20
    • 77949366450 scopus 로고    scopus 로고
    • Histone demethylase KDM5A is an integral part of the core Notch-RBP-J repressor complex
    • Liefke R., Oswald F., Alvarado C., et al. Histone demethylase KDM5A is an integral part of the core Notch-RBP-J repressor complex. Genes and Development 2010, 24(6):590-601.
    • (2010) Genes and Development , vol.24 , Issue.6 , pp. 590-601
    • Liefke, R.1    Oswald, F.2    Alvarado, C.3
  • 21
    • 79951983645 scopus 로고    scopus 로고
    • Cancer stem cell epigenetics and chemoresistance
    • Crea F., Danesi R., Farrar W.L. Cancer stem cell epigenetics and chemoresistance. Epigenomics 2009, 1(1):63-79.
    • (2009) Epigenomics , vol.1 , Issue.1 , pp. 63-79
    • Crea, F.1    Danesi, R.2    Farrar, W.L.3
  • 22
    • 67449091504 scopus 로고    scopus 로고
    • The PcG protein hPc2 interacts with the N-terminus of histone demethylase JARID1B and acts as a transcriptional co-repressor
    • Zhou W., Chen H., Zhang L. The PcG protein hPc2 interacts with the N-terminus of histone demethylase JARID1B and acts as a transcriptional co-repressor. BMB Reports 2009, 42(3):154-159.
    • (2009) BMB Reports , vol.42 , Issue.3 , pp. 154-159
    • Zhou, W.1    Chen, H.2    Zhang, L.3
  • 23
    • 84856073641 scopus 로고    scopus 로고
    • Cancer. Taking a back door to target Myc
    • Evan G. Cancer. Taking a back door to target Myc. Science 2012, 335(6066):293-294.
    • (2012) Science , vol.335 , Issue.6066 , pp. 293-294
    • Evan, G.1
  • 24
    • 64249172203 scopus 로고    scopus 로고
    • The canonical Notch signaling pathway: unfolding the activation mechanism
    • Kopan R., Ilagan M.X. The canonical Notch signaling pathway: unfolding the activation mechanism. Cell 2009, 137(2):216-233.
    • (2009) Cell , vol.137 , Issue.2 , pp. 216-233
    • Kopan, R.1    Ilagan, M.X.2
  • 25
    • 35148867907 scopus 로고    scopus 로고
    • UTX and JMJD3 are histone H3K27 demethylases involved in HOX gene regulation and development
    • Agger K., Cloos P.A., Christensen J., et al. UTX and JMJD3 are histone H3K27 demethylases involved in HOX gene regulation and development. Nature 2007, 449(7163):731-734.
    • (2007) Nature , vol.449 , Issue.7163 , pp. 731-734
    • Agger, K.1    Cloos, P.A.2    Christensen, J.3
  • 26
    • 43249102851 scopus 로고    scopus 로고
    • Erasing the methyl mark: histone demethylases at the center of cellular differentiation and disease
    • Cloos P.A., Christensen J., Agger K., Helin K. Erasing the methyl mark: histone demethylases at the center of cellular differentiation and disease. Genes and Development 2008, 22(9):1115-1140.
    • (2008) Genes and Development , vol.22 , Issue.9 , pp. 1115-1140
    • Cloos, P.A.1    Christensen, J.2    Agger, K.3    Helin, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.