메뉴 건너뛰기




Volumn 1839, Issue 12, 2014, Pages 1416-1432

Targeting histone lysine demethylases - Progress, challenges, and the future

Author keywords

Demethylase; Epigenetics; Histone; Inhibition; Lysine; Methylation

Indexed keywords

ENZYME INHIBITOR; HISTONE DEMETHYLASE; PROTEIN BINDING;

EID: 84914118716     PISSN: 18749399     EISSN: 18764320     Source Type: Journal    
DOI: 10.1016/j.bbagrm.2014.05.009     Document Type: Review
Times cited : (167)

References (157)
  • 1
    • 78149478781 scopus 로고    scopus 로고
    • Aberrant epigenetic landscape in cancer: how cellular identity goes awry
    • Berdasco M., Esteller M. Aberrant epigenetic landscape in cancer: how cellular identity goes awry. Dev. Cell 2010, 19:698-711.
    • (2010) Dev. Cell , vol.19 , pp. 698-711
    • Berdasco, M.1    Esteller, M.2
  • 2
    • 79959484677 scopus 로고    scopus 로고
    • Signals and combinatorial functions of histone modifications
    • Suganuma T., Workman J.L. Signals and combinatorial functions of histone modifications. Annu. Rev. Biochem. 2011, 80:473-499.
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 473-499
    • Suganuma, T.1    Workman, J.L.2
  • 3
    • 84875149194 scopus 로고    scopus 로고
    • Regulation of nucleosome dynamics by histone modifications
    • Zentner G.E., Henikoff S. Regulation of nucleosome dynamics by histone modifications. Nat. Struct. Mol. Biol. 2013, 20:259-266.
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 259-266
    • Zentner, G.E.1    Henikoff, S.2
  • 4
    • 84859893371 scopus 로고    scopus 로고
    • Histone methylation: a dynamic mark in health, disease and inheritance
    • Greer E.L., Shi Y. Histone methylation: a dynamic mark in health, disease and inheritance. Nat. Rev. Genet. 2012, 13:343-357.
    • (2012) Nat. Rev. Genet. , vol.13 , pp. 343-357
    • Greer, E.L.1    Shi, Y.2
  • 5
    • 77957970301 scopus 로고    scopus 로고
    • Epigenetic modifications and human disease
    • Portela A., Esteller M. Epigenetic modifications and human disease. Nat. Biotechnol. 2010, 28:1057-1068.
    • (2010) Nat. Biotechnol. , vol.28 , pp. 1057-1068
    • Portela, A.1    Esteller, M.2
  • 6
    • 84877930649 scopus 로고    scopus 로고
    • Targeting histone modifications-epigenetics in cancer
    • Waldmann T., Schneider R. Targeting histone modifications-epigenetics in cancer. Curr. Opin. Cell Biol. 2013, 25:184-189.
    • (2013) Curr. Opin. Cell Biol. , vol.25 , pp. 184-189
    • Waldmann, T.1    Schneider, R.2
  • 7
    • 34547864236 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: molecular mechanisms of action
    • Xu W.S., Parmigiani R.B., Marks P.A. Histone deacetylase inhibitors: molecular mechanisms of action. Oncogene 2007, 26:5541-5552.
    • (2007) Oncogene , vol.26 , pp. 5541-5552
    • Xu, W.S.1    Parmigiani, R.B.2    Marks, P.A.3
  • 8
    • 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. Gene Cancer 2011, 2:663-679.
    • (2011) Gene Cancer , vol.2 , pp. 663-679
    • Rotili, D.1    Mai, A.2
  • 9
    • 78649327715 scopus 로고    scopus 로고
    • Biological rationale for the use of DNA methyltransferase inhibitors as new strategy for modulation of tumor response to chemotherapy and radiation
    • Gravina G.L., Festuccia C., Marampon F., Popov V.M., Pestell R.G., Zani B.M., Tombolini V. Biological rationale for the use of DNA methyltransferase inhibitors as new strategy for modulation of tumor response to chemotherapy and radiation. Mol. Cancer 2010, 9.
    • (2010) Mol. Cancer , vol.9
    • Gravina, G.L.1    Festuccia, C.2    Marampon, F.3    Popov, V.M.4    Pestell, R.G.5    Zani, B.M.6    Tombolini, V.7
  • 12
    • 73149099403 scopus 로고    scopus 로고
    • Regulation of NF-κB activity through lysine monomethylation of p65
    • Ea C.-K., Baltimore D. Regulation of NF-κB activity through lysine monomethylation of p65. Proc. Natl. Acad. Sci. 2009, 106:18972-18977.
    • (2009) Proc. Natl. Acad. Sci. , vol.106 , pp. 18972-18977
    • Ea, C.-K.1    Baltimore, D.2
  • 14
    • 84910679144 scopus 로고    scopus 로고
    • Proteome-wide post-translational modification statistics: frequency analysis and curation of the Swiss-Prot database
    • Khoury G.A., Baliban R.C., Floudas C.A. Proteome-wide post-translational modification statistics: frequency analysis and curation of the Swiss-Prot database. Sci. Rep. 2011, 1.
    • (2011) Sci. Rep. , vol.1
    • Khoury, G.A.1    Baliban, R.C.2    Floudas, C.A.3
  • 15
    • 28044433451 scopus 로고    scopus 로고
    • Protein posttranslational modifications: the chemistry of proteome diversifications
    • Walsh C.T., Garneau-Tsodikova S., Gatto G.J. Protein posttranslational modifications: the chemistry of proteome diversifications. Angew. Chem. 2005, 44:7342-7372.
    • (2005) Angew. Chem. , vol.44 , pp. 7342-7372
    • Walsh, C.T.1    Garneau-Tsodikova, S.2    Gatto, G.J.3
  • 16
    • 77049099785 scopus 로고    scopus 로고
    • Histone methyltransferases in cancer
    • Albert M., Helin K. Histone methyltransferases in cancer. Semin. Cell Dev. Biol. 2010, 21:209-220.
    • (2010) Semin. Cell Dev. Biol. , vol.21 , pp. 209-220
    • Albert, M.1    Helin, K.2
  • 19
    • 78751662908 scopus 로고    scopus 로고
    • The Polycomb complex PRC2 and its mark in life
    • Margueron R., Reinberg D. The Polycomb complex PRC2 and its mark in life. Nature 2011, 469:343-349.
    • (2011) Nature , vol.469 , pp. 343-349
    • Margueron, R.1    Reinberg, D.2
  • 20
    • 0142105414 scopus 로고    scopus 로고
    • EZH2 is downstream of the pRB-E2F pathway, essential for proliferation and amplified in cancer
    • Bracken A.P., Pasini D., Capra M., Prosperini E., Colli E., Helin K. EZH2 is downstream of the pRB-E2F pathway, essential for proliferation and amplified in cancer. EMBO J. 2003, 22:5323-5335.
    • (2003) EMBO J. , vol.22 , pp. 5323-5335
    • Bracken, A.P.1    Pasini, D.2    Capra, M.3    Prosperini, E.4    Colli, E.5    Helin, K.6
  • 23
    • 84914097116 scopus 로고    scopus 로고
    • http://www.epizyme.com.
  • 25
    • 84863621527 scopus 로고    scopus 로고
    • Cancer epigenetics: from mechanism to therapy
    • Dawson M.A., Kouzarides T. Cancer epigenetics: from mechanism to therapy. Cell 2012, 150:12-27.
    • (2012) Cell , vol.150 , pp. 12-27
    • Dawson, M.A.1    Kouzarides, T.2
  • 27
    • 84860215207 scopus 로고    scopus 로고
    • Molecular mechanisms and potential functions of histone demethylases
    • Kooistra S.M., Helin K. Molecular mechanisms and potential functions of histone demethylases. Nat. Rev. Mol. Cell Biol. 2012, 13:297-311.
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 297-311
    • Kooistra, S.M.1    Helin, K.2
  • 30
    • 35348938519 scopus 로고    scopus 로고
    • JMJD6 is a histone arginine demethylase
    • Chang B., Chen Y., Zhao Y., Bruick R.K. JMJD6 is a histone arginine demethylase. Science 2007, 318:444-447.
    • (2007) Science , vol.318 , pp. 444-447
    • Chang, B.1    Chen, Y.2    Zhao, Y.3    Bruick, R.K.4
  • 31
    • 84894579192 scopus 로고    scopus 로고
    • Brd4 and JMJD6-associated anti-pause enhancers in regulation of transcriptional pause release
    • Liu W., Ma Q., Wong K., Li W., Ohgi K., Zhang J., Aggarwal A.K., Rosenfeld M.G. Brd4 and JMJD6-associated anti-pause enhancers in regulation of transcriptional pause release. Cell 2013, 155:1581-1595.
    • (2013) Cell , vol.155 , pp. 1581-1595
    • Liu, W.1    Ma, Q.2    Wong, K.3    Li, W.4    Ohgi, K.5    Zhang, J.6    Aggarwal, A.K.7    Rosenfeld, M.G.8
  • 33
    • 79952028556 scopus 로고    scopus 로고
    • The 2-oxoglutarate-dependent oxygenase JMJD6 catalyses oxidation of lysine residues to give 5S-hydroxylysine residues
    • Mantri M., Loik N.D., Hamed R.B., Claridge T.D., McCullagh J.S., Schofield C.J. The 2-oxoglutarate-dependent oxygenase JMJD6 catalyses oxidation of lysine residues to give 5S-hydroxylysine residues. Chembiochem 2011, 12:531-534.
    • (2011) Chembiochem , vol.12 , pp. 531-534
    • Mantri, M.1    Loik, N.D.2    Hamed, R.B.3    Claridge, T.D.4    McCullagh, J.S.5    Schofield, C.J.6
  • 34
    • 35349006314 scopus 로고    scopus 로고
    • Histone lysine demethylases: emerging roles in development, physiology and disease, Nature reviews
    • Shi Y. Histone lysine demethylases: emerging roles in development, physiology and disease, Nature reviews. Genetics 2007, 8:829-833.
    • (2007) Genetics , vol.8 , pp. 829-833
    • Shi, Y.1
  • 38
    • 34547132094 scopus 로고    scopus 로고
    • Structural basis of LSD1-CoREST selectivity in histone H3 recognition
    • Forneris F., Binda C., Adamo A., Battaglioli E., Mattevi A. Structural basis of LSD1-CoREST selectivity in histone H3 recognition. J. Biol. Chem. 2007, 282:20070-20074.
    • (2007) J. Biol. Chem. , vol.282 , pp. 20070-20074
    • Forneris, F.1    Binda, C.2    Adamo, A.3    Battaglioli, E.4    Mattevi, A.5
  • 40
    • 33747455678 scopus 로고    scopus 로고
    • JmjC-domain-containing proteins and histone demethylation
    • Klose R.J., Kallin E.M., Zhang Y. JmjC-domain-containing proteins and histone demethylation. Nat. Rev. Genet. 2006, 7:715-727.
    • (2006) Nat. Rev. Genet. , vol.7 , pp. 715-727
    • Klose, R.J.1    Kallin, E.M.2    Zhang, Y.3
  • 41
  • 44
    • 77955280094 scopus 로고    scopus 로고
    • The X-linked mental retardation gene PHF8 is a histone demethylase involved in neuronal differentiation
    • Qiu J., Shi G., Jia Y., Li J., Wu M., Li J., Dong S., Wong J. The X-linked mental retardation gene PHF8 is a histone demethylase involved in neuronal differentiation. Cell Res. 2010, 20:908-918.
    • (2010) Cell Res. , vol.20 , pp. 908-918
    • Qiu, J.1    Shi, G.2    Jia, Y.3    Li, J.4    Wu, M.5    Li, J.6    Dong, S.7    Wong, J.8
  • 45
    • 84871464403 scopus 로고    scopus 로고
    • The potential of 2-oxoglutarate oxygenases acting on nucleic acids as therapeutic targets
    • Thalhammer A., Aik W., Bagg E.A.L., Schofield C.J. The potential of 2-oxoglutarate oxygenases acting on nucleic acids as therapeutic targets. Drug Discov. Today 2012, 9:e91-e100.
    • (2012) Drug Discov. Today , vol.9 , pp. e91-e100
    • Thalhammer, A.1    Aik, W.2    Bagg, E.A.L.3    Schofield, C.J.4
  • 47
    • 77149164783 scopus 로고    scopus 로고
    • Monitoring the activity of 2-oxoglutarate dependent histone demethylases by NMR spectroscopy: direct observation of formaldehyde
    • Hopkinson R.J., Hamed R.B., Rose N.R., Claridge T.D.W., Schofield C.J. Monitoring the activity of 2-oxoglutarate dependent histone demethylases by NMR spectroscopy: direct observation of formaldehyde. Chembiochem 2010, 11:506-510.
    • (2010) Chembiochem , vol.11 , pp. 506-510
    • Hopkinson, R.J.1    Hamed, R.B.2    Rose, N.R.3    Claridge, T.D.W.4    Schofield, C.J.5
  • 50
    • 39349105090 scopus 로고    scopus 로고
    • Expanding chemical biology of 2-oxoglutarate oxygenases
    • Loenarz C., Schofield C.J. Expanding chemical biology of 2-oxoglutarate oxygenases. Nat. Chem. Biol. 2008, 4:152-156.
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 152-156
    • Loenarz, C.1    Schofield, C.J.2
  • 51
    • 0032914318 scopus 로고    scopus 로고
    • Monoamine oxidase: from genes to behavior
    • Shih J.C., Chen K., Ridd M.J. Monoamine oxidase: from genes to behavior. Annu. Rev. Neurosci. 1999, 22:197-217.
    • (1999) Annu. Rev. Neurosci. , vol.22 , pp. 197-217
    • Shih, J.C.1    Chen, K.2    Ridd, M.J.3
  • 54
    • 33745187327 scopus 로고    scopus 로고
    • Histone H3 lysine 4 demethylation is a target of nonselective antidepressive medications
    • Lee M.G., Wynder C., Schmidt D.M., McCafferty D.G., Shiekhattar R. Histone H3 lysine 4 demethylation is a target of nonselective antidepressive medications. Chem. Biol. 2006, 13:563-567.
    • (2006) Chem. Biol. , vol.13 , pp. 563-567
    • Lee, M.G.1    Wynder, C.2    Schmidt, D.M.3    McCafferty, D.G.4    Shiekhattar, R.5
  • 55
    • 34147173308 scopus 로고    scopus 로고
    • Trans-2-Phenylcyclopropylamine is a mechanism-based inactivator of the histone demethylase LSD1
    • Schmidt D.M., McCafferty D.G. trans-2-Phenylcyclopropylamine is a mechanism-based inactivator of the histone demethylase LSD1. Biochemistry 2007, 46:4408-4416.
    • (2007) Biochemistry , vol.46 , pp. 4408-4416
    • Schmidt, D.M.1    McCafferty, D.G.2
  • 57
    • 77949421463 scopus 로고    scopus 로고
    • Comparative analysis of small molecules and histone substrate analogues as LSD1 lysine demethylase inhibitors
    • Culhane J.C., Wang D., Yen P.M., Cole P.A. Comparative analysis of small molecules and histone substrate analogues as LSD1 lysine demethylase inhibitors. J. Am. Chem. Soc. 2010, 132:3164-3176.
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 3164-3176
    • Culhane, J.C.1    Wang, D.2    Yen, P.M.3    Cole, P.A.4
  • 58
    • 0014430109 scopus 로고
    • Mitochondrial monoamine oxidase. II. Action of various inhibitors for the bovine kidney enzyme. Catalytic mechanism
    • Hellerman L., Erwin V.G. Mitochondrial monoamine oxidase. II. Action of various inhibitors for the bovine kidney enzyme. Catalytic mechanism. J. Biol. Chem. 1968, 243:5234-5243.
    • (1968) J. Biol. Chem. , vol.243 , pp. 5234-5243
    • Hellerman, L.1    Erwin, V.G.2
  • 59
    • 0042693016 scopus 로고    scopus 로고
    • Insights into the mode of inhibition of human mitochondrial monoamine oxidase B from high-resolution crystal structures
    • Binda C., Li M., Hubalek F., Restelli N., Edmondson D.E., Mattevi A. Insights into the mode of inhibition of human mitochondrial monoamine oxidase B from high-resolution crystal structures. Proc. Natl. Acad. Sci. U. S. A. 2003, 100:9750-9755.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 9750-9755
    • Binda, C.1    Li, M.2    Hubalek, F.3    Restelli, N.4    Edmondson, D.E.5    Mattevi, A.6
  • 60
    • 0016373389 scopus 로고
    • Mitochondrial monoamine oxidase. Mechanism of inhibition by phenylhydrazine and by aralkylhydrazines. Role of enzymatic oxidation
    • Patek D.R., Hellerman L. Mitochondrial monoamine oxidase. Mechanism of inhibition by phenylhydrazine and by aralkylhydrazines. Role of enzymatic oxidation. J. Biol. Chem. 1974, 249:2373-2380.
    • (1974) J. Biol. Chem. , vol.249 , pp. 2373-2380
    • Patek, D.R.1    Hellerman, L.2
  • 62
    • 34447338875 scopus 로고    scopus 로고
    • Structural basis for the inhibition of the LSD1 histone demethylase by the antidepressant trans-2-phenylcyclopropylamine
    • Yang M., Culhane J.C., Szewczuk L.M., Jalili P., Ball H.L., Machius M., Cole P.A., Yu H. Structural basis for the inhibition of the LSD1 histone demethylase by the antidepressant trans-2-phenylcyclopropylamine. Biochemistry 2007, 46:8058-8065.
    • (2007) Biochemistry , vol.46 , pp. 8058-8065
    • Yang, M.1    Culhane, J.C.2    Szewczuk, L.M.3    Jalili, P.4    Ball, H.L.5    Machius, M.6    Cole, P.A.7    Yu, H.8
  • 64
    • 43549091096 scopus 로고    scopus 로고
    • Facile synthesis of substituted trans-2-arylcyclopropylamine inhibitors of the human histone demethylase LSD1 and monoamine oxidases A and B
    • Gooden D.M., Schmidt D.M., Pollock J.A., Kabadi A.M., McCafferty D.G. Facile synthesis of substituted trans-2-arylcyclopropylamine inhibitors of the human histone demethylase LSD1 and monoamine oxidases A and B. Bioorg. Med. Chem. Lett. 2008, 18:3047-3051.
    • (2008) Bioorg. Med. Chem. Lett. , vol.18 , pp. 3047-3051
    • Gooden, D.M.1    Schmidt, D.M.2    Pollock, J.A.3    Kabadi, A.M.4    McCafferty, D.G.5
  • 66
    • 77955025931 scopus 로고    scopus 로고
    • Structurally designed trans-2-phenylcyclopropylamine derivatives potently inhibit histone demethylase LSD1/KDM1
    • Mimasu S., Umezawa N., Sato S., Higuchi T., Umehara T., Yokoyama S. Structurally designed trans-2-phenylcyclopropylamine derivatives potently inhibit histone demethylase LSD1/KDM1. Biochemistry 2010, 49:6494-6503.
    • (2010) Biochemistry , vol.49 , pp. 6494-6503
    • Mimasu, S.1    Umezawa, N.2    Sato, S.3    Higuchi, T.4    Umehara, T.5    Yokoyama, S.6
  • 69
    • 84914097115 scopus 로고    scopus 로고
    • Laria, LYSINE DEMETHYLASE INHIBITORS SUCH AS CYCLYLCYLOPROPAMINE DERIVATIVES FOR USE IN THE TREATMENT OF INFLAMMATORY DISEASES OR CONDITIONS, in: S.A.C.S.F.E.C.d.L. Oryzon Genomics (Ed.), vol. EP2012/059377, WO.
    • T.C.S.F.E.C.d.L. Maes, M.C.S.F.E.C.d.L. Martinell Pedemonte, J.C.C.S.F.E.C.d.L. Castro-Palomino Laria, LYSINE DEMETHYLASE INHIBITORS SUCH AS CYCLYLCYLOPROPAMINE DERIVATIVES FOR USE IN THE TREATMENT OF INFLAMMATORY DISEASES OR CONDITIONS, in: S.A.C.S.F.E.C.d.L. Oryzon Genomics (Ed.), vol. EP2012/059377, WO, 2012.
    • (2012)
    • Maes, T.C.S.F.E.C.d.L.1    Martinell Pedemonte, M.C.S.F.E.C.d.L.2    Castro-Palomino, J.C.C.S.F.E.C.d.L.3
  • 70
    • 84914097114 scopus 로고    scopus 로고
    • TRANYLCYPROMINE DERIVATIVES AS INHIBITORS OF HISTONE DEMETHYLASE LSD1 AND/OR LSD2, P.A.M.I.R. UniversitÀ Degli Studi Di Roma "La Sapienza, V.F.I.M. Fondazione Ieo, C.S.N.I.P. UniversitÀ Degli Studi Di Pavia, V.F.d.P.I.M. UniversitÀ Degli Studi Di Milano (Eds.), vol. EP2011/055990, WO.
    • S.V.S.M.I.O. Minucci, A.V.J.F.I.R. Mai, A.V.M.I.P. Mattevi, TRANYLCYPROMINE DERIVATIVES AS INHIBITORS OF HISTONE DEMETHYLASE LSD1 AND/OR LSD2, in: P.A.M.I.R. UniversitÀ Degli Studi Di Roma "La Sapienza, V.F.I.M. Fondazione Ieo, C.S.N.I.P. UniversitÀ Degli Studi Di Pavia, V.F.d.P.I.M. UniversitÀ Degli Studi Di Milano (Eds.), vol. EP2011/055990, WO, 2011.
    • (2011)
    • Minucci, S.V.S.M.I.O.1    Mai, A.V.J.F.I.R.2    Mattevi, A.V.M.I.P.3
  • 74
  • 77
  • 83
    • 84883450643 scopus 로고    scopus 로고
    • CD86 expression as a surrogate cellular biomarker for pharmacological inhibition of the histone demethylase lysine-specific demethylase 1
    • Lynch J.T., Cockerill M.J., Hitchin J.R., Wiseman D.H., Somervaille T.C. CD86 expression as a surrogate cellular biomarker for pharmacological inhibition of the histone demethylase lysine-specific demethylase 1. Anal. Biochem. 2013, 442:104-106.
    • (2013) Anal. Biochem. , vol.442 , pp. 104-106
    • Lynch, J.T.1    Cockerill, M.J.2    Hitchin, J.R.3    Wiseman, D.H.4    Somervaille, T.C.5
  • 84
    • 84890448100 scopus 로고    scopus 로고
    • High-throughput virtual screening identifies novel N'-(1-phenylethylidene)-benzohydrazides as potent, specific, and reversible LSD1 inhibitors
    • Sorna V., Theisen E.R., Stephens B., Warner S.L., Bearss D.J., Vankayalapati H., Sharma S. High-throughput virtual screening identifies novel N'-(1-phenylethylidene)-benzohydrazides as potent, specific, and reversible LSD1 inhibitors. J. Med. Chem. 2013, 56:9496-9508.
    • (2013) J. Med. Chem. , vol.56 , pp. 9496-9508
    • Sorna, V.1    Theisen, E.R.2    Stephens, B.3    Warner, S.L.4    Bearss, D.J.5    Vankayalapati, H.6    Sharma, S.7
  • 86
    • 0023629331 scopus 로고
    • Inhibition of prolyl hydroxylation during collagen biosynthesis in human skin fibroblast cultures by ethyl 3,4-dihydroxybenzoate
    • Majamaa K., Sasaki T., Uitto J. Inhibition of prolyl hydroxylation during collagen biosynthesis in human skin fibroblast cultures by ethyl 3,4-dihydroxybenzoate. J. Investig. Dermatol. 1987, 89:405-409.
    • (1987) J. Investig. Dermatol. , vol.89 , pp. 405-409
    • Majamaa, K.1    Sasaki, T.2    Uitto, J.3
  • 87
    • 0024392827 scopus 로고
    • Inhibition of collagen hydroxylation by 2,7,8-trihydroxyanthraquinone in embryonic-chick tendon cells
    • Franklin T.J., Hitchen M. Inhibition of collagen hydroxylation by 2,7,8-trihydroxyanthraquinone in embryonic-chick tendon cells. Biochem. J. 1989, 261:127-130.
    • (1989) Biochem. J. , vol.261 , pp. 127-130
    • Franklin, T.J.1    Hitchen, M.2
  • 94
    • 70450183810 scopus 로고    scopus 로고
    • Different modes of inhibitor binding to prolyl hydroxylase by combined use of X-ray crystallography and NMR spectroscopy of paramagnetic complexes
    • Poppe L., Tegley C.M., Li V., Lewis J., Zondlo J., Yang E., Kurzeja R.J.M., Syed R. Different modes of inhibitor binding to prolyl hydroxylase by combined use of X-ray crystallography and NMR spectroscopy of paramagnetic complexes. J. Am. Chem. Soc. 2009, 131:16654-16655.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 16654-16655
    • Poppe, L.1    Tegley, C.M.2    Li, V.3    Lewis, J.4    Zondlo, J.5    Yang, E.6    Kurzeja, R.J.M.7    Syed, R.8
  • 96
    • 84860421247 scopus 로고    scopus 로고
    • Functional consequences of succinate dehydrogenase mutations
    • Opocher G., Schiavi F. Functional consequences of succinate dehydrogenase mutations. Endocr. Pract. 2011, 17:64-71.
    • (2011) Endocr. Pract. , vol.17 , pp. 64-71
    • Opocher, G.1    Schiavi, F.2
  • 101
    • 0017742181 scopus 로고
    • Mechanism of prolyl hydroxylase reaction. 2. Kinetic-analysis of reaction sequence
    • Myllyla R., Tuderman L., Kivirikko K.I. Mechanism of prolyl hydroxylase reaction. 2. Kinetic-analysis of reaction sequence. Eur. J. Biochem. 1977, 80:349-357.
    • (1977) Eur. J. Biochem. , vol.80 , pp. 349-357
    • Myllyla, R.1    Tuderman, L.2    Kivirikko, K.I.3
  • 102
    • 84862632865 scopus 로고    scopus 로고
    • Inhibition of alpha-KG-dependent histone and DNA demethylases by fumarate and succinate that are accumulated in mutations of FH and SDH tumor suppressors
    • Xiao M., Yang H., Xu W., Ma S., Lin H., Zhu H., Liu L., Liu Y., Yang C., Xu Y., Zhao S., Ye D., Xiong Y., Guan K.L. Inhibition of alpha-KG-dependent histone and DNA demethylases by fumarate and succinate that are accumulated in mutations of FH and SDH tumor suppressors. Genes Dev. 2012, 26:1326-1338.
    • (2012) Genes Dev. , vol.26 , pp. 1326-1338
    • Xiao, M.1    Yang, H.2    Xu, W.3    Ma, S.4    Lin, H.5    Zhu, H.6    Liu, L.7    Liu, Y.8    Yang, C.9    Xu, Y.10    Zhao, S.11    Ye, D.12    Xiong, Y.13    Guan, K.L.14
  • 107
    • 20144380031 scopus 로고    scopus 로고
    • Kinetic dissection of the catalytic mechanism of taurine:α-ketoglutarate dioxygenase (TauD) from Escherichia coli†
    • Price J.C., Barr E.W., Hoffart L.M., Krebs C., Bollinger J.M. Kinetic dissection of the catalytic mechanism of taurine:α-ketoglutarate dioxygenase (TauD) from Escherichia coli†. Biochemistry 2005, 44:8138-8147.
    • (2005) Biochemistry , vol.44 , pp. 8138-8147
    • Price, J.C.1    Barr, E.W.2    Hoffart, L.M.3    Krebs, C.4    Bollinger, J.M.5
  • 109
  • 115
    • 0026724983 scopus 로고
    • Novel inhibitors of prolyl 4-hydroxylase. 3. Inhibition by the substrate analog N-oxaloglycine and its derivatives
    • Cunliffe C.J., Franklin T.J., Hales N.J., Hill G.B. Novel inhibitors of prolyl 4-hydroxylase. 3. Inhibition by the substrate analog N-oxaloglycine and its derivatives. J. Med. Chem. 1992, 35:2652-2658.
    • (1992) J. Med. Chem. , vol.35 , pp. 2652-2658
    • Cunliffe, C.J.1    Franklin, T.J.2    Hales, N.J.3    Hill, G.B.4
  • 121
    • 65349129552 scopus 로고    scopus 로고
    • Synthesis and activity of N-oxalylglycine and its derivatives as Jumonji C-domain-containing histone lysine demethylase inhibitors
    • Hamada S., Kim T.-D., Suzuki T., Itoh Y., Tsumoto H., Nakagawa H., Janknecht R., Miyata N. Synthesis and activity of N-oxalylglycine and its derivatives as Jumonji C-domain-containing histone lysine demethylase inhibitors. Bioorg. Med. Chem. Lett. 2009, 19:2852-2855.
    • (2009) Bioorg. Med. Chem. Lett. , vol.19 , pp. 2852-2855
    • Hamada, S.1    Kim, T.-D.2    Suzuki, T.3    Itoh, Y.4    Tsumoto, H.5    Nakagawa, H.6    Janknecht, R.7    Miyata, N.8
  • 126
    • 0030815034 scopus 로고    scopus 로고
    • Daminozide and prohexadione have similar modes of action as inhibitors of the late stages of gibberellin metabolism
    • Brown R.G.S., Kawaide H., Yang Y.-Y., Rademacher W., Kamiya Y. Daminozide and prohexadione have similar modes of action as inhibitors of the late stages of gibberellin metabolism. Physiol. Plant. 1997, 101:309-313.
    • (1997) Physiol. Plant. , vol.101 , pp. 309-313
    • Brown, R.G.S.1    Kawaide, H.2    Yang, Y.-Y.3    Rademacher, W.4    Kamiya, Y.5
  • 131
    • 0007257190 scopus 로고
    • Influence of chelating agents on the biosynthesis of collagen
    • Hurych J., Chvapil M. Influence of chelating agents on the biosynthesis of collagen. Biochim. Biophys. Acta Gen. Subj. 1965, 97:361-363.
    • (1965) Biochim. Biophys. Acta Gen. Subj. , vol.97 , pp. 361-363
    • Hurych, J.1    Chvapil, M.2
  • 132
    • 0027138262 scopus 로고
    • Novel inhibitors of prolyl 4-hydroxylase. 5. The intriguing structure-activity relationships seen with 2,2'-bipyridine and its 5,5'-dicarboxylic acid derivatives
    • Hales N.J., Beattie J.F. Novel inhibitors of prolyl 4-hydroxylase. 5. The intriguing structure-activity relationships seen with 2,2'-bipyridine and its 5,5'-dicarboxylic acid derivatives. J. Med. Chem. 1993, 36:3853-3858.
    • (1993) J. Med. Chem. , vol.36 , pp. 3853-3858
    • Hales, N.J.1    Beattie, J.F.2
  • 135
    • 84872330923 scopus 로고    scopus 로고
    • Targeting the JMJD2 histone demethylases to epigenetically control herpesvirus infection and reactivation from latency
    • 167ra165
    • Liang Y., Vogel J.L., Arbuckle J.H., Rai G., Jadhav A., Simeonov A., Maloney D.J., Kristie T.M. Targeting the JMJD2 histone demethylases to epigenetically control herpesvirus infection and reactivation from latency. Sci. Transl. Med. 2013, 5. (167ra165, 111pp).
    • (2013) Sci. Transl. Med. , vol.5 , pp. 111
    • Liang, Y.1    Vogel, J.L.2    Arbuckle, J.H.3    Rai, G.4    Jadhav, A.5    Simeonov, A.6    Maloney, D.J.7    Kristie, T.M.8
  • 143
    • 0036299051 scopus 로고    scopus 로고
    • The dietary flavonoid quercetin modulates HIF-1 alpha activity in endothelial cells
    • Wilson W.J., Poellinger L. The dietary flavonoid quercetin modulates HIF-1 alpha activity in endothelial cells. Biochem. Biophys. Res. Commun. 2002, 293:446-450.
    • (2002) Biochem. Biophys. Res. Commun. , vol.293 , pp. 446-450
    • Wilson, W.J.1    Poellinger, L.2
  • 144
    • 11844269261 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1 activation by (-)-epicatechin gallate: potential adverse effects of cancer chemoprevention with high-dose green tea extracts
    • Zhou Y.D., Kim Y.P., Li X.C., Baerson S.R., Agarwal A.K., Hodges T.W., Ferreira D., Nagle D.G. Hypoxia-inducible factor-1 activation by (-)-epicatechin gallate: potential adverse effects of cancer chemoprevention with high-dose green tea extracts. J. Nat. Prod. 2004, 67:2063-2069.
    • (2004) J. Nat. Prod. , vol.67 , pp. 2063-2069
    • Zhou, Y.D.1    Kim, Y.P.2    Li, X.C.3    Baerson, S.R.4    Agarwal, A.K.5    Hodges, T.W.6    Ferreira, D.7    Nagle, D.G.8
  • 147
    • 84875987260 scopus 로고    scopus 로고
    • Identification of small molecule inhibitors of Jumonji AT-rich interactive domain 1B (JARID1B) histone demethylase by a sensitive high throughput screen
    • Sayegh J., Cao J., Zou M.R., Morales A., Blair L.P., Norcia M., Hoyer D., Tackett A.J., Merkel J.S., Yan Q. Identification of small molecule inhibitors of Jumonji AT-rich interactive domain 1B (JARID1B) histone demethylase by a sensitive high throughput screen. J. Biol. Chem. 2013, 288:9408-9417.
    • (2013) J. Biol. Chem. , vol.288 , pp. 9408-9417
    • Sayegh, J.1    Cao, J.2    Zou, M.R.3    Morales, A.4    Blair, L.P.5    Norcia, M.6    Hoyer, D.7    Tackett, A.J.8    Merkel, J.S.9    Yan, Q.10
  • 149
  • 150
    • 84914097109 scopus 로고    scopus 로고
    • O.M.V.D.K.C.N. Epitherapeutics Aps (Ed.), vol. DK2011/050281, WO
    • M.M.W.B.R.N.J. Labelle, C.A.G.N.R.R.W.O.O.X.D.S. Montalbetti, R.J.S.H.C.D.O.O.X.U.U. Mears, INHIBITORS OF HDME, in: O.M.V.D.K.C.N. Epitherapeutics Aps (Ed.), vol. DK2011/050281, WO, 2012.
    • (2012) INHIBITORS OF HDME
    • Labelle, M.1    Montalbetti, C.2    Mears, R.3
  • 156
    • 80455140217 scopus 로고    scopus 로고
    • Structural basis for histone H3 Lys 27 demethylation by UTX/KDM6A
    • Sengoku T., Yokoyama S. Structural basis for histone H3 Lys 27 demethylation by UTX/KDM6A. Genes Dev. 2011, 25:2266-2277.
    • (2011) Genes Dev. , vol.25 , pp. 2266-2277
    • Sengoku, T.1    Yokoyama, S.2
  • 157
    • 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.-D. Enzymatic and structural insights for substrate specificity of a family of Jumonji histone lysine demethylases. Nat. Struct. Mol. Biol. 2010, 17:38-43.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 38-43
    • Horton, J.R.1    Upadhyay, A.K.2    Qi, H.H.3    Zhang, X.4    Shi, Y.5    Cheng, X.-D.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.