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

Berdasco, 2010, Aberrant epigenetic landscape in cancer: how cellular identity goes awry, Dev. Cell, 19, 698, 10.1016/j.devcel.2010.10.005

Suganuma, 2011, Signals and combinatorial functions of histone modifications, Annu. Rev. Biochem., 80, 473, 10.1146/annurev-biochem-061809-175347

Zentner, 2013, Regulation of nucleosome dynamics by histone modifications, Nat. Struct. Mol. Biol., 20, 259, 10.1038/nsmb.2470

Greer, 2012, Histone methylation: a dynamic mark in health, disease and inheritance, Nat. Rev. Genet., 13, 343, 10.1038/nrg3173

Portela, 2010, Epigenetic modifications and human disease, Nat. Biotechnol., 28, 1057, 10.1038/nbt.1685

Waldmann, 2013, Targeting histone modifications—epigenetics in cancer, Curr. Opin. Cell Biol., 25, 184, 10.1016/j.ceb.2013.01.001

Xu, 2007, Histone deacetylase inhibitors: molecular mechanisms of action, Oncogene, 26, 5541, 10.1038/sj.onc.1210620

Rotili, 2011, Targeting histone demethylases: a new avenue for the fight against cancer, Gene Cancer, 2, 663, 10.1177/1947601911417976

Gravina, 2010, Biological rationale for the use of DNA methyltransferase inhibitors as new strategy for modulation of tumor response to chemotherapy and radiation, Mol. Cancer, 9, 10.1186/1476-4598-9-305

Chuikov, 2004, Regulation of p53 activity through lysine methylation, Nature, 432, 353, 10.1038/nature03117

Levy, 2011, Lysine methylation of the NF-[kappa]B subunit RelA by SETD6 couples activity of the histone methyltransferase GLP at chromatin to tonic repression of NF-[kappa]B signaling, Nat. Immunol., 12, 29, 10.1038/ni.1968

Ea, 2009, Regulation of NF-κB activity through lysine monomethylation of p65, Proc. Natl. Acad. Sci., 106, 18972, 10.1073/pnas.0910439106

Barski, 2007, High-resolution profiling of histone methylations in the human genome, Cell, 129, 823, 10.1016/j.cell.2007.05.009

Khoury, 2011, Proteome-wide post-translational modification statistics: frequency analysis and curation of the Swiss-Prot database, Sci. Rep., 1, 10.1038/srep00090

Walsh, 2005, Protein posttranslational modifications: the chemistry of proteome diversifications, Angew. Chem., 44, 7342, 10.1002/anie.200501023

Albert, 2010, Histone methyltransferases in cancer, Semin. Cell Dev. Biol., 21, 209, 10.1016/j.semcdb.2009.10.007

Bernt, 2011, MLL-rearranged leukemia is dependent on aberrant H3K79 methylation by DOT1L, Cancer Cell, 20, 66, 10.1016/j.ccr.2011.06.010

Okada, 2005, hDOT1L links histone methylation to leukemogenesis, Cell, 121, 167, 10.1016/j.cell.2005.02.020

Margueron, 2011, The Polycomb complex PRC2 and its mark in life, Nature, 469, 343, 10.1038/nature09784

Bracken, 2003, EZH2 is downstream of the pRB–E2F pathway, essential for proliferation and amplified in cancer, EMBO J., 22, 5323, 10.1093/emboj/cdg542

Varambally, 2002, The polycomb group protein EZH2 is involved in progression of prostate cancer, Nature, 419, 624, 10.1038/nature01075

Daigle, 2013, Potent inhibition of DOT1L as treatment of MLL-fusion leukemia, Blood, 122, 1017, 10.1182/blood-2013-04-497644

McCabe, 2012, EZH2 inhibition as a therapeutic strategy for lymphoma with EZH2-activating mutations, Nature, 492, 108, 10.1038/nature11606

Dawson, 2012, Cancer epigenetics: from mechanism to therapy, Cell, 150, 12, 10.1016/j.cell.2012.06.013

Walport, 2012, Mechanisms of human histone and nucleic acid demethylases, Curr. Opin. Chem. Biol., 16, 525, 10.1016/j.cbpa.2012.09.015

Kooistra, 2012, Molecular mechanisms and potential functions of histone demethylases, Nat. Rev. Mol. Cell Biol., 13, 297, 10.1038/nrm3327

Wang, 2004, Human PAD4 regulates histone arginine methylation levels via demethylimination, Science, 306, 279, 10.1126/science.1101400

Cuthbert, 2004, Histone deimination antagonizes arginine methylation, Cell, 118, 545, 10.1016/j.cell.2004.08.020

Chang, 2007, JMJD6 is a histone arginine demethylase, Science, 318, 444, 10.1126/science.1145801

Liu, 2013, Brd4 and JMJD6-associated anti-pause enhancers in regulation of transcriptional pause release, Cell, 155, 1581, 10.1016/j.cell.2013.10.056

Webby, 2009, Jmjd6 catalyses lysyl-hydroxylation of U2AF65, a protein associated with RNA splicing, Science, 325, 90, 10.1126/science.1175865

Mantri, 2011, The 2-oxoglutarate-dependent oxygenase JMJD6 catalyses oxidation of lysine residues to give 5S-hydroxylysine residues, Chembiochem, 12, 531, 10.1002/cbic.201000641

Shi, 2007, Histone lysine demethylases: emerging roles in development, physiology and disease, Nature reviews, Genetics, 8, 829

Hayami, 2011, Overexpression of LSD1 contributes to human carcinogenesis through chromatin regulation in various cancers, Int. J. Cancer, 128, 574, 10.1002/ijc.25349

Harris, 2012, The histone demethylase KDM1A sustains the oncogenic potential of MLL-AF9 leukemia stem cells, Cancer Cell, 21, 473, 10.1016/j.ccr.2012.03.014

Hoffmann, 2012, The role of histone demethylases in cancer therapy, Mol. Oncol., 6, 683, 10.1016/j.molonc.2012.07.004

Forneris, 2007, Structural basis of LSD1-CoREST selectivity in histone H3 recognition, J. Biol. Chem., 282, 20070, 10.1074/jbc.C700100200

Metzger, 2005, LSD1 demethylates repressive histone marks to promote androgen-receptor-dependent transcription, Nature, 437, 436, 10.1038/nature04020

Klose, 2006, JmjC-domain-containing proteins and histone demethylation, Nat. Rev. Genet., 7, 715, 10.1038/nrg1945

Tahiliani, 2007, The histone H3K4 demethylase SMCX links REST target genes to X-linked mental retardation, Nature, 447, 601, 10.1038/nature05823

Castermans, 2007, Identification and characterization of the TRIP8 and REEP3 genes on chromosome 10q21.3 as novel candidate genes for autism, Eur. J. Hum. Genet., 15, 422, 10.1038/sj.ejhg.5201785

Laumonnier, 2005, Mutations in PHF8 are associated with X linked mental retardation and cleft lip/cleft palate, J. Med. Genet., 42, 780, 10.1136/jmg.2004.029439

Qiu, 2010, The X-linked mental retardation gene PHF8 is a histone demethylase involved in neuronal differentiation, Cell Res., 20, 908, 10.1038/cr.2010.81

Thalhammer, 2012, The potential of 2-oxoglutarate oxygenases acting on nucleic acids as therapeutic targets, Drug Discov. Today, 9, e91

Tsukada, 2006, Histone demethylation by a family of JmjC domain-containing proteins, Nature, 439, 811, 10.1038/nature04433

Hopkinson, 2010, Monitoring the activity of 2-oxoglutarate dependent histone demethylases by NMR spectroscopy: direct observation of formaldehyde, Chembiochem, 11, 506, 10.1002/cbic.200900713

Shi, 2004, Histone demethylation mediated by the nuclear amine oxidase homolog LSD1, Cell, 119, 941, 10.1016/j.cell.2004.12.012

Willmann, 2012, Impairment of prostate cancer cell growth by a selective and reversible lysine-specific demethylase 1 inhibitor, Int. J. Cancer, 131, 2704, 10.1002/ijc.27555

Loenarz, 2008, Expanding chemical biology of 2-oxoglutarate oxygenases, Nat. Chem. Biol., 4, 152, 10.1038/nchembio0308-152

Shih, 1999, Monoamine oxidase: from genes to behavior, Annu. Rev. Neurosci., 22, 197, 10.1146/annurev.neuro.22.1.197

Rose, 2010, Selective inhibitors of the JMJD2 histone demethylases: combined nondenaturing mass spectrometric screening and crystallographic approaches, J. Med. Chem., 53, 1810, 10.1021/jm901680b

Hopkinson, 2013, 5-Carboxy-8-hydroxyquinoline is a broad spectrum 2-oxoglutarate oxygenase inhibitor which causes iron translocation, Chem. Sci., 4, 3110, 10.1039/c3sc51122g

Lee, 2006, Histone H3 lysine 4 demethylation is a target of nonselective antidepressive medications, Chem. Biol., 13, 563, 10.1016/j.chembiol.2006.05.004

Schmidt, 2007, trans-2-Phenylcyclopropylamine is a mechanism-based inactivator of the histone demethylase LSD1, Biochemistry, 46, 4408, 10.1021/bi0618621

Forneris, 2005, Human histone demethylase LSD1 reads the histone code, J. Biol. Chem., 280, 41360, 10.1074/jbc.M509549200

Culhane, 2010, Comparative analysis of small molecules and histone substrate analogues as LSD1 lysine demethylase inhibitors, J. Am. Chem. Soc., 132, 3164, 10.1021/ja909996p

Hellerman, 1968, Mitochondrial monoamine oxidase. II. Action of various inhibitors for the bovine kidney enzyme. Catalytic mechanism, J. Biol. Chem., 243, 5234, 10.1016/S0021-9258(18)91942-3

Binda, 2003, Insights into the mode of inhibition of human mitochondrial monoamine oxidase B from high-resolution crystal structures, Proc. Natl. Acad. Sci. U. S. A., 100, 9750, 10.1073/pnas.1633804100

Patek, 1974, Mitochondrial monoamine oxidase. Mechanism of inhibition by phenylhydrazine and by aralkylhydrazines. Role of enzymatic oxidation, J. Biol. Chem., 249, 2373, 10.1016/S0021-9258(19)42740-3

Binda, 2010, Biochemical, structural, and biological evaluation of tranylcypromine derivatives as inhibitors of histone demethylases LSD1 and LSD2, J. Am. Chem. Soc., 132, 6827, 10.1021/ja101557k

Yang, 2007, Structural basis for the inhibition of the LSD1 histone demethylase by the antidepressant trans-2-phenylcyclopropylamine, Biochemistry, 46, 8058, 10.1021/bi700664y

Mimasu, 2008, Crystal structure of histone demethylase LSD1 and tranylcypromine at 2.25 A, Biochem. Biophys. Res. Commun., 366, 15, 10.1016/j.bbrc.2007.11.066

Gooden, 2008, Facile synthesis of substituted trans-2-arylcyclopropylamine inhibitors of the human histone demethylase LSD1 and monoamine oxidases A and B, Bioorg. Med. Chem. Lett., 18, 3047, 10.1016/j.bmcl.2008.01.003

Ueda, 2009, Identification of cell-active lysine specific demethylase 1-selective inhibitors, J. Am. Chem. Soc., 131, 17536, 10.1021/ja907055q

Mimasu, 2010, Structurally designed trans-2-phenylcyclopropylamine derivatives potently inhibit histone demethylase LSD1/KDM1, Biochemistry, 49, 6494, 10.1021/bi100299r

Neelamegam, 2012, Brain-penetrant LSD1 inhibitors can block memory consolidation, ACS Chem. Neurosci., 3, 120, 10.1021/cn200104y

Oryzen Genomics, 2010

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.

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.

Harris, 2012, The histone demethylase KDM1A sustains the oncogenic potential of MLL-AF9 leukemia stem cells, Cancer Cell, 21, 473, 10.1016/j.ccr.2012.03.014

Maes, 2013, Preclinical characterization of a potent and selective inhibitor of the histone demethylase KDM1A for MLL leukemia, 31, e13543

Culhane, 2006, A mechanism-based inactivator for histone demethylase LSD1, J. Am. Chem. Soc., 128, 4536, 10.1021/ja0602748

Szewczuk, 2007, Mechanistic analysis of a suicide inactivator of histone demethylase LSD1, Biochemistry, 46, 6892, 10.1021/bi700414b

Federico, 2001, Inhibition of pig liver and Zea mays L. polyamine oxidase: a comparative study, J. Enzym Inhib., 16, 147, 10.1080/14756360109162364

Bianchi, 2006, Inhibition of polyamine and spermine oxidases by polyamine analogues, FEBS J., 273, 1115, 10.1111/j.1742-4658.2006.05137.x

Huang, 2007, Inhibition of lysine-specific demethylase 1 by polyamine analogues results in reexpression of aberrantly silenced genes, Proc. Natl. Acad. Sci., 104, 8023, 10.1073/pnas.0700720104

Huang, 2009, Novel oligoamine analogues inhibit lysine-specific demethylase 1 and induce reexpression of epigenetically silenced genes, Clin. Cancer Res., 15, 7217, 10.1158/1078-0432.CCR-09-1293

Sharma, 2010, (Bis)urea and (bis)thiourea inhibitors of lysine-specific demethylase 1 as epigenetic modulators, J. Med. Chem., 53, 5197, 10.1021/jm100217a

H.O.B.W.L.V.N.V. Zhang, T.S.U.T.X.N.D.S.G. Ye, J.S.U.T.X.N.D.S.G. Quan, J.S.U.T.X.N.D.S.G. Wang, HISTONE DEMETHYLASE INHIBITORS AND USES THEREOF FOR TREATMENT O F CANCER, in: O.B.W.L.V.N.V. Nevada Cancer Institute, S.U.T.X.N.D.S.G. Shenzhen Graduate School Of Peking University (Eds.), vol. US2011/061954, WO, 2012.

Liu, 2013

Hitchin, 2013, Development and evaluation of selective, reversible LSD1 inhibitors derived from fragments, Med. Chem. Commun., 4, 1513, 10.1039/c3md00226h

Lynch, 2013, CD86 expression as a surrogate cellular biomarker for pharmacological inhibition of the histone demethylase lysine-specific demethylase 1, Anal. Biochem., 442, 104, 10.1016/j.ab.2013.07.032

Sorna, 2013, High-throughput virtual screening identifies novel N′-(1-phenylethylidene)-benzohydrazides as potent, specific, and reversible LSD1 inhibitors, J. Med. Chem., 56, 9496, 10.1021/jm400870h

Dhanak, 2013, Drugging the cancer genome

Majamaa, 1987, Inhibition of prolyl hydroxylation during collagen biosynthesis in human skin fibroblast cultures by ethyl 3,4-dihydroxybenzoate, J. Investig. Dermatol., 89, 405, 10.1111/1523-1747.ep12471775

Franklin, 1989, Inhibition of collagen hydroxylation by 2,7,8-trihydroxyanthraquinone in embryonic-chick tendon cells, Biochem. J., 261, 127, 10.1042/bj2610127

Rose, 2011, Inhibition of 2-oxoglutarate dependent oxygenases, Chem. Soc. Rev., 40, 4364, 10.1039/c0cs00203h

Schofield, 2004, Oxygen sensing by HIF hydroxylases, Nat. Rev. Mol. Cell Biol., 5, 343, 10.1038/nrm1366

Clifton, 2006, Structural studies on 2-oxoglutarate oxygenases and related double-stranded β-helix fold proteins, J. Inorg. Biochem., 100, 644, 10.1016/j.jinorgbio.2006.01.024

McDonough, 2010, Structural studies on human 2-oxoglutarate dependent oxygenases, Curr. Opin. Struct. Biol., 20, 659, 10.1016/j.sbi.2010.08.006

Aik, 2012, Role of the jelly-roll fold in substrate binding by 2-oxoglutarate oxygenases, Curr. Opin. Struct. Biol., 22, 691, 10.1016/j.sbi.2012.10.001

Kruidenier, 2012, A selective Jumonji H3K27 demethylase inhibitor modulates the proinflammatory macrophage response, Nature, 488, 404, 10.1038/nature11262

Poppe, 2009, 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., 131, 16654, 10.1021/ja907933p

Bleijlevens, 2008, Dynamic states of the DNA repair enzyme AlkB regulate product release, EMBO Rep., 9, 872, 10.1038/embor.2008.120

Opocher, 2011, Functional consequences of succinate dehydrogenase mutations, Endocr. Pract., 17, 64, 10.4158/EP11070.RA

Dang, 2009, Cancer-associated IDH1 mutations produce 2-hydroxyglutarate, Nature, 462, 739, 10.1038/nature08617

Losman, 2013, (R)-2-Hydroxyglutarate is sufficient to promote leukemogenesis and its effects are reversible, Science, 339, 1621, 10.1126/science.1231677

Zhao, 2009, Glioma-derived mutations in IDH1 dominantly inhibit IDH1 catalytic activity and induce HIF-1alpha, Science, 324, 261, 10.1126/science.1170944

Puistola, 1980, Studies on the lysyl hydroxylase reaction. 1. Initial velocity kinetics and related aspects, Biochim. Biophys. Acta, 611, 40, 10.1016/0005-2744(80)90040-6

Myllyla, 1977, Mechanism of prolyl hydroxylase reaction. 2. Kinetic-analysis of reaction sequence, Eur. J. Biochem., 80, 349, 10.1111/j.1432-1033.1977.tb11889.x

Xiao, 2012, 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., 26, 1326, 10.1101/gad.191056.112

Rose, 2008, Inhibitor scaffolds for 2-oxoglutarate-dependent histone lysine demethylases, J. Med. Chem., 51, 7053, 10.1021/jm800936s

Chowdhury, 2011, The oncometabolite 2-hydroxyglutarate inhibits histone lysine demethylases, EMBO Rep., 12, 463, 10.1038/embor.2011.43

Xu, 2011, Oncometabolite 2-hydroxyglutarate is a competitive inhibitor of alpha-ketoglutarate-dependent dioxygenases, Cancer Cell, 19, 17, 10.1016/j.ccr.2010.12.014

Couture, 2007, Specificity and mechanism of JMJD2A, a trimethyllysine-specific histone demethylase, Nat. Struct. Mol. Biol., 14, 689, 10.1038/nsmb1273

Price, 2005, Kinetic dissection of the catalytic mechanism of taurine:α-ketoglutarate dioxygenase (TauD) from Escherichia coli†, Biochemistry, 44, 8138, 10.1021/bi050227c

Welford, 2003, The selectivity and inhibition of AlkB, J. Biol. Chem., 278, 10157, 10.1074/jbc.M211058200

Rydzik, 2012, Development and application of a fluoride-detection-based fluorescence assay for gamma-butyrobetaine hydroxylase, Chembiochem, 13, 1559, 10.1002/cbic.201200256

MacKenzie, 2007, Cell-permeating alpha-ketoglutarate derivatives alleviate pseudohypoxia in succinate dehydrogenase-deficient cells, Mol. Cell. Biol., 27, 3282, 10.1128/MCB.01927-06

Sekirnik, 2009, Inhibition of the histone lysine demethylase JMJD2A by ejection of structural Zn(ii), Chem. Commun., 6376, 10.1039/b916357c

Woon, 2012, Dynamic combinatorial mass spectrometry leads to inhibitors of a 2-oxoglutarate-dependent nucleic acid demethylase, J. Med. Chem., 55, 2173, 10.1021/jm201417e

Chen, 2012, Development of cell-active N6-methyladenosine RNA demethylase FTO inhibitor, J. Am. Chem. Soc., 134, 17963, 10.1021/ja3064149

Aik, 2013, Structural basis for inhibition of the fat mass and obesity associated protein (FTO), J. Med. Chem., 56, 3680, 10.1021/jm400193d

Cunliffe, 1992, Novel inhibitors of prolyl 4-hydroxylase. 3. Inhibition by the substrate analog N-oxaloglycine and its derivatives, J. Med. Chem., 35, 2652, 10.1021/jm00092a016

Mole, 2003, 2-Oxoglutarate analogue inhibitors of hif prolyl hydroxylase, Bioorg. Med. Chem. Lett., 13, 2677, 10.1016/S0960-894X(03)00539-0

Rankin, 2012, The HIF signaling pathway in osteoblasts directly modulates erythropoiesis through the production of EPO, Cell, 149, 63, 10.1016/j.cell.2012.01.051

Tian, 2011, Differential sensitivity of hypoxia inducible factor hydroxylation sites to hypoxia and hydroxylase inhibitors, J. Biol. Chem., 286, 13041, 10.1074/jbc.M110.211110

McDonough, 2005, Selective inhibition of factor inhibiting hypoxia-inducible factor, J. Am. Chem. Soc., 127, 7680, 10.1021/ja050841b

Ng, 2007, Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity, Nature, 448, 87, 10.1038/nature05971

Hamada, 2009, Synthesis and activity of N-oxalylglycine and its derivatives as Jumonji C-domain-containing histone lysine demethylase inhibitors, Bioorg. Med. Chem. Lett., 19, 2852, 10.1016/j.bmcl.2009.03.098

Hamada, 2010, Design, synthesis, enzyme-inhibitory activity, and effect on human cancer cells of a novel series of Jumonji domain-containing protein 2 histone demethylase inhibitors, J. Med. Chem., 53, 5629, 10.1021/jm1003655

Rose, 2012, Plant growth regulator daminozide is a selective inhibitor of human KDM2/7 histone demethylases, J. Med. Chem., 55, 6639, 10.1021/jm300677j

Suzuki, 2013, Identification of the KDM2/7 histone lysine demethylase subfamily inhibitor and its antiproliferative activity, J. Med. Chem., 56, 7222, 10.1021/jm400624b

Luo, 2011, A selective inhibitor and probe of the cellular functions of Jumonji C domain-containing histone demethylases, J. Am. Chem. Soc., 133, 9451, 10.1021/ja201597b

Brown, 1997, Daminozide and prohexadione have similar modes of action as inhibitors of the late stages of gibberellin metabolism, Physiol. Plant., 101, 309, 10.1111/j.1399-3054.1997.tb01001.x

Mackeen, 2010, Small-molecule-based inhibition of histone demethylation in cells assessed by quantitative mass spectrometry, J. Proteome Res., 9, 4082, 10.1021/pr100269b

Thalhammer, 2011, Inhibition of the histone demethylase JMJD2E by 3-substituted pyridine 2,4-dicarboxylates, Org. Biomol. Chem., 9, 127, 10.1039/C0OB00592D

Barker, 2013

Wang, 2013, A small molecule modulates Jumonji histone demethylase activity and selectively inhibits cancer growth, Nat. Commun., 4, 2035, 10.1038/ncomms3035

Hurych, 1965, Influence of chelating agents on the biosynthesis of collagen, Biochim. Biophys. Acta Gen. Subj., 97, 361, 10.1016/0304-4165(65)90108-X

Hales, 1993, 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., 36, 3853, 10.1021/jm00076a014

Chang, 2011, Inhibition of histone demethylases by 4-carboxy-2,2′-bipyridyl compounds, ChemMedChem, 6, 759, 10.1002/cmdc.201100026

King, 2010, Quantitative high-throughput screening identifies 8-hydroxyquinolines as cell-active histone demethylase inhibitors, PLoS ONE, 5, e15535, 10.1371/journal.pone.0015535

Liang, 2013, Targeting the JMJD2 histone demethylases to epigenetically control herpesvirus infection and reactivation from latency, Sci. Transl. Med., 5, 10.1126/scitranslmed.3005145

Geurink, 2012, Photoaffinity labeling in activity-based protein profiling, vol. 324, 85

Rotili, 2011, A photoreactive small-molecule probe for 2-oxoglutarate oxygenases, Chem. Biol., 18, 642, 10.1016/j.chembiol.2011.03.007

Bush, 2013, The Ugi four-component reaction enables expedient synthesis and comparison of photoaffinity probes, Chem. Sci., 4, 4115, 10.1039/c3sc51708j

Lohse, 2011, Targeting histone lysine demethylases by truncating the histone 3 tail to obtain selective substrate-based inhibitors, Angew. Chem. Int. Ed., 50, 9100, 10.1002/anie.201101849

Woon, 2012, Linking of 2-oxoglutarate and substrate binding sites enables potent and highly selective inhibition of JmjC histone demethylases, Angew. Chem. Int. Ed., 51, 1631, 10.1002/anie.201107833

Upadhyay, 2012, An analog of BIX-01294 selectively inhibits a family of histone H3 lysine 9 Jumonji demethylases, J. Mol. Biol., 416, 319, 10.1016/j.jmb.2011.12.036

Murray, 1977, Inhibition of lysyl hydroxylase by catechol analogs, Biochim. Biophys. Acta, 481, 63, 10.1016/0005-2744(77)90137-1

Wilson, 2002, The dietary flavonoid quercetin modulates HIF-1 alpha activity in endothelial cells, Biochem. Biophys. Res. Commun., 293, 446, 10.1016/S0006-291X(02)00244-9

Zhou, 2004, Hypoxia-inducible factor-1 activation by (-)-epicatechin gallate: potential adverse effects of cancer chemoprevention with high-dose green tea extracts, J. Nat. Prod., 67, 2063, 10.1021/np040140c

Sakurai, 2010, A miniaturized screen for inhibitors of Jumonji histone demethylases, Mol. BioSyst., 6, 357, 10.1039/B912993F

Nielsen, 2012, Identification of catechols as histone-lysine demethylase inhibitors, FEBS Lett., 586, 1190, 10.1016/j.febslet.2012.03.001

Sayegh, 2013, Identification of small molecule inhibitors of Jumonji AT-rich interactive domain 1B (JARID1B) histone demethylase by a sensitive high throughput screen, J. Biol. Chem., 288, 9408, 10.1074/jbc.M112.419861

Kim, 2013, Tripartin, a histone demethylase inhibitor from a bacterium associated with a dung beetle larva, Org. Lett., 15, 1834, 10.1021/ol4004417

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, J.L.G.W.O.O.X.N.Y. Vile, D.M.F.A.M.E.V. Gelman, X.B.D.W.O.O.X.B.H. Gai, O.R.C.C.L.W.O.O.X.N.S. Barker, H.J.C.O.C.D.O.O.X.A.X. Deboves, S.P.T.C.W.O.O.X.B.B. East, T.L.t.D.K.C.Ø. Boesen, INHIBITORS OF HDME, in: O.M.V.D.K.C.N. Epitherapeutics Aps (Ed.), vol. DK2011/050280, WO, 2012.

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.

Wissmann, 2007, Cooperative demethylation by JMJD2C and LSD1 promotes androgen receptor-dependent gene expression, Nat. Cell Biol., 9, 347, 10.1038/ncb1546

Rotili, 2014, Pan-histone demethylase inhibitors simultaneously targeting Jumonji C and lysine-specific demethylases display high anticancer activities, J. Med. Chem., 57, 42, 10.1021/jm4012802

Sedgwick, 2007, Repair of alkylated DNA: recent advances, DNA Repair, 6, 429, 10.1016/j.dnarep.2006.10.005

Yang, 2007, Structural basis of histone demethylation by LSD1 revealed by suicide inactivation, Nat. Struct. Mol. Biol., 14, 535, 10.1038/nsmb1255

Fang, 2013, LSD2/KDM1B and its cofactor NPAC/GLYR1 endow a structural and molecular model for regulation of H3K4 demethylation, Mol. Cell, 49, 558, 10.1016/j.molcel.2012.11.019

Sengoku, 2011, Structural basis for histone H3 Lys 27 demethylation by UTX/KDM6A, Genes Dev., 25, 2266, 10.1101/gad.172296.111

Horton, 2010, Enzymatic and structural insights for substrate specificity of a family of Jumonji histone lysine demethylases, Nat. Struct. Mol. Biol., 17, 38, 10.1038/nsmb.1753