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Volumn 92, Issue , 2015, Pages 377-386

Further insights into the SAR of α-substituted cyclopropylamine derivatives as inhibitors of histone demethylase KDM1A

Author keywords

Epigenetic; Lysine demethylase; Tranylcypromine

Indexed keywords

1 (ETHOXYCARBONYL) 2 PHENYLCYCLOPROPANECARBOXYLIC ACID; 1 PHENYL 4,7 DIAZASPIRO[2.5]OCTAN 8 ONE; 1 PHENYL 7 OXA 4 AZASPIRO[2.5]OCTAN 5 ONE; 1 [(TERT BUTOXYCARBONYL)AMINO] 2 PHENYLCYCLOPANECARBOXYLATE; 2 BROMO N [1 (HYDROXYMETHYL) 2 PHENYLCYCLOPROPYL]ACETAMIDE; 3 (4 CHLOROPHENYL) 2 PHENYL PROP 2 ENOIC ACID; ANTINEOPLASTIC AGENT; DIETHYL 2 BENZYLIDENEMALONATE; DIETHYL 2 PHENYLCYCLOPROPANE 1,1 DICARBOXYLATE; ETHYL1 [[2 [(TERT BUTOXYCARBONYL)AMINO]ETHYL]AMINO] 2 PHENYLCYCLOPROPANECARBOXYLATE; HISTONE DEMETHYLASE; OXYGENASE INHIBITOR; SELEGILINE; TERT BUTYL [1 (HYDROXYMETHYL) 2 PHENYLCYCLOPROPYL]CARBAMATE; TRANYLCYPROMINE DERIVATIVE; UNCLASSIFIED DRUG; CYCLOPROPANE DERIVATIVE; CYCLOPROPYLAMINE; KDM1A PROTEIN, HUMAN; RECOMBINANT PROTEIN;

EID: 84920853656     PISSN: 02235234     EISSN: 17683254     Source Type: Journal    
DOI: 10.1016/j.ejmech.2014.12.032     Document Type: Article
Times cited : (31)

References (50)
  • 1
    • 0036532026 scopus 로고    scopus 로고
    • Histone modifications in transcriptional regulation
    • S.L. Berger, Histone modifications in transcriptional regulation, Curr. Opin. Genet. Dev. 12 (2002) 142-148.
    • (2002) Curr. Opin. Genet. Dev. , vol.12 , pp. 142-148
    • Berger, S.L.1
  • 2
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • T. Jenuwein, C.D. Allis, Translating the histone code, Science 293 (2001) 1074-1080, http://dx.doi.org/10.1126/science.1063127.
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 3
    • 84877830475 scopus 로고    scopus 로고
    • Chromatin organization and transcriptional regulation
    • M.R. Hübner, M.A. Eckersley-Maslin, D.L. Spector, Chromatin organization and transcriptional regulation, Curr. Opin. Genet. Dev. 23 (2013) 89-95, http://dx.doi.org/10.1016/j.gde.2012.11.006.
    • (2013) Curr. Opin. Genet. Dev. , vol.23 , pp. 89-95
    • Hübner, M.R.1    Eckersley-Maslin, M.A.2    Spector, D.L.3
  • 4
    • 77951616674 scopus 로고    scopus 로고
    • The nuclear envelope in genome organization, expression and stability
    • K. Mekhail, D. Moazed, The nuclear envelope in genome organization, expression and stability, Nat. Rev. Mol. Cell. Biol. 11 (2010) 317-328, http://dx.doi.org/10.1038/nrm2894.
    • (2010) Nat. Rev. Mol. Cell. Biol. , vol.11 , pp. 317-328
    • Mekhail, K.1    Moazed, D.2
  • 5
    • 0020699979 scopus 로고
    • Hypomethylation distinguishes genes of some human cancers from their normal counterparts
    • A.P. Feinberg, B. Vogelstein, Hypomethylation distinguishes genes of some human cancers from their normal counterparts, Nature 301 (1983) 89-92, http://dx.doi.org/10.1038/301089a0.
    • (1983) Nature , vol.301 , pp. 89-92
    • Feinberg, A.P.1    Vogelstein, B.2
  • 6
    • 33845615494 scopus 로고    scopus 로고
    • Cancer biology: Mechanism of antitumour action of vorinostat (suberoylanilide hydroxamic acid), a novel histone deacetylase inhibitor
    • V.M. Richon, Cancer biology: mechanism of antitumour action of vorinostat (suberoylanilide hydroxamic acid), a novel histone deacetylase inhibitor, Br. J. Cancer 95 (2006) S2-S6, http://dx.doi.org/10.1038/sj.bjc.6603463.
    • (2006) Br. J. Cancer , vol.95 , pp. S2-S6
    • Richon, V.M.1
  • 7
    • 0344431240 scopus 로고    scopus 로고
    • FR901228, a potent antitumor antibiotic, is a novel histone deacetylase inhibitor
    • H. Nakajima, Y.B. Kim, H. Terano, M. Yoshida, S. Horinouchi, FR901228, a potent antitumor antibiotic, is a novel histone deacetylase inhibitor, Exp. Cell. Res. 241 (1998) 126-133, http://dx.doi.org/10.1006/excr.1998.4027.
    • (1998) Exp. Cell. Res. , vol.241 , pp. 126-133
    • Nakajima, H.1    Kim, Y.B.2    Terano, H.3    Yoshida, M.4    Horinouchi, S.5
  • 8
    • 57749170458 scopus 로고    scopus 로고
    • The many roles of histone deacetylases in development and physiology: Implications for disease and therapy
    • M. Haberland, R.L. Montgomery, E.N. Olson, The many roles of histone deacetylases in development and physiology: implications for disease and therapy, Nat. Rev. Genet. 10 (2009) 32-42, http://dx.doi.org/10.1038/nrg2485.
    • (2009) Nat. Rev. Genet. , vol.10 , pp. 32-42
    • Haberland, M.1    Montgomery, R.L.2    Olson, E.N.3
  • 9
    • 0037444803 scopus 로고    scopus 로고
    • Histone deacetylases (HDACs): Characterization of the classical HDAC family
    • A.J.M. de Ruijter, A.H. van Gennip, H.N. Caron, S. Kemp, A.B.P. van Kuilenburg, Histone deacetylases (HDACs): characterization of the classical HDAC family, Biochem. J. 370 (2003) 737-749, http://dx.doi.org/10.1042/BJ20021321.
    • (2003) Biochem. J. , vol.370 , pp. 737-749
    • De Ruijter, A.J.M.1    Van Gennip, A.H.2    Caron, H.N.3    Kemp, S.4    Van Kuilenburg, A.B.P.5
  • 10
    • 84899973908 scopus 로고    scopus 로고
    • Targeting bromodomains: Epigenetic readers of lysine acetylation
    • P. Filippakopoulos, S. Knapp, Targeting bromodomains: epigenetic readers of lysine acetylation, Nat. Rev. Drug Discov. 13 (2014) 337-356, http://dx.doi.org/10.1038/nrd4286.
    • (2014) Nat. Rev. Drug Discov. , vol.13 , pp. 337-356
    • Filippakopoulos, P.1    Knapp, S.2
  • 11
    • 84903155987 scopus 로고    scopus 로고
    • Histone lysine demethylase (KDM) subfamily 4: Structures, functions and therapeutic potential
    • R.M. Labbe, A. Holowatyj, Z.-Q. Yang, Histone lysine demethylase (KDM) subfamily 4: structures, functions and therapeutic potential, Am. J. Transl. Res. 6 (2013) 1-15.
    • (2013) Am. J. Transl. Res. , vol.6 , pp. 1-15
    • Labbe, R.M.1    Holowatyj, A.2    Yang, Z.-Q.3
  • 12
    • 27644589675 scopus 로고    scopus 로고
    • The diverse functions of histone lysine methylation
    • C. Martin, Y. Zhang, The diverse functions of histone lysine methylation, Nat. Rev. Mol. Cell. Biol. 6 (2005) 838-849, http://dx.doi.org/10.1038/nrm1761.
    • (2005) Nat. Rev. Mol. Cell. Biol. , vol.6 , pp. 838-849
    • Martin, C.1    Zhang, Y.2
  • 13
    • 80054787805 scopus 로고    scopus 로고
    • Targeting histone demethylases a new avenue for the fight against cancer
    • D. Rotili, A. Mai, Targeting histone demethylases a new avenue for the fight against cancer, Genes. Cancer 2 (2011) 663-679, http://dx.doi.org/10.1177/1947601911417976.
    • (2011) Genes. Cancer , vol.2 , pp. 663-679
    • Rotili, D.1    Mai, A.2
  • 14
    • 77953644347 scopus 로고    scopus 로고
    • Reversal of histone methylation: Biochemical and molecular mechanisms of histone demethylases
    • N. Mosammaparast, Y. Shi, Reversal of histone methylation: biochemical and molecular mechanisms of histone demethylases, Annu. Rev. Biochem. 79 (2010) 155-179, http://dx.doi.org/10.1146/annurev.biochem.78.070907.103946.
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 155-179
    • Mosammaparast, N.1    Shi, Y.2
  • 16
    • 39349105090 scopus 로고    scopus 로고
    • Expanding chemical biology of 2-oxoglutarate oxygenases
    • C. Loenarz, C.J. Schofield, Expanding chemical biology of 2-oxoglutarate oxygenases, Nat. Chem. Biol. 4 (2008) 152-156, http://dx.doi.org/10.1038/nchembio0308-152.
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 152-156
    • Loenarz, C.1    Schofield, C.J.2
  • 17
    • 41549132495 scopus 로고    scopus 로고
    • LSD1: Oxidative chemistry for multifaceted functions in chromatin regulation
    • F. Forneris, C. Binda, E. Battaglioli, A. Mattevi, LSD1: oxidative chemistry for multifaceted functions in chromatin regulation, Trends Biochem. Sci. 33 (2008) 181-189, http://dx.doi.org/10.1016/j.tibs.2008.01.003.
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 181-189
    • Forneris, F.1    Binda, C.2    Battaglioli, E.3    Mattevi, A.4
  • 18
    • 11144332565 scopus 로고    scopus 로고
    • Histone demethylation mediated by the nuclear amine oxidase homolog LSD1
    • Y. Shi, F. Lan, C. Matson, P. Mulligan, J.R. Whetstine, P.A. Cole, et al., Histone demethylation mediated by the nuclear amine oxidase homolog LSD1, Cell 119 (2004) 941-953, http://dx.doi.org/10.1016/j.cell.2004.12.012.
    • (2004) Cell , vol.119 , pp. 941-953
    • Shi, Y.1    Lan, F.2    Matson, C.3    Mulligan, P.4    Whetstine, J.R.5    Cole, P.A.6
  • 19
    • 70349272130 scopus 로고    scopus 로고
    • KDM1B is a histone H3K4 demethylase required to establish maternal genomic imprints
    • D.N. Ciccone, H. Su, S. Hevi, F. Gay, H. Lei, J. Bajko, et al., KDM1B is a histone H3K4 demethylase required to establish maternal genomic imprints, Nature 461 (2009) 415-418, http://dx.doi.org/10.1038/nature08315.
    • (2009) Nature , vol.461 , pp. 415-418
    • Ciccone, D.N.1    Su, H.2    Hevi, S.3    Gay, F.4    Lei, H.5    Bajko, J.6
  • 20
    • 84862777766 scopus 로고    scopus 로고
    • Inhibition of the LSD1 (KDM1A) demethylase reactivates the all-trans-retinoic acid differentiation pathway in acute myeloid leukemia
    • T. Schenk, W.C. Chen, S. Göllner, L. Howell, L. Jin, K. Hebestreit, et al., Inhibition of the LSD1 (KDM1A) demethylase reactivates the all-trans-retinoic acid differentiation pathway in acute myeloid leukemia, Nat. Med. 18 (2012) 605-611, http://dx.doi.org/10.1038/nm.2661.
    • (2012) Nat. Med. , vol.18 , pp. 605-611
    • Schenk, T.1    Chen, W.C.2    Göllner, S.3    Howell, L.4    Jin, L.5    Hebestreit, K.6
  • 21
    • 62449197931 scopus 로고    scopus 로고
    • Lysine-specific demethylase 1 is strongly expressed in poorly differentiated neuroblastoma: Implications for therapy
    • J.H. Schulte, S. Lim, A. Schramm, N. Friedrichs, J. Koster, R. Versteeg, et al., Lysine-specific demethylase 1 is strongly expressed in poorly differentiated neuroblastoma: implications for therapy, Cancer Res. 69 (2009) 2065-2071, http://dx.doi.org/10.1158/0008-5472.CAN-08-1735.
    • (2009) Cancer Res. , vol.69 , pp. 2065-2071
    • Schulte, J.H.1    Lim, S.2    Schramm, A.3    Friedrichs, N.4    Koster, J.5    Versteeg, R.6
  • 22
    • 84864510460 scopus 로고    scopus 로고
    • The emerging role of histone lysine demethylases in prostate cancer
    • F. Crea, L. Sun, A. Mai, Y.T. Chiang, W.L. Farrar, R. Danesi, et al., The emerging role of histone lysine demethylases in prostate cancer, Mol. Cancer 11 (2012) 52, http://dx.doi.org/10.1186/1476-4598-11-52.
    • (2012) Mol. Cancer , vol.11 , pp. 52
    • Crea, F.1    Sun, L.2    Mai, A.3    Chiang, Y.T.4    Farrar, W.L.5    Danesi, R.6
  • 23
    • 84055211870 scopus 로고    scopus 로고
    • Lysine demethylases inhibitors
    • T. Suzuki, N. Miyata, Lysine demethylases inhibitors, J. Med. Chem. 54 (2011) 8236-8250, http://dx.doi.org/10.1021/jm201048w.
    • (2011) J. Med. Chem. , vol.54 , pp. 8236-8250
    • Suzuki, T.1    Miyata, N.2
  • 24
    • 84906839626 scopus 로고    scopus 로고
    • Synthesis, biological activity and mechanistic insights of 1-substituted cyclopropylamine derivatives: A novel class of irreversible inhibitors of histone demethylase KDM1A
    • P. Vianello, O.A. Botrugno, A. Cappa, G. Ciossani, P. Dessanti, A. Mai, et al., Synthesis, biological activity and mechanistic insights of 1-substituted cyclopropylamine derivatives: a novel class of irreversible inhibitors of histone demethylase KDM1A, Eur. J. Med. Chem. 86 (2014) 352-363, http://dx.doi.org/10.1016/j.ejmech.2014.08.068.
    • (2014) Eur. J. Med. Chem. , vol.86 , pp. 352-363
    • Vianello, P.1    Botrugno, O.A.2    Cappa, A.3    Ciossani, G.4    Dessanti, P.5    Mai, A.6
  • 25
    • 34147173308 scopus 로고    scopus 로고
    • trans-2-Phenylcyclopropylamine is a mechanism-based inactivator of the histone demethylase LSD1
    • D.M.Z. Schmidt, D.G. McCafferty, trans-2-Phenylcyclopropylamine is a mechanism-based inactivator of the histone demethylase LSD1, Biochem. Mosc. 46 (2007) 4408-4416, http://dx.doi.org/10.1021/bi0618621.
    • (2007) Biochem. Mosc. , vol.46 , pp. 4408-4416
    • Schmidt, D.M.Z.1    McCafferty, D.G.2
  • 26
    • 33745187327 scopus 로고    scopus 로고
    • Histone H3 lysine 4 demethylation is a target of nonselective antidepressive medications
    • M.G. Lee, C. Wynder, D.M. Schmidt, D.G. McCafferty, R. Shiekhattar, Histone H3 lysine 4 demethylation is a target of nonselective antidepressive medications, Chem. Biol. 13 (2006) 563-567, http://dx.doi.org/10.1016/j.chembiol.2006.05.004.
    • (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
  • 27
    • 34447338875 scopus 로고    scopus 로고
    • Structural basis for the inhibition of the LSD1 histone demethylase by the antidepressant trans-2-phenylcyclopropylamine
    • M. Yang, J.C. Culhane, L.M. Szewczuk, P. Jalili, H.L. Ball, M. Machius, et al., Structural basis for the inhibition of the LSD1 histone demethylase by the antidepressant trans-2-phenylcyclopropylamine, Biochem. Mosc. 46 (2007) 8058-8065, http://dx.doi.org/10.1021/bi700664y.
    • (2007) Biochem. Mosc. , 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
  • 28
    • 77949421463 scopus 로고    scopus 로고
    • Comparative analysis of small molecules and histone substrate analogues as LSD1 lysine demethylase inhibitors
    • J.C. Culhane, D. Wang, P.M. Yen, P.A. Cole, Comparative analysis of small molecules and histone substrate analogues as LSD1 lysine demethylase inhibitors, J. Am. Chem. Soc. 132 (2010) 3164-3176, http://dx.doi.org/10.1021/ja909996p.
    • (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
  • 29
    • 24144462170 scopus 로고    scopus 로고
    • LSD1 demethylates repressive histone marks to promote androgen-receptor-dependent transcription
    • E. Metzger, M. Wissmann, N. Yin, J.M. Müller, R. Schneider, A.H.F.M. Peters, et al., LSD1 demethylates repressive histone marks to promote androgen-receptor-dependent transcription, Nature 437 (2005) 436-439, http://dx.doi.org/10.1038/nature04020.
    • (2005) Nature , vol.437 , pp. 436-439
    • Metzger, E.1    Wissmann, M.2    Yin, N.3    Müller, J.M.4    Schneider, R.5    Peters, A.H.F.M.6
  • 30
    • 34249934238 scopus 로고    scopus 로고
    • Inhibition of lysine-specific demethylase 1 by polyamine analogues results in reexpression of aberrantly silenced genes
    • Y. Huang, E. Greene, T.M. Stewart, A.C. Goodwin, S.B. Baylin, P.M. Woster, et al., Inhibition of lysine-specific demethylase 1 by polyamine analogues results in reexpression of aberrantly silenced genes, Proc. Natl. Acad. Sci. 104 (2007) 8023-8028, http://dx.doi.org/10.1073/pnas.0700720104.
    • (2007) Proc. Natl. Acad. Sci. , vol.104 , pp. 8023-8028
    • Huang, Y.1    Greene, E.2    Stewart, T.M.3    Goodwin, A.C.4    Baylin, S.B.5    Woster, P.M.6
  • 31
    • 77954691054 scopus 로고    scopus 로고
    • (Bis)urea and (Bis)thiourea inhibitors of lysine-specific demethylase 1 as epigenetic modulators
    • S.K. Sharma, Y. Wu, N. Steinbergs, M.L. Crowley, A.S. Hanson, R.A. Casero, et al., (Bis)urea and (Bis)thiourea inhibitors of lysine-specific demethylase 1 as epigenetic modulators, J. Med. Chem. 53 (2010) 5197-5212, http://dx.doi.org/10.1021/jm100217a.
    • (2010) J. Med. Chem. , vol.53 , pp. 5197-5212
    • Sharma, S.K.1    Wu, Y.2    Steinbergs, N.3    Crowley, M.L.4    Hanson, A.S.5    Casero, R.A.6
  • 32
    • 82655179979 scopus 로고    scopus 로고
    • Novel histone demethylase LSD1 inhibitors selectively target cancer cells with pluripotent stem cell properties
    • J. Wang, F. Lu, Q. Ren, H. Sun, Z. Xu, R. Lan, et al., Novel histone demethylase LSD1 inhibitors selectively target cancer cells with pluripotent stem cell properties, Cancer Res. 71 (2011) 7238-7249, http://dx.doi.org/10.1158/0008-5472.CAN-11-0896.
    • (2011) Cancer Res. , vol.71 , pp. 7238-7249
    • Wang, J.1    Lu, F.2    Ren, Q.3    Sun, H.4    Xu, Z.5    Lan, R.6
  • 33
    • 84890448100 scopus 로고    scopus 로고
    • High-throughput virtual screening identifies novel N′-(1-phenylethylidene)-benzohydrazides as potent, specific, and reversible LSD1 inhibitors
    • V. Sorna, E.R. Theisen, B. Stephens, S.L. Warner, D.J. Bearss, H. Vankayalapati, et al., High-throughput virtual screening identifies novel N′-(1-phenylethylidene)-benzohydrazides as potent, specific, and reversible LSD1 inhibitors, J. Med. Chem. 56 (2013) 9496-9508, http://dx.doi.org/10.1021/jm400870h.
    • (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
  • 34
    • 84906836964 scopus 로고    scopus 로고
    • Cyclopropylamines as Lsd1 Inhibitors
    • WO accessed 26.09.14
    • N. Johnson, J. Kasparec, W. Miller, M. Rouse, D. Suarez, X. Tian, 2012, Cyclopropylamines as Lsd1 Inhibitors, WO/2012/135113, http://patentscope.wipo.int/search/en/detail.jsf?docId=WO2012135113&recNum=66&docAn= US2012030552&queryString=EN-ALL:nmr%20AND%20PA:glaxosmithkline&maxRec=557 (accessed 26.09.14).
    • (2012)
    • Johnson, N.1    Kasparec, J.2    Miller, W.3    Rouse, M.4    Suarez, D.5    Tian, X.6
  • 35
    • 84906837990 scopus 로고    scopus 로고
    • (Hetero)aryl Cyclopropylamine Compounds as Lsd1 Inhibitors
    • WO accessed 26.09.14
    • A. Ortega Muñoz, M.C.T. Fyfe, M. Martinell Pedemonte, M. de los Á. Estiarte Martínez, N. Valls Vidal, G. Kurz, et al., 2012, (Hetero)aryl Cyclopropylamine Compounds as Lsd1 Inhibitors, WO/2013/057320, http://patentscope.wipo.int/search/en/detail.jsf?docId=WO2013057320 &recNum=2&docAn=EP2012070898 &queryString=&maxRec=17259 (accessed 26.09.14).
    • (2012)
    • Ortega Muñoz, A.1    Fyfe, M.C.T.2    Martinell Pedemonte, M.3    De Los Á Estiarte Martínez, M.4    Valls Vidal, N.5    Kurz, G.6
  • 37
    • 34147173308 scopus 로고    scopus 로고
    • trans-2-Phenylcyclopropylamine is a mechanism-based Inactivator of the histone demethylase LSD1
    • D.M.Z. Schmidt, D.G. McCafferty, trans-2-Phenylcyclopropylamine is a mechanism-based Inactivator of the histone demethylase LSD1, Biochem. Mosc. 46 (2007) 4408-4416, http://dx.doi.org/10.1021/bi0618621.
    • (2007) Biochem. Mosc. , vol.46 , pp. 4408-4416
    • Schmidt, D.M.Z.1    McCafferty, D.G.2
  • 38
    • 77955404853 scopus 로고    scopus 로고
    • Stereocontrolled synthesis of quaternary cyclopropyl esters
    • C.D. Bray, F. Minicone, Stereocontrolled synthesis of quaternary cyclopropyl esters, Chem. Commun. 46 (2010) 5867-5869, http://dx.doi.org/10.1039/C0CC01333A.
    • (2010) Chem. Commun. , vol.46 , pp. 5867-5869
    • Bray, C.D.1    Minicone, F.2
  • 39
    • 61349194588 scopus 로고    scopus 로고
    • Novel N-substituted 2-phenyl-1-sulfonylamino-cyclopropane carboxylates as selective ADAMTS-5 (aggrecanase-2) inhibitors
    • M. Shiozaki, K. Maeda, T. Miura, Y. Ogoshi, J. Haas, A.M. Fryer, et al., Novel N-substituted 2-phenyl-1-sulfonylamino-cyclopropane carboxylates as selective ADAMTS-5 (aggrecanase-2) inhibitors, Bioorg. Med. Chem. Lett. 19 (2009) 1575-1580, http://dx.doi.org/10.1016/j.bmcl.2009.02.024.
    • (2009) Bioorg. Med. Chem. Lett. , vol.19 , pp. 1575-1580
    • Shiozaki, M.1    Maeda, K.2    Miura, T.3    Ogoshi, Y.4    Haas, J.5    Fryer, A.M.6
  • 43
    • 37549022689 scopus 로고    scopus 로고
    • Crystal structure of histone demethylase LSD1 and tranylcypromine at 2.25 A
    • S. Mimasu, T. Sengoku, S. Fukuzawa, T. Umehara, S. Yokoyama, Crystal structure of histone demethylase LSD1 and tranylcypromine at 2.25 A, Biochem. Biophys. Res. Commun. 366 (2008) 15-22, http://dx.doi.org/10.1016/j.bbrc.2007.11.066.
    • (2008) Biochem. Biophys. Res. Commun. , vol.366 , pp. 15-22
    • Mimasu, S.1    Sengoku, T.2    Fukuzawa, S.3    Umehara, T.4    Yokoyama, S.5
  • 45
    • 84863098116 scopus 로고    scopus 로고
    • Schrödinger, LLC, New York, NY
    • Prime, version 3.0, Schrödinger, LLC, New York, NY, 2011.
    • (2011) Prime, Version 3.0
  • 46
    • 77956064328 scopus 로고    scopus 로고
    • Schrödinger, LLC, New York, NY
    • Protein Preparation Wizard, Schrödinger, LLC, New York, NY, 2011.
    • (2011) Protein Preparation Wizard
  • 47
    • 84899573359 scopus 로고    scopus 로고
    • Schrödinger, LLC, New York, NY
    • LigPrep, version 2.8, Schrödinger, LLC, New York, NY, 2013.
    • (2013) LigPrep, Version 2.8
  • 48
    • 84916892271 scopus 로고    scopus 로고
    • Schrödinger, LLC, New York, NY
    • Jaguar, version 8.2, Schrödinger, LLC, New York, NY, 2013.
    • (2013) Jaguar, Version 8.2
  • 49
    • 0038661201 scopus 로고    scopus 로고
    • Conceptual density functional theory
    • P. Geerlings, F. De Proft, W. Langenaeker, Conceptual density functional theory, Chem. Rev. 103 (2003) 1793-1874, http://dx.doi.org/10.1021/cr990029p.
    • (2003) Chem. Rev. , vol.103 , pp. 1793-1874
    • Geerlings, P.1    De Proft, F.2    Langenaeker, W.3
  • 50
    • 0030180875 scopus 로고    scopus 로고
    • New model for calculation of solvation free energies: Correction of selfconsistent reaction field continuum dielectric theory for short-range hydrogen-bonding effects
    • B. Marten, K. Kim, C. Cortis, R.A. Friesner, R.B. Murphy, M.N. Ringnalda, et al., New model for calculation of solvation free energies: correction of selfconsistent reaction field continuum dielectric theory for short-range hydrogen-bonding effects, J. Phys. Chem. 100 (1996) 11775-11788, http://dx.doi.org/10.1021/jp953087x. dx.doi.org/10.1021/jp953087x.
    • (1996) J. Phys. Chem. , vol.100 , pp. 11775-11788
    • Marten, B.1    Kim, K.2    Cortis, C.3    Friesner, R.A.4    Murphy, R.B.5    Ringnalda, M.N.6


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