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Volumn 10, Issue 10, 2015, Pages

Mycobacterium tuberculosis IMPDH in complexes with substrates, products and antitubercular compounds

Author keywords

[No Author keywords available]

Indexed keywords

BENZIMIDAZOLE DERIVATIVE; BENZOXAZOLE DERIVATIVE; GUANINE NUCLEOTIDE; INOSINATE DEHYDROGENASE; INOSINATE DEHYDROGENASE INHIBITOR; ISONIAZID; NICOTINAMIDE ADENINE DINUCLEOTIDE; OXIDOREDUCTASE; PHTHALAZINONE; TUBERCULOSTATIC AGENT; UNCLASSIFIED DRUG; UREA DERIVATIVE; ENZYME INHIBITOR; PROTEIN BINDING;

EID: 84947901377     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0138976     Document Type: Article
Times cited : (35)

References (55)
  • 2
    • 84861116576 scopus 로고    scopus 로고
    • The chemotherapy of tuberculosis: Past, present and future
    • PMID: 22613684
    • Mitchison D, Davies G (2012) The chemotherapy of tuberculosis: past, present and future. Int J Tuberc Lung Dis 16: 724-732. doi: 10.5588/ijtld.12.0083 PMID: 22613684
    • (2012) Int J Tuberc Lung Dis , vol.16 , pp. 724-732
    • Mitchison, D.1    Davies, G.2
  • 3
    • 70449705831 scopus 로고    scopus 로고
    • The spectrum of latent tuberculosis: Rethinking the biology and intervention strategies
    • PMID: 19855401
    • Barry CE, Boshoff HI, Dartois V, Dick T, Ehrt S, Flynn J, et al. (2009) The spectrum of latent tuberculosis: rethinking the biology and intervention strategies. Nat Rev Microbiol 7: 845-855. doi: 10.1038/nrmicro2236 PMID: 19855401
    • (2009) Nat Rev Microbiol , vol.7 , pp. 845-855
    • Barry, C.E.1    Boshoff, H.I.2    Dartois, V.3    Dick, T.4    Ehrt, S.5    Flynn, J.6
  • 4
    • 84871859996 scopus 로고    scopus 로고
    • Dynamic Persistence of Antibiotic-Stressed Mycobacteria
    • PMID: 23288538
    • Wakamoto Y, Dhar N, Chait R, Schneider K, Signorino-Gelo Fß, Leibler S, et al. (2013) Dynamic Persistence of Antibiotic-Stressed Mycobacteria. Science 339: 91-95. doi: 10.1126/science.1229858 PMID: 23288538
    • (2013) Science , vol.339 , pp. 91-95
    • Wakamoto, Y.1    Dhar, N.2    Chait, R.3    Schneider, K.4    Signorino-Gelo, F.ß.5    Leibler, S.6
  • 5
    • 33847704942 scopus 로고    scopus 로고
    • Challenges in tuberculosis drug research and development
    • PMID: 17342142
    • Ginsberg AM, Spigelman M (2007) Challenges in tuberculosis drug research and development. Nat Med 13: 290-294. PMID: 17342142
    • (2007) Nat Med , vol.13 , pp. 290-294
    • Ginsberg, A.M.1    Spigelman, M.2
  • 6
    • 77952542701 scopus 로고    scopus 로고
    • Multidrug-resistant and extensively drug-resistant tuberculosis: A threat to global control of tuberculosis
    • Gandhi NR, Nunn P, Dheda K, Schaaf HS, Zignol M, van Soolingen D, et al. (2010) Multidrug-resistant and extensively drug-resistant tuberculosis: a threat to global control of tuberculosis. The Lancet 375: 1830-1843.
    • (2010) The Lancet , vol.375 , pp. 1830-1843
    • Gandhi, N.R.1    Nunn, P.2    Dheda, K.3    Schaaf, H.S.4    Zignol, M.5    Van Soolingen, D.6
  • 7
    • 77951796544 scopus 로고    scopus 로고
    • Extensively Drug-Resistant Tuberculosis: "There must be some kind of way out of here"
    • PMID: 20397948
    • Cegielski JP (2010) Extensively Drug-Resistant Tuberculosis: "There must be some kind of way out of here". Clin Infect Dis 50: S195-S200. doi: 10.1086/651491 PMID: 20397948
    • (2010) Clin Infect Dis , vol.50 , pp. S195-S200
    • Cegielski, J.P.1
  • 8
    • 84871927537 scopus 로고    scopus 로고
    • Para-Aminosalicylic Acid Acts as an Alternative Substrate of Folate Metabolism in Mycobacterium tuberculosis
    • PMID: 23118010
    • Chakraborty S, Gruber T, Barry CE, Boshoff HI, Rhee KY (2013) Para-Aminosalicylic Acid Acts as an Alternative Substrate of Folate Metabolism in Mycobacterium tuberculosis. Science 339: 88-91. doi: 10.1126/science.1228980 PMID: 23118010
    • (2013) Science , vol.339 , pp. 88-91
    • Chakraborty, S.1    Gruber, T.2    Barry, C.E.3    Boshoff, H.I.4    Rhee, K.Y.5
  • 9
    • 19944429772 scopus 로고    scopus 로고
    • A Diarylquinoline Drug Active on the ATP Synthase of Mycobacterium tuberculosis
    • PMID: 15591164
    • Andries K, Verhasselt P, Guillemont J, Göhlmann HWH, Neefs J-M, Winkler H, et al. (2005) A Diarylquinoline Drug Active on the ATP Synthase of Mycobacterium tuberculosis. Science 307: 223-227. PMID: 15591164
    • (2005) Science , vol.307 , pp. 223-227
    • Andries, K.1    Verhasselt, P.2    Guillemont, J.3    Göhlmann, H.W.H.4    Neefs, J.-M.5    Winkler, H.6
  • 10
    • 79957938394 scopus 로고    scopus 로고
    • The Antibiotic Potential of Prokaryotic IMP Dehydrogenase Inhibitors
    • PMID: 21517780
    • Hedstrom L, Liechti G, Goldberg JB, Gollapalli DR (2011) The Antibiotic Potential of Prokaryotic IMP Dehydrogenase Inhibitors. Curr Med Chem 18: 1909-1918. PMID: 21517780
    • (2011) Curr Med Chem , vol.18 , pp. 1909-1918
    • Hedstrom, L.1    Liechti, G.2    Goldberg, J.B.3    Gollapalli, D.R.4
  • 11
    • 84956665250 scopus 로고    scopus 로고
    • Nucleotide Metabolism and DNA Replication
    • PMID: 26104350
    • Warner DF, Evans JC, Mizrahi V (2014) Nucleotide Metabolism and DNA Replication. Microbiology Spectrum 2. doi: 10.1128/microbiolspec.MGM2-0001-2013 PMID: 26104350
    • (2014) Microbiology Spectrum , vol.2
    • Warner, D.F.1    Evans, J.C.2    Mizrahi, V.3
  • 12
    • 57349119221 scopus 로고    scopus 로고
    • Structural Biology of the Purine Biosynthetic Pathway
    • PMID: 18712276
    • Zhang Y, Morar M, Ealick SE (2008) Structural Biology of the Purine Biosynthetic Pathway. Cellular and molecular life sciences: CMLS 65: 3699-3724. doi: 10.1007/s00018-008-8295-8 PMID: 18712276
    • (2008) Cellular and Molecular Life Sciences: CMLS , vol.65 , pp. 3699-3724
    • Zhang, Y.1    Morar, M.2    Ealick, S.E.3
  • 13
    • 0032508046 scopus 로고    scopus 로고
    • Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence
    • PMID: 9634230
    • Cole ST, Brosch R, Parkhill J, Garnier T, Churcher C, Harris D, et al. (1998) Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 393: 537-544. PMID: 9634230
    • (1998) Nature , vol.393 , pp. 537-544
    • Cole, S.T.1    Brosch, R.2    Parkhill, J.3    Garnier, T.4    Churcher, C.5    Harris, D.6
  • 14
    • 78650744683 scopus 로고    scopus 로고
    • Identification of novel diphenyl urea inhibitors of Mt-GuaB2 active against Mycobacterium tuberculosis
    • PMID: 21081761
    • Usha V, Gurcha SS, Lovering AL, Lloyd AJ, Papaemmanouil A, Reynolds RC, et al. (2011) Identification of novel diphenyl urea inhibitors of Mt-GuaB2 active against Mycobacterium tuberculosis. Microbiology 157: 290-299. doi: 10.1099/mic.0.042549-0 PMID: 21081761
    • (2011) Microbiology , vol.157 , pp. 290-299
    • Usha, V.1    Gurcha, S.S.2    Lovering, A.L.3    Lloyd, A.J.4    Papaemmanouil, A.5    Reynolds, R.C.6
  • 15
    • 0345701347 scopus 로고    scopus 로고
    • Genes required for mycobacterial growth defined by high density mutagenesis
    • PMID: 12657046
    • Sassetti CM, Boyd DH, Rubin EJ (2003) Genes required for mycobacterial growth defined by high density mutagenesis. Mol Microbiol 48: 77-84. PMID: 12657046
    • (2003) Mol Microbiol , vol.48 , pp. 77-84
    • Sassetti, C.M.1    Boyd, D.H.2    Rubin, E.J.3
  • 16
    • 77953800819 scopus 로고    scopus 로고
    • Triazole-Linked Inhibitors of Inosine Monophosphate Dehydrogenase from Human and Mycobacterium tuberculosis
    • PMID: 20491506
    • Chen L, Wilson DJ, Xu Y, Aldrich CC, Felczak K, Sham YY, et al. (2010) Triazole-Linked Inhibitors of Inosine Monophosphate Dehydrogenase from Human and Mycobacterium tuberculosis. J Med Chem 53: 4768-4778. doi: 10.1021/jm100424m PMID: 20491506
    • (2010) J Med Chem , vol.53 , pp. 4768-4778
    • Chen, L.1    Wilson, D.J.2    Xu, Y.3    Aldrich, C.C.4    Felczak, K.5    Sham, Y.Y.6
  • 17
    • 84859075290 scopus 로고    scopus 로고
    • Identification of Novel Mt-Guab2 Inhibitor Series Active against M. tuberculosis
    • 33881-33812. PMID: 22479467
    • Usha V, Hobrath JV, Gurcha SS, Reynolds RC, Besra GS (2012) Identification of Novel Mt-Guab2 Inhibitor Series Active against M. tuberculosis. PLoS ONE 7: e33886 (33881-33812). doi: 10.1371/journal.pone.0033886 PMID: 22479467
    • (2012) PLoS ONE , vol.7
    • Usha, V.1    Hobrath, J.V.2    Gurcha, S.S.3    Reynolds, R.C.4    Besra, G.S.5
  • 18
    • 67650649489 scopus 로고    scopus 로고
    • IMP Dehydrogenase: Structure, Mechanism, and Inhibition
    • PMID: 19480389
    • Hedstrom L (2009) IMP Dehydrogenase: Structure, Mechanism, and Inhibition. Chem Rev 109: 2903-2928. doi: 10.1021/cr900021w PMID: 19480389
    • (2009) Chem Rev , vol.109 , pp. 2903-2928
    • Hedstrom, L.1
  • 19
    • 34447642328 scopus 로고    scopus 로고
    • Recent developments of IMP dehydrogenase inhibitors for the treatment of cancer
    • Chen L, Pankiewicz Krzysztof W (2007) Recent developments of IMP dehydrogenase inhibitors for the treatment of cancer. Curr Opin Drug Discovery Dev 10: 403-412.
    • (2007) Curr Opin Drug Discovery Dev , vol.10 , pp. 403-412
    • Chen, L.1    Pankiewicz Krzysztof, W.2
  • 20
    • 0033616611 scopus 로고    scopus 로고
    • Crystal structure of human type II inosine monophosphate dehydrogenase: Implications for ligand binding and drug design
    • PMID: 10097070
    • Colby TD, Vanderveen K, Strickler MD, Markham GD, Goldstein BM (1999) Crystal structure of human type II inosine monophosphate dehydrogenase: implications for ligand binding and drug design. Proc Natl Acad Sci U S A 96: 3531-3536. PMID: 10097070
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 3531-3536
    • Colby, T.D.1    Vanderveen, K.2    Strickler, M.D.3    Markham, G.D.4    Goldstein, B.M.5
  • 21
    • 84923791158 scopus 로고    scopus 로고
    • A novel cofactor binding mode in bacterial IMP dehydrogenases explains inhibitor selectivity
    • PMID: 25572472
    • Makowska-Grzyska M, Kim Y, Maltseva N, Osipiuk J, Gu M, Zhang M, et al. (2015) A novel cofactor binding mode in bacterial IMP dehydrogenases explains inhibitor selectivity. J Biol Chem 290: 5893-5911. doi: 10.1074/jbc.M114.619767 PMID: 25572472
    • (2015) J Biol Chem , vol.290 , pp. 5893-5911
    • Makowska-Grzyska, M.1    Kim, Y.2    Maltseva, N.3    Osipiuk, J.4    Gu, M.5    Zhang, M.6
  • 22
    • 38349082511 scopus 로고    scopus 로고
    • Targeting a Prokaryotic Protein in a Eukaryotic Pathogen: Identification of Lead Compounds against Cryptosporidiosis
    • PMID: 18215774
    • Umejiego NN, Gollapalli D, Sharling L, Volftsun A, Lu J, Benjamin NN, et al. (2008) Targeting a Prokaryotic Protein in a Eukaryotic Pathogen: Identification of Lead Compounds against Cryptosporidiosis. Chem Biol 15: 70-77. doi: 10.1016/j.chembiol.2007.12.010 PMID: 18215774
    • (2008) Chem Biol , vol.15 , pp. 70-77
    • Umejiego, N.N.1    Gollapalli, D.2    Sharling, L.3    Volftsun, A.4    Lu, J.5    Benjamin, N.N.6
  • 23
    • 78149262280 scopus 로고    scopus 로고
    • A Screening Pipeline for Antiparasitic Agents Targeting Cryptosporidium Inosine Monophosphate Dehydrogenase
    • 791-712. PMID: 20706578
    • Sharling L, Liu X, Gollapalli DR, Maurya SK, Hedstrom L, Striepen B (2010) A Screening Pipeline for Antiparasitic Agents Targeting Cryptosporidium Inosine Monophosphate Dehydrogenase. PLoS Negl Trop Dis 4: e794 (791-712). doi: 10.1371/journal.pntd.0000794 PMID: 20706578
    • (2010) PLoS Negl Trop Dis , vol.4 , pp. e794
    • Sharling, L.1    Liu, X.2    Gollapalli, D.R.3    Maurya, S.K.4    Hedstrom, L.5    Striepen, B.6
  • 24
    • 68549104260 scopus 로고    scopus 로고
    • Triazole Inhibitors of Cryptosporidium parvum Inosine 5′-Monophosphate Dehydrogenase
    • PMID: 19624136
    • Maurya SK, Gollapalli DR, Kirubakaran S, Zhang M, Johnson CR, Benjamin NN, et al. (2009) Triazole Inhibitors of Cryptosporidium parvum Inosine 5′-Monophosphate Dehydrogenase. J Med Chem 52: 4623-4630. doi: 10.1021/jm900410u PMID: 19624136
    • (2009) J Med Chem , vol.52 , pp. 4623-4630
    • Maurya, S.K.1    Gollapalli, D.R.2    Kirubakaran, S.3    Zhang, M.4    Johnson, C.R.5    Benjamin, N.N.6
  • 25
    • 84862810288 scopus 로고    scopus 로고
    • Structure-activity relationship study of selective benzimidazole-based inhibitors of Cryptosporidium parvum IMPDH
    • PMID: 22310229
    • Kirubakaran S, Gorla SK, Sharling L, Zhang M, Liu X, Ray SS, et al. (2012) Structure-activity relationship study of selective benzimidazole-based inhibitors of Cryptosporidium parvum IMPDH. Bioorg Med Chem Lett 22: 1985-1988. doi: 10.1016/j.bmcl.2012.01.029 PMID: 22310229
    • (2012) Bioorg Med Chem Lett , vol.22 , pp. 1985-1988
    • Kirubakaran, S.1    Gorla, S.K.2    Sharling, L.3    Zhang, M.4    Liu, X.5    Ray, S.S.6
  • 26
    • 84866324636 scopus 로고    scopus 로고
    • Selective and Potent Urea Inhibitors of Cryptosporidium parvum Inosine 5′-Monophosphate Dehydrogenase
    • PMID: 22950983
    • Gorla SK, Kavitha M, Zhang M, Liu X, Sharling L, Gollapalli DR, et al. (2012) Selective and Potent Urea Inhibitors of Cryptosporidium parvum Inosine 5′-Monophosphate Dehydrogenase. J Med Chem 55: 7759-7771. doi: 10.1021/jm3007917 PMID: 22950983
    • (2012) J Med Chem , vol.55 , pp. 7759-7771
    • Gorla, S.K.1    Kavitha, M.2    Zhang, M.3    Liu, X.4    Sharling, L.5    Gollapalli, D.R.6
  • 27
    • 84878093192 scopus 로고    scopus 로고
    • Optimization of Benzoxazole- Based Inhibitors of Cryptosporidium parvum Inosine 5′-Monophosphate Dehydrogenase
    • PMID: 23668331
    • Gorla SK, Kavitha M, Zhang M, Chin JEW, Liu X, Striepen B, et al. (2013) Optimization of Benzoxazole- Based Inhibitors of Cryptosporidium parvum Inosine 5′-Monophosphate Dehydrogenase. J Med Chem 56: 4028-4043. doi: 10.1021/jm400241j PMID: 23668331
    • (2013) J Med Chem , vol.56 , pp. 4028-4043
    • Gorla, S.K.1    Kavitha, M.2    Zhang, M.3    Chin, J.E.W.4    Liu, X.5    Striepen, B.6
  • 28
    • 84872979660 scopus 로고    scopus 로고
    • Phthalazinone inhibitors of inosine-5′-monophosphate dehydrogenase from Cryptosporidium parvum
    • PMID: 23324406
    • Johnson CR, Gorla SK, Kavitha M, Zhang M, Liu X, Striepen B, et al. (2013) Phthalazinone inhibitors of inosine-5′-monophosphate dehydrogenase from Cryptosporidium parvum. Bioorg Med Chem Lett 23: 1004-1007. doi: 10.1016/j.bmcl.2012.12.037 PMID: 23324406
    • (2013) Bioorg Med Chem Lett , vol.23 , pp. 1004-1007
    • Johnson, C.R.1    Gorla, S.K.2    Kavitha, M.3    Zhang, M.4    Liu, X.5    Striepen, B.6
  • 29
    • 84920129978 scopus 로고    scopus 로고
    • Synthesis, in Vitro Evaluation and Cocrystal Structure of 4-Oxo-[1]benzopyrano[4,3-c]pyrazole Cryptosporidium parvum Inosine 5′-Monophosphate Dehydrogenase (CpIMPDH) Inhibitors
    • PMID: 25474504
    • Sun Z, Khan J, Makowska-Grzyska M, Zhang M, Cho JH, Suebsuwong C, et al. (2014) Synthesis, in Vitro Evaluation and Cocrystal Structure of 4-Oxo-[1]benzopyrano[4,3-c]pyrazole Cryptosporidium parvum Inosine 5′-Monophosphate Dehydrogenase (CpIMPDH) Inhibitors. J Med Chem 57: 10544-10550. doi: 10.1021/jm501527z PMID: 25474504
    • (2014) J Med Chem , vol.57 , pp. 10544-10550
    • Sun, Z.1    Khan, J.2    Makowska-Grzyska, M.3    Zhang, M.4    Cho, J.H.5    Suebsuwong, C.6
  • 30
    • 77950442655 scopus 로고    scopus 로고
    • The Structural Basis of Cryptosporidium-Specific IMP Dehydrogenase Inhibitor Selectivity
    • PMID: 20052976
    • MacPherson IS, Kirubakaran S, Gorla SK, Riera TV, D'Aquino JA, Zhang M, et al. (2010) The Structural Basis of Cryptosporidium-Specific IMP Dehydrogenase Inhibitor Selectivity. J Am Chem Soc 132: 1230-1231. doi: 10.1021/ja909947a PMID: 20052976
    • (2010) J Am Chem Soc , vol.132 , pp. 1230-1231
    • MacPherson, I.S.1    Kirubakaran, S.2    Gorla, S.K.3    Riera, T.V.4    D'Aquino, J.A.5    Zhang, M.6
  • 31
    • 78049383245 scopus 로고    scopus 로고
    • Structural Determinants of Inhibitor Selectivity in Prokaryotic IMP Dehydrogenases
    • PMID: 21035731
    • Gollapalli DR, MacPherson IS, Liechti G, Gorla SK, Goldberg JB, Hedstrom L (2010) Structural Determinants of Inhibitor Selectivity in Prokaryotic IMP Dehydrogenases. Chem Biol 17: 1084-1091. doi: 10.1016/j.chembiol.2010.07.014 PMID: 21035731
    • (2010) Chem Biol , vol.17 , pp. 1084-1091
    • Gollapalli, D.R.1    MacPherson, I.S.2    Liechti, G.3    Gorla, S.K.4    Goldberg, J.B.5    Hedstrom, L.6
  • 32
    • 84864673403 scopus 로고    scopus 로고
    • Bacillus anthracis Inosine 5′-Monophosphate Dehydrogenase in Action: The First Bacterial Series of Structures of Phosphate Ion-, Substrate-, and Product-Bound Complexes
    • PMID: 22788966
    • Makowska-Grzyska M, Kim Y, Wu R, Wilton R, Gollapalli DR, Wang XK, et al. (2012) Bacillus anthracis Inosine 5′-Monophosphate Dehydrogenase in Action: The First Bacterial Series of Structures of Phosphate Ion-, Substrate-, and Product-Bound Complexes. Biochemistry 51: 6148-6163. PMID: 22788966
    • (2012) Biochemistry , vol.51 , pp. 6148-6163
    • Makowska-Grzyska, M.1    Kim, Y.2    Wu, R.3    Wilton, R.4    Gollapalli, D.R.5    Wang, X.K.6
  • 33
    • 0027717956 scopus 로고
    • Characterization of Human Type I and Type II IMP Dehydrogenase
    • PMID: 7903306
    • Carr SF, Papp E, Wu J, Natsumeda Y (1993) Characterization of Human Type I and Type II IMP Dehydrogenase. J Biol Chem 268: 27286-27290. PMID: 7903306
    • (1993) J Biol Chem , vol.268 , pp. 27286-27290
    • Carr, S.F.1    Papp, E.2    Wu, J.3    Natsumeda, Y.4
  • 34
    • 0029050393 scopus 로고
    • Recombinant Human Inosine Monophosphate Dehydrogenase Type I and Type II Proteins
    • PMID: 7763314
    • Hager PW, Collart FR, Huberman E, Mitchell BS (1995) Recombinant Human Inosine Monophosphate Dehydrogenase Type I and Type II Proteins. Biochem Pharmacol 49: 1323-1329. PMID: 7763314
    • (1995) Biochem Pharmacol , vol.49 , pp. 1323-1329
    • Hager, P.W.1    Collart, F.R.2    Huberman, E.3    Mitchell, B.S.4
  • 35
    • 23944520368 scopus 로고    scopus 로고
    • Autosomal dominant retinitis pigmentosa mutations in inosine 5′-monophosphate dehydrogenase type I disrupt nucleic acid binding
    • PMID: 15882147
    • Mortimer SE, Hedstrom L (2005) Autosomal dominant retinitis pigmentosa mutations in inosine 5′-monophosphate dehydrogenase type I disrupt nucleic acid binding. Biochem J 390: 41-47. PMID: 15882147
    • (2005) Biochem J , vol.390 , pp. 41-47
    • Mortimer, S.E.1    Hedstrom, L.2
  • 36
    • 0030849948 scopus 로고    scopus 로고
    • Kinetic Mechanism of Human Inosine 5′-Monophosphate Dehydrogenase Type II: Random Addition of Substrates and Ordered Release of Products
    • PMID: 9214292
    • Wang W, Hedstrom L (1997) Kinetic Mechanism of Human Inosine 5′-Monophosphate Dehydrogenase Type II: Random Addition of Substrates and Ordered Release of Products. Biochemistry 36: 8479-8483. PMID: 9214292
    • (1997) Biochemistry , vol.36 , pp. 8479-8483
    • Wang, W.1    Hedstrom, L.2
  • 37
    • 84906241587 scopus 로고    scopus 로고
    • Repurposing Cryptosporidium inosine 5′-monophosphate dehydrogenase inhibitors as potential antibacterial agents
    • PMID: 25147601
    • Mandapati K, Gorla SK, House AL, McKenney ES, Rao SN, Gollapalli DR, et al. (2014) Repurposing Cryptosporidium inosine 5′-monophosphate dehydrogenase inhibitors as potential antibacterial agents. ACS Med Chem Lett 5: 846-850. doi: 10.1021/ml500203p PMID: 25147601
    • (2014) ACS Med Chem Lett , vol.5 , pp. 846-850
    • Mandapati, K.1    Gorla, S.K.2    House, A.L.3    McKenney, E.S.4    Rao, S.N.5    Gollapalli, D.R.6
  • 38
    • 84896873219 scopus 로고    scopus 로고
    • Validation of IMP dehydrogenase inhibitors in a mouse model of cryptosporidiosis
    • PMID: 24366728
    • Gorla SK, McNair NN, Yang G, Gao S, Hu M, Jala VR, et al. (2014) Validation of IMP dehydrogenase inhibitors in a mouse model of cryptosporidiosis. Antimicrob Agents Chemother 58: 1603-1614. doi: 10.1128/AAC.02075-13 PMID: 24366728
    • (2014) Antimicrob Agents Chemother , vol.58 , pp. 1603-1614
    • Gorla, S.K.1    McNair, N.N.2    Yang, G.3    Gao, S.4    Hu, M.5    Jala, V.R.6
  • 39
    • 33746911968 scopus 로고    scopus 로고
    • Novel Methylenephosphophosphonate Analogues of Mycophenolic Adenine Dinucleotide. Inhibition of Inosine Monophosphate Dehydrogenase
    • PMID: 16884314
    • Rejman D, Olesiak M, Chen L, Patterson SE, Wilson D, Jayaram HN, et al. (2006) Novel Methylenephosphophosphonate Analogues of Mycophenolic Adenine Dinucleotide. Inhibition of Inosine Monophosphate Dehydrogenase. J Med Chem 49: 5018-5022. PMID: 16884314
    • (2006) J Med Chem , vol.49 , pp. 5018-5022
    • Rejman, D.1    Olesiak, M.2    Chen, L.3    Patterson, S.E.4    Wilson, D.5    Jayaram, H.N.6
  • 40
    • 0032510138 scopus 로고    scopus 로고
    • Synthesis of a Methylenebis(phosphonate) Analogue of Mycophenolic Adenine Dinucleotide: A Glucuronidation-Resistant MAD Analogue of NAD
    • PMID: 9484510
    • Lesiak K, Watanabe KA, Majumdar A, Powell J, Seidman M, Vanderveen K, et al. (1998) Synthesis of a Methylenebis(phosphonate) Analogue of Mycophenolic Adenine Dinucleotide: A Glucuronidation-Resistant MAD Analogue of NAD. J Med Chem 41: 618-622. PMID: 9484510
    • (1998) J Med Chem , vol.41 , pp. 618-622
    • Lesiak, K.1    Watanabe, K.A.2    Majumdar, A.3    Powell, J.4    Seidman, M.5    Vanderveen, K.6
  • 41
    • 0029899127 scopus 로고    scopus 로고
    • Structure and mechanism of inosine monophosphate dehydrogenase in complex with the immunosuppressant mycophenolic acid
    • PMID: 8681386
    • Sintchak MD, Fleming MA, Futer O, Raybuck SA, Chambers SP, Caron PR, et al. (1996) Structure and mechanism of inosine monophosphate dehydrogenase in complex with the immunosuppressant mycophenolic acid. Cell 85: 921-930. PMID: 8681386
    • (1996) Cell , vol.85 , pp. 921-930
    • Sintchak, M.D.1    Fleming, M.A.2    Futer, O.3    Raybuck, S.A.4    Chambers, S.P.5    Caron, P.R.6
  • 42
    • 0347297575 scopus 로고    scopus 로고
    • Crystal structure of Tritrichomonas foetus inosine monophosphate dehydrogenase in complex with the inhibitor ribavirin monophosphate reveals a catalysis-dependent ion-binding site
    • PMID: 12235158
    • Prosise GL, Wu JZ, Luecke H (2002) Crystal structure of Tritrichomonas foetus inosine monophosphate dehydrogenase in complex with the inhibitor ribavirin monophosphate reveals a catalysis-dependent ion-binding site. J Biol Chem 277: 50654-50659. PMID: 12235158
    • (2002) J Biol Chem , vol.277 , pp. 50654-50659
    • Prosise, G.L.1    Wu, J.Z.2    Luecke, H.3
  • 43
    • 79959326215 scopus 로고    scopus 로고
    • Linking Distinct Conformations of Nicotinamide Adenine Dinucleotide with Protein Fold/Function
    • PMID: 21612228
    • Kuppuraj G, Sargsyan K, Hua Y-H, Merrill AR, Lim C (2011) Linking Distinct Conformations of Nicotinamide Adenine Dinucleotide with Protein Fold/Function. J Phys Chem B 115: 7932-7939. doi: 10.1021/jp1118663 PMID: 21612228
    • (2011) J Phys Chem B , vol.115 , pp. 7932-7939
    • Kuppuraj, G.1    Sargsyan, K.2    Hua, Y.-H.3    Merrill, A.R.4    Lim, C.5
  • 44
    • 0037435776 scopus 로고    scopus 로고
    • Crystal structures of Tritrichomonas foetus inosine monophosphate dehydrogenase in complex with substrate, cofactor and analogs: A structural basis for the random-in ordered-out kinetic mechanism
    • PMID: 12559919
    • Prosise GL, Luecke H (2003) Crystal structures of Tritrichomonas foetus inosine monophosphate dehydrogenase in complex with substrate, cofactor and analogs: a structural basis for the random-in ordered-out kinetic mechanism. J Mol Biol 326: 517-527. PMID: 12559919
    • (2003) J Mol Biol , vol.326 , pp. 517-527
    • Prosise, G.L.1    Luecke, H.2
  • 45
    • 0023645821 scopus 로고
    • A simple method for the rapid determination of the stereospecificity of NAD-dependent dehydrogenases applied to mammalian IMP dehydrogenase and bacterial NADH peroxidase
    • Cooney D, Hamel E, Cohen M, Kang GJ, Dalal M, Marquez V (1987) A simple method for the rapid determination of the stereospecificity of NAD-dependent dehydrogenases applied to mammalian IMP dehydrogenase and bacterial NADH peroxidase. Biochim Biophys Acta, Protein Struct Mol Enzymol 916: 89-93.
    • (1987) Biochim Biophys Acta, Protein Struct Mol Enzymol , vol.916 , pp. 89-93
    • Cooney, D.1    Hamel, E.2    Cohen, M.3    Kang, G.J.4    Dalal, M.5    Marquez, V.6
  • 46
    • 0031574463 scopus 로고    scopus 로고
    • Probing the mechanism of inosine monophosphate dehydrogenase with kinetic isotope effects and NMR determination of the hydride transfer stereospecificity
    • PMID: 9434751
    • Xiang B, Markham GD (1997) Probing the mechanism of inosine monophosphate dehydrogenase with kinetic isotope effects and NMR determination of the hydride transfer stereospecificity. Arch Biochem Biophys 348: 378-382. PMID: 9434751
    • (1997) Arch Biochem Biophys , vol.348 , pp. 378-382
    • Xiang, B.1    Markham, G.D.2
  • 47
    • 67849128457 scopus 로고    scopus 로고
    • Halogen bonds as orthogonal molecular interactions to hydrogen bonds
    • PMID: 21378804
    • Voth AR, Khuu P, Oishi K, Ho PS (2009) Halogen bonds as orthogonal molecular interactions to hydrogen bonds. Nat Chem 1: 74-79. doi: 10.1038/nchem.112 PMID: 21378804
    • (2009) Nat Chem , vol.1 , pp. 74-79
    • Voth, A.R.1    Khuu, P.2    Oishi, K.3    Ho, P.S.4
  • 48
    • 77953631827 scopus 로고    scopus 로고
    • A Medicinal Chemist's Guide to Molecular Interactions
    • PMID: 20345171
    • Bissantz C, Kuhn B, Stahl M (2010) A Medicinal Chemist's Guide to Molecular Interactions. J Med Chem 53: 5061-5084. doi: 10.1021/jm100112j PMID: 20345171
    • (2010) J Med Chem , vol.53 , pp. 5061-5084
    • Bissantz, C.1    Kuhn, B.2    Stahl, M.3
  • 49
    • 0035094747 scopus 로고    scopus 로고
    • The Crystal Structure of an Asymmetric Complex of the Two Nucleotide Binding Components of Proton-Translocating Transhydrogenase
    • PMID: 11250201
    • Cotton NPJ, White SA, Peake SJ, McSweeney S, Jackson JB (2001) The Crystal Structure of an Asymmetric Complex of the Two Nucleotide Binding Components of Proton-Translocating Transhydrogenase. Structure 9: 165-176. PMID: 11250201
    • (2001) Structure , vol.9 , pp. 165-176
    • Cotton, N.P.J.1    White, S.A.2    Peake, S.J.3    McSweeney, S.4    Jackson, J.B.5
  • 50
    • 0029877040 scopus 로고    scopus 로고
    • Crystal Structures of the Oxidized and Reduced Forms of UDP-galactose 4-Epimerase Isolated from Escherichia coli
    • PMID: 8611559
    • Thoden JB, Frey PA, Holden HM (1996) Crystal Structures of the Oxidized and Reduced Forms of UDP-galactose 4-Epimerase Isolated from Escherichia coli. Biochemistry 35: 2557-2566. PMID: 8611559
    • (1996) Biochemistry , vol.35 , pp. 2557-2566
    • Thoden, J.B.1    Frey, P.A.2    Holden, H.M.3
  • 51
    • 0034947940 scopus 로고    scopus 로고
    • Integration of PCR Fragments at any Specific Site within Cloning Vectors without the Use of Restriction Enzymes and DNA Ligase
    • PMID: 11464525
    • Geiser M, Cèbe R, Drewello D, Schmitz R (2001) Integration of PCR Fragments at any Specific Site within Cloning Vectors without the Use of Restriction Enzymes and DNA Ligase Biotechniques 31: 88-92. PMID: 11464525
    • (2001) Biotechniques , vol.31 , pp. 88-92
    • Geiser, M.1    Cèbe, R.2    Drewello, D.3    Schmitz, R.4
  • 52
    • 80053639801 scopus 로고    scopus 로고
    • High-throughput protein purification and quality assessment for crystallization
    • PMID: 21907284
    • Kim Y, Babnigg G, Jedrzejczak R, Eschenfeldt WH, Li H, Maltseva N, et al. (2011) High-throughput protein purification and quality assessment for crystallization. Methods 55: 12-28. doi: 10.1016/j.ymeth.2011.07.010 PMID: 21907284
    • (2011) Methods , vol.55 , pp. 12-28
    • Kim, Y.1    Babnigg, G.2    Jedrzejczak, R.3    Eschenfeldt, W.H.4    Li, H.5    Maltseva, N.6
  • 53
    • 84867806558 scopus 로고    scopus 로고
    • Development of a Selective Activity-Based Probe for Adenylating Enzymes: Profiling MbtA Involved in Siderophore Biosynthesis from Mycobacterium tuberculosis
    • PMID: 22796950
    • Duckworth BP, Wilson DJ, Nelson KM, Boshoff HI, Barry CE, Aldrich CC (2012) Development of a Selective Activity-Based Probe for Adenylating Enzymes: Profiling MbtA Involved in Siderophore Biosynthesis from Mycobacterium tuberculosis. ACS Chem Biol 7: 1653-1658. doi: 10.1021/cb300112x PMID: 22796950
    • (2012) ACS Chem Biol , vol.7 , pp. 1653-1658
    • Duckworth, B.P.1    Wilson, D.J.2    Nelson, K.M.3    Boshoff, H.I.4    Barry, C.E.5    Aldrich, C.C.6
  • 54
    • 0024297354 scopus 로고
    • Multiple sequence alignment with hierarchical clustering
    • PMID: 2849754
    • Corpet F (1988) Multiple sequence alignment with hierarchical clustering. Nucleic Acids Res 16: 10881-10890. PMID: 2849754
    • (1988) Nucleic Acids Res , vol.16 , pp. 10881-10890
    • Corpet, F.1
  • 55
    • 84904790793 scopus 로고    scopus 로고
    • Deciphering key features in protein structures with the new ENDscript server
    • PMID: 24753421
    • Robert X, Gouet P (2014) Deciphering key features in protein structures with the new ENDscript server. Nucleic Acids Res 42: W320-W324. doi: 10.1093/nar/gku316 PMID: 24753421
    • (2014) Nucleic Acids Res , vol.42 , pp. W320-W324
    • Robert, X.1    Gouet, P.2


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