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Volumn 82, Issue 9, 2014, Pages 1869-1883

Identification of the bona fide DHDPS from a common plant pathogen

Author keywords

Allostery; Analytical ultracentrifugation; Crown gall disease; Dihydrodipicolinate synthase; Enzyme kinetics; Enzyme structure; Lysine biosynthesis; X ray crystallography

Indexed keywords

BACTERIAL ENZYME; DIHYDRODIPICOLINATE SYNTHASE; RECOMBINANT PROTEIN; SYNTHETASE; TETRAMER; UNCLASSIFIED DRUG; HYDROLYASE;

EID: 84906310372     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24539     Document Type: Article
Times cited : (15)

References (82)
  • 1
    • 38249040020 scopus 로고
    • The potential for biological control of crown gall disease on grapevines
    • Thomson JA. The potential for biological control of crown gall disease on grapevines. Trends Biotech 1986;4:219-224.
    • (1986) Trends Biotech , vol.4 , pp. 219-224
    • Thomson, J.A.1
  • 2
    • 1842791637 scopus 로고
    • The host range of crown gall
    • De Cleene M, De Ley J. The host range of crown gall. Bot Rev 1976;42:389-466.
    • (1976) Bot Rev , vol.42 , pp. 389-466
    • De Cleene, M.1    De Ley, J.2
  • 4
    • 0031792275 scopus 로고    scopus 로고
    • Crown gall of grape: biology of Agrobacterium vitis and the development of disease control strategies
    • Burr TJ, Bazzi C, Süle S, Otten L. Crown gall of grape: biology of Agrobacterium vitis and the development of disease control strategies. Plant Dis 1998;82:1288-1297.
    • (1998) Plant Dis , vol.82 , pp. 1288-1297
    • Burr, T.J.1    Bazzi, C.2    Süle, S.3    Otten, L.4
  • 5
    • 0000829946 scopus 로고
    • Agrobacterium-mediated plant transformation and its further applications to plant biology
    • Klee H, Horsch R, Rogers S. Agrobacterium-mediated plant transformation and its further applications to plant biology. Ann Rev Plant Physiol 1987;38:467-486.
    • (1987) Ann Rev Plant Physiol , vol.38 , pp. 467-486
    • Klee, H.1    Horsch, R.2    Rogers, S.3
  • 6
    • 0037337257 scopus 로고    scopus 로고
    • Agrobacterium-mediated plant transformation: the biology behind the "Gene-Jockeying" Tool
    • Gelvin SB. Agrobacterium-mediated plant transformation: the biology behind the "Gene-Jockeying" Tool. Microbiol Mol Bio Rev 2003;67:16-37.
    • (2003) Microbiol Mol Bio Rev , vol.67 , pp. 16-37
    • Gelvin, S.B.1
  • 7
    • 78649775121 scopus 로고    scopus 로고
    • Crown gall of stone fruits and nuts, economic significance and diversity of its causal agents: tumorigenic Agrobacterium spp
    • Pulawska J. Crown gall of stone fruits and nuts, economic significance and diversity of its causal agents: tumorigenic Agrobacterium spp. J Plant Pathol 2010;92:S1.87-S1.98.
    • (2010) J Plant Pathol , vol.92
    • Pulawska, J.1
  • 10
    • 34250692637 scopus 로고    scopus 로고
    • Inhibition of lysine biosynthesis: an evolving antibiotic strategy
    • Hutton CA, Perugini MA, Gerrard JA. Inhibition of lysine biosynthesis: an evolving antibiotic strategy. Mol Biosyst 2007;3:458-65.
    • (2007) Mol Biosyst , vol.3 , pp. 458-465
    • Hutton, C.A.1    Perugini, M.A.2    Gerrard, J.A.3
  • 13
    • 0015028609 scopus 로고
    • Mutants of Escherichia coli with a growth requirement for either lysine or pyridoxine
    • Bukhari AI, Taylor AL. Mutants of Escherichia coli with a growth requirement for either lysine or pyridoxine. J Bacteriol 1971;105:988-98.
    • (1971) J Bacteriol , vol.105 , pp. 988-998
    • Bukhari, A.I.1    Taylor, A.L.2
  • 14
    • 0015029675 scopus 로고
    • Genetic analysis of diaminopimelic acid- and lysine-requiring mutants of Escherichia coli
    • Bukhari AI, Taylor AL. Genetic analysis of diaminopimelic acid- and lysine-requiring mutants of Escherichia coli. J Bacteriol 1971;105:844-54.
    • (1971) J Bacteriol , vol.105 , pp. 844-854
    • Bukhari, A.I.1    Taylor, A.L.2
  • 16
    • 25144446271 scopus 로고    scopus 로고
    • The crystal structures of native and (S)-lysine-bound dihydrodipicolinate synthase from Escherichia coli with improved resolution show new features of biological significance
    • Dobson RC, Griffin MD, Jameson GB, Gerrard JA. The crystal structures of native and (S)-lysine-bound dihydrodipicolinate synthase from Escherichia coli with improved resolution show new features of biological significance. Acta Crysta D Biol Crystallogr 2005;61:1116-24.
    • (2005) Acta Crysta D Biol Crystallogr , vol.61 , pp. 1116-1124
    • Dobson, R.C.1    Griffin, M.D.2    Jameson, G.B.3    Gerrard, J.A.4
  • 18
    • 0031566028 scopus 로고    scopus 로고
    • Structure of dihydrodipicolinate synthase of Nicotiana sylvestris reveals novel quaternary structure
    • Blickling S, Beisel HG, Bozic D, Knablein J, Laber B, Huber R. Structure of dihydrodipicolinate synthase of Nicotiana sylvestris reveals novel quaternary structure. J Mol Biol 1997;274:608-21.
    • (1997) J Mol Biol , vol.274 , pp. 608-621
    • Blickling, S.1    Beisel, H.G.2    Bozic, D.3    Knablein, J.4    Laber, B.5    Huber, R.6
  • 21
    • 48749085398 scopus 로고    scopus 로고
    • Structural and functional characterization of Staphylococcus aureus dihydrodipicolinate synthase
    • Girish TS, Sharma E, Gopal B. Structural and functional characterization of Staphylococcus aureus dihydrodipicolinate synthase. FEBS Lett 2008;582:2923-30.
    • (2008) FEBS Lett , vol.582 , pp. 2923-2930
    • Girish, T.S.1    Sharma, E.2    Gopal, B.3
  • 25
    • 74149094662 scopus 로고    scopus 로고
    • Exploring the dihydrodipicolinate synthase tetramer: how resilient is the dimer-dimer interface?
    • Griffin MDW, Dobson RCJ, Gerrard JA, Perugini MA. Exploring the dihydrodipicolinate synthase tetramer: how resilient is the dimer-dimer interface? Arch Biochem Biophys 2010;494:58-63.
    • (2010) Arch Biochem Biophys , vol.494 , pp. 58-63
    • Griffin, M.D.W.1    Dobson, R.C.J.2    Gerrard, J.A.3    Perugini, M.A.4
  • 29
    • 33646455178 scopus 로고    scopus 로고
    • Cloning of Lactobacillus plantarum IAM 12477 lysine biosynthetic genes encoding functional aspartate semialdehyde dehydrogenase, dihydrodipicolinate synthase, and dihydrodipicolinate reductase
    • Cahyanto M, Kawasaki H, Fujiyama K, Seki T. Cloning of Lactobacillus plantarum IAM 12477 lysine biosynthetic genes encoding functional aspartate semialdehyde dehydrogenase, dihydrodipicolinate synthase, and dihydrodipicolinate reductase. World J Microbiol Biotech 2006;22:409-416.
    • (2006) World J Microbiol Biotech , vol.22 , pp. 409-416
    • Cahyanto, M.1    Kawasaki, H.2    Fujiyama, K.3    Seki, T.4
  • 30
    • 30744458839 scopus 로고    scopus 로고
    • Regulation of aspartokinase, aspartate semialdehyde dehydrogenase, dihydrodipicolinate synthase and dihydrodipicolinate reductase in Lactobacillus plantarum
    • Cahyanto MN, Kawasaki H, Nagashio M, Fujiyama K, Seki T. Regulation of aspartokinase, aspartate semialdehyde dehydrogenase, dihydrodipicolinate synthase and dihydrodipicolinate reductase in Lactobacillus plantarum. Microbiol 2006;152:105-12.
    • (2006) Microbiol , vol.152 , pp. 105-112
    • Cahyanto, M.N.1    Kawasaki, H.2    Nagashio, M.3    Fujiyama, K.4    Seki, T.5
  • 31
    • 77952542453 scopus 로고    scopus 로고
    • Crystal structure of dihydrodipicolinate synthase from Hahella chejuensis at 1.5Å resolution
    • Kang BS, Kim Y-G, Ahn J-W, Kim K-J. Crystal structure of dihydrodipicolinate synthase from Hahella chejuensis at 1.5Å resolution. Int J Biol Macromol 2010;46:512-516.
    • (2010) Int J Biol Macromol , vol.46 , pp. 512-516
    • Kang, B.S.1    Kim, Y.-G.2    Ahn, J.-W.3    Kim, K.-J.4
  • 32
    • 84876489799 scopus 로고    scopus 로고
    • Chloride and organic osmolytes: a hybrid strategy to cope with elevated salinities by the moderately halophilic, chloride-dependent bacterium Halobacillus halophilus
    • Saum SH, Pfeiffer F, Palm P, Rampp M, Schuster SC, Müller V, Oesterhelt D. Chloride and organic osmolytes: a hybrid strategy to cope with elevated salinities by the moderately halophilic, chloride-dependent bacterium Halobacillus halophilus. Environ Microbiol 2012;1619-1633.
    • (2012) Environ Microbiol , pp. 1619-1633
    • Saum, S.H.1    Pfeiffer, F.2    Palm, P.3    Rampp, M.4    Schuster, S.C.5    Müller, V.6    Oesterhelt, D.7
  • 33
    • 84865746469 scopus 로고    scopus 로고
    • Cloning, expression, purification and crystallization of dihydrodipicolinate synthase from Agrobacterium tumefaciens
    • Atkinson SC, Dogovski C, Dobson RC, Perugini MA. Cloning, expression, purification and crystallization of dihydrodipicolinate synthase from Agrobacterium tumefaciens. Acta Crysta Sect F Struct Biol Cryst Commun 2012;68:1040-7.
    • (2012) Acta Crysta Sect F Struct Biol Cryst Commun , vol.68 , pp. 1040-1047
    • Atkinson, S.C.1    Dogovski, C.2    Dobson, R.C.3    Perugini, M.A.4
  • 34
    • 1842425027 scopus 로고    scopus 로고
    • Properties of GDP-mannose pyrophosphorylase, a critical enzyme and drug target in Leishmania mexicana
    • Davis AJ, Perugini MA, Smith BJ, Stewart JD, Ilg T, Hodder AN, Handman E. Properties of GDP-mannose pyrophosphorylase, a critical enzyme and drug target in Leishmania mexicana. J Biol Chem 2004;279:12462-12468.
    • (2004) J Biol Chem , vol.279 , pp. 12462-12468
    • Davis, A.J.1    Perugini, M.A.2    Smith, B.J.3    Stewart, J.D.4    Ilg, T.5    Hodder, A.N.6    Handman, E.7
  • 35
    • 1842452651 scopus 로고    scopus 로고
    • The crystal structure of three site-directed mutants of Escherichia coli dihydrodipicolinate synthase: further evidence for a catalytic triad
    • Dobson RC, Valegard K, Gerrard JA. The crystal structure of three site-directed mutants of Escherichia coli dihydrodipicolinate synthase: further evidence for a catalytic triad. J Mol Biol 2004;338:329-39.
    • (2004) J Mol Biol , vol.338 , pp. 329-339
    • Dobson, R.C.1    Valegard, K.2    Gerrard, J.A.3
  • 36
    • 33744816438 scopus 로고    scopus 로고
    • UltraScan. A comprehensive data analysis software package for analytical ultracentrifugation experiments
    • Scott DJ, Harding SE, Rowe AJ, editors. Cambridge, UK: Royal Society of Chemistry;.
    • Demeler B. UltraScan. A comprehensive data analysis software package for analytical ultracentrifugation experiments. In: Scott DJ, Harding SE, Rowe AJ, editors. Modern analytical ultracentrifugation: techniques and methods. Cambridge, UK: Royal Society of Chemistry; 2005, pp 210-229.
    • (2005) Modern analytical ultracentrifugation: techniques and methods , pp. 210-229
    • Demeler, B.1
  • 37
    • 34548068467 scopus 로고    scopus 로고
    • Bioinformatics basics: applications in biological science and medicine
    • 2nd ed. In: Rashidi EH, Buehler L, editors. CRC Press LLC: Boca Raton, Florida, USA;.
    • Demeler B, Bioinformatics basics: applications in biological science and medicine, 2nd ed. In: Rashidi EH, Buehler L, editors. Hydrodynamic methods. CRC Press LLC: Boca Raton, Florida, USA; 2005, pp 226-255.
    • (2005) Hydrodynamic methods , pp. 226-255
    • Demeler, B.1
  • 38
    • 8844265931 scopus 로고    scopus 로고
    • Sedimentation velocity analysis of highly heterogeneous systems
    • Demeler B, van Holde KE. Sedimentation velocity analysis of highly heterogeneous systems. Anal Biochem 2004;335:279-88.
    • (2004) Anal Biochem , vol.335 , pp. 279-288
    • Demeler, B.1    van Holde, K.E.2
  • 39
    • 0031020113 scopus 로고    scopus 로고
    • Identification and interpretation of complexity in sedimentation velocity boundaries
    • Demeler B, Saber H, Hansen JC. Identification and interpretation of complexity in sedimentation velocity boundaries. Biophys J 1997;72:397-407.
    • (1997) Biophys J , vol.72 , pp. 397-407
    • Demeler, B.1    Saber, H.2    Hansen, J.C.3
  • 40
    • 77950581757 scopus 로고    scopus 로고
    • A two-dimensional spectrum analysis for sedimentation velocity experiments of mixtures with heterogeneity in molecular weight and shape
    • Brookes E, Cao W, Demeler B. A two-dimensional spectrum analysis for sedimentation velocity experiments of mixtures with heterogeneity in molecular weight and shape. Eur Biophys J 2010;39:405-14.
    • (2010) Eur Biophys J , vol.39 , pp. 405-414
    • Brookes, E.1    Cao, W.2    Demeler, B.3
  • 41
  • 42
  • 43
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project Number 4.
    • Collaborative Computational Project Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 1994;50:760-763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
  • 45
    • 43749083257 scopus 로고    scopus 로고
    • CHAINSAW: a program for mutating pdb files used as templates in molecular replacement
    • Stein N. CHAINSAW: a program for mutating pdb files used as templates in molecular replacement. J Appl Crystallogr 2008;41:641-643.
    • (2008) J Appl Crystallogr , vol.41 , pp. 641-643
    • Stein, N.1
  • 49
    • 0013827137 scopus 로고
    • The condensation step in diaminopimelate synthesis
    • Yugari Y, Gilvarg C. The condensation step in diaminopimelate synthesis. J Biol Chem 1965;240:4710-6.
    • (1965) J Biol Chem , vol.240 , pp. 4710-4716
    • Yugari, Y.1    Gilvarg, C.2
  • 52
    • 67649444194 scopus 로고    scopus 로고
    • Specificity versus catalytic potency: the role of threonine 44 in Escherichia coli dihydrodipicolinate synthase mediated catalysis
    • Dobson RC, Perugini MA, Jameson GB, Gerrard JA. Specificity versus catalytic potency: the role of threonine 44 in Escherichia coli dihydrodipicolinate synthase mediated catalysis. Biochimie 2009;91:1036-44.
    • (2009) Biochimie , vol.91 , pp. 1036-1044
    • Dobson, R.C.1    Perugini, M.A.2    Jameson, G.B.3    Gerrard, J.A.4
  • 53
    • 67349221170 scopus 로고    scopus 로고
    • Cloning and characterisation of dihydrodipicolinate synthase from the pathogen Neisseria meningitidis
    • Devenish SR, Huisman FH, Parker EJ, Hadfield AT, Gerrard JA. Cloning and characterisation of dihydrodipicolinate synthase from the pathogen Neisseria meningitidis. Biochim Biophys Acta 2009;1794:1168-74.
    • (2009) Biochim Biophys Acta , vol.1794 , pp. 1168-1174
    • Devenish, S.R.1    Huisman, F.H.2    Parker, E.J.3    Hadfield, A.T.4    Gerrard, J.A.5
  • 54
    • 0031037267 scopus 로고    scopus 로고
    • Dihydrodipicolinate synthase from Escherichia coli: pH dependent changes in the kinetic mechanism and kinetic mechanism of allosteric inhibition by L-lysine
    • Karsten WE. Dihydrodipicolinate synthase from Escherichia coli: pH dependent changes in the kinetic mechanism and kinetic mechanism of allosteric inhibition by L-lysine. Biochem 1997;36:1730-9.
    • (1997) Biochem , vol.36 , pp. 1730-1739
    • Karsten, W.E.1
  • 55
    • 0021245679 scopus 로고
    • Lysine biosynthesis in Methanobacterium thermoautotrophicum is by the diaminopimelic acid pathway
    • Bakhiet N, Forney, F.W., Stahly, D. P., Daniels, L. Lysine biosynthesis in Methanobacterium thermoautotrophicum is by the diaminopimelic acid pathway. Curr Microbiol 1984;10:195-198.
    • (1984) Curr Microbiol , vol.10 , pp. 195-198
    • Bakhiet, N.1    Forney, F.W.2    Stahly, D.P.3    Daniels, L.4
  • 56
    • 0028907826 scopus 로고
    • The crystal structure of dihydrodipicolinate synthase from Escherichia coli at 2.5 A resolution
    • Mirwaldt C, Korndorfer I, Huber R. The crystal structure of dihydrodipicolinate synthase from Escherichia coli at 2.5 A resolution. J Mol Biol 1995;246:227-39.
    • (1995) J Mol Biol , vol.246 , pp. 227-239
    • Mirwaldt, C.1    Korndorfer, I.2    Huber, R.3
  • 58
    • 0026486643 scopus 로고
    • Escherichia coli dihydrodipicolinate synthase. Identification of the active site and crystallization
    • Laber B, Gomis-Ruth FX, Romao MJ, Huber R. Escherichia coli dihydrodipicolinate synthase. Identification of the active site and crystallization. Biochem J 1992;288(Pt 2):691-5.
    • (1992) Biochem J , vol.288 , Issue.PT 2 , pp. 691-695
    • Laber, B.1    Gomis-Ruth, F.X.2    Romao, M.J.3    Huber, R.4
  • 60
    • 0032719440 scopus 로고    scopus 로고
    • Crown gall of grape: biology and disease management
    • Burr TJ, Otten L. Crown gall of grape: biology and disease management. Ann Rev Phytopathol 1999;37:53-80.
    • (1999) Ann Rev Phytopathol , vol.37 , pp. 53-80
    • Burr, T.J.1    Otten, L.2
  • 61
    • 38949153158 scopus 로고    scopus 로고
    • Salicylic acid and systemic acquired resistance play a role in attenuating crown gall disease caused by Agrobacterium tumefaciens
    • Anand A, Uppalapati SR, Ryu CM, Allen SN, Kang L, Tang Y, Mysore KS. Salicylic acid and systemic acquired resistance play a role in attenuating crown gall disease caused by Agrobacterium tumefaciens. Plant Physiol 2008;146:703-15.
    • (2008) Plant Physiol , vol.146 , pp. 703-715
    • Anand, A.1    Uppalapati, S.R.2    Ryu, C.M.3    Allen, S.N.4    Kang, L.5    Tang, Y.6    Mysore, K.S.7
  • 64
    • 0347093427 scopus 로고    scopus 로고
    • Crown-gall-resistant transgenic apple trees that Silence Agrobacterium tumefaciens oncogenes
    • Viss WJ, Pitrak J, Humann J, Cook M, Driver J, Ream W. Crown-gall-resistant transgenic apple trees that Silence Agrobacterium tumefaciens oncogenes. Mol Breeding 2003;12:283-295.
    • (2003) Mol Breeding , vol.12 , pp. 283-295
    • Viss, W.J.1    Pitrak, J.2    Humann, J.3    Cook, M.4    Driver, J.5    Ream, W.6
  • 67
    • 0028773463 scopus 로고
    • The three-dimensional structure of N-acetylneuraminate lyase from Escherichia coli
    • Izard T, Lawrence MC, Malby RL, Lilley GG, Colman PM. The three-dimensional structure of N-acetylneuraminate lyase from Escherichia coli. Structure 1994;2:361-9.
    • (1994) Structure , vol.2 , pp. 361-369
    • Izard, T.1    Lawrence, M.C.2    Malby, R.L.3    Lilley, G.G.4    Colman, P.M.5
  • 68
    • 6344289413 scopus 로고    scopus 로고
    • The structural basis for substrate promiscuity in 2-keto-3-deoxygluconate aldolase from the Entner-Doudoroff pathway in Sulfolobus solfataricus
    • Theodossis A, Walden H, Westwick EJ, Connaris H, Lamble HJ, Hough DW, Danson MJ, Taylor GL. The structural basis for substrate promiscuity in 2-keto-3-deoxygluconate aldolase from the Entner-Doudoroff pathway in Sulfolobus solfataricus. J Biol Chem 2004;279:43886-92.
    • (2004) J Biol Chem , vol.279 , pp. 43886-43892
    • Theodossis, A.1    Walden, H.2    Westwick, E.J.3    Connaris, H.4    Lamble, H.J.5    Hough, D.W.6    Danson, M.J.7    Taylor, G.L.8
  • 69
    • 84874301737 scopus 로고    scopus 로고
    • Structural, kinetic and computational investigation of Vitis vinifera DHDPS reveals new insight into the mechanism of lysine-mediated allosteric inhibition
    • Atkinson SC, Dogovski C, Downton MT, Czabotar PE, Dobson RCJ, Gerrard JA, Wagner J, Perugini MA. Structural, kinetic and computational investigation of Vitis vinifera DHDPS reveals new insight into the mechanism of lysine-mediated allosteric inhibition. Plant Mol Biol 2013;81:431-46.
    • (2013) Plant Mol Biol , vol.81 , pp. 431-446
    • Atkinson, S.C.1    Dogovski, C.2    Downton, M.T.3    Czabotar, P.E.4    Dobson, R.C.J.5    Gerrard, J.A.6    Wagner, J.7    Perugini, M.A.8
  • 70
    • 0032878308 scopus 로고    scopus 로고
    • Escherichia coli dihydrodipicolinate synthase and dihydrodipicolinate reductase: kinetic and inhibition studies of two putative herbicide targets
    • Coulter CV, Gerrard JA, Kraunsoe JAE, Pratt AJ. Escherichia coli dihydrodipicolinate synthase and dihydrodipicolinate reductase: kinetic and inhibition studies of two putative herbicide targets. Pesticide Sci 1999;55:887-895.
    • (1999) Pesticide Sci , vol.55 , pp. 887-895
    • Coulter, C.V.1    Gerrard, J.A.2    Kraunsoe, J.A.E.3    Pratt, A.J.4
  • 72
    • 13844317354 scopus 로고    scopus 로고
    • Heterocyclic inhibitors of dihydrodipicolinate synthase are not competitive
    • Turner JJ, Gerrard JA, Hutton CA. Heterocyclic inhibitors of dihydrodipicolinate synthase are not competitive. Bioorg Med Chem 2005;13:2133-40.
    • (2005) Bioorg Med Chem , vol.13 , pp. 2133-2140
    • Turner, J.J.1    Gerrard, J.A.2    Hutton, C.A.3
  • 73
    • 16244417783 scopus 로고    scopus 로고
    • Two new irreversible inhibitors of dihydrodipicolinate synthase: diethyl (E,E)-4-oxo-2,5-heptadienedioate and diethyl (E)-4-oxo-2-heptenedioate
    • Turner JJ, Healy JP, Dobson RC, Gerrard JA, Hutton CA. Two new irreversible inhibitors of dihydrodipicolinate synthase: diethyl (E, E)-4-oxo-2, 5-heptadienedioate and diethyl (E)-4-oxo-2-heptenedioate. Bioorg Med Chem Lett 2005;15:995-8.
    • (2005) Bioorg Med Chem Lett , vol.15 , pp. 995-998
    • Turner, J.J.1    Healy, J.P.2    Dobson, R.C.3    Gerrard, J.A.4    Hutton, C.A.5
  • 74
    • 38149080516 scopus 로고    scopus 로고
    • Conformationally constrained diketopimelic acid analogues as inhibitors of dihydrodipicolinate synthase
    • Boughton BA, Dobson RC, Gerrard JA, Hutton CA. Conformationally constrained diketopimelic acid analogues as inhibitors of dihydrodipicolinate synthase. Bioorg Med Chem Lett 2008;18:460-3.
    • (2008) Bioorg Med Chem Lett , vol.18 , pp. 460-463
    • Boughton, B.A.1    Dobson, R.C.2    Gerrard, J.A.3    Hutton, C.A.4
  • 75
    • 84858296060 scopus 로고    scopus 로고
    • 1,3-Phenylene bis(ketoacid) derivatives as inhibitors of Escherichia coli dihydrodipicolinate synthase
    • Boughton BA, Hor L, Gerrard JA, Hutton CA. 1, 3-Phenylene bis(ketoacid) derivatives as inhibitors of Escherichia coli dihydrodipicolinate synthase. Bioorg Med Chem 2012;20:2419-2426.
    • (2012) Bioorg Med Chem , vol.20 , pp. 2419-2426
    • Boughton, B.A.1    Hor, L.2    Gerrard, J.A.3    Hutton, C.A.4
  • 78
    • 33847778677 scopus 로고    scopus 로고
    • Inhibiting protein-protein interactions as an emerging paradigm for drug discovery
    • Gerrard JA, Hutton CA, Perugini MA. Inhibiting protein-protein interactions as an emerging paradigm for drug discovery. Mini Rev Med Chem 2007;7:151-57.
    • (2007) Mini Rev Med Chem , vol.7 , pp. 151-157
    • Gerrard, J.A.1    Hutton, C.A.2    Perugini, M.A.3
  • 79
    • 37249004920 scopus 로고    scopus 로고
    • Reaching for high-hanging fruit in drug discovery at protein-protein interfaces
    • Wells JA, McClendon CL. Reaching for high-hanging fruit in drug discovery at protein-protein interfaces. Nature 2007;450:1001-9.
    • (2007) Nature , vol.450 , pp. 1001-1009
    • Wells, J.A.1    McClendon, C.L.2
  • 80
    • 0036428535 scopus 로고    scopus 로고
    • Modulation of the oligomeric structures of HIV-1 retroviral enzymes by synthetic peptides and small molecules
    • Sluis-Cremer N, Tachedjian G. Modulation of the oligomeric structures of HIV-1 retroviral enzymes by synthetic peptides and small molecules. Euro J Biochem 2002;269:5103-5111.
    • (2002) Euro J Biochem , vol.269 , pp. 5103-5111
    • Sluis-Cremer, N.1    Tachedjian, G.2
  • 81
    • 3142781225 scopus 로고    scopus 로고
    • Small-molecule inhibitors of protein-protein interactions: progressing towards the dream
    • Arkin MR, Wells JA. Small-molecule inhibitors of protein-protein interactions: progressing towards the dream. Nat Rev Drug Discov 2004;3:301-317.
    • (2004) Nat Rev Drug Discov , vol.3 , pp. 301-317
    • Arkin, M.R.1    Wells, J.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.