메뉴 건너뛰기




Volumn 8, Issue 10, 2013, Pages

Isozyme-Specific Ligands for O-acetylserine sulfhydrylase, a Novel Antibiotic Target

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE SYNTHASE; ISOENZYME; S SULFOCYSTEINE SYNTHASE; UNCLASSIFIED DRUG; ANTIINFECTIVE AGENT; BACTERIAL PROTEIN; CYSTEINE; ENZYME INHIBITOR;

EID: 84886040250     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0077558     Document Type: Article
Times cited : (50)

References (124)
  • 1
    • 33750083296 scopus 로고    scopus 로고
    • Enzymatic activation of sulfur for incorporation into biomolecules in prokaryotes
    • Kessler D, (2006) Enzymatic activation of sulfur for incorporation into biomolecules in prokaryotes. FEMS Microbiol Rev 30: 825-840.
    • (2006) FEMS Microbiol Rev , vol.30 , pp. 825-840
    • Kessler, D.1
  • 2
    • 0033829523 scopus 로고    scopus 로고
    • A tribute to sulfur
    • Beinert H, (2000) A tribute to sulfur. Eur J Biochem 267: 5657-5664.
    • (2000) Eur J Biochem , vol.267 , pp. 5657-5664
    • Beinert, H.1
  • 3
    • 33748755115 scopus 로고    scopus 로고
    • Cysteine biosynthesis in Trichomonas vaginalis involves cysteine synthase utilizing O-phosphoserine
    • Westrop GD, Goodall G, Mottram JC, Coombs GH, (2006) Cysteine biosynthesis in Trichomonas vaginalis involves cysteine synthase utilizing O-phosphoserine. J Biol Chem 281: 25062-25075.
    • (2006) J Biol Chem , vol.281 , pp. 25062-25075
    • Westrop, G.D.1    Goodall, G.2    Mottram, J.C.3    Coombs, G.H.4
  • 4
    • 34547095000 scopus 로고    scopus 로고
    • Drug targets in mycobacterial sulfur metabolism
    • Bhave DP, Muse WB, (2007) Drug targets in mycobacterial sulfur metabolism. Infect Disord Drug Targets 7: 140-158.
    • (2007) Infect Disord Drug Targets , vol.7 , pp. 140-158
    • Bhave, D.P.1    Muse, W.B.2
  • 6
    • 77957256320 scopus 로고    scopus 로고
    • Cysteine biosynthesis, oxidative stress and antibiotic resistance in Salmonella typhimurium
    • Turnbull AL, Surette MG, (2010) Cysteine biosynthesis, oxidative stress and antibiotic resistance in Salmonella typhimurium. Res Microbiol 161: 643-650.
    • (2010) Res Microbiol , vol.161 , pp. 643-650
    • Turnbull, A.L.1    Surette, M.G.2
  • 7
    • 84863179892 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress-sensing mechanism is activated in Entamoeba histolytica upon treatment with nitric oxide
    • Santi-Rocca J, Smith S, Weber C, Pineda E, Hon CC, et al. (2012) Endoplasmic reticulum stress-sensing mechanism is activated in Entamoeba histolytica upon treatment with nitric oxide. PLoS One 7: e31777.
    • (2012) PLoS One , vol.7
    • Santi-Rocca, J.1    Smith, S.2    Weber, C.3    Pineda, E.4    Hon, C.C.5
  • 8
    • 0043142536 scopus 로고    scopus 로고
    • Transcriptional adaptation of Mycobacterium tuberculosis within macrophages: Insights into the phagosomal environment
    • Schnappinger D, Ehrt S, Voskuil MI, Liu Y, Mangan JA, et al. (2003) Transcriptional adaptation of Mycobacterium tuberculosis within macrophages: Insights into the phagosomal environment. J Exp Med 198: 693-704.
    • (2003) J Exp Med , vol.198 , pp. 693-704
    • Schnappinger, D.1    Ehrt, S.2    Voskuil, M.I.3    Liu, Y.4    Mangan, J.A.5
  • 9
    • 39149131054 scopus 로고    scopus 로고
    • Global transcriptional profile of Mycobacterium tuberculosis during THP-1 human macrophage infection
    • Fontan P, Aris V, Ghanny S, Soteropoulos P, Smith I, (2008) Global transcriptional profile of Mycobacterium tuberculosis during THP-1 human macrophage infection. Infect Immun 76: 717-725.
    • (2008) Infect Immun , vol.76 , pp. 717-725
    • Fontan, P.1    Aris, V.2    Ghanny, S.3    Soteropoulos, P.4    Smith, I.5
  • 10
    • 33846503255 scopus 로고    scopus 로고
    • Current therapeutics, their problems, and sulfur-containing-amino-acid metabolism as a novel target against infections by "amitochondriate" protozoan parasites
    • Ali V, Nozaki T, (2007) Current therapeutics, their problems, and sulfur-containing-amino-acid metabolism as a novel target against infections by "amitochondriate" protozoan parasites. Clin Microbiol Rev 20: 164-187.
    • (2007) Clin Microbiol Rev , vol.20 , pp. 164-187
    • Ali, V.1    Nozaki, T.2
  • 11
    • 84857099645 scopus 로고    scopus 로고
    • Virtual screening, identification and in vitro testing of novel inhibitors of O-acetyl-L-serine sulfhydrylase of Entamoeba histolytica
    • Nagpal I, Raj I, Subbarao N, Gourinath S, (2012) Virtual screening, identification and in vitro testing of novel inhibitors of O-acetyl-L-serine sulfhydrylase of Entamoeba histolytica. PLoS One 7: e30305.
    • (2012) PLoS One , vol.7
    • Nagpal, I.1    Raj, I.2    Subbarao, N.3    Gourinath, S.4
  • 12
    • 33749675294 scopus 로고    scopus 로고
    • Sulfate metabolism in mycobacteria
    • Schelle MW, Bertozzi CR, (2006) Sulfate metabolism in mycobacteria. Chembiochem 7: 1516-1524.
    • (2006) Chembiochem , vol.7 , pp. 1516-1524
    • Schelle, M.W.1    Bertozzi, C.R.2
  • 13
    • 33750432874 scopus 로고    scopus 로고
    • Substrate recognition, protein dynamics, and iron-sulfur cluster in Pseudomonas aeruginosa adenosine 5′-phosphosulfate reductase
    • Chartron J, Carroll KS, Shiau C, Gao H, Leary JA, et al. (2006) Substrate recognition, protein dynamics, and iron-sulfur cluster in Pseudomonas aeruginosa adenosine 5′-phosphosulfate reductase. J Mol Biol 364: 152-169.
    • (2006) J Mol Biol , vol.364 , pp. 152-169
    • Chartron, J.1    Carroll, K.S.2    Shiau, C.3    Gao, H.4    Leary, J.A.5
  • 14
    • 79960957242 scopus 로고    scopus 로고
    • The regulation of sulfur metabolism in Mycobacterium tuberculosis
    • Hatzios SK, Bertozzi CR, (2011) The regulation of sulfur metabolism in Mycobacterium tuberculosis. PLoS Pathog 7: e1002036.
    • (2011) PLoS Pathog , vol.7
    • Hatzios, S.K.1    Bertozzi, C.R.2
  • 15
    • 77952310116 scopus 로고    scopus 로고
    • Structural enzymology of sulphur metabolism in Mycobacterium tuberculosis
    • Schnell R, Schneider G, (2010) Structural enzymology of sulphur metabolism in Mycobacterium tuberculosis. Biochem Biophys Res Commun 396: 33-38.
    • (2010) Biochem Biophys Res Commun , vol.396 , pp. 33-38
    • Schnell, R.1    Schneider, G.2
  • 16
    • 74849085165 scopus 로고    scopus 로고
    • Design of O-acetylserine sulfhydrylase inhibitors by mimicking nature
    • Salsi E, Bayden AS, Spyrakis F, Amadasi A, Campanini B, et al. (2010) Design of O-acetylserine sulfhydrylase inhibitors by mimicking nature. J Med Chem 53: 345-356.
    • (2010) J Med Chem , vol.53 , pp. 345-356
    • Salsi, E.1    Bayden, A.S.2    Spyrakis, F.3    Amadasi, A.4    Campanini, B.5
  • 18
    • 84865490293 scopus 로고    scopus 로고
    • Design and synthesis of trans-2-substituted-cyclopropane-1-carboxylic acids as the first non-natural small molecule inhibitors of O-acetylserine sulfhydrylase
    • Amori L, Katkevica S, Bruno A, Campanini B, Felici P, et al. (2012) Design and synthesis of trans-2-substituted-cyclopropane-1-carboxylic acids as the first non-natural small molecule inhibitors of O-acetylserine sulfhydrylase. MedChemComm 3: 1111-1116.
    • (2012) MedChemComm , vol.3 , pp. 1111-1116
    • Amori, L.1    Katkevica, S.2    Bruno, A.3    Campanini, B.4    Felici, P.5
  • 19
    • 84870231300 scopus 로고    scopus 로고
    • Fine tuning of the active site modulates specificity in the interaction of O-acetylserine sulfhydrylase isozymes with serine acetyltransferase
    • Spyrakis F, Felici P, Bayden AS, Salsi E, Miggiano R, et al. (2013) Fine tuning of the active site modulates specificity in the interaction of O-acetylserine sulfhydrylase isozymes with serine acetyltransferase. Biochim Biophys Acta 1834: 169-181.
    • (2013) Biochim Biophys Acta , vol.1834 , pp. 169-181
    • Spyrakis, F.1    Felici, P.2    Bayden, A.S.3    Salsi, E.4    Miggiano, R.5
  • 20
    • 56249117015 scopus 로고    scopus 로고
    • Structure-based virtual screening and biological evaluation of Mycobacterium tuberculosis adenosine 5′-phosphosulfate reductase inhibitors
    • Cosconati S, Hong JA, Novellino E, Carroll KS, Goodsell DS, et al. (2008) Structure-based virtual screening and biological evaluation of Mycobacterium tuberculosis adenosine 5′-phosphosulfate reductase inhibitors. J Med Chem 51: 6627-6630.
    • (2008) J Med Chem , vol.51 , pp. 6627-6630
    • Cosconati, S.1    Hong, J.A.2    Novellino, E.3    Carroll, K.S.4    Goodsell, D.S.5
  • 21
    • 37249032585 scopus 로고    scopus 로고
    • Inhibitors of Escherichia coli serine acetyltransferase block proliferation of Entamoeba histolytica trophozoites
    • Agarwal SM, Jain R, Bhattacharya A, Azam A, (2008) Inhibitors of Escherichia coli serine acetyltransferase block proliferation of Entamoeba histolytica trophozoites. Int J Parasitol 38: 137-141.
    • (2008) Int J Parasitol , vol.38 , pp. 137-141
    • Agarwal, S.M.1    Jain, R.2    Bhattacharya, A.3    Azam, A.4
  • 22
    • 33645462886 scopus 로고    scopus 로고
    • 5′-Adenosinephosphosulphate reductase (CysH) protects Mycobacterium tuberculosis against free radicals during chronic infection phase in mice
    • Senaratne RH, De Silva AD, Williams SJ, Mougous JD, Reader JR, et al. (2006) 5′-Adenosinephosphosulphate reductase (CysH) protects Mycobacterium tuberculosis against free radicals during chronic infection phase in mice. Mol Microbiol 59: 1744-1753.
    • (2006) Mol Microbiol , vol.59 , pp. 1744-1753
    • Senaratne, R.H.1    De Silva, A.D.2    Williams, S.J.3    Mougous, J.D.4    Reader, J.R.5
  • 24
    • 57349162179 scopus 로고    scopus 로고
    • L-Cysteine is required for induced antibiotic resistance in actively swarming Salmonella enterica serovar Typhimurium
    • Turnbull AL, Surette MG, (2008) L-Cysteine is required for induced antibiotic resistance in actively swarming Salmonella enterica serovar Typhimurium. Microbiology 154: 3410-3419.
    • (2008) Microbiology , vol.154 , pp. 3410-3419
    • Turnbull, A.L.1    Surette, M.G.2
  • 26
    • 0002624786 scopus 로고    scopus 로고
    • Biosynthesis of cysteine
    • In: Neidhardt FC, editor, 2nd ed. Washington: ASM Press
    • Kredich NM (1996) Biosynthesis of cysteine. In: Neidhardt FC, editor. Escherichia coli and Salmonella. 2nd ed. Washington: ASM Press. pp. 514-527.
    • (1996) Escherichia coli and Salmonella , pp. 514-527
    • Kredich, N.M.1
  • 27
    • 0027183564 scopus 로고
    • Kinetic mechanisms of the A and B isozymes of O-acetylserine sulfhydrylase from Salmonella typhimurium LT-2 using the natural and alternative reactants
    • Tai CH, Nalabolu SR, Jacobson TM, Minter DE, Cook PF, (1993) Kinetic mechanisms of the A and B isozymes of O-acetylserine sulfhydrylase from Salmonella typhimurium LT-2 using the natural and alternative reactants. Biochemistry 32: 6433-6442.
    • (1993) Biochemistry , vol.32 , pp. 6433-6442
    • Tai, C.H.1    Nalabolu, S.R.2    Jacobson, T.M.3    Minter, D.E.4    Cook, P.F.5
  • 28
    • 80054687027 scopus 로고    scopus 로고
    • The multifaceted pyridoxal 5′-phosphate-dependent O-acetylserine sulfhydrylase
    • Mozzarelli A, Bettati S, Campanini B, Salsi E, Raboni S, et al. (2011) The multifaceted pyridoxal 5′-phosphate-dependent O-acetylserine sulfhydrylase. Biochim Biophys Acta 1814: 1497-1510.
    • (2011) Biochim Biophys Acta , vol.1814 , pp. 1497-1510
    • Mozzarelli, A.1    Bettati, S.2    Campanini, B.3    Salsi, E.4    Raboni, S.5
  • 29
    • 0028174296 scopus 로고
    • Product binding to the alpha-carboxyl subsite results in a conformational change at the active site of O-acetylserine sulfhydrylase-A: evidence from fluorescence spectroscopy
    • McClure GD Jr, Cook PF, (1994) Product binding to the alpha-carboxyl subsite results in a conformational change at the active site of O-acetylserine sulfhydrylase-A: evidence from fluorescence spectroscopy. Biochemistry 33: 1674-1683.
    • (1994) Biochemistry , vol.33 , pp. 1674-1683
    • McClure Jr., G.D.1    Cook, P.F.2
  • 30
    • 0033038799 scopus 로고    scopus 로고
    • Conformational probes of O-acetylserine sulfhydrylase: fluorescence of tryptophans 50 and 161
    • Benci S, Bettati S, Vaccari S, Schianchi G, Mozzarelli A, et al. (1999) Conformational probes of O-acetylserine sulfhydrylase: fluorescence of tryptophans 50 and 161. J Photochem Photobiol B 48: 17-26.
    • (1999) J Photochem Photobiol B , vol.48 , pp. 17-26
    • Benci, S.1    Bettati, S.2    Vaccari, S.3    Schianchi, G.4    Mozzarelli, A.5
  • 31
    • 0030722376 scopus 로고    scopus 로고
    • Time-resolved fluorescence of O-acetylserine sulfhydrylase catalytic intermediates
    • Benci S, Vaccari S, Mozzarelli A, Cook PF, (1997) Time-resolved fluorescence of O-acetylserine sulfhydrylase catalytic intermediates. Biochemistry 36: 15419-15427.
    • (1997) Biochemistry , vol.36 , pp. 15419-15427
    • Benci, S.1    Vaccari, S.2    Mozzarelli, A.3    Cook, P.F.4
  • 33
    • 0141621191 scopus 로고    scopus 로고
    • Surface-exposed tryptophan residues are essential for O-acetylserine sulfhydrylase structure, function, and stability
    • Campanini B, Raboni S, Vaccari S, Zhang L, Cook PF, et al. (2003) Surface-exposed tryptophan residues are essential for O-acetylserine sulfhydrylase structure, function, and stability. J Biol Chem 278: 37511-37519.
    • (2003) J Biol Chem , vol.278 , pp. 37511-37519
    • Campanini, B.1    Raboni, S.2    Vaccari, S.3    Zhang, L.4    Cook, P.F.5
  • 34
    • 0034704154 scopus 로고    scopus 로고
    • Role of pyridoxal 5′-phosphate in the structural stabilization of O-acetylserine sulfhydrylase
    • Bettati S, Benci S, Campanini B, Raboni S, Chirico G, et al. (2000) Role of pyridoxal 5′-phosphate in the structural stabilization of O-acetylserine sulfhydrylase. J Biol Chem 275: 40244-40251.
    • (2000) J Biol Chem , vol.275 , pp. 40244-40251
    • Bettati, S.1    Benci, S.2    Campanini, B.3    Raboni, S.4    Chirico, G.5
  • 35
    • 0036538773 scopus 로고    scopus 로고
    • Unfolding of pyridoxal 5′-phosphate-dependent O-acetylserine sulfhydrylase probed by time-resolved tryptophan fluorescence
    • Bettati S, Campanini B, Vaccari S, Mozzarelli A, Schianchi G, et al. (2002) Unfolding of pyridoxal 5′-phosphate-dependent O-acetylserine sulfhydrylase probed by time-resolved tryptophan fluorescence. Biochim Biophys Acta 1596: 47-54.
    • (2002) Biochim Biophys Acta , vol.1596 , pp. 47-54
    • Bettati, S.1    Campanini, B.2    Vaccari, S.3    Mozzarelli, A.4    Schianchi, G.5
  • 36
    • 34447554594 scopus 로고    scopus 로고
    • Structure, mechanism, and conformational dynamics of O-acetylserine sulfhydrylase from Salmonella typhimurium: comparison of A and B isozymes
    • Chattopadhyay A, Meier M, Ivaninskii S, Burkhard P, Speroni F, et al. (2007) Structure, mechanism, and conformational dynamics of O-acetylserine sulfhydrylase from Salmonella typhimurium: comparison of A and B isozymes. Biochemistry 46: 8315-8330.
    • (2007) Biochemistry , vol.46 , pp. 8315-8330
    • Chattopadhyay, A.1    Meier, M.2    Ivaninskii, S.3    Burkhard, P.4    Speroni, F.5
  • 37
    • 0029046782 scopus 로고
    • Modeling of the spatial structure of eukaryotic ornithine decarboxylases
    • Grishin NV, Phillips MA, Goldsmith EJ, (1995) Modeling of the spatial structure of eukaryotic ornithine decarboxylases. Protein Sci 4: 1291-1304.
    • (1995) Protein Sci , vol.4 , pp. 1291-1304
    • Grishin, N.V.1    Phillips, M.A.2    Goldsmith, E.J.3
  • 38
    • 0026086276 scopus 로고
    • Structural basis for catalysis by tryptophan synthase
    • Miles EW, (1991) Structural basis for catalysis by tryptophan synthase. Adv Enzymol Relat Areas Mol Biol 64: 93-172.
    • (1991) Adv Enzymol Relat Areas Mol Biol , vol.64 , pp. 93-172
    • Miles, E.W.1
  • 39
    • 67650409780 scopus 로고    scopus 로고
    • Tryptophan synthase: a mine for enzymologists
    • Raboni S, Bettati S, Mozzarelli A, (2009) Tryptophan synthase: a mine for enzymologists. Cell Mol Life Sci 66: 2391-2403.
    • (2009) Cell Mol Life Sci , vol.66 , pp. 2391-2403
    • Raboni, S.1    Bettati, S.2    Mozzarelli, A.3
  • 40
    • 58149488752 scopus 로고    scopus 로고
    • The C-terminal of CysM from Mycobacterium tuberculosis protects the aminoacrylate intermediate and is involved in sulfur donor selectivity
    • Agren D, Schnell R, Schneider G, (2009) The C-terminal of CysM from Mycobacterium tuberculosis protects the aminoacrylate intermediate and is involved in sulfur donor selectivity. FEBS Lett 583: 330-336.
    • (2009) FEBS Lett , vol.583 , pp. 330-336
    • Agren, D.1    Schnell, R.2    Schneider, G.3
  • 41
    • 52949126017 scopus 로고    scopus 로고
    • Crystal structure of a sulfur carrier protein complex found in the cysteine biosynthetic pathway of Mycobacterium tuberculosis
    • Jurgenson CT, Burns KE, Begley TP, Ealick SE, (2008) Crystal structure of a sulfur carrier protein complex found in the cysteine biosynthetic pathway of Mycobacterium tuberculosis. Biochemistry 47: 10354-10364.
    • (2008) Biochemistry , vol.47 , pp. 10354-10364
    • Jurgenson, C.T.1    Burns, K.E.2    Begley, T.P.3    Ealick, S.E.4
  • 42
    • 57649136751 scopus 로고    scopus 로고
    • Cysteine synthase (CysM) of Mycobacterium tuberculosis is an O-phosphoserine sulfhydrylase: evidence for an alternative cysteine biosynthesis pathway in mycobacteria
    • Agren D, Schnell R, Oehlmann W, Singh M, Schneider G, (2008) Cysteine synthase (CysM) of Mycobacterium tuberculosis is an O-phosphoserine sulfhydrylase: evidence for an alternative cysteine biosynthesis pathway in mycobacteria. J Biol Chem 283: 31567-31574.
    • (2008) J Biol Chem , vol.283 , pp. 31567-31574
    • Agren, D.1    Schnell, R.2    Oehlmann, W.3    Singh, M.4    Schneider, G.5
  • 43
    • 34548188995 scopus 로고    scopus 로고
    • Structural insights into catalysis and inhibition of O-acetylserine sulfhydrylase from Mycobacterium tuberculosis. Crystal structures of the enzyme alpha-aminoacrylate intermediate and an enzyme-inhibitor complex
    • Schnell R, Oehlmann W, Singh M, Schneider G, (2007) Structural insights into catalysis and inhibition of O-acetylserine sulfhydrylase from Mycobacterium tuberculosis. Crystal structures of the enzyme alpha-aminoacrylate intermediate and an enzyme-inhibitor complex. J Biol Chem 282: 23473-23481.
    • (2007) J Biol Chem , vol.282 , pp. 23473-23481
    • Schnell, R.1    Oehlmann, W.2    Singh, M.3    Schneider, G.4
  • 44
    • 20544435016 scopus 로고    scopus 로고
    • Structure of the O-acetylserine sulfhydrylase isoenzyme CysM from Escherichia coli
    • Claus MT, Zocher GE, Maier TH, Schulz GE, (2005) Structure of the O-acetylserine sulfhydrylase isoenzyme CysM from Escherichia coli. Biochemistry 44: 8620-8626.
    • (2005) Biochemistry , vol.44 , pp. 8620-8626
    • Claus, M.T.1    Zocher, G.E.2    Maier, T.H.3    Schulz, G.E.4
  • 45
    • 17644423923 scopus 로고    scopus 로고
    • The active site of O-acetylserine sulfhydrylase is the anchor point for bienzyme complex formation with serine acetyltransferase
    • Huang B, Vetting MW, Roderick SL, (2005) The active site of O-acetylserine sulfhydrylase is the anchor point for bienzyme complex formation with serine acetyltransferase. J Bacteriol 187: 3201-3205.
    • (2005) J Bacteriol , vol.187 , pp. 3201-3205
    • Huang, B.1    Vetting, M.W.2    Roderick, S.L.3
  • 46
    • 3042848356 scopus 로고    scopus 로고
    • Crystal structure of O-acetylserine sulfhydrylase (TM0665) from Thermotoga maritima at 1.8 A resolution
    • Heine A, Canaves JM, von Delft F, Brinen LS, Dai X, et al. (2004) Crystal structure of O-acetylserine sulfhydrylase (TM0665) from Thermotoga maritima at 1.8 A resolution. Proteins 56: 387-391.
    • (2004) Proteins , vol.56 , pp. 387-391
    • Heine, A.1    Canaves, J.M.2    von Delft, F.3    Brinen, L.S.4    Dai, X.5
  • 47
    • 0344157394 scopus 로고    scopus 로고
    • Three-dimensional structure of O-acetylserine sulfhydrylase from Salmonella typhimurium
    • Burkhard P, Rao GS, Hohenester E, Schnackerz KD, Cook PF, et al. (1998) Three-dimensional structure of O-acetylserine sulfhydrylase from Salmonella typhimurium. J Mol Biol 283: 121-133.
    • (1998) J Mol Biol , vol.283 , pp. 121-133
    • Burkhard, P.1    Rao, G.S.2    Hohenester, E.3    Schnackerz, K.D.4    Cook, P.F.5
  • 48
    • 0034692879 scopus 로고    scopus 로고
    • Identification of an allosteric anion-binding site on O-acetylserine sulfhydrylase: structure of the enzyme with chloride bound
    • Burkhard P, Tai CH, Jansonius JN, Cook PF, (2000) Identification of an allosteric anion-binding site on O-acetylserine sulfhydrylase: structure of the enzyme with chloride bound. J Mol Biol 303: 279-286.
    • (2000) J Mol Biol , vol.303 , pp. 279-286
    • Burkhard, P.1    Tai, C.H.2    Jansonius, J.N.3    Cook, P.F.4
  • 49
    • 0033609810 scopus 로고    scopus 로고
    • Ligand binding induces a large conformational change in O-acetylserine sulfhydrylase from Salmonella typhimurium
    • Burkhard P, Tai CH, Ristroph CM, Cook PF, Jansonius JN, (1999) Ligand binding induces a large conformational change in O-acetylserine sulfhydrylase from Salmonella typhimurium. J Mol Biol 291: 941-953.
    • (1999) J Mol Biol , vol.291 , pp. 941-953
    • Burkhard, P.1    Tai, C.H.2    Ristroph, C.M.3    Cook, P.F.4    Jansonius, J.N.5
  • 50
    • 33644685874 scopus 로고    scopus 로고
    • Molecular basis of cysteine biosynthesis in plants: structural and functional analysis of O-acetylserine sulfhydrylase from Arabidopsis thaliana
    • Bonner ER, Cahoon RE, Knapke SM, Jez JM, (2005) Molecular basis of cysteine biosynthesis in plants: structural and functional analysis of O-acetylserine sulfhydrylase from Arabidopsis thaliana. J Biol Chem 280: 38803-38813.
    • (2005) J Biol Chem , vol.280 , pp. 38803-38813
    • Bonner, E.R.1    Cahoon, R.E.2    Knapke, S.M.3    Jez, J.M.4
  • 51
    • 33947545688 scopus 로고    scopus 로고
    • Structural basis for interaction of O-acetylserine sulfhydrylase and serine acetyltransferase in the Arabidopsis cysteine synthase complex
    • Francois JA, Kumaran S, Jez JM, (2006) Structural basis for interaction of O-acetylserine sulfhydrylase and serine acetyltransferase in the Arabidopsis cysteine synthase complex. Plant Cell 18: 3647-3655.
    • (2006) Plant Cell , vol.18 , pp. 3647-3655
    • Francois, J.A.1    Kumaran, S.2    Jez, J.M.3
  • 52
    • 51349147518 scopus 로고    scopus 로고
    • Crystal structure of native O-acetyl-serine sulfhydrylase from Entamoeba histolytica and its complex with cysteine: structural evidence for cysteine binding and lack of interactions with serine acetyl transferase
    • Chinthalapudi K, Kumar M, Kumar S, Jain S, Alam N, et al. (2008) Crystal structure of native O-acetyl-serine sulfhydrylase from Entamoeba histolytica and its complex with cysteine: structural evidence for cysteine binding and lack of interactions with serine acetyl transferase. Proteins 72: 1222-1232.
    • (2008) Proteins , vol.72 , pp. 1222-1232
    • Chinthalapudi, K.1    Kumar, M.2    Kumar, S.3    Jain, S.4    Alam, N.5
  • 53
    • 22444433528 scopus 로고    scopus 로고
    • Three-dimensional structure of a new enzyme, O-phosphoserine sulfhydrylase, involved in l-cysteine biosynthesis by a hyperthermophilic archaeon, Aeropyrum pernix K1, at 2.0 Å resolution
    • Oda Y, Mino K, Ishikawa K, Ataka M, (2005) Three-dimensional structure of a new enzyme, O-phosphoserine sulfhydrylase, involved in l-cysteine biosynthesis by a hyperthermophilic archaeon, Aeropyrum pernix K1, at 2.0 Å resolution. J Mol Biol 351: 334-344.
    • (2005) J Mol Biol , vol.351 , pp. 334-344
    • Oda, Y.1    Mino, K.2    Ishikawa, K.3    Ataka, M.4
  • 55
    • 23644440099 scopus 로고    scopus 로고
    • Interaction of serine acetyltransferase with O-acetylserine sulfhydrylase active site: evidence from fluorescence spectroscopy
    • Campanini B, Speroni F, Salsi E, Cook PF, Roderick SL, et al. (2005) Interaction of serine acetyltransferase with O-acetylserine sulfhydrylase active site: evidence from fluorescence spectroscopy. Protein Sci 14: 2115-2124.
    • (2005) Protein Sci , vol.14 , pp. 2115-2124
    • Campanini, B.1    Speroni, F.2    Salsi, E.3    Cook, P.F.4    Roderick, S.L.5
  • 56
    • 0014670816 scopus 로고
    • Pleiotrophy in a cysteine-requiring mutant of Samonella typhimurium resulting from altered protein-protein interaction
    • Becker MA, Tomkins GM, (1969) Pleiotrophy in a cysteine-requiring mutant of Samonella typhimurium resulting from altered protein-protein interaction. J Biol Chem 244: 6023-6030.
    • (1969) J Biol Chem , vol.244 , pp. 6023-6030
    • Becker, M.A.1    Tomkins, G.M.2
  • 57
    • 0014670046 scopus 로고
    • Purification and characterization of cysteine synthetase, a bifunctional protein complex, from Salmonella typhimurium
    • Kredich NM, Becker MA, Tomkins GM, (1969) Purification and characterization of cysteine synthetase, a bifunctional protein complex, from Salmonella typhimurium. J Biol Chem 244: 2428-2439.
    • (1969) J Biol Chem , vol.244 , pp. 2428-2439
    • Kredich, N.M.1    Becker, M.A.2    Tomkins, G.M.3
  • 58
    • 0017594294 scopus 로고
    • Initial kinetic characterization of the multienzyme complex, cysteine synthetase
    • Cook PF, Wedding RT, (1977) Initial kinetic characterization of the multienzyme complex, cysteine synthetase. Arch Biochem Biophys 178: 293-302.
    • (1977) Arch Biochem Biophys , vol.178 , pp. 293-302
    • Cook, P.F.1    Wedding, R.T.2
  • 59
    • 0018265576 scopus 로고
    • Cysteine synthetase from Salmonella typhimurium LT-2. Aggregation, kinetic behavior, and effect of modifiers
    • Cook PF, Wedding RT, (1978) Cysteine synthetase from Salmonella typhimurium LT-2. Aggregation, kinetic behavior, and effect of modifiers. J Biol Chem 253: 7874-7879.
    • (1978) J Biol Chem , vol.253 , pp. 7874-7879
    • Cook, P.F.1    Wedding, R.T.2
  • 60
    • 0032610016 scopus 로고    scopus 로고
    • Purification and characterization of serine acetyltransferase from Escherichia coli partially truncated at the C-terminal region
    • Mino K, Yamanoue T, Sakiyama T, Eisaki N, Matsuyama A, et al. (1999) Purification and characterization of serine acetyltransferase from Escherichia coli partially truncated at the C-terminal region. Biosci Biotechnol Biochem 63: 168-179.
    • (1999) Biosci Biotechnol Biochem , vol.63 , pp. 168-179
    • Mino, K.1    Yamanoue, T.2    Sakiyama, T.3    Eisaki, N.4    Matsuyama, A.5
  • 61
    • 0034278207 scopus 로고    scopus 로고
    • Characteristics of serine acetyltransferase from Escherichia coli deleting different lengths of amino acid residues from the C-terminus
    • Mino K, Hiraoka K, Imamura K, Sakiyama T, Eisaki N, et al. (2000) Characteristics of serine acetyltransferase from Escherichia coli deleting different lengths of amino acid residues from the C-terminus. Biosci Biotechnol Biochem 64: 1874-1880.
    • (2000) Biosci Biotechnol Biochem , vol.64 , pp. 1874-1880
    • Mino, K.1    Hiraoka, K.2    Imamura, K.3    Sakiyama, T.4    Eisaki, N.5
  • 62
    • 0034251888 scopus 로고    scopus 로고
    • Effects of bienzyme complex formation of cysteine synthetase from Escherichia coli on some properties and kinetics
    • Mino K, Yamanoue T, Sakiyama T, Eisaki N, Matsuyama A, et al. (2000) Effects of bienzyme complex formation of cysteine synthetase from Escherichia coli on some properties and kinetics. Biosci Biotechnol Biochem 64: 1628-1640.
    • (2000) Biosci Biotechnol Biochem , vol.64 , pp. 1628-1640
    • Mino, K.1    Yamanoue, T.2    Sakiyama, T.3    Eisaki, N.4    Matsuyama, A.5
  • 63
    • 84863022494 scopus 로고    scopus 로고
    • Three-stage assembly of the cysteine synthase complex from Escherichia coli
    • Wang T, Leyh TS, (2012) Three-stage assembly of the cysteine synthase complex from Escherichia coli. J Biol Chem 287: 4360-4367.
    • (2012) J Biol Chem , vol.287 , pp. 4360-4367
    • Wang, T.1    Leyh, T.S.2
  • 64
    • 77951212184 scopus 로고    scopus 로고
    • A two-step process controls the formation of the bienzyme cysteine synthase complex
    • Salsi E, Campanini B, Bettati S, Raboni S, Roderick SL, et al. (2010) A two-step process controls the formation of the bienzyme cysteine synthase complex. J Biol Chem 285: 12813-12822.
    • (2010) J Biol Chem , vol.285 , pp. 12813-12822
    • Salsi, E.1    Campanini, B.2    Bettati, S.3    Raboni, S.4    Roderick, S.L.5
  • 65
    • 32344445371 scopus 로고    scopus 로고
    • On the interaction site of serine acetyltransferase in the cysteine synthase complex from Escherichia coli
    • Zhao C, Moriga Y, Feng B, Kumada Y, Imanaka H, et al. (2006) On the interaction site of serine acetyltransferase in the cysteine synthase complex from Escherichia coli. Biochem Biophys Res Commun 341: 911-916.
    • (2006) Biochem Biophys Res Commun , vol.341 , pp. 911-916
    • Zhao, C.1    Moriga, Y.2    Feng, B.3    Kumada, Y.4    Imanaka, H.5
  • 66
    • 84864865811 scopus 로고    scopus 로고
    • The narrow active-site cleft of O-acetylserine sulfhydrylase from Leishmania donovani allows complex formation with serine acetyltransferases with a range of C-terminal sequences
    • Raj I, Kumar S, Gourinath S, (2012) The narrow active-site cleft of O-acetylserine sulfhydrylase from Leishmania donovani allows complex formation with serine acetyltransferases with a range of C-terminal sequences. Acta Crystallogr D Biol Crystallogr 68: 909-919.
    • (2012) Acta Crystallogr D Biol Crystallogr , vol.68 , pp. 909-919
    • Raj, I.1    Kumar, S.2    Gourinath, S.3
  • 67
    • 84873723914 scopus 로고    scopus 로고
    • Discovery of novel inhibitors targeting the Mycobacterium tuberculosis O-acetylserine sulfhydrylase (CysK1) using virtual high-throughput screening
    • Kumar JVU, Poyraz O, Saxena S, Schnell R, Yogeeswari P, et al. (2013) Discovery of novel inhibitors targeting the Mycobacterium tuberculosis O-acetylserine sulfhydrylase (CysK1) using virtual high-throughput screening. Bioorg Med Chem Lett 23: 1182-1186.
    • (2013) Bioorg Med Chem Lett , vol.23 , pp. 1182-1186
    • Kumar, J.V.U.1    Poyraz, O.2    Saxena, S.3    Schnell, R.4    Yogeeswari, P.5
  • 68
    • 13844312649 scopus 로고    scopus 로고
    • ZINC-a free database of commercially available compounds for virtual screening
    • Irwin JJ, Shoichet BK, (2005) ZINC-a free database of commercially available compounds for virtual screening. J Chem Inf Model 45: 177-182.
    • (2005) J Chem Inf Model , vol.45 , pp. 177-182
    • Irwin, J.J.1    Shoichet, B.K.2
  • 69
    • 34247263219 scopus 로고    scopus 로고
    • A common reference framework for analyzing/comparing proteins and ligands. Fingerprints for Ligands and Proteins (FLAP): theory and application
    • Baroni M, Cruciani G, Sciabola S, Perruccio F, Mason JS, (2007) A common reference framework for analyzing/comparing proteins and ligands. Fingerprints for Ligands and Proteins (FLAP): theory and application. J Chem Inf Model 47: 279-294.
    • (2007) J Chem Inf Model , vol.47 , pp. 279-294
    • Baroni, M.1    Cruciani, G.2    Sciabola, S.3    Perruccio, F.4    Mason, J.S.5
  • 70
    • 0028854034 scopus 로고
    • Molecular recognition of receptor sites using a genetic algorithm with a description of desolvation
    • Jones G, Willett P, Glen RC, (1995) Molecular recognition of receptor sites using a genetic algorithm with a description of desolvation. J Mol Biol 245: 43-53.
    • (1995) J Mol Biol , vol.245 , pp. 43-53
    • Jones, G.1    Willett, P.2    Glen, R.C.3
  • 71
    • 0031552362 scopus 로고    scopus 로고
    • Development and validation of a genetic algorithm for flexible docking
    • Jones G, Willett P, Glen RC, Leach AR, Taylor R, (1997) Development and validation of a genetic algorithm for flexible docking. J Mol Biol 267: 727-748.
    • (1997) J Mol Biol , vol.267 , pp. 727-748
    • Jones, G.1    Willett, P.2    Glen, R.C.3    Leach, A.R.4    Taylor, R.5
  • 72
    • 0343517556 scopus 로고    scopus 로고
    • Hydrophobicity: is LogPo/w more than the sum of its parts?
    • Kellogg EG, Abraham DJ, (2000) Hydrophobicity: is LogPo/w more than the sum of its parts? Eur J Med Chem 35: 651-661.
    • (2000) Eur J Med Chem , vol.35 , pp. 651-661
    • Kellogg, E.G.1    Abraham, D.J.2
  • 73
    • 84873686290 scopus 로고    scopus 로고
    • Drug repositioning by structure-based virtual screening
    • Ma DL, Chan DS, Leung CH, (2013) Drug repositioning by structure-based virtual screening. Chem Soc Rev 42: 2130-2141.
    • (2013) Chem Soc Rev , vol.42 , pp. 2130-2141
    • Ma, D.L.1    Chan, D.S.2    Leung, C.H.3
  • 74
    • 10344230435 scopus 로고    scopus 로고
    • Molecular similarity: a key technique in molecular informatics
    • Bender A, Glen RC, (2004) Molecular similarity: a key technique in molecular informatics. Org Biomol Chem 2: 3204-3218.
    • (2004) Org Biomol Chem , vol.2 , pp. 3204-3218
    • Bender, A.1    Glen, R.C.2
  • 76
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function
    • Morris GM, Goodsell DS, Halliday RS, Huey R, Hart WE, et al. (1998) Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function. Journal of Computational Chemistry 19: 1639-1662.
    • (1998) Journal of Computational Chemistry , vol.19 , pp. 1639-1662
    • Morris, G.M.1    Goodsell, D.S.2    Halliday, R.S.3    Huey, R.4    Hart, W.E.5
  • 77
    • 0036137713 scopus 로고    scopus 로고
    • Automated docking to multiple target structures: incorporation of protein mobility and structural water heterogeneity in AutoDock
    • Osterberg F, Morris GM, Sanner MF, Olson AJ, Goodsell DS, (2002) Automated docking to multiple target structures: incorporation of protein mobility and structural water heterogeneity in AutoDock. Proteins 46: 34-40.
    • (2002) Proteins , vol.46 , pp. 34-40
    • Osterberg, F.1    Morris, G.M.2    Sanner, M.F.3    Olson, A.J.4    Goodsell, D.S.5
  • 78
    • 76149120388 scopus 로고    scopus 로고
    • AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading
    • Trott O, Olson AJ, (2010) AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. J Comput Chem 31: 455-461.
    • (2010) J Comput Chem , vol.31 , pp. 455-461
    • Trott, O.1    Olson, A.J.2
  • 80
    • 0035025191 scopus 로고    scopus 로고
    • DOCK 4.0: search strategies for automated molecular docking of flexible molecule databases
    • Ewing TJ, Makino S, Skillman AG, Kuntz ID, (2001) DOCK 4.0: search strategies for automated molecular docking of flexible molecule databases. J Comput Aided Mol Des 15: 411-428.
    • (2001) J Comput Aided Mol Des , vol.15 , pp. 411-428
    • Ewing, T.J.1    Makino, S.2    Skillman, A.G.3    Kuntz, I.D.4
  • 81
    • 66449110287 scopus 로고    scopus 로고
    • DOCK 6: combining techniques to model RNA-small molecule complexes
    • Lang PT, Brozell SR, Mukherjee S, Pettersen EF, Meng EC, et al. (2009) DOCK 6: combining techniques to model RNA-small molecule complexes. RNA 15: 1219-1230.
    • (2009) RNA , vol.15 , pp. 1219-1230
    • Lang, P.T.1    Brozell, S.R.2    Mukherjee, S.3    Pettersen, E.F.4    Meng, E.C.5
  • 82
    • 0030599010 scopus 로고    scopus 로고
    • A fast flexible docking method using an incremental construction algorithm
    • Rarey M, Kramer B, Lengauer T, Klebe G, (1996) A fast flexible docking method using an incremental construction algorithm. J Mol Biol 261: 470-489.
    • (1996) J Mol Biol , vol.261 , pp. 470-489
    • Rarey, M.1    Kramer, B.2    Lengauer, T.3    Klebe, G.4
  • 83
    • 12144289984 scopus 로고    scopus 로고
    • Glide: a new approach for rapid, accurate docking and scoring. 1. Method and assessment of docking accuracy
    • Friesner RA, Banks JL, Murphy RB, Halgren TA, Klicic JJ, et al. (2004) Glide: a new approach for rapid, accurate docking and scoring. 1. Method and assessment of docking accuracy. J Med Chem 47: 1739-1749.
    • (2004) J Med Chem , vol.47 , pp. 1739-1749
    • Friesner, R.A.1    Banks, J.L.2    Murphy, R.B.3    Halgren, T.A.4    Klicic, J.J.5
  • 86
    • 0037434582 scopus 로고    scopus 로고
    • Surflex: fully automatic flexible molecular docking using a molecular similarity-based search engine
    • Jain AN, (2003) Surflex: fully automatic flexible molecular docking using a molecular similarity-based search engine. J Med Chem 46: 499-511.
    • (2003) J Med Chem , vol.46 , pp. 499-511
    • Jain, A.N.1
  • 87
    • 34247343346 scopus 로고    scopus 로고
    • Surflex-Dock 2.1: Robust performance from ligand energetic modeling, ring flexibility, and knowledge-based search
    • Jain A, (2007) Surflex-Dock 2.1: Robust performance from ligand energetic modeling, ring flexibility, and knowledge-based search. J Comput Aided Mol Des 21: 281-306.
    • (2007) J Comput Aided Mol Des , vol.21 , pp. 281-306
    • Jain, A.1
  • 88
    • 79952779478 scopus 로고    scopus 로고
    • A novel approach for predicting P-glycoprotein (ABCB1) inhibition using molecular interaction fields
    • Broccatelli F, Carosati E, Neri A, Frosini M, Goracci L, et al. (2011) A novel approach for predicting P-glycoprotein (ABCB1) inhibition using molecular interaction fields. J Med Chem 54: 1740-1751.
    • (2011) J Med Chem , vol.54 , pp. 1740-1751
    • Broccatelli, F.1    Carosati, E.2    Neri, A.3    Frosini, M.4    Goracci, L.5
  • 89
    • 34247855958 scopus 로고    scopus 로고
    • Virtual screening for novel openers of pancreatic K(ATP) channels
    • Carosati E, Mannhold R, Wahl P, Hansen JB, Fremming T, et al. (2007) Virtual screening for novel openers of pancreatic K(ATP) channels. J Med Chem 50: 2117-2126.
    • (2007) J Med Chem , vol.50 , pp. 2117-2126
    • Carosati, E.1    Mannhold, R.2    Wahl, P.3    Hansen, J.B.4    Fremming, T.5
  • 90
    • 52449104613 scopus 로고    scopus 로고
    • Discovery of novel and cardioselective diltiazem-like calcium channel blockers via virtual screening
    • Carosati E, Budriesi R, Ioan P, Ugenti MP, Frosini M, et al. (2008) Discovery of novel and cardioselective diltiazem-like calcium channel blockers via virtual screening. J Med Chem 51: 5552-5565.
    • (2008) J Med Chem , vol.51 , pp. 5552-5565
    • Carosati, E.1    Budriesi, R.2    Ioan, P.3    Ugenti, M.P.4    Frosini, M.5
  • 91
    • 73749087803 scopus 로고    scopus 로고
    • Molecular fields in drug discovery: getting old or reaching maturity?
    • Cross S, Cruciani G, (2010) Molecular fields in drug discovery: getting old or reaching maturity? Drug Discov Today 15: 23-32.
    • (2010) Drug Discov Today , vol.15 , pp. 23-32
    • Cross, S.1    Cruciani, G.2
  • 92
    • 78449259019 scopus 로고    scopus 로고
    • Ligand-based virtual screening and ADME-tox guided approach to identify triazolo-quinoxalines as folate cycle inhibitors
    • Carosati E, Sforna G, Pippi M, Marverti G, Ligabue A, et al. (2010) Ligand-based virtual screening and ADME-tox guided approach to identify triazolo-quinoxalines as folate cycle inhibitors. Bioorg Med Chem 18: 7773-7785.
    • (2010) Bioorg Med Chem , vol.18 , pp. 7773-7785
    • Carosati, E.1    Sforna, G.2    Pippi, M.3    Marverti, G.4    Ligabue, A.5
  • 93
    • 78651073856 scopus 로고    scopus 로고
    • Discovery of novel inhibitors of the NorA multidrug transporter of Staphylococcus aureus
    • Brincat JP, Carosati E, Sabatini S, Manfroni G, Fravolini A, et al. (2011) Discovery of novel inhibitors of the NorA multidrug transporter of Staphylococcus aureus. J Med Chem 54: 354-365.
    • (2011) J Med Chem , vol.54 , pp. 354-365
    • Brincat, J.P.1    Carosati, E.2    Sabatini, S.3    Manfroni, G.4    Fravolini, A.5
  • 94
    • 84877651696 scopus 로고    scopus 로고
    • Ligand-, structure- and pharmacophore-based molecular fingerprints: a case study on adenosine A(1), A (2A), A (2B), and A (3) receptor antagonists
    • Sirci F, Goracci L, Rodriguez D, van Muijlwijk-Koezen J, Gutierrez-de-Teran H, et al. (2012) Ligand-, structure- and pharmacophore-based molecular fingerprints: a case study on adenosine A(1), A (2A), A (2B), and A (3) receptor antagonists. J Comput Aided Mol Des 26: 1247-1266.
    • (2012) J Comput Aided Mol Des , vol.26 , pp. 1247-1266
    • Sirci, F.1    Goracci, L.2    Rodriguez, D.3    van Muijlwijk-Koezen, J.4    Gutierrez-de-Teran, H.5
  • 95
    • 84867812471 scopus 로고    scopus 로고
    • GRID-based three-dimensional pharmacophores II: PharmBench, a benchmark data set for evaluating pharmacophore elucidation methods
    • Cross S, Ortuso F, Baroni M, Costa G, Distinto S, et al. (2012) GRID-based three-dimensional pharmacophores II: PharmBench, a benchmark data set for evaluating pharmacophore elucidation methods. J Chem Inf Model 52: 2599-2608.
    • (2012) J Chem Inf Model , vol.52 , pp. 2599-2608
    • Cross, S.1    Ortuso, F.2    Baroni, M.3    Costa, G.4    Distinto, S.5
  • 96
    • 84867763360 scopus 로고    scopus 로고
    • GRID-based three-dimensional pharmacophores I: FLAPpharm, a novel approach for pharmacophore elucidation
    • Cross S, Baroni M, Goracci L, Cruciani G, (2012) GRID-based three-dimensional pharmacophores I: FLAPpharm, a novel approach for pharmacophore elucidation. J Chem Inf Model 52: 2587-2598.
    • (2012) J Chem Inf Model , vol.52 , pp. 2587-2598
    • Cross, S.1    Baroni, M.2    Goracci, L.3    Cruciani, G.4
  • 97
    • 84871596792 scopus 로고    scopus 로고
    • Virtual Fragment Screening: Discovery of Histamine H3 Receptor Ligands Using Ligand-Based and Protein-Based Molecular Fingerprints
    • Sirci F, Istyastono EP, Vischer HF, Kooistra AJ, Nijmeijer S, et al. (2012) Virtual Fragment Screening: Discovery of Histamine H3 Receptor Ligands Using Ligand-Based and Protein-Based Molecular Fingerprints. J Chem Inf Model 52: 3308-3324.
    • (2012) J Chem Inf Model , vol.52 , pp. 3308-3324
    • Sirci, F.1    Istyastono, E.P.2    Vischer, H.F.3    Kooistra, A.J.4    Nijmeijer, S.5
  • 98
    • 84870013070 scopus 로고    scopus 로고
    • Inhibitor of ovarian cancer cells growth by virtual screening: a new thiazole derivative targeting human thymidylate synthase
    • Carosati E, Tochowicz A, Marverti G, Guaitoli G, Benedetti P, et al. (2012) Inhibitor of ovarian cancer cells growth by virtual screening: a new thiazole derivative targeting human thymidylate synthase. J Med Chem 55: 10272-10276.
    • (2012) J Med Chem , vol.55 , pp. 10272-10276
    • Carosati, E.1    Tochowicz, A.2    Marverti, G.3    Guaitoli, G.4    Benedetti, P.5
  • 99
    • 77955552577 scopus 로고    scopus 로고
    • Extending pKa prediction accuracy: high-throughput pKa measurements to understand pKa modulation of new chemical series
    • Milletti F, Storchi L, Goracci L, Bendels S, Wagner B, et al. (2010) Extending pKa prediction accuracy: high-throughput pKa measurements to understand pKa modulation of new chemical series. Eur J Med Chem 45: 4270-4279.
    • (2010) Eur J Med Chem , vol.45 , pp. 4270-4279
    • Milletti, F.1    Storchi, L.2    Goracci, L.3    Bendels, S.4    Wagner, B.5
  • 100
    • 61949390938 scopus 로고    scopus 로고
    • Tautomer enumeration and stability prediction for virtual screening on large chemical databases
    • Milletti F, Storchi L, Sforna G, Cross S, Cruciani G, (2009) Tautomer enumeration and stability prediction for virtual screening on large chemical databases. J Chem Inf Model 49: 68-75.
    • (2009) J Chem Inf Model , vol.49 , pp. 68-75
    • Milletti, F.1    Storchi, L.2    Sforna, G.3    Cross, S.4    Cruciani, G.5
  • 101
    • 37249023309 scopus 로고    scopus 로고
    • New and original pKa prediction method using grid molecular interaction fields
    • Milletti F, Storchi L, Sforna G, Cruciani G, (2007) New and original pKa prediction method using grid molecular interaction fields. J Chem Inf Model 47: 2172-2181.
    • (2007) J Chem Inf Model , vol.47 , pp. 2172-2181
    • Milletti, F.1    Storchi, L.2    Sforna, G.3    Cruciani, G.4
  • 102
    • 0024583269 scopus 로고
    • The role of hydrogen-bonds in drug binding
    • Wade R, Goodford P, (1989) The role of hydrogen-bonds in drug binding. Prog Clin Biol Res 289: 433-444.
    • (1989) Prog Clin Biol Res , vol.289 , pp. 433-444
    • Wade, R.1    Goodford, P.2
  • 103
    • 77956019866 scopus 로고    scopus 로고
    • FLAP: GRID molecular interaction fields in virtual screening. validation using the DUD data set
    • Cross S, Baroni M, Carosati E, Benedetti P, Clementi S, (2010) FLAP: GRID molecular interaction fields in virtual screening. validation using the DUD data set. J Chem Inf Model 50: 1442-1450.
    • (2010) J Chem Inf Model , vol.50 , pp. 1442-1450
    • Cross, S.1    Baroni, M.2    Carosati, E.3    Benedetti, P.4    Clementi, S.5
  • 104
    • 0035055493 scopus 로고    scopus 로고
    • Very empirical treatment of solvation and entropy: a force field derived from log Po/w
    • Kellogg GE, Burnett JC, Abraham DJ, (2001) Very empirical treatment of solvation and entropy: a force field derived from log Po/w. J Comput Aided Mol Des 15: 381-393.
    • (2001) J Comput Aided Mol Des , vol.15 , pp. 381-393
    • Kellogg, G.E.1    Burnett, J.C.2    Abraham, D.J.3
  • 105
    • 0037030649 scopus 로고    scopus 로고
    • Simple, intuitive calculations of free energy of binding for protein-ligand complexes. 1. Models without explicit constrained water
    • Cozzini P, Fornabaio M, Marabotti A, Abraham DJ, Kellogg GE, et al. (2002) Simple, intuitive calculations of free energy of binding for protein-ligand complexes. 1. Models without explicit constrained water. J Med Chem 45: 2469-2483.
    • (2002) J Med Chem , vol.45 , pp. 2469-2483
    • Cozzini, P.1    Fornabaio, M.2    Marabotti, A.3    Abraham, D.J.4    Kellogg, G.E.5
  • 107
    • 33645106609 scopus 로고    scopus 로고
    • Mapping the energetics of water-protein and water-ligand interactions with the "natural" HINT forcefield: predictive tools for characterizing the roles of water in biomolecules
    • Amadasi A, Spyrakis F, Cozzini P, Abraham DJ, Kellogg GE, et al. (2006) Mapping the energetics of water-protein and water-ligand interactions with the "natural" HINT forcefield: predictive tools for characterizing the roles of water in biomolecules. J Mol Biol 358: 289-309.
    • (2006) J Mol Biol , vol.358 , pp. 289-309
    • Amadasi, A.1    Spyrakis, F.2    Cozzini, P.3    Abraham, D.J.4    Kellogg, G.E.5
  • 108
    • 79251577981 scopus 로고    scopus 로고
    • Applying an empirical hydropathic forcefield in refinement may improve low-resolution protein X-ray crystal structures
    • Koparde VN, Scarsdale JN, Kellogg GE, (2011) Applying an empirical hydropathic forcefield in refinement may improve low-resolution protein X-ray crystal structures. PLoS One 6: e15920.
    • (2011) PLoS One , vol.6
    • Koparde, V.N.1    Scarsdale, J.N.2    Kellogg, G.E.3
  • 109
    • 84864621172 scopus 로고    scopus 로고
    • Structural Analysis of the Substrate Recognition Mechanism in O-Phosphoserine Sulfhydrylase from the Hyperthermophilic Archaeon Aeropyrum pernix K1
    • Nakamura T, Kawai Y, Kunimoto K, Iwasaki Y, Nishii K, et al. (2012) Structural Analysis of the Substrate Recognition Mechanism in O-Phosphoserine Sulfhydrylase from the Hyperthermophilic Archaeon Aeropyrum pernix K1. J Mol Biol 422: 33-44.
    • (2012) J Mol Biol , vol.422 , pp. 33-44
    • Nakamura, T.1    Kawai, Y.2    Kunimoto, K.3    Iwasaki, Y.4    Nishii, K.5
  • 110
    • 84878660678 scopus 로고    scopus 로고
    • Correct Protonation States and Relevant Waters = Better Computational Simulations?
    • Spyrakis F, Dellafiora L, Da C, Kellogg GE, Cozzini P, (2013) Correct Protonation States and Relevant Waters = Better Computational Simulations? Curr Pharm Des. 19: 4291-4309.
    • (2013) Curr Pharm Des , vol.19 , pp. 4291-4309
    • Spyrakis, F.1    Dellafiora, L.2    Da, C.3    Kellogg, G.E.4    Cozzini, P.5
  • 111
    • 4143081344 scopus 로고    scopus 로고
    • Simple, intuitive calculations of free energy of binding for protein-ligand complexes. 3. The free energy contribution of structural water molecules in HIV-1 protease complexes
    • Fornabaio M, Spyrakis F, Mozzarelli A, Cozzini P, Abraham DJ, et al. (2004) Simple, intuitive calculations of free energy of binding for protein-ligand complexes. 3. The free energy contribution of structural water molecules in HIV-1 protease complexes. J Med Chem 47: 4507-4516.
    • (2004) J Med Chem , vol.47 , pp. 4507-4516
    • Fornabaio, M.1    Spyrakis, F.2    Mozzarelli, A.3    Cozzini, P.4    Abraham, D.J.5
  • 112
    • 84883167771 scopus 로고    scopus 로고
    • Structure-Guided Design of Novel Thiazolidine Inhibitors of O-Acetyl Serine Sulfhydrylase from Mycobacterium tuberculosis
    • Poyraz O, Jeankumar VU, Saxena S, Schnell R, Haraldsson M, et al. (2013) Structure-Guided Design of Novel Thiazolidine Inhibitors of O-Acetyl Serine Sulfhydrylase from Mycobacterium tuberculosis. J Med Chem 56: 6457-6466.
    • (2013) J Med Chem , vol.56 , pp. 6457-6466
    • Poyraz, O.1    Jeankumar, V.U.2    Saxena, S.3    Schnell, R.4    Haraldsson, M.5
  • 114
    • 0014669977 scopus 로고
    • The purification and characterization of O-acetylserine sulfhydrylase-A from Salmonella typhimurium
    • Becker MA, Kredich NM, Tomkins GM, (1969) The purification and characterization of O-acetylserine sulfhydrylase-A from Salmonella typhimurium. J Biol Chem 244: 2418-2427.
    • (1969) J Biol Chem , vol.244 , pp. 2418-2427
    • Becker, M.A.1    Kredich, N.M.2    Tomkins, G.M.3
  • 115
    • 0022498408 scopus 로고
    • Cloning and characterization of the cysAMK region of Salmonella typhimurium
    • Hulanicka MD, Garrett C, Jagura-Burdzy G, Kredich NM, (1986) Cloning and characterization of the cysAMK region of Salmonella typhimurium. J Bacteriol 168: 322-327.
    • (1986) J Bacteriol , vol.168 , pp. 322-327
    • Hulanicka, M.D.1    Garrett, C.2    Jagura-Burdzy, G.3    Kredich, N.M.4
  • 116
    • 0021090902 scopus 로고
    • Evidence that thiosulfate assimilation by Salmonella typhimurium is catalyzed by cysteine synthase B
    • Nakamura T, Kon Y, Iwahashi H, Eguchi Y, (1983) Evidence that thiosulfate assimilation by Salmonella typhimurium is catalyzed by cysteine synthase B. J Bacteriol. 156: 656-662.
    • (1983) J Bacteriol , vol.156 , pp. 656-662
    • Nakamura, T.1    Kon, Y.2    Iwahashi, H.3    Eguchi, Y.4
  • 117
    • 84861120403 scopus 로고    scopus 로고
    • Enhancement of thioredoxin/glutaredoxin-mediated L-cysteine synthesis from S-sulfocysteine increases L-cysteine production in Escherichia coli
    • Nakatani T, Ohtsu I, Nonaka G, Wiriyathanawudhiwong N, Morigasaki S, et al. (2012) Enhancement of thioredoxin/glutaredoxin-mediated L-cysteine synthesis from S-sulfocysteine increases L-cysteine production in Escherichia coli. Microb Cell Fact 11: 62.
    • (2012) Microb Cell Fact , vol.11 , pp. 62
    • Nakatani, T.1    Ohtsu, I.2    Nonaka, G.3    Wiriyathanawudhiwong, N.4    Morigasaki, S.5
  • 118
    • 84857892780 scopus 로고    scopus 로고
    • Identification of a target cell permissive factor required for contact-dependent growth inhibition (CDI)
    • Diner EJ, Beck CM, Webb JS, Low DA, Hayes CS, (2012) Identification of a target cell permissive factor required for contact-dependent growth inhibition (CDI). Genes Dev 26: 515-525.
    • (2012) Genes Dev , vol.26 , pp. 515-525
    • Diner, E.J.1    Beck, C.M.2    Webb, J.S.3    Low, D.A.4    Hayes, C.S.5
  • 119
    • 78549266157 scopus 로고    scopus 로고
    • A widespread family of polymorphic contact-dependent toxin delivery systems in bacteria
    • Aoki SK, Diner EJ, de Roodenbeke CT, Burgess BR, Poole SJ, et al. (2010) A widespread family of polymorphic contact-dependent toxin delivery systems in bacteria. Nature 468: 439-442.
    • (2010) Nature , vol.468 , pp. 439-442
    • Aoki, S.K.1    Diner, E.J.2    de Roodenbeke, C.T.3    Burgess, B.R.4    Poole, S.J.5
  • 120
    • 0033995794 scopus 로고    scopus 로고
    • Sulfur metabolism in Escherichia coli and related bacteria: facts and fiction
    • Sekowska A, Kung HF, Danchin A, (2000) Sulfur metabolism in Escherichia coli and related bacteria: facts and fiction. J Mol Microbiol Biotechnol 2: 145-177.
    • (2000) J Mol Microbiol Biotechnol , vol.2 , pp. 145-177
    • Sekowska, A.1    Kung, H.F.2    Danchin, A.3
  • 121
    • 44349161838 scopus 로고    scopus 로고
    • Rv2131c from Mycobacterium tuberculosis is a CysQ 3′-phosphoadenosine-5′-phosphatase
    • Hatzios SK, Iavarone AT, Bertozzi CR, (2008) Rv2131c from Mycobacterium tuberculosis is a CysQ 3′-phosphoadenosine-5′-phosphatase. Biochemistry 47: 5823-5831.
    • (2008) Biochemistry , vol.47 , pp. 5823-5831
    • Hatzios, S.K.1    Iavarone, A.T.2    Bertozzi, C.R.3
  • 122
    • 3042581007 scopus 로고    scopus 로고
    • Flexible structure alignment by chaining aligned fragment pairs allowing twists
    • Ye Y, Godzik A, (2003) Flexible structure alignment by chaining aligned fragment pairs allowing twists. Bioinformatics 19Suppl 2: ii246-255.
    • (2003) Bioinformatics , vol.19
    • Ye, Y.1    Godzik, A.2
  • 123
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: analysis of multiple sequence alignments in PostScript
    • Gouet P, Courcelle E, Stuart DI, Metoz F, (1999) ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics 15: 305-308.
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4
  • 124
    • 80054911951 scopus 로고    scopus 로고
    • LigPlot+: multiple ligand-protein interaction diagrams for drug discovery
    • Laskowski RA, Swindells MB, (2011) LigPlot+: multiple ligand-protein interaction diagrams for drug discovery. J Chem Inf Model 51: 2778-2786.
    • (2011) J Chem Inf Model , vol.51 , pp. 2778-2786
    • Laskowski, R.A.1    Swindells, M.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.