메뉴 건너뛰기




Volumn 74, Issue 6, 2007, Pages 831-840

Inhibition of bacterial cell division protein FtsZ by cinnamaldehyde

Author keywords

Cell division; Cinnamaldehyde; FtsZ; GTPase; Polymerization; Z ring

Indexed keywords

CINNAMALDEHYDE; FTSZ PROTEIN; GUANOSINE TRIPHOSPHATE;

EID: 34547655715     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcp.2007.06.029     Document Type: Article
Times cited : (234)

References (53)
  • 1
    • 33750376659 scopus 로고    scopus 로고
    • The prokaryotic cytoskeleton: a putative target for inhibitors and antibiotics?
    • Vollmer W. The prokaryotic cytoskeleton: a putative target for inhibitors and antibiotics?. Appl Microbiol Biotechnol 73 (2006) 37-47
    • (2006) Appl Microbiol Biotechnol , vol.73 , pp. 37-47
    • Vollmer, W.1
  • 2
    • 0026059127 scopus 로고
    • FtsZ ring structure associated with division in Escherichia coli
    • Bi E.F., and Lutkenhaus J. FtsZ ring structure associated with division in Escherichia coli. Nature 354 (1991) 161-164
    • (1991) Nature , vol.354 , pp. 161-164
    • Bi, E.F.1    Lutkenhaus, J.2
  • 4
    • 0242582382 scopus 로고    scopus 로고
    • Discovery of a small molecule that inhibits cell division by blocking FtsZ, a novel therapeutic target of antibiotics
    • Wang J., Galgoci A., Kodali S., Herath K.B., Jayasuriya H., Dorso K., et al. Discovery of a small molecule that inhibits cell division by blocking FtsZ, a novel therapeutic target of antibiotics. J Biol Chem 278 (2003) 44424-44428
    • (2003) J Biol Chem , vol.278 , pp. 44424-44428
    • Wang, J.1    Galgoci, A.2    Kodali, S.3    Herath, K.B.4    Jayasuriya, H.5    Dorso, K.6
  • 5
    • 29444442409 scopus 로고    scopus 로고
    • Synthesis of antimicrobial natural products targeting FtsZ: (+/-)-dichamanetin and (+/-)-2′ ″-hydroxy-5′ ′-benzylisouvarinol-B
    • Urgaonkar S., La Pierre H.S., Meir I., Lund H., RayChaudhuri D., and Shaw J.T. Synthesis of antimicrobial natural products targeting FtsZ: (+/-)-dichamanetin and (+/-)-2′ ″-hydroxy-5′ ′-benzylisouvarinol-B. Org Lett 7 (2005) 5609-5612
    • (2005) Org Lett , vol.7 , pp. 5609-5612
    • Urgaonkar, S.1    La Pierre, H.S.2    Meir, I.3    Lund, H.4    RayChaudhuri, D.5    Shaw, J.T.6
  • 6
    • 4143110291 scopus 로고    scopus 로고
    • Targeting cell division: small-molecule inhibitors of FtsZ GTPase perturb cytokinetic ring assembly and induce bacterial lethality
    • Margalit D.N., Romberg L., Mets R.B., Hebert A.M., Mitchison T.J., Kirschner M.W., et al. Targeting cell division: small-molecule inhibitors of FtsZ GTPase perturb cytokinetic ring assembly and induce bacterial lethality. Proc Natl Acad Sci USA 101 (2004) 11821-11826
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 11821-11826
    • Margalit, D.N.1    Romberg, L.2    Mets, R.B.3    Hebert, A.M.4    Mitchison, T.J.5    Kirschner, M.W.6
  • 7
    • 29244432515 scopus 로고    scopus 로고
    • Sanguinarine blocks cytokinesis in bacteria by inhibiting FtsZ assembly and bundling
    • Beuria T.K., Santra M.K., and Panda D. Sanguinarine blocks cytokinesis in bacteria by inhibiting FtsZ assembly and bundling. Biochemistry 44 (2005) 16584-16593
    • (2005) Biochemistry , vol.44 , pp. 16584-16593
    • Beuria, T.K.1    Santra, M.K.2    Panda, D.3
  • 8
    • 33750360813 scopus 로고    scopus 로고
    • A 4-aminofurazan derivative - A189 - inhibits assembly of bacterial cell division protein FtsZ in vitro and in vivo
    • Ito H., Ura A., Oyamada Y., Tanitame A., Yoshida H., Yamada S., et al. A 4-aminofurazan derivative - A189 - inhibits assembly of bacterial cell division protein FtsZ in vitro and in vivo. Microbiol Immunol 50 (2006) 759-764
    • (2006) Microbiol Immunol , vol.50 , pp. 759-764
    • Ito, H.1    Ura, A.2    Oyamada, Y.3    Tanitame, A.4    Yoshida, H.5    Yamada, S.6
  • 9
    • 30044452328 scopus 로고    scopus 로고
    • Antimicrobial activities of eugenol and cinnamaldehyde against the human gastric pathogen Helicobacter pylori
    • Ali S.M., Khan A.A., Ahmed I., Musaddiq M., Ahmed K.S., Polasa H., et al. Antimicrobial activities of eugenol and cinnamaldehyde against the human gastric pathogen Helicobacter pylori. Ann Clin Microbiol Antimicrob 4 (2005) 20
    • (2005) Ann Clin Microbiol Antimicrob , vol.4 , pp. 20
    • Ali, S.M.1    Khan, A.A.2    Ahmed, I.3    Musaddiq, M.4    Ahmed, K.S.5    Polasa, H.6
  • 10
    • 29844458278 scopus 로고    scopus 로고
    • Simultaneous determination of cinnamaldehyde, eugenol and paeonol in traditional Chinese medicinal preparations by capillary GC-FID
    • Yu B.S., Lai S.G., and Tan Q.L. Simultaneous determination of cinnamaldehyde, eugenol and paeonol in traditional Chinese medicinal preparations by capillary GC-FID. Chem Pharm Bull 54 (2006) 114-116
    • (2006) Chem Pharm Bull , vol.54 , pp. 114-116
    • Yu, B.S.1    Lai, S.G.2    Tan, Q.L.3
  • 11
    • 33845370282 scopus 로고    scopus 로고
    • Cinnamaldehyde induces endothelium-dependent and -independent vasorelaxant action on isolated rat aorta
    • Yanaga A., Goto H., Nakagawa T., Hikiami H., Shibahara N., and Shimada Y. Cinnamaldehyde induces endothelium-dependent and -independent vasorelaxant action on isolated rat aorta. Biol Pharm Bull 29 (2006) 2415-2418
    • (2006) Biol Pharm Bull , vol.29 , pp. 2415-2418
    • Yanaga, A.1    Goto, H.2    Nakagawa, T.3    Hikiami, H.4    Shibahara, N.5    Shimada, Y.6
  • 12
    • 16244397279 scopus 로고    scopus 로고
    • A toxologic and dermatologic assessment of cinnamyl alcohol, cinnamaldehyde and cinnamic acid when used as fragrance ingredients. The RIFM expert panel
    • Bickers D., Calow P., Greim H., Hanifin J.M., Rogers A.E., Saurat J.H., et al. A toxologic and dermatologic assessment of cinnamyl alcohol, cinnamaldehyde and cinnamic acid when used as fragrance ingredients. The RIFM expert panel. Food Chem Toxicol 43 (2005) 799-836
    • (2005) Food Chem Toxicol , vol.43 , pp. 799-836
    • Bickers, D.1    Calow, P.2    Greim, H.3    Hanifin, J.M.4    Rogers, A.E.5    Saurat, J.H.6
  • 13
    • 0032102145 scopus 로고    scopus 로고
    • Reduction of Escherichia coli O157:H7 populations in soy sauce, a fermented seasoning
    • Masuda S., Hara-Kudo Y., and Kumagai S. Reduction of Escherichia coli O157:H7 populations in soy sauce, a fermented seasoning. J Food Prot 61 (1998) 657-661
    • (1998) J Food Prot , vol.61 , pp. 657-661
    • Masuda, S.1    Hara-Kudo, Y.2    Kumagai, S.3
  • 14
    • 0026495752 scopus 로고
    • Antibacterial activity of essential oil components
    • Moleyar V., and Narasimham P. Antibacterial activity of essential oil components. Int J Food Microbiol 16 (1992) 337-342
    • (1992) Int J Food Microbiol , vol.16 , pp. 337-342
    • Moleyar, V.1    Narasimham, P.2
  • 15
    • 0003053267 scopus 로고    scopus 로고
    • Growth-inhibiting effects of Cinnamomum cassia bark-derived materials on human intestinal bacteria
    • Lee H.S., and Ahn Y.J. Growth-inhibiting effects of Cinnamomum cassia bark-derived materials on human intestinal bacteria. J Agric Food Chem 46 (1998) 8-12
    • (1998) J Agric Food Chem , vol.46 , pp. 8-12
    • Lee, H.S.1    Ahn, Y.J.2
  • 16
    • 0038480090 scopus 로고    scopus 로고
    • Bacteriocidal effects and inhibition of cell separation of cinnamic aldehyde on Bacillus cereus
    • Kwon J.A., Yu C.B., and Park H.D. Bacteriocidal effects and inhibition of cell separation of cinnamic aldehyde on Bacillus cereus. Lett Appl Microbiol 37 (2003) 61-65
    • (2003) Lett Appl Microbiol , vol.37 , pp. 61-65
    • Kwon, J.A.1    Yu, C.B.2    Park, H.D.3
  • 17
    • 0033553844 scopus 로고    scopus 로고
    • Characterization of ligand binding by saturation transfer difference NMR spectroscopy
    • Mayer M., and Meyer B. Characterization of ligand binding by saturation transfer difference NMR spectroscopy. Angew Chem Int Ed 38 (1999) 1784-1788
    • (1999) Angew Chem Int Ed , vol.38 , pp. 1784-1788
    • Mayer, M.1    Meyer, B.2
  • 18
    • 0037463033 scopus 로고    scopus 로고
    • NMR spectroscopy techniques for screening and identifying ligand binding to protein receptors
    • Meyer B., and Peters T. NMR spectroscopy techniques for screening and identifying ligand binding to protein receptors. Angew Chem Int Ed 42 (2003) 864-890
    • (2003) Angew Chem Int Ed , vol.42 , pp. 864-890
    • Meyer, B.1    Peters, T.2
  • 19
    • 0346786324 scopus 로고    scopus 로고
    • Saturation transfer difference NMR and computational modelling of a sialoadhesin-sialyl lactose complex
    • Bhunia A., Jayalakshmi V., Benie A.J., Schuster O., Kelm S., Ramakrishna N., et al. Saturation transfer difference NMR and computational modelling of a sialoadhesin-sialyl lactose complex. Carbohydr Res 339 (2004) 259-267
    • (2004) Carbohydr Res , vol.339 , pp. 259-267
    • Bhunia, A.1    Jayalakshmi, V.2    Benie, A.J.3    Schuster, O.4    Kelm, S.5    Ramakrishna, N.6
  • 20
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a Lamarckian genetic algorithm and empirical binding free energy function
    • Morris G.M., Goodsell D.S., Halliday R.S., Huey R., Hart W.E., Belew R.K., et al. Automated docking using a Lamarckian genetic algorithm and empirical binding free energy function. J Comp Chem 19 (1998) 1639-1662
    • (1998) J Comp Chem , vol.19 , pp. 1639-1662
    • Morris, G.M.1    Goodsell, D.S.2    Halliday, R.S.3    Huey, R.4    Hart, W.E.5    Belew, R.K.6
  • 21
    • 0030903133 scopus 로고    scopus 로고
    • Microplate Alamar Blue assay versus BACTEC 460 system, for high-throughput screening of compounds against Mycobacterium tuberculosis and Mycobacterium avium
    • Collins L.A., and Franzblau S.G. Microplate Alamar Blue assay versus BACTEC 460 system, for high-throughput screening of compounds against Mycobacterium tuberculosis and Mycobacterium avium. Antimicrob Agents Chemother 41 (1997) 1004-1009
    • (1997) Antimicrob Agents Chemother , vol.41 , pp. 1004-1009
    • Collins, L.A.1    Franzblau, S.G.2
  • 22
    • 34547716604 scopus 로고    scopus 로고
    • National Committee for Clinical Laboratory Standards. Methods for dilution antimicrobial susceptibility tests for bacteria that grow aerobically, fourth edition: approved standard, M7-A4. Villanova, Pennsylvania: National Committee for Clinical Laboratory Standards, 1997.
  • 23
    • 33646576163 scopus 로고    scopus 로고
    • Inhibition of plant-pathogenic bacteria by short synthetic cecropin A-melittin hybrid peptides
    • Ferre R., Badosa E., Feliu L., Planas M., Montesinos E., and Bardaji E. Inhibition of plant-pathogenic bacteria by short synthetic cecropin A-melittin hybrid peptides. Appl Environ Microbiol. 72 (2006) 3302-3308
    • (2006) Appl Environ Microbiol. , vol.72 , pp. 3302-3308
    • Ferre, R.1    Badosa, E.2    Feliu, L.3    Planas, M.4    Montesinos, E.5    Bardaji, E.6
  • 24
    • 33646568438 scopus 로고    scopus 로고
    • Complete set of ORF clones of Escherichia coli ASKA library (A Complete Set of E. coli K-12 ORF Archive): unique resources for biological research
    • Kitagawa M., Ara T., Arifuzzaman M., Nakamichi T., Inamoto E., Toyonaga H., et al. Complete set of ORF clones of Escherichia coli ASKA library (A Complete Set of E. coli K-12 ORF Archive): unique resources for biological research. DNA Res 12 (2005) 291-299
    • (2005) DNA Res , vol.12 , pp. 291-299
    • Kitagawa, M.1    Ara, T.2    Arifuzzaman, M.3    Nakamichi, T.4    Inamoto, E.5    Toyonaga, H.6
  • 25
    • 0032916717 scopus 로고    scopus 로고
    • Analysis of FtsZ assembly by light scattering and determination of the role of divalent metal cations
    • Mukherjee A., and Lutkenhaus J. Analysis of FtsZ assembly by light scattering and determination of the role of divalent metal cations. J Bacteriol 181 (1999) 823-832
    • (1999) J Bacteriol , vol.181 , pp. 823-832
    • Mukherjee, A.1    Lutkenhaus, J.2
  • 26
    • 0025967969 scopus 로고
    • A malachite green colorimetric assay for protein phosphatase activity
    • Geladopoulos T.P., Sotiroudis T.G., and Evangelopoulos A.E. A malachite green colorimetric assay for protein phosphatase activity. Anal Biochem 192 (1991) 112-116
    • (1991) Anal Biochem , vol.192 , pp. 112-116
    • Geladopoulos, T.P.1    Sotiroudis, T.G.2    Evangelopoulos, A.E.3
  • 27
    • 28644447479 scopus 로고    scopus 로고
    • Deuterium oxide promotes assembly and bundling of FtsZ protofilaments
    • Santra M.K., Dasgupta D., and Panda D. Deuterium oxide promotes assembly and bundling of FtsZ protofilaments. Proteins 61 (2005) 1101-1110
    • (2005) Proteins , vol.61 , pp. 1101-1110
    • Santra, M.K.1    Dasgupta, D.2    Panda, D.3
  • 28
    • 0030815131 scopus 로고    scopus 로고
    • 2+ mediated GTP-dependent dynamic assembly of bacterial cell division protein FtsZ into asters and polymer networks in vitro
    • 2+ mediated GTP-dependent dynamic assembly of bacterial cell division protein FtsZ into asters and polymer networks in vitro. EMBO J 16 (1997) 5455-5463
    • (1997) EMBO J , vol.16 , pp. 5455-5463
    • Yu, X.C.1    Margolin, W.2
  • 29
    • 0037296423 scopus 로고    scopus 로고
    • Bis-ANS binding to tubulin: isothermal titration calorimetry the site-specific proteolysis reveal the GTP-induced structural stability of tubulin
    • Gupta S., Chakraborty S., Poddar A., Sarkar N., Das K.P., and Bhattacharyya B. Bis-ANS binding to tubulin: isothermal titration calorimetry the site-specific proteolysis reveal the GTP-induced structural stability of tubulin. Proteins 50 (2003) 283-289
    • (2003) Proteins , vol.50 , pp. 283-289
    • Gupta, S.1    Chakraborty, S.2    Poddar, A.3    Sarkar, N.4    Das, K.P.5    Bhattacharyya, B.6
  • 30
    • 3042809541 scopus 로고    scopus 로고
    • Saturation transfer difference (STD) 1H-NMR experiments and in silico docking experiments to probe the binding of N-acetylneuraminic acid and derivatives to Vibrio cholerae sialidase
    • Haselhorst T., Wilson J.C., Thomson R.J., McAtamney S., Menting J.G., Coppel R.L., et al. Saturation transfer difference (STD) 1H-NMR experiments and in silico docking experiments to probe the binding of N-acetylneuraminic acid and derivatives to Vibrio cholerae sialidase. Proteins 56 (2004) 346-353
    • (2004) Proteins , vol.56 , pp. 346-353
    • Haselhorst, T.1    Wilson, J.C.2    Thomson, R.J.3    McAtamney, S.4    Menting, J.G.5    Coppel, R.L.6
  • 31
    • 2642593025 scopus 로고    scopus 로고
    • Crystal structure of the bacterial cell-division protein FtsZ
    • Lowe J., and Amos L.A. Crystal structure of the bacterial cell-division protein FtsZ. Nature 391 (1998) 203-206
    • (1998) Nature , vol.391 , pp. 203-206
    • Lowe, J.1    Amos, L.A.2
  • 32
    • 0034897697 scopus 로고    scopus 로고
    • Antibacterial activity of leaf essential oils and their constituents from Cinnamomum osmophloeum
    • Chang S.T., Chen P.F., and Chang S.C. Antibacterial activity of leaf essential oils and their constituents from Cinnamomum osmophloeum. J Ethnopharmacol 77 (2001) 123-127
    • (2001) J Ethnopharmacol , vol.77 , pp. 123-127
    • Chang, S.T.1    Chen, P.F.2    Chang, S.C.3
  • 33
    • 29244431975 scopus 로고    scopus 로고
    • Effects of antimicrobial components of essential oils on growth of Bacillus cereus INRA L2104 in and the sensory qualities of carrot broth
    • Valero M., and Giner M.J. Effects of antimicrobial components of essential oils on growth of Bacillus cereus INRA L2104 in and the sensory qualities of carrot broth. Int J Food Microbiol 106 (2006) 90-94
    • (2006) Int J Food Microbiol , vol.106 , pp. 90-94
    • Valero, M.1    Giner, M.J.2
  • 34
    • 10444254017 scopus 로고    scopus 로고
    • Colorimetric method for identifying plant essential oil components that affect biofilm formation and structure
    • Niu C., and Gilbert E.S. Colorimetric method for identifying plant essential oil components that affect biofilm formation and structure. Appl Environ Microbiol 70 (2004) 6951-6956
    • (2004) Appl Environ Microbiol , vol.70 , pp. 6951-6956
    • Niu, C.1    Gilbert, E.S.2
  • 35
    • 0037407703 scopus 로고    scopus 로고
    • Growth rate-dependent regulation of medial FtsZ ring formation
    • Weart R.B., and Levin P.A. Growth rate-dependent regulation of medial FtsZ ring formation. J Bacteriol 185 (2003) 2826-2834
    • (2003) J Bacteriol , vol.185 , pp. 2826-2834
    • Weart, R.B.1    Levin, P.A.2
  • 37
    • 23444456920 scopus 로고
    • Prevention of drug access to bacterial targets: permeability barriers and active efflux
    • Nikaido H. Prevention of drug access to bacterial targets: permeability barriers and active efflux. Science 264 (1994) 382-388
    • (1994) Science , vol.264 , pp. 382-388
    • Nikaido, H.1
  • 38
    • 0026985714 scopus 로고
    • The antibacterial component from Cinnamomi cortex against a cariogenic bacterium Streptococcus mutans OMZ 176
    • Bae K.H., Ji J.M., and Park K.L. The antibacterial component from Cinnamomi cortex against a cariogenic bacterium Streptococcus mutans OMZ 176. Arch Pharm Res 15 (1992) 239-241
    • (1992) Arch Pharm Res , vol.15 , pp. 239-241
    • Bae, K.H.1    Ji, J.M.2    Park, K.L.3
  • 39
    • 0034331402 scopus 로고    scopus 로고
    • Human skin absorption and metabolism of the contact allergens, cinnamic aldehyde and cinnamic alcohol
    • Smith C.K., Moore C.A., Elahi E.N., Smart A.T., and Hotchkiss S.A. Human skin absorption and metabolism of the contact allergens, cinnamic aldehyde and cinnamic alcohol. Toxicol Appl Pharmacol 168 (2000) 189-199
    • (2000) Toxicol Appl Pharmacol , vol.168 , pp. 189-199
    • Smith, C.K.1    Moore, C.A.2    Elahi, E.N.3    Smart, A.T.4    Hotchkiss, S.A.5
  • 40
    • 33646678386 scopus 로고    scopus 로고
    • Antimicrobial activities of cinnamon oil and cinnamaldehyde from the Chinese medicinal herb Cinnamomum cassia Blume
    • Ooi L.S., Li Y., Kam S.L., Wang H., Wong E.Y., and Ooi V.E. Antimicrobial activities of cinnamon oil and cinnamaldehyde from the Chinese medicinal herb Cinnamomum cassia Blume. Am J Chin Med 34 (2006) 511-522
    • (2006) Am J Chin Med , vol.34 , pp. 511-522
    • Ooi, L.S.1    Li, Y.2    Kam, S.L.3    Wang, H.4    Wong, E.Y.5    Ooi, V.E.6
  • 43
    • 33746503699 scopus 로고    scopus 로고
    • Microencapsulation of Cinnamon Oleoresin by spray drying using different wall materials
    • Vaidya S., Bhosale R., and Singhal R.S. Microencapsulation of Cinnamon Oleoresin by spray drying using different wall materials. Drying Technol. 24 (2006) 983-992
    • (2006) Drying Technol. , vol.24 , pp. 983-992
    • Vaidya, S.1    Bhosale, R.2    Singhal, R.S.3
  • 44
    • 33847635652 scopus 로고    scopus 로고
    • Inhibitory effect of cinnamaldehyde, derived from Cinnamomi cortex, on the growth of influenza A/PR/8 virus in vitro and in vivo
    • Hayashi K., Imanishi N., Kashiwayama Y., Kawano A., Terasawa K., Shimada Y., et al. Inhibitory effect of cinnamaldehyde, derived from Cinnamomi cortex, on the growth of influenza A/PR/8 virus in vitro and in vivo. Antiviral Res 74 (2007) 1-8
    • (2007) Antiviral Res , vol.74 , pp. 1-8
    • Hayashi, K.1    Imanishi, N.2    Kashiwayama, Y.3    Kawano, A.4    Terasawa, K.5    Shimada, Y.6
  • 45
    • 0036836538 scopus 로고    scopus 로고
    • Structural parameterization of the binding enthalpy of small ligands
    • Luque I., and Freire E. Structural parameterization of the binding enthalpy of small ligands. Proteins 49 (2002) 181-190
    • (2002) Proteins , vol.49 , pp. 181-190
    • Luque, I.1    Freire, E.2
  • 46
    • 34547694845 scopus 로고    scopus 로고
    • ITC in drug design
    • Hamacher M., Marcus K., Stühler K., Hall A., Warscheid B., and Meyer H.E. (Eds), Wiley-Liss, New York
    • Moll D., Zimmermann B., Gesellchen F., and Herberg F.W. ITC in drug design. In: Hamacher M., Marcus K., Stühler K., Hall A., Warscheid B., and Meyer H.E. (Eds). Proteomics in drug research (2006), Wiley-Liss, New York 163-164
    • (2006) Proteomics in drug research , pp. 163-164
    • Moll, D.1    Zimmermann, B.2    Gesellchen, F.3    Herberg, F.W.4
  • 47
    • 0015861774 scopus 로고
    • Relationship between the inhibition constant (K1) and the concentration of inhibitor which causes 50 per cent inhibition (I50) of an enzymatic reaction
    • Cheng Y., and Prusoff W.H. Relationship between the inhibition constant (K1) and the concentration of inhibitor which causes 50 per cent inhibition (I50) of an enzymatic reaction. Biochem. Pharmacol 22 (1973) 3099-3108
    • (1973) Biochem. Pharmacol , vol.22 , pp. 3099-3108
    • Cheng, Y.1    Prusoff, W.H.2
  • 48
    • 0029169535 scopus 로고
    • Inhibition of amino acid decarboxylase activity of Enterobacter aerogenes by active components in spices
    • Wendakoon C.N., and Sakaguchi M. Inhibition of amino acid decarboxylase activity of Enterobacter aerogenes by active components in spices. J Food Prot 58 (1995) 280-283
    • (1995) J Food Prot , vol.58 , pp. 280-283
    • Wendakoon, C.N.1    Sakaguchi, M.2
  • 49
    • 0024552774 scopus 로고
    • Interaction of cinnamaldehyde (a sensitizer in fragrance) with protein
    • Weibel H., and Hansen J. Interaction of cinnamaldehyde (a sensitizer in fragrance) with protein. Cont Dermatitis 20 (1989) 161-166
    • (1989) Cont Dermatitis , vol.20 , pp. 161-166
    • Weibel, H.1    Hansen, J.2
  • 50
    • 0016427874 scopus 로고
    • The binding of non specific transition state analogue to alpha chymotrypsin
    • ShultZ R.M., and Cheerva A.C. The binding of non specific transition state analogue to alpha chymotrypsin. FEBS Lett 50 (1975) 47-49
    • (1975) FEBS Lett , vol.50 , pp. 47-49
    • ShultZ, R.M.1    Cheerva, A.C.2
  • 51
    • 0000473838 scopus 로고
    • The geometry of intermolecular interactions in some crystalline fluorine-containing organic compounds
    • Shimoni L., and Glusker J.P. The geometry of intermolecular interactions in some crystalline fluorine-containing organic compounds. Struct Chem 5 (1994) 383-397
    • (1994) Struct Chem , vol.5 , pp. 383-397
    • Shimoni, L.1    Glusker, J.P.2
  • 52
    • 0037080162 scopus 로고    scopus 로고
    • GTP hydrolysis of cell division protein FtsZ: evidence that the active site is formed by the association of monomers
    • Scheffers D.J., de Wit J.G., den Blaauwen T., and Driessen A.J. GTP hydrolysis of cell division protein FtsZ: evidence that the active site is formed by the association of monomers. Biochemistry 41 (2002) 521-529
    • (2002) Biochemistry , vol.41 , pp. 521-529
    • Scheffers, D.J.1    de Wit, J.G.2    den Blaauwen, T.3    Driessen, A.J.4
  • 53
    • 0038610624 scopus 로고    scopus 로고
    • Crystal structure of the SOS cell division inhibitor SulA and in complex with FtsZ
    • Cordell S.C., Robinson E.J.H., and Lowe J. Crystal structure of the SOS cell division inhibitor SulA and in complex with FtsZ. Proc Natl Acad Sci USA 100 (2003) 7889-7894
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 7889-7894
    • Cordell, S.C.1    Robinson, E.J.H.2    Lowe, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.