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Volumn 95, Issue 3, 2008, Pages 1336-1348

Defining the epitope region of a peptide from the Streptomyces coelicolor phosphoenolpyruvate:sugar phosphotransferase system able to bind to the enzyme I

Author keywords

[No Author keywords available]

Indexed keywords

EPITOPE; PEPTIDE; PHOSPHOENOLPYRUVATE PROTEIN PHOSPHOTRANSFERASE; PHOSPHOENOLPYRUVATE SUGAR PHOSPHOTRANSFERASE; PHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE; PHOSPHOTRANSFERASE;

EID: 51049123874     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1529/biophysj.107.126664     Document Type: Article
Times cited : (11)

References (47)
  • 1
    • 10944272743 scopus 로고    scopus 로고
    • Antibacterial resistance worldwide: Causes, challenges and responses
    • Levy, S. B., and B. Marshall. 2004. Antibacterial resistance worldwide: causes, challenges and responses. Nat. Med. 10:S122-S129.
    • (2004) Nat. Med , vol.10
    • Levy, S.B.1    Marshall, B.2
  • 2
    • 33845903833 scopus 로고    scopus 로고
    • Drugs for bad bugs: Confronting the challenges of antibacterial discovery
    • Payne, D. J., M. N. Gwynn, D. J. Holmes, and D. L. Pompliano. 2007. Drugs for bad bugs: confronting the challenges of antibacterial discovery. Nat. Rev. Drug Discov. 6:29-40.
    • (2007) Nat. Rev. Drug Discov , vol.6 , pp. 29-40
    • Payne, D.J.1    Gwynn, M.N.2    Holmes, D.J.3    Pompliano, D.L.4
  • 3
    • 0027291428 scopus 로고
    • Phosphoenolpyruvate carbohydrate phosphotransferase systems of bacteria
    • Postma, P. W., J. W. Lengeler, and G. R. Jacobson. 1993. Phosphoenolpyruvate carbohydrate phosphotransferase systems of bacteria. Microbiol. Rev. 57:543-594.
    • (1993) Microbiol. Rev , vol.57 , pp. 543-594
    • Postma, P.W.1    Lengeler, J.W.2    Jacobson, G.R.3
  • 4
    • 0037046271 scopus 로고    scopus 로고
    • Carbon catabolite repression in bacteria: Choice of the carbon source and autoregulatory limitation of sugar utilization
    • Brückner, R., and F. Titgemeyer. 2002. Carbon catabolite repression in bacteria: choice of the carbon source and autoregulatory limitation of sugar utilization. FEMS Microbiol. Lett. 209:141-148.
    • (2002) FEMS Microbiol. Lett , vol.209 , pp. 141-148
    • Brückner, R.1    Titgemeyer, F.2
  • 5
    • 0037082106 scopus 로고    scopus 로고
    • Enzyme I: The gateway to the bacterial phosphoenolpyruvate:sugar phosphotransferase system
    • Ginsburg, A., and A. Peterkofsky. 2002. Enzyme I: the gateway to the bacterial phosphoenolpyruvate:sugar phosphotransferase system. Arch. Biochem. Biophys. 397:273-278.
    • (2002) Arch. Biochem. Biophys , vol.397 , pp. 273-278
    • Ginsburg, A.1    Peterkofsky, A.2
  • 6
    • 0037046560 scopus 로고    scopus 로고
    • Bentley, S. D., K. F. Chater, A. M. Cerdeno-Tarraga, G. L. Challis, N. R. Thomson, K. D. James, D. E. Harris, M. A. Quail, H. Kieser, D. Harper, A. Bateman, S. Brown, G. Chandra, C. W. Chen, M. Collins, A. Cronin, A. Fraser, A. Goble, J. Hidalgo, T. Hornsby, S. Howarth, C. H. Huang, T. Kieser, L. Larke, L. Murphy, K. Oliver, S. O'Neil, E. Rabbinowitsch, M. A. Rajandream, K. Rutherford, S. Rutter, K. Seeger, D. Saunders, S. Sharp, R. Squares, S. Squares, K. Taylor, T. Warren, A. Wietzorrek, J. Woodward, B. G. Barrell, J. Parkhill, and D. A. Hopwood. 2002. Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2). Nature. 417:141-147.
    • Bentley, S. D., K. F. Chater, A. M. Cerdeno-Tarraga, G. L. Challis, N. R. Thomson, K. D. James, D. E. Harris, M. A. Quail, H. Kieser, D. Harper, A. Bateman, S. Brown, G. Chandra, C. W. Chen, M. Collins, A. Cronin, A. Fraser, A. Goble, J. Hidalgo, T. Hornsby, S. Howarth, C. H. Huang, T. Kieser, L. Larke, L. Murphy, K. Oliver, S. O'Neil, E. Rabbinowitsch, M. A. Rajandream, K. Rutherford, S. Rutter, K. Seeger, D. Saunders, S. Sharp, R. Squares, S. Squares, K. Taylor, T. Warren, A. Wietzorrek, J. Woodward, B. G. Barrell, J. Parkhill, and D. A. Hopwood. 2002. Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2). Nature. 417:141-147.
  • 7
    • 0346690417 scopus 로고    scopus 로고
    • The PTS system of Streptomyces coelicolor: Identification and biochemical analysis of a histidine phosphocarrier protein HPr encoded by the gene ptsH
    • Parche, S., R. Schmid, and F. Titgemeyer. 1999. The PTS system of Streptomyces coelicolor: identification and biochemical analysis of a histidine phosphocarrier protein HPr encoded by the gene ptsH. Eur. J. Biochem. 265:308-317.
    • (1999) Eur. J. Biochem , vol.265 , pp. 308-317
    • Parche, S.1    Schmid, R.2    Titgemeyer, F.3
  • 8
    • 0345687895 scopus 로고    scopus 로고
    • The phosphotransferase system of Streptomyces coelicolor is biased for N-acetylglucosamine metabolism
    • Nothaft, H., D. Dresel, A. Willimek, K. Mahr, M. Niederweis, and F. Titgemeyer. 2003. The phosphotransferase system of Streptomyces coelicolor is biased for N-acetylglucosamine metabolism. J. Bacteriol. 185:7019-7023.
    • (2003) J. Bacteriol , vol.185 , pp. 7019-7023
    • Nothaft, H.1    Dresel, D.2    Willimek, A.3    Mahr, K.4    Niederweis, M.5    Titgemeyer, F.6
  • 9
    • 0037854716 scopus 로고    scopus 로고
    • The histidine-phosphocarrier protein of Streptomyces coelicolor folds by a partially folded species at low pH
    • Fernández-Ballester, G., J. Maya, A. Martin, S. Parche, J. Gómez, F. Titgemeyer, and J. L. Neira. 2003. The histidine-phosphocarrier protein of Streptomyces coelicolor folds by a partially folded species at low pH. Eur. J. Biochem. 270:2254-2267.
    • (2003) Eur. J. Biochem , vol.270 , pp. 2254-2267
    • Fernández-Ballester, G.1    Maya, J.2    Martin, A.3    Parche, S.4    Gómez, J.5    Titgemeyer, F.6    Neira, J.L.7
  • 10
    • 2942544263 scopus 로고    scopus 로고
    • The conformational stability of the Streptomyces coelicolor histidine-phosphocarrier protein. Characterization of cold denaturation and urea-protein interactions
    • Neira, J. L., and J. Gómez. 2004. The conformational stability of the Streptomyces coelicolor histidine-phosphocarrier protein. Characterization of cold denaturation and urea-protein interactions. Eur. J. Biochem. 271:2165-2181.
    • (2004) Eur. J. Biochem , vol.271 , pp. 2165-2181
    • Neira, J.L.1    Gómez, J.2
  • 11
    • 14744269542 scopus 로고    scopus 로고
    • Structure and conformational stability of the enzyme I of Streptomyces coelicolor explored by FTIR and circular dichroism
    • Hurtado-Gómez, E., F. N. Barrera, and J. L. Neira. 2005. Structure and conformational stability of the enzyme I of Streptomyces coelicolor explored by FTIR and circular dichroism. Biophys. Chem. 115:229-233.
    • (2005) Biophys. Chem , vol.115 , pp. 229-233
    • Hurtado-Gómez, E.1    Barrera, F.N.2    Neira, J.L.3
  • 12
    • 33744812700 scopus 로고    scopus 로고
    • Structure, association and conformational stability of the Enzyme I of the Streptomyces coelicolor phosphoenolpyruvate: Sugar phosphotransferase system
    • Hurtado-Gómez, E., G. Fernández-Ballester, H. Nothaft, J. Gómez, F. Titgemeyer, and J. L. Neira. 2006. Structure, association and conformational stability of the Enzyme I of the Streptomyces coelicolor phosphoenolpyruvate: sugar phosphotransferase system. Biophys. J. 90:4592-4604.
    • (2006) Biophys. J , vol.90 , pp. 4592-4604
    • Hurtado-Gómez, E.1    Fernández-Ballester, G.2    Nothaft, H.3    Gómez, J.4    Titgemeyer, F.5    Neira, J.L.6
  • 13
    • 0028360724 scopus 로고
    • The high-resolution structure of the histidine-containing phosphocarrier protein HPr from Escherichia coli determined by restrained molecular dynamics from nuclear magnetic resonance nuclear Overhauser effect data
    • Van Nuland, N. A. J., I. W. Hangyi, R. C. Van Schaik, H. J. C. Berendsen, W. F. Van Gusteren, R. M. Scheek, and G. T. Robillard. 1994. The high-resolution structure of the histidine-containing phosphocarrier protein HPr from Escherichia coli determined by restrained molecular dynamics from nuclear magnetic resonance nuclear Overhauser effect data. J. Mol. Biol. 237:544-559.
    • (1994) J. Mol. Biol , vol.237 , pp. 544-559
    • Van Nuland, N.A.J.1    Hangyi, I.W.2    Van Schaik, R.C.3    Berendsen, H.J.C.4    Van Gusteren, W.F.5    Scheek, R.M.6    Robillard, G.T.7
  • 14
    • 0034829186 scopus 로고    scopus 로고
    • Three-dimensional structure of the histidine-containing phosphocarrier protein (HPr) from Enterococcus faecalis in solution
    • Maurer, T., R. Doker, A. Gorler, W. Hengstenberg, and H. R. Kalbitzer. 2001. Three-dimensional structure of the histidine-containing phosphocarrier protein (HPr) from Enterococcus faecalis in solution. Eur. J. Biochem. 268:635-644.
    • (2001) Eur. J. Biochem , vol.268 , pp. 635-644
    • Maurer, T.1    Doker, R.2    Gorler, A.3    Hengstenberg, W.4    Kalbitzer, H.R.5
  • 15
    • 0026534155 scopus 로고
    • Structure of the histidine-containing phosphocarrier protein HPr from Bacillus subtilis at 2.0-Å resolution
    • Herzberg, O., P. Reddy, S. Sutrina, M. H. Saier, Jr., J. Reizer, and G. Kapadia. 1992. Structure of the histidine-containing phosphocarrier protein HPr from Bacillus subtilis at 2.0-Å resolution. Proc. Natl. Acad. Sci. USA. 89:2499-2503.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 2499-2503
    • Herzberg, O.1    Reddy, P.2    Sutrina, S.3    Saier Jr., M.H.4    Reizer, J.5    Kapadia, G.6
  • 16
    • 0027340388 scopus 로고
    • The 2.0-Å resolution structure of Escherichia coli histidine-containing phosphocarrier protein HPr: A redetermination
    • Jia, Z., J. W. Quail, E. B. Waygood, and L. T. J. Delbaere. 1993. The 2.0-Å resolution structure of Escherichia coli histidine-containing phosphocarrier protein HPr: a redetermination. J. Biol. Chem. 268:22490-22501.
    • (1993) J. Biol. Chem , vol.268 , pp. 22490-22501
    • Jia, Z.1    Quail, J.W.2    Waygood, E.B.3    Delbaere, L.T.J.4
  • 17
    • 0032939176 scopus 로고    scopus 로고
    • Solution structure of the 40,000 Mr phosphoryl transfer complex between the N-terminal domain of enzyme I and HPr
    • Garrett, D. S., Y. J. Seok, A. Peterkofsky, A. M. Gronenborn, and G. M. Clore. 1999. Solution structure of the 40,000 Mr phosphoryl transfer complex between the N-terminal domain of enzyme I and HPr. Nat. Struct. Biol. 6:166-173.
    • (1999) Nat. Struct. Biol , vol.6 , pp. 166-173
    • Garrett, D.S.1    Seok, Y.J.2    Peterkofsky, A.3    Gronenborn, A.M.4    Clore, G.M.5
  • 18
    • 0034595712 scopus 로고    scopus 로고
    • A common interface on histidine-containing phosphocarrier protein for interaction with its partner proteins
    • Wang, G., M. Sondej, D. S. Garret, A. Peterkofsky, and G. M. Clore. 2000. A common interface on histidine-containing phosphocarrier protein for interaction with its partner proteins. J. Biol. Chem. 275:16401-16403.
    • (2000) J. Biol. Chem , vol.275 , pp. 16401-16403
    • Wang, G.1    Sondej, M.2    Garret, D.S.3    Peterkofsky, A.4    Clore, G.M.5
  • 19
    • 0033598701 scopus 로고    scopus 로고
    • Reconstitution studies using the helical and carboxy-terminal domains of enzyme I of the phosphoenolpyruvate: Sugar phosphotransferase system
    • Zhu, P.-P., R. H. Szczepanowski, N. J. Nosworthy, A. Ginsburg, and A. Peterkofsky. 1999. Reconstitution studies using the helical and carboxy-terminal domains of enzyme I of the phosphoenolpyruvate: sugar phosphotransferase system. Biochemistry. 38:15470-15479.
    • (1999) Biochemistry , vol.38 , pp. 15470-15479
    • Zhu, P.-P.1    Szczepanowski, R.H.2    Nosworthy, N.J.3    Ginsburg, A.4    Peterkofsky, A.5
  • 20
    • 0029959329 scopus 로고    scopus 로고
    • The N-terminal domain of Escherichia coli enzyme I of the phosphoenolpyruvate/ glycose phosphotransferase system: Molecular cloning and characterization
    • Chauvin, F., A. Fomenkov, C. R. Johnson, and S. Roseman. 1996. The N-terminal domain of Escherichia coli enzyme I of the phosphoenolpyruvate/ glycose phosphotransferase system: molecular cloning and characterization. Proc. Natl. Acad. Sci. USA. 93:7028-7031.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 7028-7031
    • Chauvin, F.1    Fomenkov, A.2    Johnson, C.R.3    Roseman, S.4
  • 21
    • 0033945086 scopus 로고    scopus 로고
    • Conformational stability changes of the amino terminal domain of enzyme I of the Escherichia coli phosphotransferase system produced by substituting alanine or glutamate for the active-site histidine 189: Implications for phosphorylation effects
    • Ginsburg, A., R. H. Szczepanowski, S. B. Ruvinov, N. J. Nosworthy, M. Sondej, T. C. Umland, and A. Peterkofsky. 2000. Conformational stability changes of the amino terminal domain of enzyme I of the Escherichia coli phosphotransferase system produced by substituting alanine or glutamate for the active-site histidine 189: implications for phosphorylation effects. Protein Sci. 9:1085-1094.
    • (2000) Protein Sci , vol.9 , pp. 1085-1094
    • Ginsburg, A.1    Szczepanowski, R.H.2    Ruvinov, S.B.3    Nosworthy, N.J.4    Sondej, M.5    Umland, T.C.6    Peterkofsky, A.7
  • 22
    • 85031348827 scopus 로고    scopus 로고
    • nd ed. T. E. Creighton, editor. 253-259, Oxford University Press, New York. 253-259.
    • nd ed. T. E. Creighton, editor. 253-259, Oxford University Press, New York. 253-259.
  • 23
    • 2642628181 scopus 로고
    • A two-dimensional nuclear Overhauser experiment with pure absorption phase in four quadrants
    • States, D. J., R. A. Haberkorn, and D. J. Ruben. 1982. A two-dimensional nuclear Overhauser experiment with pure absorption phase in four quadrants. J. Magn. Reson. 48:286-292.
    • (1982) J. Magn. Reson , vol.48 , pp. 286-292
    • States, D.J.1    Haberkorn, R.A.2    Ruben, D.J.3
  • 24
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto, M., V. Saudek, and V. Sklenar. 1992. Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J. Biomol. NMR. 2:661-665.
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 25
    • 5144233105 scopus 로고
    • MLEV-17 based two-dimensional homonuclear magnetization transfer spectroscopy
    • Bax, A., and D. G. Davis. 1985. MLEV-17 based two-dimensional homonuclear magnetization transfer spectroscopy. J. Magn. Reson. 65:355-360.
    • (1985) J. Magn. Reson , vol.65 , pp. 355-360
    • Bax, A.1    Davis, D.G.2
  • 26
    • 33847721421 scopus 로고    scopus 로고
    • The helical structure propensity in the first helix of the histidine phosphocarrier protein of Streptomyces coelicolor
    • Hurtado-Gómez, E., M. Caprini, A. Prieto, and J. L. Neira. 2007. The helical structure propensity in the first helix of the histidine phosphocarrier protein of Streptomyces coelicolor. Protein Pept. Lett. 14:281-290.
    • (2007) Protein Pept. Lett , vol.14 , pp. 281-290
    • Hurtado-Gómez, E.1    Caprini, M.2    Prieto, A.3    Neira, J.L.4
  • 27
    • 0033553844 scopus 로고    scopus 로고
    • Mayer, M., and B. Meyer. 1999. Characterization of ligand binding by saturation transfer difference NMR spectroscopy. Angew. Int. Chem. Int. Ed. 38:1784-1788.
    • Mayer, M., and B. Meyer. 1999. Characterization of ligand binding by saturation transfer difference NMR spectroscopy. Angew. Int. Chem. Int. Ed. 38:1784-1788.
  • 28
    • 0034823890 scopus 로고    scopus 로고
    • Group epitope mapping by saturation transfer difference NMR to identify segments of ligand in direct contact with protein receptor
    • Mayer, M., and B. Meyer. 2001. Group epitope mapping by saturation transfer difference NMR to identify segments of ligand in direct contact with protein receptor. J. Am. Chem. Soc. 123:6108-6117.
    • (2001) J. Am. Chem. Soc , vol.123 , pp. 6108-6117
    • Mayer, M.1    Meyer, B.2
  • 29
    • 0033538283 scopus 로고    scopus 로고
    • Detecting binding affinity to immobilized receptor proteins in compound libraries by HR-MAS STD NMR
    • Klein, J., R. Meinekee, M. Mayer, and B. Meyer. 1999. Detecting binding affinity to immobilized receptor proteins in compound libraries by HR-MAS STD NMR. J. Am. Chem. Soc. 121:5336-5337.
    • (1999) J. Am. Chem. Soc , vol.121 , pp. 5336-5337
    • Klein, J.1    Meinekee, R.2    Mayer, M.3    Meyer, B.4
  • 30
    • 0043032424 scopus 로고    scopus 로고
    • The effect of relaxation on the epitope mapping by saturation transfer difference NMR
    • Yan, J., A. D. Kline, H. Mo, M. J. Shapiro, and E. R. Zartler. 2003. The effect of relaxation on the epitope mapping by saturation transfer difference NMR. J. Magn. Reson. 163:270-276.
    • (2003) J. Magn. Reson , vol.163 , pp. 270-276
    • Yan, J.1    Kline, A.D.2    Mo, H.3    Shapiro, M.J.4    Zartler, E.R.5
  • 31
    • 0036924955 scopus 로고    scopus 로고
    • A simple scheme for the design of solvent-suppression pulses
    • Prost, E., P. Sizun, M. Piotto, and J. M. Nuzillard. 2002. A simple scheme for the design of solvent-suppression pulses. J. Magn. Reson. 159:76-81.
    • (2002) J. Magn. Reson , vol.159 , pp. 76-81
    • Prost, E.1    Sizun, P.2    Piotto, M.3    Nuzillard, J.M.4
  • 32
    • 0037463033 scopus 로고    scopus 로고
    • Meyer, B., and T. Peters. 2003. NMR spectroscopy techniques for screening and identifying ligand binding to protein receptors. Angew Int. Chem. Int. Ed. 42:864-890.
    • Meyer, B., and T. Peters. 2003. NMR spectroscopy techniques for screening and identifying ligand binding to protein receptors. Angew Int. Chem. Int. Ed. 42:864-890.
  • 33
    • 0030886370 scopus 로고    scopus 로고
    • Phage display selection of peptides against enzyme I of the phosphoenolpyruvate-sugar phosphotransferase system (PTS)
    • Mukhija, S., and B. Erni. 1997. Phage display selection of peptides against enzyme I of the phosphoenolpyruvate-sugar phosphotransferase system (PTS). Mol. Microbiol. 25:1159-1166.
    • (1997) Mol. Microbiol , vol.25 , pp. 1159-1166
    • Mukhija, S.1    Erni, B.2
  • 35
    • 0029080864 scopus 로고
    • Thermodynamic mapping of the inhibitor site of the aspartic protease endothiapepsin
    • Gómez, J., and E. Freire. 1995. Thermodynamic mapping of the inhibitor site of the aspartic protease endothiapepsin. J. Mol. Biol. 252:337-350.
    • (1995) J. Mol. Biol , vol.252 , pp. 337-350
    • Gómez, J.1    Freire, E.2
  • 36
    • 34247621230 scopus 로고    scopus 로고
    • Thermodynamic characterization of the protein-protein interaction in the heteromeric Bacillus subtilis pyridoxalphosphate synthase
    • Neuwirth, M., K. Flicker, M. Strohmeier, I. Tews, and P. Macheroux. 2007. Thermodynamic characterization of the protein-protein interaction in the heteromeric Bacillus subtilis pyridoxalphosphate synthase. Biochemistry. 46:5131-5139.
    • (2007) Biochemistry , vol.46 , pp. 5131-5139
    • Neuwirth, M.1    Flicker, K.2    Strohmeier, M.3    Tews, I.4    Macheroux, P.5
  • 37
    • 33745828088 scopus 로고    scopus 로고
    • The monomer/dimer transition of enzyme I of the Escherichia coli phosphotransfrase system
    • Patel, H. V., K. A. Vyas, R. Savtchenko, and S. Roseman. 2006. The monomer/dimer transition of enzyme I of the Escherichia coli phosphotransfrase system. J. Biol. Chem. 281:17570-17578.
    • (2006) J. Biol. Chem , vol.281 , pp. 17570-17578
    • Patel, H.V.1    Vyas, K.A.2    Savtchenko, R.3    Roseman, S.4
  • 38
    • 0041312697 scopus 로고    scopus 로고
    • Diversity of protein-protein interactions
    • Nooren, I. M., and J. M. Thornton. 2003. Diversity of protein-protein interactions. EMBO J. 22:3486-3492.
    • (2003) EMBO J , vol.22 , pp. 3486-3492
    • Nooren, I.M.1    Thornton, J.M.2
  • 39
    • 0042971650 scopus 로고    scopus 로고
    • Molecular interactions mediating T cell antigen recognition
    • van der Merwe, P. A., and S. J. Davis. 2003. Molecular interactions mediating T cell antigen recognition. Annu. Rev. Immunol. 21:659-684.
    • (2003) Annu. Rev. Immunol , vol.21 , pp. 659-684
    • van der Merwe, P.A.1    Davis, S.J.2
  • 40
    • 37249004920 scopus 로고    scopus 로고
    • Reaching for high-hanging fruit in drug discovery at protein-protein interfaces
    • Wells, J. A., and C. L. McClendon. 2007. Reaching for high-hanging fruit in drug discovery at protein-protein interfaces. Nature. 450:1001-1009.
    • (2007) Nature , vol.450 , pp. 1001-1009
    • Wells, J.A.1    McClendon, C.L.2
  • 41
    • 39649098475 scopus 로고    scopus 로고
    • Solution NMR characterization and dynamics of equine infectious anaemia virus matrix protein and its interaction with PIP2
    • Chen, K., I. Bachtiar, G. Piszczek, F. Bouamr, C. Carter, and N. Tjandra. 2008. Solution NMR characterization and dynamics of equine infectious anaemia virus matrix protein and its interaction with PIP2. Biochemistry. 47:1928-1937.
    • (2008) Biochemistry , vol.47 , pp. 1928-1937
    • Chen, K.1    Bachtiar, I.2    Piszczek, G.3    Bouamr, F.4    Carter, C.5    Tjandra, N.6
  • 42
    • 25444463274 scopus 로고    scopus 로고
    • Transient state kinetics of enzyme I of the phosphoenolpyruvate: Glycose phosphotransferase system of Escherichia coli: equilibrium and second order rate constants for the phosphotransfer reactions with phosphoenolpyruvate and HPr
    • Meadow, N. D., R. L. Mattoo, R. S. Savtchenko, and S. Roseman. 2005. Transient state kinetics of enzyme I of the phosphoenolpyruvate: glycose phosphotransferase system of Escherichia coli: equilibrium and second order rate constants for the phosphotransfer reactions with phosphoenolpyruvate and HPr. Biochemistry. 44:12790-12796.
    • (2005) Biochemistry , vol.44 , pp. 12790-12796
    • Meadow, N.D.1    Mattoo, R.L.2    Savtchenko, R.S.3    Roseman, S.4
  • 43
    • 0028050518 scopus 로고
    • Sugar transport by the bacterial phosphotransferase system. Characterization of the Escherichia coli enzyme I monomer/dimer transition kinetics by fluorescence anisotropy I
    • Chauvin, F., L. Brand, and S. Roseman. 1994. Sugar transport by the bacterial phosphotransferase system. Characterization of the Escherichia coli enzyme I monomer/dimer transition kinetics by fluorescence anisotropy I. J. Biol. Chem. 269:20263-20269.
    • (1994) J. Biol. Chem , vol.269 , pp. 20263-20269
    • Chauvin, F.1    Brand, L.2    Roseman, S.3
  • 44
    • 0028147241 scopus 로고
    • Sugar transport by the bacterial phosphotransferase system. Characterization of the Escherichia coli enzyme I monomer/dimer transition kinetics by fluorescence anisotropy II
    • Chauvin, F., L. Brand, and S. Roseman. 1994. Sugar transport by the bacterial phosphotransferase system. Characterization of the Escherichia coli enzyme I monomer/dimer transition kinetics by fluorescence anisotropy II. J. Biol. Chem. 269:20270-20274.
    • (1994) J. Biol. Chem , vol.269 , pp. 20270-20274
    • Chauvin, F.1    Brand, L.2    Roseman, S.3
  • 45
    • 0037154115 scopus 로고    scopus 로고
    • Interdomain interaction and substrate coupling effects of dimerization and conformational stability of Enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system
    • Dimitrova, M. N., R. H. Szczepanowski, S. B. Ruvinov, A. Peterkofsky, and A. Ginsburg. 2002. Interdomain interaction and substrate coupling effects of dimerization and conformational stability of Enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system. Biochemistry. 41:906-913.
    • (2002) Biochemistry , vol.41 , pp. 906-913
    • Dimitrova, M.N.1    Szczepanowski, R.H.2    Ruvinov, S.B.3    Peterkofsky, A.4    Ginsburg, A.5
  • 46
    • 0021174821 scopus 로고
    • Subunit association of enzyme I of the Salmonella typhimurium phosphoenolpyruvate:glycose phosphotransferase system: Temperature dependence and thermodynamic properties
    • Kukuruzinska, M. A., B. W. Turner, G. K. Ackers, and S. Roseman. 1984. Subunit association of enzyme I of the Salmonella typhimurium phosphoenolpyruvate:glycose phosphotransferase system: temperature dependence and thermodynamic properties. J. Biol. Chem. 259:11679-11682.
    • (1984) J. Biol. Chem , vol.259 , pp. 11679-11682
    • Kukuruzinska, M.A.1    Turner, B.W.2    Ackers, G.K.3    Roseman, S.4
  • 47
    • 0031473847 scopus 로고    scopus 로고
    • Swiss-model and the Swiss-PDB viewer: An environment for comparative protein modelling
    • Guex, N., and M. C. Peitsch. 1997. Swiss-model and the Swiss-PDB viewer: an environment for comparative protein modelling. Electrophoresis. 18:2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2


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