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Volumn 18, Issue 9, 2011, Pages 1276-1285

Analysis of molecular targets of mycobacterium tuberculosis by analytical ultracentrifugation

Author keywords

Analytical ultracentrifugation; Anti tuberculosis agents; Mycobacterium tuberculosis; Protein folding; Protein structure function

Indexed keywords

ADENOSINE KINASE; DIHYDRODIPICOLINATE REDUCTASE; ISONIAZID; NUCLEOSIDE ANALOG; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; RNA POLYMERASE; TUBERCULOSTATIC AGENT;

EID: 79952787283     PISSN: 09298673     EISSN: None     Source Type: Journal    
DOI: 10.2174/092986711795029537     Document Type: Article
Times cited : (35)

References (86)
  • 3
    • 0035443198 scopus 로고    scopus 로고
    • Biophysical studies by ultracentrifugation
    • DOI 10.1016/S0959-440X(00)00250-5
    • Laue, T. Biophysical studies by ultracentrifugation. Curr. Opin. Chem. Biol. 2001, 11 (5), 579-583. (Pubitemid 32972020)
    • (2001) Current Opinion in Structural Biology , vol.11 , Issue.5 , pp. 579-583
    • Laue, T.1
  • 4
    • 0012200139 scopus 로고    scopus 로고
    • Sedimentation equilibrium in the analytical ultracentrifuge
    • Harding, S. E., Chowdhry, B. Z., Eds.; Oxford University Press: Oxford
    • Harding, S. E.; Winzor, D. J. Sedimentation equilibrium in the analytical ultracentrifuge. In Protein-ligand interactions: Hydrodynamics and calorimetry: Partical Approach, Harding, S. E., Chowdhry, B. Z., Eds.; Oxford University Press: Oxford, 2001; pp 105-135.
    • (2001) Protein-Ligand Interactions: Hydrodynamics and Calorimetry: Partical Approach , pp. 105-135
    • Harding, S.E.1    Winzor, D.J.2
  • 6
    • 0036707991 scopus 로고    scopus 로고
    • Modern analytical ultracentrifugation in protein science: A tutorial review
    • DOI 10.1110/ps.0207702
    • Lebowitz, J.; Lewis, M. S.; Schuck, P. Modern analytical ultracentrifugation in protein science: A tutorial review. Protein Sci. 2002, 11 (9), 2067-2079. (Pubitemid 34919611)
    • (2002) Protein Science , vol.11 , Issue.9 , pp. 2067-2079
    • Lebowitz, J.1    Lewis, M.S.2    Schuck, P.3
  • 7
    • 33748565349 scopus 로고    scopus 로고
    • Analytical ultracentrifugation for the study of protein association and assembly
    • DOI 10.1016/j.cbpa.2006.08.017, PII S1367593106001244, Analytical Techniques/Mechanisms
    • Howlett, G.J.; Minton, A.P.; Rivas G. Analytical ultracentrifugation for the study of protein association and assembly. Curr. Opin. Chem. Biol. 2006, 10 (5), 430-436. (Pubitemid 44375070)
    • (2006) Current Opinion in Chemical Biology , vol.10 , Issue.5 , pp. 430-436
    • Howlett, G.J.1    Minton, A.P.2    Rivas, G.3
  • 8
    • 0001479980 scopus 로고
    • A new method for the determination of the molecular weight of the proteins
    • Svedberg, T.; Fahraeus, R. A new method for the determination of the molecular weight of the proteins. J. Am. Chem. Soc. 1926, 48 (1), 430-438.
    • (1926) J. Am. Chem. Soc. , vol.48 , Issue.1 , pp. 430-438
    • Svedberg, T.1    Fahraeus, R.2
  • 9
    • 0012452115 scopus 로고
    • Ultra centrifugal dispersion determination in protein solutions
    • Svedberg, T. Ultra centrifugal dispersion determination in protein solutions. Kollid Z. 1930, 51 (1), 10-24.
    • (1930) Kollid Z. , vol.51 , Issue.1 , pp. 10-24
    • Svedberg, T.1
  • 12
    • 0008221693 scopus 로고
    • The optima XL-A: A new analytical ultracentrifuge with a novel precision absorption optical system
    • Harding, S., Rowe AJ, Horton JC, Eds.; Royal Society of Chemistry: Cambridge
    • Giebeler, R. The optima XL-A: A new analytical ultracentrifuge with a novel precision absorption optical system. In Analytical ultracentrifugation in biochemistry and polymer science, Harding, S., Rowe AJ, Horton JC, Eds.; Royal Society of Chemistry: Cambridge, 1992; pp 16-25.
    • (1992) Analytical Ultracentrifugation in Biochemistry and Polymer Science , pp. 16-25
    • Giebeler, R.1
  • 14
    • 0030875214 scopus 로고    scopus 로고
    • The XL-I analytical ultracentrifuge with Rayleigh interference optics
    • DOI 10.1007/s002490050043
    • Furst, A. The XL-I analytical ultracentrifuge with Rayleigh interference optics. Eur. Biophys. J. Biophys. Lett. 1997, 25 (5-6), 307-310. (Pubitemid 27305847)
    • (1997) European Biophysics Journal , vol.25 , Issue.5-6 , pp. 307-310
    • Furst, A.1
  • 15
    • 0001490673 scopus 로고
    • A fuorescence detection system for the analytical ultracentrifuge and its application to proteins, nucleic acids, viroids and viruses
    • Harding, S. E., Rowe, A. J., Horton, J. C., Eds.; The Royal Society of Chemistry: Cambridge
    • Schmidt, B.; Riesner, B. A fuorescence detection system for the analytical ultracentrifuge and its application to proteins, nucleic acids, viroids and viruses. In Analytical ultracentrifugation in biochemistry and polymer science, Harding, S. E., Rowe, A. J., Horton, J. C., Eds.; The Royal Society of Chemistry: Cambridge, 1992; pp. 176-207.
    • (1992) Analytical Ultracentrifugation in Biochemistry and Polymer Science , pp. 176-207
    • Schmidt, B.1    Riesner, B.2
  • 16
    • 1642325812 scopus 로고    scopus 로고
    • Fluorescence detection for the XLI analytical ultracentrifuge
    • DOI 10.1016/j.bpc.2003.10.018, PII S0301462203003041
    • MacGregor, I. K.; Anderson, A. L.; Laue, T. M. Fluorescence detection for the XLI analytical ultracentrifuge. Biophys. Chem. 2004, 108 (1-3), 165-185. (Pubitemid 38388487)
    • (2004) Biophysical Chemistry , vol.108 , Issue.1-3 , pp. 165-185
    • MacGregor, I.K.1    Anderson, A.L.2    Laue, T.M.3
  • 17
    • 84977586068 scopus 로고
    • The motion of elements suspended in static liquids as claimed in the molecular kinetic theory of heat
    • Einstein, A. The motion of elements suspended in static liquids as claimed in the molecular kinetic theory of heat. Ann. Phys. 1905, 17 (8), 549-560.
    • (1905) Ann. Phys. , vol.17 , Issue.8 , pp. 549-560
    • Einstein, A.1
  • 19
    • 0018339645 scopus 로고
    • The translational friction coefficient of proteins
    • Teller, D. C.; Swanson, E.; de Haon, C. The translational friction coefficient of proteins. Methods Enzymol. 1979, Vol. 61, 104-124.
    • (1979) Methods Enzymol. , vol.61 , pp. 104-124
    • Teller, D.C.1    Swanson, E.2    De Haon, C.3
  • 20
    • 0003502254 scopus 로고
    • Bridging the macroscopic and microscopic
    • Forkner M., Ed.; The Benjamin/Cummings Publishing Company: Menlo Park
    • Eisenberg, D.; Crothers, D. Bridging the macroscopic and microscopic. In Physical Chemistry with application to the Life Sciences, Forkner, M., Ed.; The Benjamin/Cummings Publishing Company: Menlo Park, 1979; pp 700- 745.
    • (1979) Physical Chemistry with application to the Life Sciences , pp. 700-745
    • Eisenberg, D.1    Crothers, D.2
  • 21
    • 0003159229 scopus 로고
    • Die Differentialgleichung der Ultrazentrifugierung
    • Lamm, O. Die Differentialgleichung der Ultrazentrifugierung. Ark. Mat. Astr. Fys 1929, 21B (2), 1-4.
    • (1929) Ark. Mat. Astr. Fys , vol.21 B , Issue.2 , pp. 1-4
    • Lamm, O.1
  • 22
    • 67449094633 scopus 로고    scopus 로고
    • Characterization of nucleotide-induced changes on the quaternary structure of human 70 kDa heat shock protein Hsp70.1 by analytical ultracentrifugation
    • Borges, J. C.; Ramos, C. H. I. Characterization of nucleotide-induced changes on the quaternary structure of human 70 kDa heat shock protein Hsp70.1 by analytical ultracentrifugation. BMB Rep. 2009, 42 (3), 166-171.
    • (2009) BMB Rep. , vol.42 , Issue.3 , pp. 166-171
    • Borges, J.C.1    Ramos, C.H.I.2
  • 24
    • 33749372201 scopus 로고    scopus 로고
    • Role of analytical ultracentrifugation in assessing the aggregation of protein biopharmaceuticals
    • Berkowitz, S. A. Role of analytical ultracentrifugation in assessing the aggregation of protein biopharmaceuticals. AAPS J., 2006, 8 (3), E590-E605.
    • (2006) AAPS J. , vol.8 , Issue.3
    • Berkowitz, S.A.1
  • 25
    • 33749452453 scopus 로고    scopus 로고
    • A critical review of analytical ultracentrifugation and field flow fractionation methods for measuring protein aggregation
    • DOI 10.1208/aapsj080367, 67
    • Liu, J.; Andya, J. D.; Shire, S. J. A critical review of analytical ultracentrifugation and field flow fractionation methods for measuring protein aggregation. AAPS J. 2006, 8 (3), E580-E589. (Pubitemid 44507669)
    • (2006) AAPS Journal , vol.8 , Issue.3
    • Liu, J.1    Andaya, J.D.2    Shire, S.J.3
  • 26
    • 33748742268 scopus 로고    scopus 로고
    • Is any measurement method optimal for all aggregate sizes and types?
    • Philo, J. S. Is any measurement method optimal for all aggregate sizes and types? AAPS J. 2006, 8 (3), E564-E571.
    • (2006) AAPS J. , vol.8 , Issue.3
    • Philo, J.S.1
  • 29
    • 79952789172 scopus 로고    scopus 로고
    • Center for analytical ultracentrifugation of macromolecular assemblies
    • Hardware. (Accessed March 18 2010)
    • Schirf, V.; Planken, K. L. Center for Analytical Ultracentrifugation of Macromolecular Assemblies. Analytical Ultracentrifuge User Guide Volume 1: Hardware. http://ultrascan.uthscsa.edu/AUCuserGuideVolume-1-Hardware. pdf (Accessed March 18, 2010) 2008.
    • (2008) Analytical Ultracentrifuge User Guide , vol.1
    • Schirf, V.1    Planken, K.L.2
  • 30
    • 78650931151 scopus 로고    scopus 로고
    • Assembly loading, and alignment of an analytical ultracentrifuge sample cell
    • (Accessed April 01 2010)
    • Balbo, A.; Zhao, H.; Brown, P.; Schuck, P. Assembly, loading, and alignment of an analytical ultracentrifuge sample cell. JoVE 2009, 33, http://www.jove.com/index/details.stp?id=1530 (Accessed April 01, 2010).
    • (2009) JoVE , pp. 33
    • Balbo, A.1    Zhao, H.2    Brown, P.3    Schuck, P.4
  • 32
    • 0037415748 scopus 로고    scopus 로고
    • Two distinct myosin light chain structures are induced by specific variations within the bound IQ motifs - Functional implications
    • DOI 10.1093/emboj/cdg058
    • Terrak, M.; Wu, G. M.; Stafford, W. F.; Lu, R. C.; Dominguez, R. Two distinct myosin light chain structures are induced by specific variations within the bound IQ motifs- functional implications. EMBO J. 2003, 22 (3), 362-371. (Pubitemid 36193582)
    • (2003) EMBO Journal , vol.22 , Issue.3 , pp. 362-371
    • Terrak, M.1    Wu, G.2    Stafford, W.F.3    Lu, R.C.4    Dominguez, R.5
  • 33
    • 0042197692 scopus 로고
    • Sedimentation coefficients of small molecules- methods of measurement based on the refractive-index gradient curve- The sedimentation coefficient of polyglucose-A
    • Baldwin, R. L. Sedimentation coefficients of small molecules- methods of measurement based on the refractive-index gradient curve- the sedimentation coefficient of polyglucose-A. Biochem. J. 1953, 55 (4), 644-648.
    • (1953) Biochem. J. , vol.55 , Issue.4 , pp. 644-648
    • Baldwin, R.L.1
  • 34
    • 8644270952 scopus 로고
    • Sedimentation in the ultracentrifuge
    • Goldberg, R. J. Sedimentation in the ultracentrifuge. J. Phys. Chem. 1953, 57 (2), 194-202.
    • (1953) J. Phys. Chem. , vol.57 , Issue.2 , pp. 194-202
    • Goldberg, R.J.1
  • 35
    • 0016492159 scopus 로고
    • Direct analysis of sedimentation equilibrium results obtained with polymerizing systems
    • Milthorpe, B. K.; Jeffrey, P. D.; Nichol, L. W. Direct analysis of sedimentation equilibrium results obtained with polymerizing systems. Biophys. Chem. 1975, 3 (2), 169-176.
    • (1975) Biophys. Chem. , vol.3 , Issue.2 , pp. 169-176
    • Milthorpe, B.K.1    Jeffrey, P.D.2    Nichol, L.W.3
  • 36
    • 0017611984 scopus 로고
    • The concentration dependence of transport processes: a general description applicable to the sedimentation, translational diffusion, and viscosity coefficients of macromolecular solutes
    • Rowe, A. J. Concentration-dependence of transport processes- general description applicable to sedimentation, translational diffusion, and viscosity coefficients of macromolecular solutes. Biopolymers 1977, 16 (12), 2595-2611. (Pubitemid 8255428)
    • (1977) Biopolymers , vol.16 , Issue.12 , pp. 2595-2611
    • Rowe, A.J.1
  • 37
    • 0017806223 scopus 로고
    • Boundary analysis of sedimentation-velocity experiments with monodisperse and paucidisperse solutes
    • DOI 10.1002/bip.1978.360170602
    • van Holde, K. E.; Weischet, W. O. Boundary analysis of sedimentationvelocity experiments with monodisperse and paucidisperse solutes. Biopolymers 1978, 17 (6), 1387-1403. (Pubitemid 8345344)
    • (1978) Biopolymers , vol.17 , Issue.6 , pp. 1387-1403
    • Van Holde, K.E.1    Weischet, W.O.2
  • 38
    • 0000198303 scopus 로고
    • Approximate solution to the lamm equation
    • Holladay, L. A. Approximate solution to the lamm equation. Biophys. Chem. 1979, 10 (2), 187-190.
    • (1979) Biophys. Chem. , vol.10 , Issue.2 , pp. 187-190
    • Holladay, L.A.1
  • 39
    • 0019756004 scopus 로고
    • Analysis of data from the analytical ultra-centrifuge by non-linear least-squares techniques
    • Johnson, M. L.; Correia, J. J.; Yphantis, D. A.; Halvorson, H. R. Analysis of data from the analytical ultra-centrifuge by non-linear least-squares techniques. Biophys. J. 1981, 36 (3), 575-588.
    • (1981) Biophys. J. , vol.36 , Issue.3 , pp. 575-588
    • Johnson, M.L.1    Correia, J.J.2    Yphantis, D.A.3    Halvorson, H.R.4
  • 40
    • 0026718393 scopus 로고
    • Parameter-estimation by least-squares methods
    • Johnson, M. L.; Faunt, L. M. Parameter-estimation by least-squares methods. Methods Enzymol. 1992, 210, 1-37.
    • (1992) Methods Enzymol. , vol.210 , pp. 1-37
    • Johnson, M.L.1    Faunt, L.M.2
  • 41
    • 0026747656 scopus 로고
    • Boundary analysis in sedimentation transport experiments- A procedure for obtaining sedimentation coefficient distributions using the time derivative of the concentration profile
    • Stafford, W. F. Boundary analysis in sedimentation transport experiments- A procedure for obtaining sedimentation coefficient distributions using the time derivative of the concentration profile. Anal. Biochem. 1992, 203 (2), 295-301.
    • (1992) Anal. Biochem. , vol.203 , Issue.2 , pp. 295-301
    • Stafford, W.F.1
  • 42
    • 0028149245 scopus 로고
    • Analytical ultracentrifugation of complex macromolecular systems
    • DOI 10.1021/bi00249a001
    • Hansen, J. C.; Lebowitz, J.; Demeler, B. Analytical ultracentrifugation of complex macromolecular systems. Biochemistry 1994, 33 (45), 13155-13163. (Pubitemid 24373229)
    • (1994) Biochemistry , vol.33 , Issue.45 , pp. 13155-13163
    • Hansen, J.C.1    Lebowitz, J.2    Demeler, B.3
  • 43
    • 0028672523 scopus 로고
    • Boundary analysis in sedimentation velocity experiments
    • Stafford, W. F. Boundary analysis in sedimentation velocity experiments. Methods Enzymol. 1994, 240, 478-501.
    • (1994) Methods Enzymol. , vol.240 , pp. 478-501
    • Stafford, W.F.1
  • 44
    • 0031029481 scopus 로고    scopus 로고
    • Molecular mass determination by sedimentation velocity experiments and direct fitting of the concentration profiles
    • Behlke, J.; Ristau, O. Molecular mass determination by sedimentation velocity experiments and direct fitting of the concentration profiles. Biophys. J. 1997, 72 (1), 428-434. (Pubitemid 27043454)
    • (1997) Biophysical Journal , vol.72 , Issue.1 , pp. 428-434
    • Behlke, J.1    Ristau, O.2
  • 45
    • 0031020113 scopus 로고    scopus 로고
    • Identification and interpretation of complexity in sedimentation velocity boundaries
    • Demeler, B.; Saber, H.; Hansen, J. C. Identification and interpretation of complexity in sedimentation velocity boundaries. Biophys. J. 1997, 72 (1), 397-407. (Pubitemid 27043451)
    • (1997) Biophysical Journal , vol.72 , Issue.1 , pp. 397-407
    • Demeler, B.1    Saber, H.2    Hansen, J.C.3
  • 46
    • 0031036440 scopus 로고    scopus 로고
    • An improved function for fitting sedimentation velocity data for low- molecular-weight solutes
    • Philo, J. S. An improved function for fitting sedimentation velocity data for low-molecular-weight solutes. Biophys. J. 1997, 72 (1), 435-444. (Pubitemid 27043455)
    • (1997) Biophysical Journal , vol.72 , Issue.1 , pp. 435-444
    • Philo, J.S.1
  • 47
    • 0031982612 scopus 로고    scopus 로고
    • Determination of molecular parameters by fitting sedimentation data to finite-element solutions of the Lamm equation
    • Demeler, B.; Saber, H. Determination of molecular parameters by fitting sedimentation data to finite-element solutions of the Lamm equation. Biophys. J. 1998, 74 (1), 444-454. (Pubitemid 28041772)
    • (1998) Biophysical Journal , vol.74 , Issue.1 , pp. 444-454
    • Demeler, B.1    Saber, H.2
  • 48
    • 0031688168 scopus 로고    scopus 로고
    • Sedimentation analysis of noninteracting and self-associating solutes using numerical solutions to the Lamm equation
    • Schuck, P. Sedimentation analysis of noninteracting and self-associating solutes using numerical solutions to the Lamm equation. Biophys. J. 1998, 75 (3), 1503-1512. (Pubitemid 28397620)
    • (1998) Biophysical Journal , vol.75 , Issue.3 , pp. 1503-1512
    • Schuck, P.1
  • 49
    • 0032562170 scopus 로고    scopus 로고
    • Direct analysis of sedimentation equilibrium distributions reflecting complex formation between dissimilar reactants
    • DOI 10.1021/bi972211v
    • Winzor, D. J.; Jacobsen, M. P.; Wills, P. R. Direct analysis of sedimentation equilibrium distributions reflecting complex formation between dissimilar reactants. Biochemistry 1998, 37 (8), 2226-2233. (Pubitemid 28119295)
    • (1998) Biochemistry , vol.37 , Issue.8 , pp. 2226-2233
    • Winzor, D.J.1    Jacobsen, M.P.2    Wills, P.R.3
  • 51
    • 0033921410 scopus 로고    scopus 로고
    • Sedimentation equilibrium analysis of mixed associations using numerical constraints to impose mass or signal conservation
    • Philo, J. S. Sedimentation equilibrium analysis of mixed associations using numerical constraints to impose mass or signal conservation. Methods Enzymol. 2000, Volume 321, 100-120. (Pubitemid 30457541)
    • (2000) Methods in Enzymology , vol.321 , pp. 100-120
    • Philo, J.S.1
  • 52
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling
    • Schuck, P. Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling. Biophys. J. 2000, 78 (3), 1606-1619. (Pubitemid 30141584)
    • (2000) Biophysical Journal , vol.78 , Issue.3 , pp. 1606-1619
    • Schuck, P.1
  • 53
    • 0036154258 scopus 로고    scopus 로고
    • Size-distribution analysis of proteins by analytical ultracentrifugation: Strategies and application to model systems
    • Schuck, P.; Perugini, M. A.; Gonzales, N. R.; Howlett, G. J.; Schubert, D. Size-distribution analysis of proteins by analytical ultracentrifugation: Strategies and application to model systems. Biophys. J. 2002, 82 (2), 1096-1111. (Pubitemid 34111246)
    • (2002) Biophysical Journal , vol.82 , Issue.2 , pp. 1096-1111
    • Schuck, P.1    Perugini, M.A.2    Gonzales, N.R.3    Hewlett, G.J.4    Schubert, D.5
  • 54
    • 0042855798 scopus 로고    scopus 로고
    • On the analysis of protein self-association by sedimentation velocity analytical ultracentrifugation
    • DOI 10.1016/S0003-2697(03)00289-6
    • Schuck, P. On the analysis of protein self-association by sedimentation velocity analytical ultracentrifugation. Anal. Biochem. 2003, 320 (1), 104-124. (Pubitemid 36937072)
    • (2003) Analytical Biochemistry , vol.320 , Issue.1 , pp. 104-124
    • Schuck, P.1
  • 55
    • 1642368109 scopus 로고    scopus 로고
    • Analysis of heterologous interacting systems by sedimentation velocity: Curve fitting algorithms for estimation of sedimentation coefficients, equilibrium and kinetic constants
    • DOI 10.1016/j.bpc.2003.10.028, PII S0301462203003090
    • Stafford, W. F.; Sherwood, P. J. Analysis of heterologous interacting systems by sedimentation velocity: Curve fitting algorithms for estimation of sedimentation coefficients, equilibrium and kinetic constants. Biophys. Chem. 2004, 108 (1-3), 231-243. (Pubitemid 38388491)
    • (2004) Biophysical Chemistry , vol.108 , Issue.1-3 , pp. 231-243
    • Stafford, W.F.1    Sherwood, P.J.2
  • 56
    • 70349696256 scopus 로고    scopus 로고
    • On the analysis of sedimentation velocity in the study of protein complexes
    • Brown, P. H.; Balbo, A.; Schuck, P. On the analysis of sedimentation velocity in the study of protein complexes. Eur. Biophys. J. Biophys. Lett. 2009, 38 (8), 1079-1099.
    • (2009) Eur. Biophys. J. Biophys. Lett. , vol.38 , Issue.8 , pp. 1079-1099
    • Brown, P.H.1    Balbo, A.2    Schuck, P.3
  • 57
    • 77950552976 scopus 로고    scopus 로고
    • The implementation of SOMO (SOlution MOdeller) in the UltraScan analytical ultracentrifugation data analysis suite: Enhanced capabilities allow the reliable hydrodynamic modeling of virtually any kind of biomacromolecule
    • Brookes, E.; Demeler, B.; Rosano, C.; Rocco, M. The implementation of SOMO (SOlution MOdeller) in the UltraScan analytical ultracentrifugation data analysis suite: Enhanced capabilities allow the reliable hydrodynamic modeling of virtually any kind of biomacromolecule. Eur. Biophys. J. 2010, 39 (3), 423-435.
    • (2010) Eur. Biophys. J. , vol.39 , Issue.3 , pp. 423-435
    • Brookes, E.1    Demeler, B.2    Rosano, C.3    Rocco, M.4
  • 58
    • 79952778845 scopus 로고    scopus 로고
    • (Accessed March 24, 2010)
    • Philo, J. S. SEDNTERP. http://jphilo.mailway.com/download.htm (Accessed March 24, 2010) 2006.
    • (2006) SEDNTERP
    • Philo, J.S.1
  • 62
    • 0011523808 scopus 로고    scopus 로고
    • Global tuberculosis control: Surveillance, planning, financing
    • World Health Organization
    • World Health Organization Global tuberculosis control: Surveillance, planning, financing. WHO report 2009.
    • (2009) WHO Report
  • 63
    • 20144370344 scopus 로고    scopus 로고
    • Evolution of tuberculosis control and prospects for reducing tuberculosis incidence, prevalence, and deaths globally
    • DOI 10.1001/jama.293.22.2767
    • Dye, C.; Watt, C. J.; Bleed, D. M.; Hosseini, S. M.; Raviglione, M. C. Evolution of tuberculosis control and prospects for reducing tuberculosis incidence, prevalence, and deaths globally. JAMA 2005, 293 (22), 2767-2775. (Pubitemid 40965089)
    • (2005) Journal of the American Medical Association , vol.293 , Issue.22 , pp. 2767-2775
    • Dye, C.1    Watt, C.J.2    Bleed, D.M.3    Hosseini, S.M.4    Raviglione, M.C.5
  • 65
    • 0034737570 scopus 로고    scopus 로고
    • Infectious disease- Drug-resistant TB on the rise
    • Stokstad, E. Infectious disease- Drug-resistant TB on the rise. Science 2000, 287 (5462), 2391.
    • (2000) Science , vol.287 , Issue.5462 , pp. 2391
    • Stokstad, E.1
  • 67
    • 0035969950 scopus 로고    scopus 로고
    • Spectroscopic and thermodynamic characterization of the transcription antitermination factor NusE and its interaction with NusB from Mycobacterium tuberculosis
    • DOI 10.1021/bi0018279
    • Gopal, B.; Papavinasasundaram, K. G.; Dodson, G.; Colston, M. J.; Major, S. A.; Lane, A. N. Spectroscopic and thermodynamic characterization of the transcription antitermination factor NusE and its interaction with NusB from Mycobacterium tuberculosis. Biochemistry 2001, 40 (4), 920-928. (Pubitemid 32108584)
    • (2001) Biochemistry , vol.40 , Issue.4 , pp. 920-928
    • Gopal, B.1    Papavinasasundaram, K.G.2    Dodson, G.3    Colston, M.J.4    Major, S.A.5    Lane, A.N.6
  • 68
    • 33947393189 scopus 로고    scopus 로고
    • Characterization of the helicase activity and substrate specificity of Mycobacterium tuberculosis UvrD
    • DOI 10.1128/JB.01421-06
    • Curti, E.; Smerdon, S. J.; Davis, E. O. Characterization of the helicase activity and substrate specificity of Mycobacterium tuberculosis UvrD. J. Bacteriol. 2007, 189 (5), 1542-1555. (Pubitemid 46446115)
    • (2007) Journal of Bacteriology , vol.189 , Issue.5 , pp. 1542-1555
    • Curti, E.1    Smerdon, S.J.2    Davis, E.O.3
  • 69
    • 0242659213 scopus 로고    scopus 로고
    • Identification and Characterization of a Unique Adenosine Kinase from Mycobacterium tuberculosis
    • DOI 10.1128/JB.185.22.6548-6555.2003
    • Long, M. C.; Escuyer, V.; Parker, W. B. Identification and characterization of a unique adenosine kinase from Mycobacterium tuberculosis. J. Bacteriol. 2003, 185 (22), 6548-6555. (Pubitemid 37385873)
    • (2003) Journal of Bacteriology , vol.185 , Issue.22 , pp. 6548-6555
    • Long, M.C.1    Escuyer, V.2    Parker, W.B.3
  • 71
    • 77649270286 scopus 로고    scopus 로고
    • Crystal structure of ArgP from Mycobacterium tuberculosis confirms two distinct conformations of full-length LysR transcriptional regulators and reveals its function in DNA binding and transcriptional regulation
    • Zhou, X.; Lou, Z.; Fu, S.; Yang, A.; Shen, H.; Li, Z.; Feng, Y.; Bartlam, M.; Wang, H.; Rao, Z. Crystal structure of ArgP from Mycobacterium tuberculosis confirms two distinct conformations of full-length LysR transcriptional regulators and reveals its function in DNA binding and transcriptional regulation. J. Mol. Biol. 2010, 396 (4), 1012-1024.
    • (2010) J. Mol. Biol. , vol.396 , Issue.4 , pp. 1012-1024
    • Zhou, X.1    Lou, Z.2    Fu, S.3    Yang, A.4    Shen, H.5    Li, Z.6    Feng, Y.7    Bartlam, M.8    Wang, H.9    Rao, Z.10
  • 72
    • 0034076849 scopus 로고    scopus 로고
    • Bacterial diaminopimelate metabolism as a target for antibiotic design
    • DOI 10.1016/S0968-0896(00)00044-4, PII S0968089600000444
    • Cox, R. J.; Sutherland, A.; Vederas, J. C. Bacterial diaminopimelate metabolism as a target for antibiotic design. Bioorg. Med. Chem. 2000, 8 (5), 843-871. (Pubitemid 30336382)
    • (2000) Bioorganic and Medicinal Chemistry , vol.8 , Issue.5 , pp. 843-871
    • Cox, R.J.1    Sutherland, A.2    Vederas, J.C.3
  • 76
    • 33750068255 scopus 로고    scopus 로고
    • Metal-linked dimerization in the iron-dependent regulator from Mycobacterium tuberculosis
    • DOI 10.1021/bi060797s
    • Semavina, M.; Beckett, D.; Logan, T. M. Metal-linked dimerization in the iron-dependent regulator from Mycobacterium tuberculosis. Biochemistry 2006, 45 (41), 12480-12490. (Pubitemid 44583690)
    • (2006) Biochemistry , vol.45 , Issue.41 , pp. 12480-12490
    • Semavina, M.1    Beckett, D.2    Logan, T.M.3
  • 78
    • 34547576168 scopus 로고    scopus 로고
    • Probing mechanisms of resistance to the tuberculosis drug isoniazid: Conformational changes caused by inhibition of InhA, the enoyl reductase from Mycobacterium tuberculosis
    • DOI 10.1110/ps.062749007
    • Kruh, N. A.; Rawat, R.; Ruzsicska, B. P.; Tonge, P. J. Probing mechanisms of resistance to the tuberculosis drug isoniazid: Conformational changes caused by inhibition of InhA, the enoyl reductase from Mycobacterium tuberculosis. Protein Sci. 2007, 16 (8), 1617-1627. (Pubitemid 47195689)
    • (2007) Protein Science , vol.16 , Issue.8 , pp. 1617-1627
    • Kruh, N.A.1    Rawat, R.2    Ruzsicska, B.P.3    Tonge, P.J.4
  • 79
  • 80
    • 48349110666 scopus 로고    scopus 로고
    • Novel intermolecular iterative mechanism for biosynthesis of mycoketide synthase by a bimodular polyketide synthase
    • Chopra, T.; Banerjee, S.; Gupta, S.; Yadav, G.; Anand, S.; Surolia, A.; Roy, R. P.; Mohanty, D.; Gokhale, R. S. Novel intermolecular iterative mechanism for biosynthesis of mycoketide synthase by a bimodular polyketide synthase. PLoS Biol. 2008, 6 (7), 1584-1598.
    • (2008) PLoS Biol. , vol.6 , Issue.7 , pp. 1584-1598
    • Chopra, T.1    Banerjee, S.2    Gupta, S.3    Yadav, G.4    Anand, S.5    Surolia, A.6    Roy, R.P.7    Mohanty, D.8    Gokhale, R.S.9
  • 81
    • 70450224660 scopus 로고    scopus 로고
    • Predicted structural basis for CD1c presentation of mycobacterial branched polyketides and long lipopeptide antigens
    • Garzon, D.; Bond, P. J.; Faraldo-Gomez, J. D. Predicted structural basis for CD1c presentation of mycobacterial branched polyketides and long lipopeptide antigens. Mol. Immunol. 2009, 47 (2-3), 253-260.
    • (2009) Mol. Immunol. , vol.47 , Issue.2-3 , pp. 253-260
    • Garzon, D.1    Bond, P.J.2    Faraldo-Gomez, J.D.3
  • 84
    • 12544259906 scopus 로고    scopus 로고
    • Characterization of the secreted chorismate mutase from the pathogen mycobacterium tuberculosis
    • Sasso, S.; Ramakrishnan, C.; Gamper, M.; Hilvert, D.; Kast, P. Characterization of the secreted chorismate mutase from the pathogen Mycobacterium tuberculosis. FEBS J. 2005, 272 (2), 375-389.
    • (2005) FEBS J. , vol.272 , Issue.2 , pp. 375-389
    • Sasso, S.1    Ramakrishnan, C.2    Gamper, M.3    Hilvert, D.4    Kast, P.5


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