메뉴 건너뛰기




Volumn 32, Issue 2, 2014, Pages 209-221

Drug resistance mechanism of PncA in Mycobacterium tuberculosis

Author keywords

Docking; Molecular dynamic simulation; Pyrazinamidase; Pyrazinamide; Resistance

Indexed keywords

BACTERIAL ENZYME; MUTANT PROTEIN; PYRAZINAMIDASE; PYRAZINAMIDE; UNCLASSIFIED DRUG;

EID: 84889685004     PISSN: 07391102     EISSN: 15380254     Source Type: Journal    
DOI: 10.1080/07391102.2012.759885     Document Type: Article
Times cited : (167)

References (60)
  • 3
    • 0036890007 scopus 로고    scopus 로고
    • Molecular modelling of membrane sterols with the use of the GROMOS 96 force field
    • Baran, M., & Mazerski, J. (2002). Molecular modelling of membrane sterols with the use of the GROMOS 96 force field. Chemistry and Physics of Lipids, 120, 21-31.
    • (2002) Chemistry and Physics of Lipids , vol.120 , pp. 21-31
    • Baran, M.1    Mazerski, J.2
  • 6
    • 80052860158 scopus 로고    scopus 로고
    • Pyrazinamide susceptibility testing in Mycobacterium tuberculosis: A systematic review with meta-analyses
    • Chang, K. C., Yew, W. W., & Zhang, Y. (2011). Pyrazinamide susceptibility testing in Mycobacterium tuberculosis: A systematic review with meta-analyses. Antimicrobial Agents and Chemotherapy, 55, 4499-4505.
    • (2011) Antimicrobial Agents and Chemotherapy , vol.55 , pp. 4499-4505
    • Chang, K.C.1    Yew, W.W.2    Zhang, Y.3
  • 7
    • 0016708122 scopus 로고
    • Principles of protein-protein recognition
    • Chothia, C., & Janin, J. (1975). Principles of protein-protein recognition. Nature, 256, 705-708.
    • (1975) Nature , vol.256 , pp. 705-708
    • Chothia, C.1    Janin, J.2
  • 8
  • 9
    • 28644438570 scopus 로고    scopus 로고
    • An intuitive approach to measuring protein surface curvature
    • Coleman, R. G., Burr, M. A., Souvaine, D. L., & Cheng, C. (2005). An intuitive approach to measuring protein surface curvature. Proteins, 61, 1068-1074.
    • (2005) Proteins , vol.61 , pp. 1068-1074
    • Coleman, R.G.1    Burr, M.A.2    Souvaine, D.L.3    Cheng, C.4
  • 10
    • 33748102999 scopus 로고    scopus 로고
    • Travel depth, a new shape descriptor for macromolecules: Application to ligand binding
    • Coleman, R. G., & Sharp, K. M. (2006). Travel depth, a new shape descriptor for macromolecules: Application to ligand binding. Journal of Molecular Biology, 362, 441-458.
    • (2006) Journal of Molecular Biology , vol.362 , pp. 441-458
    • Coleman, R.G.1    Sharp, K.M.2
  • 13
    • 0035960636 scopus 로고    scopus 로고
    • Crystal structure and mechanism of catalysis of a pyrazinamidase from Pyrococcus horikoshii
    • Du, X., Wang, W., Kim, R., Yakota, H., Nguyen, H., & Kim, S. H. (2001). Crystal structure and mechanism of catalysis of a pyrazinamidase from Pyrococcus horikoshii. Biochemistry, 40, 14166-14172.
    • (2001) Biochemistry , vol.40 , pp. 14166-14172
    • Du, X.1    Wang, W.2    Kim, R.3    Yakota, H.4    Nguyen, H.5    Kim, S.H.6
  • 14
    • 33747818007 scopus 로고    scopus 로고
    • CASTp: Computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues
    • Dundas, J., Ouyang, Z., Tseng, J., Binkowski, A., Turpaz, Y., & Liang, J. (2006). CASTp: Computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues. Nucleic Acid Research, 34, 116-118.
    • (2006) Nucleic Acid Research , vol.34 , pp. 116-118
    • Dundas, J.1    Ouyang, Z.2    Tseng, J.3    Binkowski, A.4    Turpaz, Y.5    Liang, J.6
  • 15
    • 0031459734 scopus 로고    scopus 로고
    • Molecular interactions between inhaled anesthetics and proteins
    • Eckenhoff, R. G., & Johansson, J. S. (1997). Molecular interactions between inhaled anesthetics and proteins. Pharmacological Reviews, 49, 343-367.
    • (1997) Pharmacological Reviews , vol.49 , pp. 343-367
    • Eckenhoff, R.G.1    Johansson, J.S.2
  • 16
    • 0030462271 scopus 로고    scopus 로고
    • Hydrophobic regions on protein surfaces: Definition based on hydration shell structure and a quick method for their computation
    • Eisenhabe, F., & Argos, P. (1996). Hydrophobic regions on protein surfaces: definition based on hydration shell structure and a quick method for their computation. Protein Engineering, 9, 1121-1133.
    • (1996) Protein Engineering , vol.9 , pp. 1121-1133
    • Eisenhabe, F.1    Argos, P.2
  • 20
    • 33344474627 scopus 로고    scopus 로고
    • A complete small molecule dataset from the protein data bank
    • Feldman, H. J., Snyder, K. A., Ticoll, A., Pintilie, G., & Hogue, C. W. (2006). A complete small molecule dataset from the protein data bank. FEBS Letters, 580, 1649-1653.
    • (2006) FEBS Letters , vol.580 , pp. 1649-1653
    • Feldman, H.J.1    Snyder, K.A.2    Ticoll, A.3    Pintilie, G.4    Hogue, C.W.5
  • 22
    • 0032771444 scopus 로고    scopus 로고
    • Drug susceptibility testing of Mycobacterium tuberculosis: A neglected problem at the turn of the century
    • Heifets, L. B., & Cangelosi, G. A. (1999). Drug susceptibility testing of Mycobacterium tuberculosis: A neglected problem at the turn of the century. International Journal of Tuberculosis and Lung Disease, 3, 564-581.
    • (1999) International Journal of Tuberculosis and Lung Disease , vol.3 , pp. 564-581
    • Heifets, L.B.1    Cangelosi, G.A.2
  • 23
    • 0026794683 scopus 로고
    • Pyrazinamide sterilizing activity in vitro against semidormant Mycobacterium tuberculosis bacterial populations
    • Heifets, L. B., & Lindholm-Levy, P. (1992). Pyrazinamide sterilizing activity in vitro against semidormant Mycobacterium tuberculosis bacterial populations. Am Rev Respir Dis, 145, 1223-1225.
    • (1992) Am Rev Respir Dis , vol.145 , pp. 1223-1225
    • Heifets, L.B.1    Lindholm-Levy, P.2
  • 24
  • 26
    • 0014062867 scopus 로고
    • Pyrazinamide susceptibility and amidase activity of tubercle bacilli
    • Konno, K., Feldmann, F. M., & McDermott, W. (1967). Pyrazinamide susceptibility and amidase activity of tubercle bacilli. Am Rev Respir Dis, 95, 461-469.
    • (1967) Am Rev Respir Dis , vol.95 , pp. 461-469
    • Konno, K.1    Feldmann, F.M.2    McDermott, W.3
  • 27
    • 84861790146 scopus 로고    scopus 로고
    • Computational investigation of pathogenic nsSNPs in CEP63 protein
    • Kumar, A., & Purohit, R. (2012a). Computational investigation of pathogenic nsSNPs in CEP63 protein. Gene, 503, 75-82.
    • (2012) Gene , vol.503 , pp. 75-82
    • Kumar, A.1    Purohit, R.2
  • 28
    • 84867629652 scopus 로고    scopus 로고
    • Computational centrosomics: An approach to understand the dynamic behaviour of centrosome
    • Kumar, A., & Purohit, R. (2012b). Computational centrosomics: An approach to understand the dynamic behaviour of centrosome. Gene, 511, 125-126.
    • (2012) Gene , vol.511 , pp. 125-126
    • Kumar, A.1    Purohit, R.2
  • 29
    • 84872270918 scopus 로고    scopus 로고
    • Computational screening and molecular dynamics simulation of disease associated nsSNPs in CENP-E
    • Kumar, A., & Purohit, R. (2012c). Computational screening and molecular dynamics simulation of disease associated nsSNPs in CENP-E. Mutation Research, 738-739, 28-37.
    • (2012) Mutation Research , vol.738-739 , pp. 28-37
    • Kumar, A.1    Purohit, R.2
  • 30
    • 84867464864 scopus 로고    scopus 로고
    • In silico prediction of a diseaseassociated STIL mutant and its affect on the recruitment of centromere protein J (CENPJ)
    • Kumar, A., Rajendran, V., Sethumadhavan, R. & Purohit, R. (2012). In silico prediction of a diseaseassociated STIL mutant and its affect on the recruitment of centromere protein J (CENPJ). FEBS Open Bio, 2, 285-293.
    • (2012) FEBS Open Bio , vol.2 , pp. 285-293
    • Kumar, A.1    Rajendran, V.2    Sethumadhavan, R.3    Purohit, R.4
  • 31
    • 0035252725 scopus 로고    scopus 로고
    • Study of the structure-activity relationships for the pyrazinamidase (PncA) from Mycobacterium tuberculosis
    • Lemaitre, N., Callebaut, I., Frenois, F., Jarlier, V., & Sougakoff, W. (2001). Study of the structure-activity relationships for the pyrazinamidase (PncA) from Mycobacterium tuberculosis. Biochemical Journal, 353, 453-458.
    • (2001) Biochemical Journal , vol.353 , pp. 453-458
    • Lemaitre, N.1    Callebaut, I.2    Frenois, F.3    Jarlier, V.4    Sougakoff, W.5
  • 32
    • 0032799334 scopus 로고    scopus 로고
    • Characterization of new mutations in pyrazinamideresistant strains of Mycobacterium tuberculosis and identification of conserved regions important for the catalytic activity of the pyrazinamidase PncA
    • Lemaitre, N., Sougakoff, W., Truffot-Pernot, C., & Jarlier, V. (1999). Characterization of new mutations in pyrazinamideresistant strains of Mycobacterium tuberculosis and identification of conserved regions important for the catalytic activity of the pyrazinamidase PncA. Antimicrob Agents Chemotherapy, 43, 1761-1763.
    • (1999) Antimicrob Agents Chemotherapy , vol.43 , pp. 1761-1763
    • Lemaitre, N.1    Sougakoff, W.2    Truffot-Pernot, C.3    Jarlier, V.4
  • 33
    • 79953291598 scopus 로고    scopus 로고
    • Treatment of latent infection with Mycobacterium tuberculosis: Update 2010
    • Leung, C. C., Rieder, H. L., Lange, C., & Yew, W. W. (2011). Treatment of latent infection with Mycobacterium tuberculosis: Update 2010. European Respiratory Journal, 37, 690-711.
    • (2011) European Respiratory Journal , vol.37 , pp. 690-711
    • Leung, C.C.1    Rieder, H.L.2    Lange, C.3    Yew, W.W.4
  • 34
    • 0031687653 scopus 로고    scopus 로고
    • Anatomy of protein pockets and cavities: Measurement of binding site geometry and implications for ligand design
    • Liang, J., Edelsbrunner, H., & Woodward, C. (1998). Anatomy of protein pockets and cavities: Measurement of binding site geometry and implications for ligand design. Protein Science, 7, 1884-1897.
    • (1998) Protein Science , vol.7 , pp. 1884-1897
    • Liang, J.1    Edelsbrunner, H.2    Woodward, C.3
  • 35
    • 84655163942 scopus 로고    scopus 로고
    • A quality assessment tool for tuberculosis control activities in resource limited settings
    • McQuade Billingsley, K., Smith, N., Shirley, R., Achieng, L., & Keiser, P. (2011). A quality assessment tool for tuberculosis control activities in resource limited settings. Tuberculosis, 91, 49-53.
    • (2011) Tuberculosis , vol.91 , pp. 49-53
    • McQuade Billingsley, K.1    Smith, N.2    Shirley, R.3    Achieng, L.4    Keiser, P.5
  • 37
    • 33646757492 scopus 로고    scopus 로고
    • On the nature of cavities on protein surfaces: Application to the identification of drugbinding sites
    • Nayal, M., & Honig, B. (2006). On the nature of cavities on protein surfaces: Application to the identification of drugbinding sites. Proteins, 63, 892-906.
    • (2006) Proteins , vol.63 , pp. 892-906
    • Nayal, M.1    Honig, B.2
  • 38
    • 70350648031 scopus 로고    scopus 로고
    • Characterisation of pncA mutations in clinical Mycobacterium tuberculosis isolates in New Zealand
    • Pandey, S., Newton, S., Upton, A., Roberts, S., & Drinković, D. (2009). Characterisation of pncA mutations in clinical Mycobacterium tuberculosis isolates in New Zealand. Pathology, 41, 582-586.
    • (2009) Pathology , vol.41 , pp. 582-586
    • Pandey, S.1    Newton, S.2    Upton, A.3    Roberts, S.4    Drinković, D.5
  • 39
    • 79551528767 scopus 로고    scopus 로고
    • Crystal structure of the pyrazinamidase of Mycobacterium tuberculosis: Insights into natural and acquired resistance to pyrazinamide
    • Petrella, S., Gelus-Ziental, N., Maudry, A., Laurans, C., Boudjelloul, R., & Sougakoff, W. (2011). Crystal structure of the pyrazinamidase of Mycobacterium tuberculosis: Insights into natural and acquired resistance to pyrazinamide. PLoS ONE, 24, 15785.
    • (2011) PLoS ONE , vol.24 , pp. 15785
    • Petrella, S.1    Gelus-Ziental, N.2    Maudry, A.3    Laurans, C.4    Boudjelloul, R.5    Sougakoff, W.6
  • 41
    • 79958089433 scopus 로고    scopus 로고
    • Relationship between mutation of serine residue at 315th position in M. Tuberculosis catalase-peroxidase enzyme and Isoniazid susceptibility: An in silico analysis
    • Purohit, R., Rajendran, V., & Sethumadhavan, R. (2011a). Relationship between mutation of serine residue at 315th position in M. tuberculosis catalase-peroxidase enzyme and Isoniazid susceptibility: An in silico analysis. Journal of Molecular Modeling, 17, 869-877.
    • (2011) Journal of Molecular Modeling , vol.17 , pp. 869-877
    • Purohit, R.1    Rajendran, V.2    Sethumadhavan, R.3
  • 42
    • 79959449643 scopus 로고    scopus 로고
    • Studies on adaptability of binding residues and flap region of TMC-114 resistance HIV-1 protease mutants
    • Purohit, R., Rajendran, V., & Sethumadhavan, R. (2011b). Studies on adaptability of binding residues and flap region of TMC-114 resistance HIV-1 protease mutants. Journal of Biomolecular Structure & Dynamics, 29, 137-152.
    • (2011) Journal of Biomolecular Structure & Dynamics , vol.29 , pp. 137-152
    • Purohit, R.1    Rajendran, V.2    Sethumadhavan, R.3
  • 43
    • 77956634216 scopus 로고    scopus 로고
    • Structural basis for the resilience of Darunavir (TMC114) resistance major flap mutations of HIV-1 protease
    • Purohit, R., & Sethumadhavan, R. (2009). Structural basis for the resilience of Darunavir (TMC114) resistance major flap mutations of HIV-1 protease. Interdisciplinary science, 1, 320-328.
    • (2009) Interdisciplinary Science , vol.1 , pp. 320-328
    • Purohit, R.1    Sethumadhavan, R.2
  • 44
    • 84864771186 scopus 로고    scopus 로고
    • In silico investigation of molecular mechanism of laminopathy cause by a point mutation (R482W) in lamin A/C protein
    • Rajendran V., Purohit R., & Sethumadhavan, R. (2012). In silico investigation of molecular mechanism of laminopathy cause by a point mutation (R482W) in lamin A/C protein. Amino Acids, 43, 603-615.
    • (2012) Amino Acids , vol.43 , pp. 603-615
    • Rajendran, V.1    Purohit, R.2    Sethumadhavan, R.3
  • 45
    • 0031718310 scopus 로고    scopus 로고
    • Homology modeling, model and software evaluation: Three related resources
    • Rodriguez, R., Chinea, G., Lopez, N., Pons, T., & Vriend, G. (1998). Homology modeling, model and software evaluation: Three related resources. Bioinformatics, 14, 523-528.
    • (1998) Bioinformatics , vol.14 , pp. 523-528
    • Rodriguez, R.1    Chinea, G.2    Lopez, N.3    Pons, T.4    Vriend, G.5
  • 47
    • 36749077465 scopus 로고    scopus 로고
    • Automatic prediction of protein interactions with large scale motion
    • Schneidman-Duhovny, D., Nussinov, R., & Wolfson, H. J. (2007). Automatic prediction of protein interactions with large scale motion. Protein, 69, 764-773.
    • (2007) Protein , vol.69 , pp. 764-773
    • Schneidman-Duhovny, D.1    Nussinov, R.2    Wolfson, H.J.3
  • 48
    • 0029954860 scopus 로고    scopus 로고
    • Mutations in pncA, a gene encoding pyrazinamidase/nicotinamidase, cause resistance to the antituberculous drug pyrazinamie in tubercle bacillus
    • Scorpio, A., & Zhang, Y. (1996). Mutations in pncA, a gene encoding pyrazinamidase/nicotinamidase, cause resistance to the antituberculous drug pyrazinamie in tubercle bacillus. Nature Medicine, 2, 662-667.
    • (1996) Nature Medicine , vol.2 , pp. 662-667
    • Scorpio, A.1    Zhang, Y.2
  • 52
    • 66149099261 scopus 로고    scopus 로고
    • Epidemiology of antituberculosis drug resistance 2002-07: An update analysis of the Global Project on Anti-tuberculosis Drug Resistance Surveillance
    • Global Project on Anti-Tuberculosis Drug Resistance Surveillance
    • Wright, A., Zignol, M., Van Deun, A., Falzon, D., Gerdes, S. R., Feldman, K., ... Global Project on Anti-Tuberculosis Drug Resistance Surveillance (2009). Epidemiology of antituberculosis drug resistance 2002-07: An update analysis of the Global Project on Anti-tuberculosis Drug Resistance Surveillance. Lancet, 373, 1861-1873.
    • (2009) Lancet , vol.373 , pp. 1861-1873
    • Wright, A.1    Zignol, M.2    Van Deun, A.3    Falzon, D.4    Gerdes, S.R.5    Feldman, K.6
  • 53
    • 0028332007 scopus 로고
    • A role for surface hydrophobicity in protein-protein recognition
    • Young, L., Jernigan, R. L., & Covell, D. G. (1994). A role for surface hydrophobicity in protein-protein recognition. Protein Science, 3, 717-729.
    • (1994) Protein Science , vol.3 , pp. 717-729
    • Young, L.1    Jernigan, R.L.2    Covell, D.G.3
  • 55
    • 67649935699 scopus 로고    scopus 로고
    • Characterization of pncA mutations of pyrazinamide-resistant Mycobacterium tuberculosis in Turkey
    • Yüksel, P., & Tansel, O. (2009). Characterization of pncA mutations of pyrazinamide-resistant Mycobacterium tuberculosis in Turkey. New Microbiologica, 32, 153-158.
    • (2009) New Microbiologica , vol.32 , pp. 153-158
    • Yüksel, P.1    Tansel, O.2
  • 56
    • 38549101919 scopus 로고    scopus 로고
    • Characterization of Mycobacterium tuberculosis nicotinamidase/ pyrazinamidase
    • Zhang, H., Deng, J. Y., Bi, L. J., Zhou, Y. F., Zhang, Z. P., Zhang, C. G., ... Zhang, X. E. (2008). Characterization of Mycobacterium tuberculosis nicotinamidase/pyrazinamidase. FEBS Journal, 275, 753-762.
    • (2008) FEBS Journal , vol.275 , pp. 753-762
    • Zhang, H.1    Deng, J.Y.2    Bi, L.J.3    Zhou, Y.F.4    Zhang, Z.P.5    Zhang, C.G.6    Zhang, X.E.7
  • 58
    • 0031552370 scopus 로고    scopus 로고
    • Determination of atomic desolvation energies from the structures of crystallized proteins
    • Zhang, C., Vasmatzis, G., Cornette, J. L., & DeLisi, C. (1997). Determination of atomic desolvation energies from the structures of crystallized proteins. Journal of Molecular Biology, 267, 707-726.
    • (1997) Journal of Molecular Biology , vol.267 , pp. 707-726
    • Zhang, C.1    Vasmatzis, G.2    Cornette, J.L.3    Delisi, C.4
  • 59
    • 0242437861 scopus 로고    scopus 로고
    • Mode of action of pyrazinamide: Disruption of Mycobacterium tuberculosis membrane transport and energetic by pyrazinoic acid
    • Zhang, Y., Wade, M. M., Scorpio, A., Zhang, H., & Sun, Z. (2003). Mode of action of pyrazinamide: Disruption of Mycobacterium tuberculosis membrane transport and energetic by pyrazinoic acid. Journal of Antimicrobial Chemotherapy, 52, 790-795.
    • (2003) Journal of Antimicrobial Chemotherapy , vol.52 , pp. 790-795
    • Zhang, Y.1    Wade, M.M.2    Scorpio, A.3    Zhang, H.4    Sun, Z.5
  • 60
    • 84862732034 scopus 로고    scopus 로고
    • Molecular dynamics simulations suggest ligand's binding to nicotinamidase/pyrazinamidase
    • Zhang, J. L., Zheng, Q. C., Li, Z. Q., & Zhang, H. X. (2012). Molecular dynamics simulations suggest ligand's binding to nicotinamidase/ pyrazinamidase. PLoS ONE, 7, 39546.
    • (2012) PLoS ONE , vol.7 , pp. 39546
    • Zhang, J.L.1    Zheng, Q.C.2    Li, Z.Q.3    Zhang, H.X.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.