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Volumn 160, Issue , 2014, Pages 2304-2318

Characterization of a dual-active enzyme, DcpA, Involved in cyclic diguanosine monophosphate turnover in Mycobacterium smegmatis

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; CYCLIC GMP DEPENDENT PROTEIN KINASE; DCPA ENZYME; DIMER; MONOMER; UNCLASSIFIED DRUG; BIS(3',5')-CYCLIC DIGUANYLIC ACID; CYCLIC GMP; DIGUANYLATE CYCLASE; ESCHERICHIA COLI PROTEIN; LYASE; PROTEIN BINDING;

EID: 84930347202     PISSN: 13500872     EISSN: 14652080     Source Type: Journal    
DOI: 10.1099/mic.0.080200-0     Document Type: Article
Times cited : (17)

References (59)
  • 2
    • 79959658770 scopus 로고    scopus 로고
    • Mass spectrometric identification of an intramolecular disulfide bond in thermally inactivated triosephosphate isomerase from a thermophilic organism Methanocaldococcus jannaschii
    • Banerjee, M., Gupta, K., Balaram, H. & Balaram, P. (2011). Mass spectrometric identification of an intramolecular disulfide bond in thermally inactivated triosephosphate isomerase from a thermophilic organism Methanocaldococcus jannaschii. Rapid Commun Mass Spectrom 25, 1915–1923.
    • (2011) Rapid Commun Mass Spectrom , vol.25 , pp. 1915-1923
    • Banerjee, M.1    Gupta, K.2    Balaram, H.3    Balaram, P.4
  • 4
    • 84861918212 scopus 로고    scopus 로고
    • A full-length bifunctional protein involved in cdi-GMP turnover is required for long-term survival under nutrient starvation in Mycobacterium smegmatis
    • Bharati, B. K., Sharma, I. M., Kasetty, S., Kumar, M., Mukherjee, R. & Chatterji, D. (2012). A full-length bifunctional protein involved in cdi-GMP turnover is required for long-term survival under nutrient starvation in Mycobacterium smegmatis. Microbiology 158, 1415–1427.
    • (2012) Microbiology , vol.158 , pp. 1415-1427
    • Bharati, B.K.1    Sharma, I.M.2    Kasetty, S.3    Kumar, M.4    Mukherjee, R.5    Chatterji, D.6
  • 5
    • 84883052624 scopus 로고    scopus 로고
    • Identification and characterization of starvation induced msdgc-1 promoter involved in the c-di-GMP turnover
    • Bharati, B. K., Swetha, R. K. & Chatterji, D. (2013). Identification and characterization of starvation induced msdgc-1 promoter involved in the c-di-GMP turnover. Gene 528, 99–108.
    • (2013) Gene , vol.528 , pp. 99-108
    • Bharati, B.K.1    Swetha, R.K.2    Chatterji, D.3
  • 6
    • 84877759068 scopus 로고    scopus 로고
    • Rapid mass spectrometric determination of disulfide connectivity in peptides and proteins
    • Bhattacharyya, M., Gupta, K., Gowd, K. H. & Balaram, P. (2013). Rapid mass spectrometric determination of disulfide connectivity in peptides and proteins. Mol Biosyst 9, 1340–1350.
    • (2013) Mol Biosyst , vol.9 , pp. 1340-1350
    • Bhattacharyya, M.1    Gupta, K.2    Gowd, K.H.3    Balaram, P.4
  • 9
    • 84865777197 scopus 로고    scopus 로고
    • Protein oligomerization monitored by fluorescence fluctuation spectroscopy: Self-assembly of rubisco activase
    • Chakraborty, M., Kuriata, A. M., Nathan Henderson, J., Salvucci, M. E., Wachter, R. M. & Levitus, M. (2012). Protein oligomerization monitored by fluorescence fluctuation spectroscopy: self-assembly of rubisco activase. Biophys J 103, 949–958.
    • (2012) Biophys J , vol.103 , pp. 949-958
    • Chakraborty, M.1    Kuriata, A.M.2    Nathan Henderson, J.3    Salvucci, M.E.4    Wachter, R.M.5    Levitus, M.6
  • 11
    • 84865502940 scopus 로고    scopus 로고
    • The prokaryote messenger c-di-GMP triggers stalk cell differentiation in Dictyostelium
    • Chen, Z. H. & Schaap, P. (2012). The prokaryote messenger c-di-GMP triggers stalk cell differentiation in Dictyostelium. Nature 488, 680–683.
    • (2012) Nature , vol.488 , pp. 680-683
    • Chen, Z.H.1    Schaap, P.2
  • 12
    • 37449010013 scopus 로고    scopus 로고
    • Identification and characterization of the dps promoter of Mycobacterium smegmatis: Promoter recognition by stress-specific extracytoplasmic function sigma factors sigmaH and sigmaF
    • Chowdhury, R. P., Gupta, S. & Chatterji, D. (2007). Identification and characterization of the dps promoter of Mycobacterium smegmatis: promoter recognition by stress-specific extracytoplasmic function sigma factors sigmaH and sigmaF. J Bacteriol 189, 8973–8981.
    • (2007) J Bacteriol , vol.189 , pp. 8973-8981
    • Chowdhury, R.P.1    Gupta, S.2    Chatterji, D.3
  • 13
    • 65349157710 scopus 로고    scopus 로고
    • Uncovering new signaling proteins and potential drug targets through the interactome analysis of Mycobacterium tuberculosis
    • Cui, T., Zhang, L., Wang, X. & He, Z. G. (2009). Uncovering new signaling proteins and potential drug targets through the interactome analysis of Mycobacterium tuberculosis. BMC Genomics 10, 118.
    • (2009) BMC Genomics , vol.10 , pp. 118
    • Cui, T.1    Zhang, L.2    Wang, X.3    He, Z.G.4
  • 16
    • 70349783823 scopus 로고    scopus 로고
    • Determinants for the activation and autoinhibition of the diguanylate cyclase response regulator WspR
    • De, N., Navarro, M. V., Raghavan, R. V. & Sondermann, H. (2009). Determinants for the activation and autoinhibition of the diguanylate cyclase response regulator WspR. J Mol Biol 393, 619–633.
    • (2009) J Mol Biol , vol.393 , pp. 619-633
    • De, N.1    Navarro, M.V.2    Raghavan, R.V.3    Sondermann, H.4
  • 17
    • 2442515282 scopus 로고    scopus 로고
    • Rv1818c-encoded PE_PGRS protein of Mycobacterium tuberculosis is surface exposed and influences bacterial cell structure
    • Delogu, G., Pusceddu, C., Bua, A., Fadda, G., Brennan, M. J. & Zanetti, S. (2004). Rv1818c-encoded PE_PGRS protein of Mycobacterium tuberculosis is surface exposed and influences bacterial cell structure. Mol Microbiol 52, 725–733.
    • (2004) Mol Microbiol , vol.52 , pp. 725-733
    • Delogu, G.1    Pusceddu, C.2    Bua, A.3    Fadda, G.4    Brennan, M.J.5    Zanetti, S.6
  • 18
    • 84868570852 scopus 로고    scopus 로고
    • An elegant way to quantitatively analyze oligomer formation in solution
    • Engelborghs, Y. (2012). An elegant way to quantitatively analyze oligomer formation in solution. Biophys J 103, 1811–1812.
    • (2012) Biophys J , vol.103 , pp. 1811-1812
    • Engelborghs, Y.1
  • 19
    • 38649102818 scopus 로고    scopus 로고
    • Vibrio parahaemolyticus ScrC modulates cyclic dimeric GMP regulation of gene expression relevant to growth on surfaces
    • Ferreira, R. B., Antunes, L. C., Greenberg, E. P. & McCarter, L. L. (2008). Vibrio parahaemolyticus ScrC modulates cyclic dimeric GMP regulation of gene expression relevant to growth on surfaces. J Bacteriol 190, 851–860.
    • (2008) J Bacteriol , vol.190 , pp. 851-860
    • Ferreira, R.B.1    Antunes, L.C.2    Greenberg, E.P.3    McCarter, L.L.4
  • 20
    • 34447505050 scopus 로고    scopus 로고
    • Identification of two Mycobacterium smegmatis lipoproteins exported by a SecA2-dependent pathway
    • Gibbons, H. S., Wolschendorf, F., Abshire, M., Niederweis, M. & Braunstein, M. (2007). Identification of two Mycobacterium smegmatis lipoproteins exported by a SecA2-dependent pathway. J Bacteriol 189, 5090–5100.
    • (2007) J Bacteriol , vol.189 , pp. 5090-5100
    • Gibbons, H.S.1    Wolschendorf, F.2    Abshire, M.3    Niederweis, M.4    Braunstein, M.5
  • 21
    • 77957293952 scopus 로고    scopus 로고
    • Disulfide bond assignments by mass spectrometry of native natural peptides: Cysteine pairing in disulfide bonded conotoxins
    • Gupta, K., Kumar, M. & Balaram, P. (2010a). Disulfide bond assignments by mass spectrometry of native natural peptides: cysteine pairing in disulfide bonded conotoxins. Anal Chem 82, 8313–8319.
    • (2010) Anal Chem , vol.82 , pp. 8313-8319
    • Gupta, K.1    Kumar, M.2    Balaram, P.3
  • 22
    • 78649800745 scopus 로고    scopus 로고
    • Identification, activity and disulfide connectivity of c-di-GMP regulating proteins in Mycobacterium tuberculosis
    • Gupta, K., Kumar, P. & Chatterji, D. (2010b). Identification, activity and disulfide connectivity of c-di-GMP regulating proteins in Mycobacterium tuberculosis. PLoS ONE 5, e15072.
    • (2010) PLoS ONE , vol.5
    • Gupta, K.1    Kumar, P.2    Chatterji, D.3
  • 23
    • 63049137897 scopus 로고    scopus 로고
    • Principles of c-di-GMP signalling in bacteria
    • Hengge, R. (2009). Principles of c-di-GMP signalling in bacteria. Nat Rev Microbiol 7, 263–273.
    • (2009) Nat Rev Microbiol , vol.7 , pp. 263-273
    • Hengge, R.1
  • 24
    • 84879571298 scopus 로고    scopus 로고
    • Subcellular clustering of the phosphorylated WspR response regulator protein stimulates its diguanylate cyclase activity
    • Huangyutitham, V., Gü vener, Z. T. & Harwood, C. S. (2013). Subcellular clustering of the phosphorylated WspR response regulator protein stimulates its diguanylate cyclase activity. MBio 4, e00242-13.
    • (2013) MBio , vol.4 , pp. e00242-e00313
    • Huangyutitham, V.1    Gü Vener, Z.T.2    Harwood, C.S.3
  • 26
    • 33744481783 scopus 로고    scopus 로고
    • Molecular dissection of the mycobacterial stringent response protein Rel
    • Jain, V., Saleem-Batcha, R., China, A. & Chatterji, D. (2006). Molecular dissection of the mycobacterial stringent response protein Rel. Protein Sci 15, 1449–1464.
    • (2006) Protein Sci , vol.15 , pp. 1449-1464
    • Jain, V.1    Saleem-Batcha, R.2    China, A.3    Chatterji, D.4
  • 27
    • 13844262033 scopus 로고    scopus 로고
    • c-di-GMP (39-59-cyclic diguanylic acid) inhibits Staphylococcus aureus cell–cell interactions and biofilm formation
    • Karaolis, D. K., Rashid, M. H., Chythanya, R., Luo, W., Hyodo, M. & Hayakawa, Y. (2005). c-di-GMP (39-59-cyclic diguanylic acid) inhibits Staphylococcus aureus cell–cell interactions and biofilm formation. Antimicrob Agents Chemother 49, 1029–1038.
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 1029-1038
    • Karaolis, D.K.1    Rashid, M.H.2    Chythanya, R.3    Luo, W.4    Hyodo, M.5    Hayakawa, Y.6
  • 28
    • 36549021125 scopus 로고    scopus 로고
    • BifA, a cyclic-Di-GMP phosphodiesterase, inversely regulates biofilm formation and swarming motility by Pseudomonas aeruginosa PA14
    • Kuchma, S. L., Brothers, K. M., Merritt, J. H., Liberati, N. T., Ausubel, F. M. & O’Toole, G. A. (2007). BifA, a cyclic-Di-GMP phosphodiesterase, inversely regulates biofilm formation and swarming motility by Pseudomonas aeruginosa PA14. J Bacteriol 189, 8165–8178.
    • (2007) J Bacteriol , vol.189 , pp. 8165-8178
    • Kuchma, S.L.1    Brothers, K.M.2    Merritt, J.H.3    Liberati, N.T.4    Ausubel, F.M.5    O’toole, G.A.6
  • 29
    • 0036707991 scopus 로고    scopus 로고
    • Modern analytical ultracentrifugation in protein science: a tutorial review
    • Lebowitz, J., Lewis, M. S. & Schuck, P. (2002). Modern analytical ultracentrifugation in protein science: a tutorial review. Protein Sci 11, 2067–2079.
    • (2002) Protein Sci , vol.11 , pp. 2067-2079
    • Lebowitz, J.1    Lewis, M.S.2    Schuck, P.3
  • 30
    • 80052419746 scopus 로고    scopus 로고
    • The atypical two-component sensor kinase Lpl0330 from Legionella pneumophila controls the bifunctional diguanylate cyclase-phosphodiesterase Lpl0329 tomodulate bis-(39-59)-cyclic dimeric GMP synthesis
    • Levet-Paulo, M., Lazzaroni, J. C., Gilbert, C., Atlan, D., Doublet, P. & Vianney, A. (2011). The atypical two-component sensor kinase Lpl0330 from Legionella pneumophila controls the bifunctional diguanylate cyclase-phosphodiesterase Lpl0329 tomodulate bis-(39-59)-cyclic dimeric GMP synthesis. J Biol Chem 286, 31136–31144.
    • (2011) J Biol Chem , vol.286 , pp. 31136-31144
    • Levet-Paulo, M.1    Lazzaroni, J.C.2    Gilbert, C.3    Atlan, D.4    Doublet, P.5    Vianney, A.6
  • 31
    • 84871200600 scopus 로고    scopus 로고
    • LtmA, a novel cyclic di-GMP-responsive activator, broadly regulates the expression of lipid transport and metabolism genes in Mycobacterium smegmatis
    • Li, W. & He, Z. G. (2012). LtmA, a novel cyclic di-GMP-responsive activator, broadly regulates the expression of lipid transport and metabolism genes in Mycobacterium smegmatis. Nucleic Acids Res 40, 11292–11307.
    • (2012) Nucleic Acids Res , vol.40 , pp. 11292-11307
    • Li, W.1    He, Z.G.2
  • 32
    • 84863229664 scopus 로고    scopus 로고
    • Nitric oxide regulation of cyclic di-GMP synthesis and hydrolysis in Shewanella woodyi
    • Liu, N., Xu, Y., Hossain, S., Huang, N., Coursolle, D., Gralnick, J. A. & Boon, E. M. (2012). Nitric oxide regulation of cyclic di-GMP synthesis and hydrolysis in Shewanella woodyi. Biochemistry 51, 2087–2099.
    • (2012) Biochemistry , vol.51 , pp. 2087-2099
    • Liu, N.1    Xu, Y.2    Hossain, S.3    Huang, N.4    Coursolle, D.5    Gralnick, J.A.6    Boon, E.M.7
  • 35
    • 33751378939 scopus 로고    scopus 로고
    • Diguanylate cyclases control magnesium-dependent motility of Vibrio fischeri
    • O’Shea, T. M., Klein, A. H., Geszvain, K., Wolfe, A. J. & Visick, K. L. (2006). Diguanylate cyclases control magnesium-dependent motility of Vibrio fischeri. J Bacteriol 188, 8196–8205.
    • (2006) J Bacteriol , vol.188 , pp. 8196-8205
    • O’shea, T.M.1    Klein, A.H.2    Geszvain, K.3    Wolfe, A.J.4    Visick, K.L.5
  • 36
    • 0033917102 scopus 로고    scopus 로고
    • High intracellular level of guanosine tetraphosphate in Mycobacterium smegmatis changes the morphology of the bacterium
    • Ojha, A. K., Mukherjee, T. K. & Chatterji, D. (2000). High intracellular level of guanosine tetraphosphate in Mycobacterium smegmatis changes the morphology of the bacterium. Infect Immun 68, 4084–4091.
    • (2000) Infect Immun , vol.68 , pp. 4084-4091
    • Ojha, A.K.1    Mukherjee, T.K.2    Chatterji, D.3
  • 37
    • 0031939281 scopus 로고    scopus 로고
    • Mechanisms of latency in Mycobacterium tuberculosis
    • Parrish, N. M., Dick, J. D. & Bishai, W. R. (1998). Mechanisms of latency in Mycobacterium tuberculosis. Trends Microbiol 6, 107–112.
    • (1998) Trends Microbiol , vol.6 , pp. 107-112
    • Parrish, N.M.1    Dick, J.D.2    Bishai, W.R.3
  • 38
    • 1842451699 scopus 로고    scopus 로고
    • Cell cycle-dependent dynamic localization of a bacterial response regulator with a novel di-guanylate cyclase output domain
    • Paul, R., Weiser, S., Amiot, N. C., Chan, C., Schirmer, T., Giese, B. & Jenal, U. (2004). Cell cycle-dependent dynamic localization of a bacterial response regulator with a novel di-guanylate cyclase output domain. Genes Dev 18, 715–727.
    • (2004) Genes Dev , vol.18 , pp. 715-727
    • Paul, R.1    Weiser, S.2    Amiot, N.C.3    Chan, C.4    Schirmer, T.5    Giese, B.6    Jenal, U.7
  • 39
    • 35748950123 scopus 로고    scopus 로고
    • Activation of the diguanylate cyclase PleD by phosphorylationmediated dimerization
    • Paul, R., Abel, S., Wassmann, P., Beck, A., Heerklotz, H. & Jenal, U. (2007). Activation of the diguanylate cyclase PleD by phosphorylationmediated dimerization. J Biol Chem 282, 29170–29177.
    • (2007) J Biol Chem , vol.282 , pp. 29170-29177
    • Paul, R.1    Abel, S.2    Wassmann, P.3    Beck, A.4    Heerklotz, H.5    Jenal, U.6
  • 40
    • 70350501347 scopus 로고    scopus 로고
    • A flavin cofactor-binding PAS domain regulates c-di-GMP synthesis in AxDGC2 fromAcetobacter xylinum
    • Qi, Y., Rao, F., Luo, Z. & Liang, Z. X. (2009). A flavin cofactor-binding PAS domain regulates c-di-GMP synthesis in AxDGC2 fromAcetobacter xylinum. Biochemistry 48, 10275–10285.
    • (2009) Biochemistry , vol.48 , pp. 10275-10285
    • Qi, Y.1    Rao, F.2    Luo, Z.3    Liang, Z.X.4
  • 41
    • 67749113278 scopus 로고    scopus 로고
    • The functional role of a conserved loop in EAL domain-based cyclic di-GMP-specific phosphodiesterase
    • Rao, F., Qi, Y., Chong, H. S., Kotaka, M., Li, B., Li, J., Lescar, J., Tang, K. & Liang, Z. X. (2009). The functional role of a conserved loop in EAL domain-based cyclic di-GMP-specific phosphodiesterase. J Bacteriol 191, 4722–4731.
    • (2009) J Bacteriol , vol.191 , pp. 4722-4731
    • Rao, F.1    Qi, Y.2    Chong, H.S.3    Kotaka, M.4    Li, B.5    Li, J.6    Lescar, J.7    Tang, K.8    Liang, Z.X.9
  • 43
    • 84874914744 scopus 로고    scopus 로고
    • Cyclic di-GMP: The first 25 years of a universal bacterial second messenger
    • Rö mling, U., Galperin, M. Y. & Gomelsky, M. (2013). Cyclic di-GMP: the first 25 years of a universal bacterial second messenger. Microbiol Mol Biol Rev 77, 1–52.
    • (2013) Microbiol Mol Biol Rev , vol.77 , pp. 1-52
    • Rö Mling, U.1    Galperin, M.Y.2    Gomelsky, M.3
  • 44
    • 84864003643 scopus 로고    scopus 로고
    • The phosphodiesterase DipA (PA5017) is essential for Pseudomonas aeruginosa biofilm dispersion
    • Roy, A. B., Petrova, O. E. & Sauer, K. (2012). The phosphodiesterase DipA (PA5017) is essential for Pseudomonas aeruginosa biofilm dispersion. J Bacteriol 194, 2904–2915.
    • (2012) J Bacteriol , vol.194 , pp. 2904-2915
    • Roy, A.B.1    Petrova, O.E.2    Sauer, K.3
  • 45
    • 14244254898 scopus 로고    scopus 로고
    • Cyclic diguanylate is a ubiquitous signaling molecule in bacteria: Insights into biochemistry of the GGDEF protein domain
    • Ryjenkov, D. A., Tarutina, M., Moskvin, O. V. & Gomelsky, M. (2005). Cyclic diguanylate is a ubiquitous signaling molecule in bacteria: insights into biochemistry of the GGDEF protein domain. J Bacteriol 187, 1792–1798.
    • (2005) J Bacteriol , vol.187 , pp. 1792-1798
    • Ryjenkov, D.A.1    Tarutina, M.2    Moskvin, O.V.3    Gomelsky, M.4
  • 46
    • 70349274104 scopus 로고    scopus 로고
    • Structural and mechanistic determinants of c-di-GMP signalling
    • Schirmer, T. & Jenal, U. (2009). Structural and mechanistic determinants of c-di-GMP signalling. Nat Rev Microbiol 7, 724–735.
    • (2009) Nat Rev Microbiol , vol.7 , pp. 724-735
    • Schirmer, T.1    Jenal, U.2
  • 47
    • 84895735604 scopus 로고    scopus 로고
    • Nonclassical transpeptidases of Mycobacterium tuberculosis alter cell size, morphology, the cytosolic matrix, protein localization, virulence, and resistance to b-lactams
    • Schoonmaker, M. K., Bishai, W. R. & Lamichhane, G. (2014). Nonclassical transpeptidases of Mycobacterium tuberculosis alter cell size, morphology, the cytosolic matrix, protein localization, virulence, and resistance to b-lactams. J Bacteriol 196, 1394–1402.
    • (2014) J Bacteriol , vol.196 , pp. 1394-1402
    • Schoonmaker, M.K.1    Bishai, W.R.2    Lamichhane, G.3
  • 48
    • 78049426911 scopus 로고    scopus 로고
    • Comparative genomics of cyclic-di-GMP signalling in bacteria: Posttranslational regulation and catalytic activity
    • Seshasayee, A. S., Fraser, G. M. & Luscombe, N. M. (2010). Comparative genomics of cyclic-di-GMP signalling in bacteria: posttranslational regulation and catalytic activity. Nucleic Acids Res 38, 5970–5981.
    • (2010) Nucleic Acids Res , vol.38 , pp. 5970-5981
    • Seshasayee, A.S.1    Fraser, G.M.2    Luscombe, N.M.3
  • 49
    • 84863772351 scopus 로고    scopus 로고
    • Synthesis and characterization of a fluorescent analogue of cyclic di-GMP
    • Sharma, I. M., Dhanaraman, T., Mathew, R. & Chatterji, D. (2012). Synthesis and characterization of a fluorescent analogue of cyclic di-GMP. Biochemistry 51, 5443–5453
    • (2012) Biochemistry , vol.51 , pp. 5443-5453
    • Sharma, I.M.1    Dhanaraman, T.2    Mathew, R.3    Chatterji, D.4
  • 50
    • 0025081151 scopus 로고
    • Isolation and characterization of efficient plasmid transformation mutants of Mycobacterium smegmatis
    • Snapper, S. B., Melton, R. E., Mustafa, S., Kieser, T. & Jacobs, W. R., Jr (1990). Isolation and characterization of efficient plasmid transformation mutants of Mycobacterium smegmatis. Mol Microbiol 4, 1911–1919.
    • (1990) Mol Microbiol , vol.4 , pp. 1911-1919
    • Snapper, S.B.1    Melton, R.E.2    Mustafa, S.3    Kieser, T.4    Jacobs, W.R.5
  • 52
    • 84896790464 scopus 로고    scopus 로고
    • Inherent regulation of EAL domaincatalyzed hydrolysis of second messenger cyclic di-GMP
    • Sundriyal, A., Massa, C., Samoray, D., Zehender, F., Sharpe, T., Jenal, U. & Schirmer, T. (2014). Inherent regulation of EAL domaincatalyzed hydrolysis of second messenger cyclic di-GMP. J Biol Chem 289, 6978–6990.
    • (2014) J Biol Chem , vol.289 , pp. 6978-6990
    • Sundriyal, A.1    Massa, C.2    Samoray, D.3    Zehender, F.4    Sharpe, T.5    Jenal, U.6    Schirmer, T.7
  • 53
    • 33845918217 scopus 로고    scopus 로고
    • An unorthodox bacteriophytochrome from Rhodobacter sphaeroides involved in turnover of the secondmessenger c-di-GMP
    • Tarutina, M., Ryjenkov, D. A. & Gomelsky, M. (2006). An unorthodox bacteriophytochrome from Rhodobacter sphaeroides involved in turnover of the secondmessenger c-di-GMP. J BiolChem281, 34751–34758.
    • (2006) J BiolChem281 , pp. 34751-34758
    • Tarutina, M.1    Ryjenkov, D.A.2    Gomelsky, M.3
  • 54
    • 34047274095 scopus 로고    scopus 로고
    • Unusual features of the cell cycle in mycobacteria: Polar-restricted growth and the snapping-model of cell division
    • Thanky, N. R., Young, D. B. & Robertson, B. D. (2007). Unusual features of the cell cycle in mycobacteria: polar-restricted growth and the snapping-model of cell division. Tuberculosis (Edinb) 87, 231–236.
    • (2007) Tuberculosis (Edinb) , vol.87 , pp. 231-236
    • Thanky, N.R.1    Young, D.B.2    Robertson, B.D.3
  • 55
    • 0031726240 scopus 로고    scopus 로고
    • An inducible expression system permitting the efficient purification of a recombinant antigen from Mycobacterium smegmatis
    • Triccas, J. A., Parish, T., Britton, W. J. & Gicquel, B. (1998). An inducible expression system permitting the efficient purification of a recombinant antigen from Mycobacterium smegmatis. FEMS Microbiol Lett 167, 151–156.
    • (1998) FEMS Microbiol Lett , vol.167 , pp. 151-156
    • Triccas, J.A.1    Parish, T.2    Britton, W.J.3    Gicquel, B.4
  • 56
    • 4644327652 scopus 로고    scopus 로고
    • Native protein mass spectrometry: From intact oligomers to functional machineries
    • van den Heuvel, R. H. H. & Heck, A. J. R. (2004). Native protein mass spectrometry: from intact oligomers to functional machineries. Curr Opin Chem Biol 8, 519–526.
    • (2004) Curr Opin Chem Biol , vol.8 , pp. 519-526
    • van den Heuvel, R.H.H.1    Heck, A.J.R.2
  • 57
    • 67649389852 scopus 로고    scopus 로고
    • Modulation of the oligomerization state of p53 by differential binding of proteins of the S100 family to p53 monomers and tetramers
    • van Dieck, J., Fernandez-Fernandez, M. R., Veprintsev, D. B. & Fersht, A. R. (2009). Modulation of the oligomerization state of p53 by differential binding of proteins of the S100 family to p53 monomers and tetramers. J Biol Chem 284, 13804–13811.
    • (2009) J Biol Chem , vol.284 , pp. 13804-13811
    • van Dieck, J.1    Fernandez-Fernandez, M.R.2    Veprintsev, D.B.3    Fersht, A.R.4
  • 59
    • 34547659282 scopus 로고    scopus 로고
    • Structure of BeF3 –-modified response regulator PleD: Implications for diguanylate cyclase activation, catalysis, and feedback inhibition
    • Wassmann, P., Chan, C., Paul, R., Beck, A., Heerklotz, H., Jenal, U. & Schirmer, T. (2007). Structure of BeF3 –-modified response regulator PleD: implications for diguanylate cyclase activation, catalysis, and feedback inhibition. Structure 15, 915–927.
    • (2007) Structure , vol.15 , pp. 915-927
    • Wassmann, P.1    Chan, C.2    Paul, R.3    Beck, A.4    Heerklotz, H.5    Jenal, U.6    Schirmer, T.7


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