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Volumn 283, Issue 7, 2016, Pages 1286-1299

The α10 helix of DevR, the Mycobacterium tuberculosis dormancy response regulator, regulates its DNA binding and activity

Author keywords

biophysical characterization; DevR DosR; dormancy regulon; M. tuberculosis; signal transduction

Indexed keywords

DEVR PROTEIN; REGULATOR PROTEIN; UNCLASSIFIED DRUG; BACTERIAL DNA; BACTERIAL PROTEIN; DOSR PROTEIN, MYCOBACTERIUM TUBERCULOSIS; PROTEIN BINDING; PROTEIN KINASE;

EID: 84975686870     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.13664     Document Type: Article
Times cited : (11)

References (63)
  • 1
    • 0347091999 scopus 로고    scopus 로고
    • M. Tuberculosis persistence, latency, and drug tolerance
    • Gomez JE, &, McKinney JD, (2004) M. tuberculosis persistence, latency, and drug tolerance. Tuberculosis 84, 29-44.
    • (2004) Tuberculosis , vol.84 , pp. 29-44
    • Gomez, J.E.1    McKinney, J.D.2
  • 2
    • 77952356637 scopus 로고    scopus 로고
    • Tuberculosis: What we don't know can, and does, hurt us
    • Russell DG, Barry CE 3rd, &, Flynn JL, (2010) Tuberculosis: what we don't know can, and does, hurt us. Science 328, 852-856.
    • (2010) Science , vol.328 , pp. 852-856
    • Russell, D.G.1    Barry, C.E.2    Flynn, J.L.3
  • 3
    • 35848943478 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis invasion of macrophages: Linking bacterial gene expression to environmental cues
    • Rohde KH, Abramovitch RB, &, Russell DG, (2007) Mycobacterium tuberculosis invasion of macrophages: linking bacterial gene expression to environmental cues. Cell Host Microbe 2, 352-364.
    • (2007) Cell Host Microbe , vol.2 , pp. 352-364
    • Rohde, K.H.1    Abramovitch, R.B.2    Russell, D.G.3
  • 4
    • 34248205790 scopus 로고    scopus 로고
    • Bacterial response regulators: Versatile regulatory strategies from common domains
    • Gao R, Mack TR, &, Stock AM, (2007) Bacterial response regulators: versatile regulatory strategies from common domains. Trends Biochem Sci 32, 225-234.
    • (2007) Trends Biochem Sci , vol.32 , pp. 225-234
    • Gao, R.1    Mack, T.R.2    Stock, A.M.3
  • 5
    • 84455173453 scopus 로고    scopus 로고
    • Adaptation to environmental stimuli within the host: Two-component signal transduction systems of Mycobacterium tuberculosis
    • Bretl DJ, Demetriadou C, &, Zahrt TC, (2011) Adaptation to environmental stimuli within the host: two-component signal transduction systems of Mycobacterium tuberculosis. Microbiol Mol Biol Rev 75, 566-582.
    • (2011) Microbiol Mol Biol Rev , vol.75 , pp. 566-582
    • Bretl, D.J.1    Demetriadou, C.2    Zahrt, T.C.3
  • 6
    • 1342292544 scopus 로고    scopus 로고
    • DevR-DevS is a bona fide two-component system of Mycobacterium tuberculosis that is hypoxia-responsive in the absence of the DNA-binding domain of DevR
    • Saini DK, Malhotra V, Dey D, Pant N, Das TK, &, Tyagi JS, (2004) DevR-DevS is a bona fide two-component system of Mycobacterium tuberculosis that is hypoxia-responsive in the absence of the DNA-binding domain of DevR. Microbiology 150, 865-875.
    • (2004) Microbiology , vol.150 , pp. 865-875
    • Saini, D.K.1    Malhotra, V.2    Dey, D.3    Pant, N.4    Das, T.K.5    Tyagi, J.S.6
  • 8
    • 43049170080 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis senses host-derived carbon monoxide during macrophage infection
    • Shiloh MU, Manzanillo P, &, Cox JS, (2008) Mycobacterium tuberculosis senses host-derived carbon monoxide during macrophage infection. Cell Host Microbe 3, 323-330.
    • (2008) Cell Host Microbe , vol.3 , pp. 323-330
    • Shiloh, M.U.1    Manzanillo, P.2    Cox, J.S.3
  • 9
    • 77956277547 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis transcriptional adaptation, growth arrest and dormancy phenotype development is triggered by Vitamin C
    • Taneja NK, Dhingra S, Mittal A, Naresh M, &, Tyagi JS, (2010) Mycobacterium tuberculosis transcriptional adaptation, growth arrest and dormancy phenotype development is triggered by vitamin C. PLoS ONE 5, e10860.
    • (2010) PLoS ONE , vol.5 , pp. e10860
    • Taneja, N.K.1    Dhingra, S.2    Mittal, A.3    Naresh, M.4    Tyagi, J.S.5
  • 13
    • 43049182981 scopus 로고    scopus 로고
    • The enduring hypoxic response of Mycobacterium tuberculosis
    • Rustad TR, Harrell MI, Liao R, &, Sherman DR, (2008) The enduring hypoxic response of Mycobacterium tuberculosis. PLoS ONE 3, e1502.
    • (2008) PLoS ONE , vol.3 , pp. e1502
    • Rustad, T.R.1    Harrell, M.I.2    Liao, R.3    Sherman, D.R.4
  • 14
    • 70350048603 scopus 로고    scopus 로고
    • Structure-based design of DevR inhibitor active against nonreplicating Mycobacterium tuberculosis
    • Gupta RK, Thakur TS, Desiraju GR, &, Tyagi JS, (2009) Structure-based design of DevR inhibitor active against nonreplicating Mycobacterium tuberculosis. J Med Chem 52, 6324-6334.
    • (2009) J Med Chem , vol.52 , pp. 6324-6334
    • Gupta, R.K.1    Thakur, T.S.2    Desiraju, G.R.3    Tyagi, J.S.4
  • 15
    • 84859436712 scopus 로고    scopus 로고
    • DevR (DosR) binding peptide inhibits adaptation of Mycobacterium tuberculosis under hypoxia
    • Dhingra S, Kaur K, Taneja NK, &, Tyagi JS, (2012) DevR (DosR) binding peptide inhibits adaptation of Mycobacterium tuberculosis under hypoxia. FEMS Microbiol Lett 330, 66-71.
    • (2012) FEMS Microbiol Lett , vol.330 , pp. 66-71
    • Dhingra, S.1    Kaur, K.2    Taneja, N.K.3    Tyagi, J.S.4
  • 16
    • 84904445853 scopus 로고    scopus 로고
    • DevR (DosR) mimetic peptides impair transcriptional regulation and survival of Mycobacterium tuberculosis under hypoxia by inhibiting the autokinase activity of DevS sensor kinase
    • Kaur K, Taneja NK, Dhingra S, &, Tyagi JS, (2014) DevR (DosR) mimetic peptides impair transcriptional regulation and survival of Mycobacterium tuberculosis under hypoxia by inhibiting the autokinase activity of DevS sensor kinase. BMC Microbiol 14, 195.
    • (2014) BMC Microbiol , vol.14 , pp. 195
    • Kaur, K.1    Taneja, N.K.2    Dhingra, S.3    Tyagi, J.S.4
  • 19
    • 70349113557 scopus 로고    scopus 로고
    • Powerful induction of divergent tgs1-Rv3131 genes in Mycobacterium tuberculosis is mediated by DevR interaction with a high-affinity site and an adjacent cryptic low-affinity site
    • Chauhan S, &, Tyagi JS, (2009) Powerful induction of divergent tgs1-Rv3131 genes in Mycobacterium tuberculosis is mediated by DevR interaction with a high-affinity site and an adjacent cryptic low-affinity site. J Bacteriol 191, 6075-6081.
    • (2009) J Bacteriol , vol.191 , pp. 6075-6081
    • Chauhan, S.1    Tyagi, J.S.2
  • 20
    • 48149089000 scopus 로고    scopus 로고
    • Interaction of DevR with multiple binding sites synergistically activates divergent transcription of narK2-Rv1738 genes in Mycobacterium tuberculosis
    • Chauhan S, &, Tyagi JS, (2008) Interaction of DevR with multiple binding sites synergistically activates divergent transcription of narK2-Rv1738 genes in Mycobacterium tuberculosis. J Bacteriol 190, 5394-5403.
    • (2008) J Bacteriol , vol.190 , pp. 5394-5403
    • Chauhan, S.1    Tyagi, J.S.2
  • 21
    • 44949128202 scopus 로고    scopus 로고
    • Cooperative binding of phosphorylated DevR to upstream sites is necessary and sufficient for activation of the Rv3134c-devRS operon in Mycobacterium tuberculosis: Implication in the induction of DevR target genes
    • Chauhan S, &, Tyagi JS, (2008) Cooperative binding of phosphorylated DevR to upstream sites is necessary and sufficient for activation of the Rv3134c-devRS operon in Mycobacterium tuberculosis: implication in the induction of DevR target genes. J Bacteriol 190, 4301-4312.
    • (2008) J Bacteriol , vol.190 , pp. 4301-4312
    • Chauhan, S.1    Tyagi, J.S.2
  • 22
    • 80052535188 scopus 로고    scopus 로고
    • Comprehensive insights into Mycobacterium tuberculosis DevR (DosR) regulon activation switch
    • Chauhan S, Sharma D, Singh A, Surolia A, &, Tyagi JS, (2011) Comprehensive insights into Mycobacterium tuberculosis DevR (DosR) regulon activation switch. Nucleic Acids Res 39, 7400-7414.
    • (2011) Nucleic Acids Res , vol.39 , pp. 7400-7414
    • Chauhan, S.1    Sharma, D.2    Singh, A.3    Surolia, A.4    Tyagi, J.S.5
  • 23
    • 79551548079 scopus 로고    scopus 로고
    • Determinants outside the DevR C-terminal domain are essential for cooperativity and robust activation of dormancy genes in Mycobacterium tuberculosis
    • Gautam US, Chauhan S, &, Tyagi JS, (2011) Determinants outside the DevR C-terminal domain are essential for cooperativity and robust activation of dormancy genes in Mycobacterium tuberculosis. PLoS ONE 6, e16500.
    • (2011) PLoS ONE , vol.6 , pp. e16500
    • Gautam, U.S.1    Chauhan, S.2    Tyagi, J.S.3
  • 24
    • 80052548122 scopus 로고    scopus 로고
    • The residue threonine 82 of DevR (DosR) is essential for DevR activation and function in Mycobacterium tuberculosis despite its atypical location
    • Gautam US, Sikri K, &, Tyagi JS, (2011) The residue threonine 82 of DevR (DosR) is essential for DevR activation and function in Mycobacterium tuberculosis despite its atypical location. J Bacteriol 193, 4849-4858.
    • (2011) J Bacteriol , vol.193 , pp. 4849-4858
    • Gautam, U.S.1    Sikri, K.2    Tyagi, J.S.3
  • 25
    • 84860380181 scopus 로고    scopus 로고
    • Appropriate DevR (DosR)-mediated signaling determines transcriptional response, hypoxic viability and virulence of Mycobacterium tuberculosis
    • Majumdar SD, Vashist A, Dhingra S, Gupta R, Singh A, Challu VK, Ramanathan VD, Kumar P, &, Tyagi JS, (2012) Appropriate DevR (DosR)-mediated signaling determines transcriptional response, hypoxic viability and virulence of Mycobacterium tuberculosis. PLoS ONE 7, e35847.
    • (2012) PLoS ONE , vol.7 , pp. e35847
    • Majumdar, S.D.1    Vashist, A.2    Dhingra, S.3    Gupta, R.4    Singh, A.5    Challu, V.K.6    Ramanathan, V.D.7    Kumar, P.8    Tyagi, J.S.9
  • 26
    • 27744477943 scopus 로고    scopus 로고
    • Structures of Mycobacterium tuberculosis DosR and DosR-DNA complex involved in gene activation during adaptation to hypoxic latency
    • Wisedchaisri G, Wu M, Rice AE, Roberts DM, Sherman DR, &, Hol WG, (2005) Structures of Mycobacterium tuberculosis DosR and DosR-DNA complex involved in gene activation during adaptation to hypoxic latency. J Mol Biol 354, 630-641.
    • (2005) J Mol Biol , vol.354 , pp. 630-641
    • Wisedchaisri, G.1    Wu, M.2    Rice, A.E.3    Roberts, D.M.4    Sherman, D.R.5    Hol, W.G.6
  • 27
    • 41149103311 scopus 로고    scopus 로고
    • Crystal structures of the response regulator DosR from Mycobacterium tuberculosis suggest a helix rearrangement mechanism for phosphorylation activation
    • Wisedchaisri G, Wu M, Sherman DR, &, Hol WG, (2008) Crystal structures of the response regulator DosR from Mycobacterium tuberculosis suggest a helix rearrangement mechanism for phosphorylation activation. J Mol Biol 378, 227-242.
    • (2008) J Mol Biol , vol.378 , pp. 227-242
    • Wisedchaisri, G.1    Wu, M.2    Sherman, D.R.3    Hol, W.G.4
  • 28
    • 84893005279 scopus 로고    scopus 로고
    • Essentiality of DevR/DosR interaction with SigA for the Dormancy Survival Programme in Mycobacterium tuberculosis
    • Gautam US, Sikri K, Vashist A, Singh V, &, Tyagi JS, (2014) Essentiality of DevR/DosR interaction with SigA for the Dormancy Survival Programme in Mycobacterium tuberculosis. J Bacteriol 196, 790-799.
    • (2014) J Bacteriol , vol.196 , pp. 790-799
    • Gautam, U.S.1    Sikri, K.2    Vashist, A.3    Singh, V.4    Tyagi, J.S.5
  • 29
    • 29244443682 scopus 로고    scopus 로고
    • Transcription and autoregulation of the Rv3134c-devR-devS operon of Mycobacterium tuberculosis
    • Bagchi G, Chauhan S, Sharma D, &, Tyagi JS, (2005) Transcription and autoregulation of the Rv3134c-devR-devS operon of Mycobacterium tuberculosis. Microbiology 151, 4045-4053.
    • (2005) Microbiology , vol.151 , pp. 4045-4053
    • Bagchi, G.1    Chauhan, S.2    Sharma, D.3    Tyagi, J.S.4
  • 30
    • 0025775119 scopus 로고
    • Modular structure of FixJ: Homology of the transcriptional activator domain with the -35 binding domain of sigma factors
    • Kahn D, &, Ditta G, (1991) Modular structure of FixJ: homology of the transcriptional activator domain with the -35 binding domain of sigma factors. Mol Microbiol 5, 987-997.
    • (1991) Mol Microbiol , vol.5 , pp. 987-997
    • Kahn, D.1    Ditta, G.2
  • 31
    • 0037168492 scopus 로고    scopus 로고
    • Effect of phosphorylation on the interdomain interaction of the response regulator, NarL
    • Eldridge AM, Kang H-S, Johnson E, Gunsalus R, &, Dahlquist FW, (2002) Effect of phosphorylation on the interdomain interaction of the response regulator, NarL. Biochemistry 41, 15173-15180.
    • (2002) Biochemistry , vol.41 , pp. 15173-15180
    • Eldridge, A.M.1    Kang, H.-S.2    Johnson, E.3    Gunsalus, R.4    Dahlquist, F.W.5
  • 33
    • 0028075844 scopus 로고
    • Acetyl phosphate and the activation of two-component response regulators
    • McCleary WR, &, Stock JB, (1994) Acetyl phosphate and the activation of two-component response regulators. J Biol Chem 269, 31567-31572.
    • (1994) J Biol Chem , vol.269 , pp. 31567-31572
    • McCleary, W.R.1    Stock, J.B.2
  • 34
    • 0029896773 scopus 로고    scopus 로고
    • The activation of PhoB by acetylphosphate
    • McCleary WR, (1996) The activation of PhoB by acetylphosphate. Mol Microbiol 20, 1155-1163.
    • (1996) Mol Microbiol , vol.20 , pp. 1155-1163
    • McCleary, W.R.1
  • 35
    • 84881237084 scopus 로고    scopus 로고
    • A link between dimerization and autophosphorylation of the response regulator PhoB
    • Creager-Allen RL, Silversmith RE, &, Bourret RB, (2013) A link between dimerization and autophosphorylation of the response regulator PhoB. J Biol Chem 288, 21755-21769.
    • (2013) J Biol Chem , vol.288 , pp. 21755-21769
    • Creager-Allen, R.L.1    Silversmith, R.E.2    Bourret, R.B.3
  • 36
    • 24344476732 scopus 로고    scopus 로고
    • Mechanism of activation for transcription factor PhoB suggested by different modes of dimerization in the inactive and active states
    • Bachhawat P, Swapna GV, Montelione GT, &, Stock AM, (2005) Mechanism of activation for transcription factor PhoB suggested by different modes of dimerization in the inactive and active states. Structure 13, 1353-1363.
    • (2005) Structure , vol.13 , pp. 1353-1363
    • Bachhawat, P.1    Swapna, G.V.2    Montelione, G.T.3    Stock, A.M.4
  • 37
    • 24344450314 scopus 로고    scopus 로고
    • An active-like structure in the unphosphorylated StyR response regulator suggests a phosphorylation-dependent allosteric activation mechanism
    • Milani M, Leoni L, Rampioni G, Zennaro E, Ascenzi P, &, Bolognesi M, (2005) An active-like structure in the unphosphorylated StyR response regulator suggests a phosphorylation-dependent allosteric activation mechanism. Structure 13, 1289-1297.
    • (2005) Structure , vol.13 , pp. 1289-1297
    • Milani, M.1    Leoni, L.2    Rampioni, G.3    Zennaro, E.4    Ascenzi, P.5    Bolognesi, M.6
  • 38
    • 0030797034 scopus 로고    scopus 로고
    • Involvement of the amino-terminal phosphorylation module of UhpA in activation of uhpT transcription in Escherichia coli
    • Webber CA, &, Kadner RJ, (1997) Involvement of the amino-terminal phosphorylation module of UhpA in activation of uhpT transcription in Escherichia coli. Mol Microbiol 24, 1039-1048.
    • (1997) Mol Microbiol , vol.24 , pp. 1039-1048
    • Webber, C.A.1    Kadner, R.J.2
  • 39
    • 0026773062 scopus 로고
    • Phosphorylation of nitrogen regulator I of Escherichia coli induces strong cooperative binding to DNA essential for activation of transcription
    • Weiss V, Claverie-Martin F, &, Magasanik B, (1992) Phosphorylation of nitrogen regulator I of Escherichia coli induces strong cooperative binding to DNA essential for activation of transcription. Proc Natl Acad Sci USA 89, 5088-5092.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 5088-5092
    • Weiss, V.1    Claverie-Martin, F.2    Magasanik, B.3
  • 40
    • 0030894489 scopus 로고    scopus 로고
    • Unusual oligomerization required for activity of NtrC, a bacterial enhancer-binding protein
    • Wyman C, Rombel I, North AK, Bustamante C, &, Kustu S, (1997) Unusual oligomerization required for activity of NtrC, a bacterial enhancer-binding protein. Science 275, 1658-1661.
    • (1997) Science , vol.275 , pp. 1658-1661
    • Wyman, C.1    Rombel, I.2    North, A.K.3    Bustamante, C.4    Kustu, S.5
  • 41
    • 34250177264 scopus 로고    scopus 로고
    • Domain orientation in the inactive response regulator Mycobacterium tuberculosis MtrA provides a barrier to activation
    • Friedland N, Mack TR, Yu M, Hung L-W, Terwilliger TC, Waldo GS, &, Stock AM, (2007) Domain orientation in the inactive response regulator Mycobacterium tuberculosis MtrA provides a barrier to activation. Biochemistry 46, 6733-6743.
    • (2007) Biochemistry , vol.46 , pp. 6733-6743
    • Friedland, N.1    Mack, T.R.2    Yu, M.3    Hung, L.-W.4    Terwilliger, T.C.5    Waldo, G.S.6    Stock, A.M.7
  • 42
    • 38949118022 scopus 로고    scopus 로고
    • PhoP-PhoP Interaction at Adjacent PhoP Binding Sites Is Influenced by Protein Phosphorylation
    • Sinha A, Gupta S, Bhutani S, Pathak A, &, Sarkar D, (2008) PhoP-PhoP Interaction at Adjacent PhoP Binding Sites Is Influenced by Protein Phosphorylation. J Bacteriol 190, 1317-1328.
    • (2008) J Bacteriol , vol.190 , pp. 1317-1328
    • Sinha, A.1    Gupta, S.2    Bhutani, S.3    Pathak, A.4    Sarkar, D.5
  • 43
    • 2542475060 scopus 로고    scopus 로고
    • Two sensor kinases contribute to the hypoxic response of Mycobacterium tuberculosis
    • Roberts DM, Liao RP, Wisedchaisri G, Hol WG, &, Sherman DR, (2004) Two sensor kinases contribute to the hypoxic response of Mycobacterium tuberculosis. J Biol Chem 279, 23082-23087.
    • (2004) J Biol Chem , vol.279 , pp. 23082-23087
    • Roberts, D.M.1    Liao, R.P.2    Wisedchaisri, G.3    Hol, W.G.4    Sherman, D.R.5
  • 44
    • 33947415761 scopus 로고    scopus 로고
    • Identification of mycobacterial sigma factor binding sites by chromatin immunoprecipitation assays
    • Rodrigue S, Brodeur J, Jacques PE, Gervais AL, Brzezinski R, &, Gaudreau L, (2007) Identification of mycobacterial sigma factor binding sites by chromatin immunoprecipitation assays. J Bacteriol 189, 1505-1513.
    • (2007) J Bacteriol , vol.189 , pp. 1505-1513
    • Rodrigue, S.1    Brodeur, J.2    Jacques, P.E.3    Gervais, A.L.4    Brzezinski, R.5    Gaudreau, L.6
  • 45
    • 33750934574 scopus 로고    scopus 로고
    • Expression of mycobacterial cell division protein, FtsZ, and dormancy proteins, DevR and Acr, within lung granulomas throughout Guinea pig infection
    • Sharma D, Bose A, Shakila H, Das TK, Tyagi JS, &, Ramanathan VD, (2006) Expression of mycobacterial cell division protein, FtsZ, and dormancy proteins, DevR and Acr, within lung granulomas throughout guinea pig infection. FEMS Immunol Med Microbiol 48, 329-336.
    • (2006) FEMS Immunol Med Microbiol , vol.48 , pp. 329-336
    • Sharma, D.1    Bose, A.2    Shakila, H.3    Das, T.K.4    Tyagi, J.S.5    Ramanathan, V.D.6
  • 46
    • 44349189806 scopus 로고    scopus 로고
    • K2D2: Estimation of protein secondary structure from circular dichroism spectra
    • Perez-Iratxeta C, &, Andrade-Navarro MA, (2008) K2D2: estimation of protein secondary structure from circular dichroism spectra. BMC Struct Biol 8, 1472-6807.
    • (2008) BMC Struct Biol , vol.8 , pp. 1472-6807
    • Perez-Iratxeta, C.1    Andrade-Navarro, M.A.2
  • 47
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W, &, Sander C, (1983) Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22, 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 48
    • 0029619259 scopus 로고
    • Knowledge-based protein secondary structure assignment
    • Frishman D, &, Argos P, (1995) Knowledge-based protein secondary structure assignment. Proteins 23, 566-579.
    • (1995) Proteins , vol.23 , pp. 566-579
    • Frishman, D.1    Argos, P.2
  • 50
    • 4143121255 scopus 로고    scopus 로고
    • Evaluation of fluorescence-based thermal shift assays for hit identification in drug discovery
    • Lo M-C, Aulabaugh A, Jin G, Cowling R, Bard J, Malamas M, &, Ellestad G, (2004) Evaluation of fluorescence-based thermal shift assays for hit identification in drug discovery. Anal Biochem 332, 153-159.
    • (2004) Anal Biochem , vol.332 , pp. 153-159
    • Lo, M.-C.1    Aulabaugh, A.2    Jin, G.3    Cowling, R.4    Bard, J.5    Malamas, M.6    Ellestad, G.7
  • 51
    • 77949887724 scopus 로고    scopus 로고
    • Molecular strategies for phosphorylation-mediated regulation of response regulator activity
    • Gao R, &, Stock AM, (2010) Molecular strategies for phosphorylation-mediated regulation of response regulator activity. Curr Opin Microbiol 13, 160-167.
    • (2010) Curr Opin Microbiol , vol.13 , pp. 160-167
    • Gao, R.1    Stock, A.M.2
  • 52
    • 34548847733 scopus 로고    scopus 로고
    • Using circular dichroism spectra to estimate protein secondary structure
    • Greenfield NJ, (2006) Using circular dichroism spectra to estimate protein secondary structure. Nat Protoc 1, 2876-2890.
    • (2006) Nat Protoc , vol.1 , pp. 2876-2890
    • Greenfield, N.J.1
  • 53
    • 0030660409 scopus 로고    scopus 로고
    • A response regulatory protein with the site of phosphorylation blocked by an arginine interaction: Crystal structure of Spo0F from Bacillus subtilis
    • Madhusudan M, Zapf J, Hoch JA, Whiteley JM, Xuong NH, &, Varughese KI, (1997) A response regulatory protein with the site of phosphorylation blocked by an arginine interaction: crystal structure of Spo0F from Bacillus subtilis. Biochemistry 36, 12739-12745.
    • (1997) Biochemistry , vol.36 , pp. 12739-12745
    • Madhusudan, M.1    Zapf, J.2    Hoch, J.A.3    Whiteley, J.M.4    Xuong, N.H.5    Varughese, K.I.6
  • 54
    • 0037489351 scopus 로고    scopus 로고
    • Thermal stability and DNA binding activity of a variant form of the Sso7d protein from the archeon Sulfolobus solfataricus truncated at leucine 54
    • Shehi E, Granata V, Del Vecchio P, Barone G, Fusi P, Tortora P, &, Graziano G, (2003) Thermal stability and DNA binding activity of a variant form of the Sso7d protein from the archeon Sulfolobus solfataricus truncated at leucine 54. Biochemistry 42, 8362-8368.
    • (2003) Biochemistry , vol.42 , pp. 8362-8368
    • Shehi, E.1    Granata, V.2    Del Vecchio, P.3    Barone, G.4    Fusi, P.5    Tortora, P.6    Graziano, G.7
  • 55
    • 10344222093 scopus 로고    scopus 로고
    • Structural and dynamic effects of alpha-helix deletion in Sso7d: Implications for protein thermal stability
    • Merlino A, Graziano G, &, Mazzarella L, (2004) Structural and dynamic effects of alpha-helix deletion in Sso7d: implications for protein thermal stability. Proteins 57, 692-701.
    • (2004) Proteins , vol.57 , pp. 692-701
    • Merlino, A.1    Graziano, G.2    Mazzarella, L.3
  • 57
    • 84876034428 scopus 로고    scopus 로고
    • Influence of crowded cellular environments on protein folding, binding, and oligomerization: Biological consequences and potentials of atomistic modeling
    • Zhou H-X, (2013) Influence of crowded cellular environments on protein folding, binding, and oligomerization: biological consequences and potentials of atomistic modeling. FEBS Lett 587, 1053-1061.
    • (2013) FEBS Lett , vol.587 , pp. 1053-1061
    • Zhou, H.-X.1
  • 58
    • 65549104421 scopus 로고    scopus 로고
    • Probing the roles of the two different dimers mediated by the receiver domain of the response regulator PhoB
    • Mack TR, Gao R, &, Stock AM, (2009) Probing the roles of the two different dimers mediated by the receiver domain of the response regulator PhoB. J Mol Biol 389, 349-364.
    • (2009) J Mol Biol , vol.389 , pp. 349-364
    • Mack, T.R.1    Gao, R.2    Stock, A.M.3
  • 59
    • 55049114750 scopus 로고    scopus 로고
    • Novel drug target strategies against Mycobacterium tuberculosis
    • Murphy DJ, &, Brown JR, (2008) Novel drug target strategies against Mycobacterium tuberculosis. Curr Opin Microbiol 11, 422-427.
    • (2008) Curr Opin Microbiol , vol.11 , pp. 422-427
    • Murphy, D.J.1    Brown, J.R.2
  • 60
    • 34548152748 scopus 로고    scopus 로고
    • Identification of gene targets against dormant phase Mycobacterium tuberculosis infections
    • Murphy DJ, &, Brown JR, (2007) Identification of gene targets against dormant phase Mycobacterium tuberculosis infections. BMC Infect Dis 7, 84.
    • (2007) BMC Infect Dis , vol.7 , pp. 84
    • Murphy, D.J.1    Brown, J.R.2
  • 61
    • 18144414619 scopus 로고    scopus 로고
    • High-throughput microplate phosphorylation assays based on DevR-DevS/Rv2027c 2-component signal transduction pathway to screen for novel antitubercular compounds
    • Saini DK, &, Tyagi JS, (2005) High-throughput microplate phosphorylation assays based on DevR-DevS/Rv2027c 2-component signal transduction pathway to screen for novel antitubercular compounds. J Biomol Screen 10, 215-224.
    • (2005) J Biomol Screen , vol.10 , pp. 215-224
    • Saini, D.K.1    Tyagi, J.S.2
  • 63
    • 0037371176 scopus 로고    scopus 로고
    • Deletion of two-component regulatory systems increases the virulence of Mycobacterium tuberculosis
    • Parish T, Smith DA, Kendall S, Casali N, Bancroft GJ, &, Stoker NG, (2003) Deletion of two-component regulatory systems increases the virulence of Mycobacterium tuberculosis. Infect Immun 71, 1134-1140.
    • (2003) Infect Immun , vol.71 , pp. 1134-1140
    • Parish, T.1    Smith, D.A.2    Kendall, S.3    Casali, N.4    Bancroft, G.J.5    Stoker, N.G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.