메뉴 건너뛰기




Volumn 185, Issue 1, 2003, Pages 285-294

Common extracellular sensory domains in transmembrane receptors for diverse signal transduction pathways in Bacteria and Archaea

Author keywords

[No Author keywords available]

Indexed keywords

ADENYLATE CYCLASE; CHEMOTAXIS AFFECTING AGENT; GUANYLATE CYCLASE; MEMBRANE RECEPTOR; PHOSPHODIESTERASE; PROTEIN HISTIDINE KINASE; PROTEIN SERINE THREONINE KINASE;

EID: 0037215715     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.185.1.285-294.2003     Document Type: Article
Times cited : (125)

References (70)
  • 3
    • 0034326854 scopus 로고    scopus 로고
    • 2+-channel subunits and a class of prokaryotic chemotaxis receptors
    • 2+-channel subunits and a class of prokaryotic chemotaxis receptors. Trends Biochem. Sci. 25:535-537.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 535-537
    • Anantharaman, V.1    Aravind, L.2
  • 4
    • 0035478909 scopus 로고    scopus 로고
    • The CHASE domain: A predicted ligand-binding module in plant cytokinin receptors and other eukaryotic and bacterial receptors
    • Anantharaman, V., and L. Aravind. 2001. The CHASE domain: A predicted ligand-binding module in plant cytokinin receptors and other eukaryotic and bacterial receptors. Trends Biochem. Sci. 26:579-582.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 579-582
    • Anantharaman, V.1    Aravind, L.2
  • 5
    • 0030595328 scopus 로고    scopus 로고
    • Signal transduction via the multistep phosphorelay: Not necessarily a road less traveled
    • Appleby, J. L., J. S. Parkinson, and R. B. Bourret. 1996. Signal transduction via the multistep phosphorelay: Not necessarily a road less traveled. Cell 86:845-848.
    • (1996) Cell , vol.86 , pp. 845-848
    • Appleby, J.L.1    Parkinson, J.S.2    Bourret, R.B.3
  • 6
    • 0032766134 scopus 로고    scopus 로고
    • The cytoplasmic helical linker domain of receptor histidine kinase and methyl-accepting proteins is common to many prokaryotic signalling proteins
    • Aravind, L., and C. P. Ponting. 1999. The cytoplasmic helical linker domain of receptor histidine kinase and methyl-accepting proteins is common to many prokaryotic signalling proteins. FEMS Microbiol. Lett. 176:111-116.
    • (1999) FEMS Microbiol. Lett. , vol.176 , pp. 111-116
    • Aravind, L.1    Ponting, C.P.2
  • 7
    • 0030712081 scopus 로고    scopus 로고
    • The GAF domain: An evolutionary link between diverse phototransducing proteins
    • Aravind, L., and C. P. Ponting. 1997. The GAF domain: An evolutionary link between diverse phototransducing proteins. Trends Biochem. Sci. 22:458-459.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 458-459
    • Aravind, L.1    Ponting, C.P.2
  • 10
    • 0033534368 scopus 로고    scopus 로고
    • Structure of CheA, a signal-transducing histidine kinase
    • Bilwes, A. M., L. A. Alex, B. R. Crane, and M. I. Simon. 1999. Structure of CheA, a signal-transducing histidine kinase. Cell 96:131-141.
    • (1999) Cell , vol.96 , pp. 131-141
    • Bilwes, A.M.1    Alex, L.A.2    Crane, B.R.3    Simon, M.I.4
  • 11
    • 0037155843 scopus 로고    scopus 로고
    • Molecular information processing: Lessons from bacterial chemotaxis
    • Bourret, R. B., and A. M. Stock. 2002. Molecular information processing: Lessons from bacterial chemotaxis. J. Biol. Chem. 277:9625-9628.
    • (2002) J. Biol. Chem. , vol.277 , pp. 9625-9628
    • Bourret, R.B.1    Stock, A.M.2
  • 12
    • 0029865503 scopus 로고    scopus 로고
    • Molecular mechanism of transmembrane signaling by the aspartate receptor: A model
    • Chervitz, S. A., and J. J. Falke. 1996. Molecular mechanism of transmembrane signaling by the aspartate receptor: A model. Proc. Natl. Acad. Sci. USA 93:2545-2550.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2545-2550
    • Chervitz, S.A.1    Falke, J.J.2
  • 13
    • 0032919372 scopus 로고    scopus 로고
    • Recent improvements of the ProDom database of protein domain families
    • Corpet, F., J. Gouzy, and D. Kahn. 1999. Recent improvements of the ProDom database of protein domain families. Nucleic Acids Res. 27:263-267.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 263-267
    • Corpet, F.1    Gouzy, J.2    Kahn, D.3
  • 14
    • 0033957841 scopus 로고    scopus 로고
    • ProDom and ProDom-CG: Tools for protein domain analysis and whole genome comparisons
    • Corpet, F., F. Servant, J. Gouzy, and D. Kahn. 2000. ProDom and ProDom-CG: tools for protein domain analysis and whole genome comparisons. Nucleic Acids Res. 28:267-269.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 267-269
    • Corpet, F.1    Servant, F.2    Gouzy, J.3    Kahn, D.4
  • 15
    • 0030759333 scopus 로고    scopus 로고
    • Prediction of transmembrane alpha-helices in prokaryotic membrane proteins: The dense alignment surface method
    • Cserzo, M., E. Wallin, I. Simon, G. von Heijne, and A. Elofsson. 1997. Prediction of transmembrane alpha-helices in prokaryotic membrane proteins: The dense alignment surface method. Protein Eng. 10:673-676.
    • (1997) Protein Eng. , vol.10 , pp. 673-676
    • Cserzo, M.1    Wallin, E.2    Simon, I.3    Von Heijne, G.4    Elofsson, A.5
  • 16
    • 0034663597 scopus 로고    scopus 로고
    • Application of multiple sequence alignment profiles to improve protein secondary structure prediction
    • Cuff, J. A., and G. J. Barton. 2000. Application of multiple sequence alignment profiles to improve protein secondary structure prediction. Proteins 40:502-511.
    • (2000) Proteins , vol.40 , pp. 502-511
    • Cuff, J.A.1    Barton, G.J.2
  • 17
    • 0034096459 scopus 로고    scopus 로고
    • Microbial relatives of the seed storage proteins of higher plants: Conservation of structure and diversification of function during evolution of the cupin superfamily
    • Dunwell, J. M., S. Khuri, and P. J. Gane. 2000. Microbial relatives of the seed storage proteins of higher plants: Conservation of structure and diversification of function during evolution of the cupin superfamily. Microbiol. Mol. Biol. Rev. 64:153-179.
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 153-179
    • Dunwell, J.M.1    Khuri, S.2    Gane, P.J.3
  • 18
    • 0032730205 scopus 로고    scopus 로고
    • Histidine kinases: Diversity of domain organization
    • Dutta, R., L. Qin, and M. Inouye. 1999. Histidine kinases: Diversity of domain organization. Mol. Microbiol. 34:633-640.
    • (1999) Mol. Microbiol. , vol.34 , pp. 633-640
    • Dutta, R.1    Qin, L.2    Inouye, M.3
  • 19
    • 0035312774 scopus 로고    scopus 로고
    • Transmembrane signaling in bacterial chemoreceptors
    • Falke, J. J., and G. L. Hazelbauer. 2001. Transmembrane signaling in bacterial chemoreceptors. Trends Biochem. Sci. 26:257-265.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 257-265
    • Falke, J.J.1    Hazelbauer, G.L.2
  • 20
    • 0035076532 scopus 로고    scopus 로고
    • Conserved "hypothetical" proteins: New hints and new puzzles
    • Galperin, M. Y. 2001, Conserved "hypothetical" proteins: New hints and new puzzles. Comp. Funct. Genomics 2:1. 4-18.
    • (2001) Comp. Funct. Genomics , vol.2 , pp. 14-18
    • Galperin, M.Y.1
  • 21
    • 0033222409 scopus 로고    scopus 로고
    • A specialized version of the HD hydrolase domain implicated in signal transduction
    • Galperin, M. Y., D. A. Natale, L. Aravind, and E. V. Koonin. 1999. A specialized version of the HD hydrolase domain implicated in signal transduction. J. Mol. Microbiol. Biotechnol. 1:303-305.
    • (1999) J. Mol. Microbiol. Biotechnol. , vol.1 , pp. 303-305
    • Galperin, M.Y.1    Natale, D.A.2    Aravind, L.3    Koonin, E.V.4
  • 22
    • 0035845587 scopus 로고    scopus 로고
    • Novel domains of the prokaryotic two-component signal transduction system
    • Galperin, M. Y., A. N. Nikolskaya, and E. V. Koonin. 2001. Novel domains of the prokaryotic two-component signal transduction system. FEMS Microbiol. Lett. 203:11-21.
    • (2001) FEMS Microbiol. Lett. , vol.203 , pp. 11-21
    • Galperin, M.Y.1    Nikolskaya, A.N.2    Koonin, E.V.3
  • 23
    • 0031750695 scopus 로고    scopus 로고
    • Unique regulation of carbohydrate chemotaxis in Bacillus subtilis by the phosphoenolpyruvate-dependent phosphotransferase system and the methyl-accepting chemotaxis protein McpC
    • Garrity, L. F., S. L. Schiel, R. Merrill, J. Reizer, M. H. Saier, Jr., and G. W. Ordal. 1998. Unique regulation of carbohydrate chemotaxis in Bacillus subtilis by the phosphoenolpyruvate-dependent phosphotransferase system and the methyl-accepting chemotaxis protein McpC. J. Bacteriol. 180:4475-4480.
    • (1998) J. Bacteriol. , vol.180 , pp. 4475-4480
    • Garrity, L.F.1    Schiel, S.L.2    Merrill, R.3    Reizer, J.4    Saier M.H., Jr.5    Ordal, G.W.6
  • 24
    • 0034830711 scopus 로고    scopus 로고
    • Characterization of PknC, a Ser/Thr kinase with broad substrate specificity from the cyanobacterium Anabaena sp. strain PCC 7120
    • Gonzalez, L., V. Phalip, and C. C. Zhang. 2001. Characterization of PknC, a Ser/Thr kinase with broad substrate specificity from the cyanobacterium Anabaena sp. strain PCC 7120. Eur. J. Biochem. 268:1869-1875.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 1869-1875
    • Gonzalez, L.1    Phalip, V.2    Zhang, C.C.3
  • 25
    • 0035898614 scopus 로고    scopus 로고
    • Adenylyl cyclase Rv1625c of Mycobacterium tuberculosis: A progenitor of mammalian adenylyl cyclases
    • Guo, Y. L., T. Seebacher, U. Kurz, J. U. Linder, and J. E. Schultz. 2001. Adenylyl cyclase Rv1625c of Mycobacterium tuberculosis: A progenitor of mammalian adenylyl cyclases. EMBO J. 20:3667-3675.
    • (2001) EMBO J. , vol.20 , pp. 3667-3675
    • Guo, Y.L.1    Seebacher, T.2    Kurz, U.3    Linder, J.U.4    Schultz, J.E.5
  • 26
    • 0028336799 scopus 로고
    • Cloning and characterization of genes encoding methyl-accepting chemotaxis proteins in Bacillus subtilis
    • Hanlon, D. W., and G. W. Ordal. 1994. Cloning and characterization of genes encoding methyl-accepting chemotaxis proteins in Bacillus subtilis. J. Biol. Chem. 269:14038-14046.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14038-14046
    • Hanlon, D.W.1    Ordal, G.W.2
  • 28
    • 0034035586 scopus 로고    scopus 로고
    • Two-component and phosphorelay signal transduction
    • Hoch, J. A. 2000. Two-component and phosphorelay signal transduction. Curr. Opin. Microbiol. 3:165-170.
    • (2000) Curr. Opin. Microbiol. , vol.3 , pp. 165-170
    • Hoch, J.A.1
  • 29
    • 0034879819 scopus 로고    scopus 로고
    • Keeping signals straight in phosphorelay signal transduction
    • , Hoch, J. A., and K. I. Varughese. 2001. Keeping signals straight in phosphorelay signal transduction. J. Bacteriol. 183:4941-4949.
    • (2001) J. Bacteriol. , vol.183 , pp. 4941-4949
    • Hoch, J.A.1    Varughese, K.I.2
  • 31
    • 0030970444 scopus 로고    scopus 로고
    • Isolation and characterization of multiple adenylate cyclase genes from the cyanobacterium Anabaena sp. strain PCC 7120
    • Katayama, M., and M. Ohmori. 1997. Isolation and characterization of multiple adenylate cyclase genes from the cyanobacterium Anabaena sp. strain PCC 7120. J. Bacteriol. 179:3588-3593.
    • (1997) J. Bacteriol. , vol.179 , pp. 3588-3593
    • Katayama, M.1    Ohmori, M.2
  • 32
    • 0034595501 scopus 로고    scopus 로고
    • Enhanced genome annotation with structural profiles in the program 3D-PSSM
    • Kelley, L. A., R. M. MacCallum, and M. J. Sternberg. 2000. Enhanced genome annotation with structural profiles in the program 3D-PSSM. J. Mol. Biol. 299:499-520.
    • (2000) J. Mol. Biol. , vol.299 , pp. 499-520
    • Kelley, L.A.1    MacCallum, R.M.2    Sternberg, M.J.3
  • 33
    • 0029743605 scopus 로고    scopus 로고
    • Fancy meeting you here! A fresh look at "prokaryotic" protein phosphorylation
    • Kennelly, P. J., and M. Potts. 1996. Fancy meeting you here! A fresh look at "prokaryotic" protein phosphorylation. J. Bacteriol. 178:4759-4764.
    • (1996) J. Bacteriol. , vol.178 , pp. 4759-4764
    • Kennelly, P.J.1    Potts, M.2
  • 34
    • 0035019043 scopus 로고    scopus 로고
    • Genomic analysis of the histidine kinase family in bacteria and archaea
    • Kim, D., and S. Forst. 2001. Genomic analysis of the histidine kinase family in bacteria and archaea. Microbiology 147:1197-1212.
    • (2001) Microbiology , vol.147 , pp. 1197-1212
    • Kim, D.1    Forst, S.2
  • 35
    • 0036283445 scopus 로고    scopus 로고
    • An adenylyl cyclase, CyaA, of Myxococcus xanthus functions in signal transduction during osmotic stress
    • Kimura, Y., Y. Mishima, H. Nakano, and K. Takegawa. 2002. An adenylyl cyclase, CyaA, of Myxococcus xanthus functions in signal transduction during osmotic stress. J. Bacteriol. 184:3578-3585.
    • (2002) J. Bacteriol. , vol.184 , pp. 3578-3585
    • Kimura, Y.1    Mishima, Y.2    Nakano, H.3    Takegawa, K.4
  • 36
    • 0033982051 scopus 로고    scopus 로고
    • BasT, a membrane-bound transducer protein for amino acid detection in Halobacterium salinarum
    • Kokoeva, M. V., and D. Oesterhelt. 2000. BasT, a membrane-bound transducer protein for amino acid detection in Halobacterium salinarum. Mol. Microbiol. 35:647-656.
    • (2000) Mol. Microbiol. , vol.35 , pp. 647-656
    • Kokoeva, M.V.1    Oesterhelt, D.2
  • 38
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • Krogh, A., B. Larsson, G. von Heijne, and E. L. Sonnhammer. 2001. Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes. J. Mol. Biol. 305:567-580.
    • (2001) J. Mol. Biol. , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    Von Heijne, G.3    Sonnhammer, E.L.4
  • 40
    • 0034005701 scopus 로고    scopus 로고
    • Functional classification of cNMP-binding proteins and nucleotide cyclases with implications for novel regulatory pathways in Mycobacterium tuberculosis
    • McCue, L. A., K. A. McDonough, and C. E. Lawrence. 2000. Functional classification of cNMP-binding proteins and nucleotide cyclases with implications for novel regulatory pathways in Mycobacterium tuberculosis. Genome Res. 10:204-219.
    • (2000) Genome Res. , vol.10 , pp. 204-219
    • McCue, L.A.1    McDonough, K.A.2    Lawrence, C.E.3
  • 41
    • 0026315513 scopus 로고
    • Three-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with and without a ligand
    • Milburn, M. V., G. G. Prive, D. L. Milligan, W. G. Scott, J. Yeh, J. Jancarik, D. E. Koshland, Jr., and S. H. Kim. 1991. Three-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with and without a ligand. Science 254:1342-1347.
    • (1991) Science , vol.254 , pp. 1342-1347
    • Milburn, M.V.1    Prive, G.G.2    Milligan, D.L.3    Scott, W.G.4    Yeh, J.5    Jancarik, J.6    Koshland D.E., Jr.7    Kim, S.H.8
  • 42
    • 0035478296 scopus 로고    scopus 로고
    • CHASE: An extracellular sensing domain common to transmembrane receptors from prokaryotes, lower eukaryotes and plants
    • Mougel, C., and I. B. Zhulin. 2001. CHASE: An extracellular sensing domain common to transmembrane receptors from prokaryotes, lower eukaryotes and plants. Trends Biochem. Sci. 26:582-584.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 582-584
    • Mougel, C.1    Zhulin, I.B.2
  • 43
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen, H., J. Engelbrecht, S. Brunak, and G. von Heijne. 1997. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng. 10:1-6.
    • (1997) Protein Eng. , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Von Heijne, G.4
  • 44
    • 0034623005 scopus 로고    scopus 로고
    • T-Coffee: A novel method for fast and accurate multiple sequence alignment
    • Notredame, C., D. G. Higgins, and J. Heringa. 2000. T-Coffee: a novel method for fast and accurate multiple sequence alignment. J. Mol. Biol. 302:205-217.
    • (2000) J. Mol. Biol. , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3
  • 46
    • 0033543590 scopus 로고    scopus 로고
    • A piston model for transmembrane signaling of the aspartate receptor
    • Ottemann, K. M., W. Xiao, Y. K. Shin, and D. E. Koshland, Jr. 1999. A piston model for transmembrane signaling of the aspartate receptor. Science 285:1751-1754.
    • (1999) Science , vol.285 , pp. 1751-1754
    • Ottemann, K.M.1    Xiao, W.2    Shin, Y.K.3    Koshland D.E., Jr.4
  • 47
    • 0027056677 scopus 로고
    • Communication modules in bacterial signaling proteins
    • Parkinson, J. S., and E. C. Kofoid. 1992. Communication modules in bacterial signaling proteins. Annu. Rev. Genet. 26:71-112.
    • (1992) Annu. Rev. Genet. , vol.26 , pp. 71-112
    • Parkinson, J.S.1    Kofoid, E.C.2
  • 48
    • 0035254950 scopus 로고    scopus 로고
    • GGDEF domain is homologous to adenylyl cyclase
    • Pei, J., and N. V. Grishin. 2001. GGDEF domain is homologous to adenylyl cyclase. Proteins 42:210-216.
    • (2001) Proteins , vol.42 , pp. 210-216
    • Pei, J.1    Grishin, N.V.2
  • 49
    • 0031262875 scopus 로고    scopus 로고
    • PAS: A multifunctional domain family comes to light
    • Ponting, C. P., and L. Aravind. 1997. PAS: A multifunctional domain family comes to light. Curr. Biol. 7:R674-R677.
    • (1997) Curr. Biol. , vol.7
    • Ponting, C.P.1    Aravind, L.2
  • 50
    • 0033057517 scopus 로고    scopus 로고
    • Eukaryotic signalling domain homologues in archaea and bacteria. Ancient ancestry and horizontal gene transfer
    • Ponting, C. P., L. Aravind, J. Schultz, P. Bork, and E. V. Koonin. 1999. Eukaryotic signalling domain homologues in archaea and bacteria. Ancient ancestry and horizontal gene transfer. J. Mol. Biol. 289:729-745.
    • (1999) J. Mol. Biol. , vol.289 , pp. 729-745
    • Ponting, C.P.1    Aravind, L.2    Schultz, J.3    Bork, P.4    Koonin, E.V.5
  • 51
    • 0031896855 scopus 로고    scopus 로고
    • Roles of DctA and DctB in signal detection by the dicarboxylic acid transport system of Rhizobium leguminosarum
    • Reid, C. J., and P. S. Poole. 1998. Roles of DctA and DctB in signal detection by the dicarboxylic acid transport system of Rhizobium leguminosarum. J. Bacteriol. 180:2660-2669.
    • (1998) J. Bacteriol. , vol.180 , pp. 2660-2669
    • Reid, C.J.1    Poole, P.S.2
  • 52
    • 0029889988 scopus 로고    scopus 로고
    • PHD: Predicting one-dimensional protein structure by profile-based neural networks
    • Rost, B. 1996. PHD: Predicting one-dimensional protein structure by profile-based neural networks. Methods Enzymol. 266:525-539.
    • (1996) Methods Enzymol. , vol.266 , pp. 525-539
    • Rost, B.1
  • 54
    • 0028337763 scopus 로고
    • VsrA, a second two-component sensor regulating virulence genes of Pseudomonas solanacearum
    • Schell, M. A., T. P. Denny, and J. Huang. 1994. VsrA, a second two-component sensor regulating virulence genes of Pseudomonas solanacearum. Mol. Microbiol. 11:489-500.
    • (1994) Mol. Microbiol. , vol.11 , pp. 489-500
    • Schell, M.A.1    Denny, T.P.2    Huang, J.3
  • 55
    • 0031764045 scopus 로고    scopus 로고
    • The serine, threonine, and/or tyrosine-specific protein kinases and protein phosphatases phosphatases of prokaryotic organisms: A family portrait
    • Shi, L., M. Potts, and P. J. Kennelly. 1998. The serine, threonine, and/or tyrosine-specific protein kinases and protein phosphatases phosphatases of prokaryotic organisms: A family portrait. FEMS Microbiol. Rev. 22:229-253.
    • (1998) FEMS Microbiol. Rev. , vol.22 , pp. 229-253
    • Shi, L.1    Potts, M.2    Kennelly, P.J.3
  • 59
    • 0033956060 scopus 로고    scopus 로고
    • The COG database: A tool for genome-scale analysis of protein functions and evolution
    • Tatusov, R. L., M. Y. Galperin, D. A. Natale, and E. V. Koonin. 2000. The COG database: A tool for genome-scale analysis of protein functions and evolution. Nucleic Acids Res. 28:33-36.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 33-36
    • Tatusov, R.L.1    Galperin, M.Y.2    Natale, D.A.3    Koonin, E.V.4
  • 60
    • 0032990441 scopus 로고    scopus 로고
    • PAS domains: Internal sensors of oxygen, redox potential, and light
    • Taylor, B. L., and I. B. Zhulin. 1999. PAS domains: Internal sensors of oxygen, redox potential, and light. Microbiol. Mol. Biol. Rev. 63:479-506.
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 479-506
    • Taylor, B.L.1    Zhulin, I.B.2
  • 61
    • 0027968068 scopus 로고
    • Clustal W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. Clustal W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 62
    • 0035369115 scopus 로고    scopus 로고
    • Histidine kinases and response regulator proteins in two-component signaling systems
    • West, A. H., and A. M. Stock. 2001. Histidine kinases and response regulator proteins in two-component signaling systems. Trends Biochem. Sci. 26:369-376.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 369-376
    • West, A.H.1    Stock, A.M.2
  • 63
    • 0032826834 scopus 로고    scopus 로고
    • Functional similarities among two-component sensors and methyl-accepting chemotaxis proteins suggest a role for linker region amphipathic helices in transmembrane signal transduction
    • Williams, S. B., and V. Stewart. 1999. Functional similarities among two-component sensors and methyl-accepting chemotaxis proteins suggest a role for linker region amphipathic helices in transmembrane signal transduction. Mol. Microbiol. 33:1093-1102.
    • (1999) Mol. Microbiol. , vol.33 , pp. 1093-1102
    • Williams, S.B.1    Stewart, V.2
  • 64
    • 0034041917 scopus 로고    scopus 로고
    • Identification and characterization of two chemotactic transducers for inorganic phosphate in Pseudomonas aeruginosa
    • Wu, H., J. Kato, A. Kuroda, T. Ikeda, N. Takiguchi, and H. Ohtake. 2000. Identification and characterization of two chemotactic transducers for inorganic phosphate in Pseudomonas aeruginosa. J. Bacteriol. 182:3400-3404.
    • (2000) J. Bacteriol. , vol.182 , pp. 3400-3404
    • Wu, H.1    Kato, J.2    Kuroda, A.3    Ikeda, T.4    Takiguchi, N.5    Ohtake, H.6
  • 65
    • 10144255829 scopus 로고    scopus 로고
    • Opposing pairs of serine protein kinases and phosphatases transmit signals of environmental stress to activate a bacterial transcription factor
    • Yang, X., C. M. Kang, M. S. Brody, and C. W. Price. 1996. Opposing pairs of serine protein kinases and phosphatases transmit signals of environmental stress to activate a bacterial transcription factor. Genes Dev. 10:2265-2275.
    • (1996) Genes Dev. , vol.10 , pp. 2265-2275
    • Yang, X.1    Kang, C.M.2    Brody, M.S.3    Price, C.W.4
  • 66
    • 0030128740 scopus 로고    scopus 로고
    • Molecular characterization of an adenylate cyclase gene of the cyanobacterium Spirulina platensis
    • Yashiro, K., T. Sakamoto, and M. Ohmori. 1996. Molecular characterization of an adenylate cyclase gene of the cyanobacterium Spirulina platensis. Plant Mol. Biol. 31:175-181.
    • (1996) Plant Mol. Biol. , vol.31 , pp. 175-181
    • Yashiro, K.1    Sakamoto, T.2    Ohmori, M.3
  • 67
    • 0027146285 scopus 로고
    • A gene encoding a protein related to eukaryotic protein kinases from the filamentous heterocystous cyanobacterium Anabaena PCC 7120
    • Zhang, C. C. 1993. A gene encoding a protein related to eukaryotic protein kinases from the filamentous heterocystous cyanobacterium Anabaena PCC 7120. Proc. Natl. Acad. Sci. USA 90:11840-11844.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 11840-11844
    • Zhang, C.C.1
  • 68
    • 0033765679 scopus 로고    scopus 로고
    • A novel phototaxis receptor hidden in the cyanobacterial genome
    • Zhulin, I. B. 2000. A novel phototaxis receptor hidden in the cyanobacterial genome. J. Mol. Microbiol. Biotechnol. 2:491-493.
    • (2000) J. Mol. Microbiol. Biotechnol. , vol.2 , pp. 491-493
    • Zhulin, I.B.1
  • 69
    • 0034964703 scopus 로고    scopus 로고
    • The superfamily of chemotaxis transducers: From physiology to genomics and back
    • Zhulin, I. B. 2001. The superfamily of chemotaxis transducers: from physiology to genomics and back. Adv. Microb. Physiol. 45:157-198.
    • (2001) Adv. Microb. Physiol. , vol.45 , pp. 157-198
    • Zhulin, I.B.1
  • 70
    • 0030884102 scopus 로고    scopus 로고
    • PAS domain S-boxes in Archaea, Bacteria and sensors for oxygen and redox
    • Zhulin I. B., B. L. Taylor, and R. Dixon. 1997. PAS domain S-boxes in Archaea, Bacteria and sensors for oxygen and redox. Trends Biochem. Sci. 22:331-333.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 331-333
    • Zhulin, I.B.1    Taylor, B.L.2    Dixon, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.