메뉴 건너뛰기




Volumn 178, Issue 23, 1996, Pages 6968-6974

Characterization of the aegA locus of Escherichia coli: Control of gene expression in response to anaerobiosis and nitrate

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; GLUTAMATE SYNTHASE; IRON SULFUR PROTEIN; NITRATE;

EID: 0029809180     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.178.23.6968-6974.1996     Document Type: Article
Times cited : (15)

References (53)
  • 1
    • 0022532411 scopus 로고
    • Oxygen-regulated stimulons of Salmonella typhimurium identified by Mu d(Ap lac) operon fusions
    • Aliabadi, Z., F. Warren, S. Mya, and J. W. Foster. 1986. Oxygen-regulated stimulons of Salmonella typhimurium identified by Mu d(Ap lac) operon fusions. J. Bacteriol. 165:780-786.
    • (1986) J. Bacteriol. , vol.165 , pp. 780-786
    • Aliabadi, Z.1    Warren, F.2    Mya, S.3    Foster, J.W.4
  • 2
    • 0026087601 scopus 로고
    • A molecular analysis of the 53.3 minute region of the Escherichia coli linkage map
    • Andrews, S. C., P. M. Harrison, and J. R. Guest. 1991. A molecular analysis of the 53.3 minute region of the Escherichia coli linkage map. J. Gen. Microbiol. 137:361-367.
    • (1991) J. Gen. Microbiol. , vol.137 , pp. 361-367
    • Andrews, S.C.1    Harrison, P.M.2    Guest, J.R.3
  • 3
    • 0027406134 scopus 로고
    • Site-directed mutagenesis of conserved cysteine residues within the β subunit of Escherichia coli nitrate reductase. Physiological, biochemical, and EPR characterization of the mutated enzymes
    • Augier, V., B. Guigliarelli, M. Asso, P. Bertrand, C. Frixon, G. Giordano, M. Chippaux, and F. Blasco. 1993. Site-directed mutagenesis of conserved cysteine residues within the β subunit of Escherichia coli nitrate reductase. Physiological, biochemical, and EPR characterization of the mutated enzymes. Biochemistry 32:2013-2023.
    • (1993) Biochemistry , vol.32 , pp. 2013-2023
    • Augier, V.1    Guigliarelli, B.2    Asso, M.3    Bertrand, P.4    Frixon, C.5    Giordano, G.6    Chippaux, M.7    Blasco, F.8
  • 4
    • 0006755020 scopus 로고
    • Physical and genetic characterization of the glnA-glnG region of the Escherichia coli chromosome
    • Backman, K., Y.-M. Chen, and B. Magasanik. 1981. Physical and genetic characterization of the glnA-glnG region of the Escherichia coli chromosome. Proc. Natl. Acad. Sci. USA 78:3743-3747.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 3743-3747
    • Backman, K.1    Chen, Y.-M.2    Magasanik, B.3
  • 5
    • 0026088264 scopus 로고
    • The role of the NAC protein in the nitrogen regulation of Klebsidla aerogenes
    • Bender, R. A. 1991. The role of the NAC protein in the nitrogen regulation of Klebsidla aerogenes. Mol. Microbiol. 5:2575-2580.
    • (1991) Mol. Microbiol. , vol.5 , pp. 2575-2580
    • Bender, R.A.1
  • 6
    • 0025788382 scopus 로고
    • Nitrate-inducihle formate dehydrogenase in Escherichia coli K-12. I. Nucleotide sequence of the fdnGHI operon and evidence that opal (UGA) encodes selenocysteine
    • Berg, B. L., J. Li, J. Heider, and V. J. Stewart. 1991. Nitrate-inducihle formate dehydrogenase in Escherichia coli K-12. I. Nucleotide sequence of the fdnGHI operon and evidence that opal (UGA) encodes selenocysteine. J. Biol. Chem. 266:22380-22385.
    • (1991) J. Biol. Chem. , vol.266 , pp. 22380-22385
    • Berg, B.L.1    Li, J.2    Heider, J.3    Stewart, V.J.4
  • 7
    • 0024451301 scopus 로고
    • Characterization of a cis regulatory DNA element necessary for formate induction of the formate dehydrogenase gene (fdnF) of Escherichia coli
    • Birkmann, A., and A. Böck. 1989. Characterization of a cis regulatory DNA element necessary for formate induction of the formate dehydrogenase gene (fdnF) of Escherichia coli. Mol Microbiol. 3:187-195.
    • (1989) Mol Microbiol. , vol.3 , pp. 187-195
    • Birkmann, A.1    Böck, A.2
  • 8
    • 0025157053 scopus 로고
    • Nucleotide sequence and expression of an operon in Escherichia coli coding for formate hydrogenlyase components
    • Boehm, R., M. Sauter, and A. Böck. 1990. Nucleotide sequence and expression of an operon in Escherichia coli coding for formate hydrogenlyase components. Mol. Microbiol. 4:231-243.
    • (1990) Mol. Microbiol. , vol.4 , pp. 231-243
    • Boehm, R.1    Sauter, M.2    Böck, A.3
  • 9
    • 0029042437 scopus 로고
    • The NarX and NarQ sensor-transmitter proteins of Escherichia coli each require two conserved histidines for nitrate-dependent signal transduction to NarL
    • Cavicchioli, R., I. Schröder, M. Constanti, and R. P. Gunsalus. 1995. The NarX and NarQ sensor-transmitter proteins of Escherichia coli each require two conserved histidines for nitrate-dependent signal transduction to NarL. J. Bacteriol. 177:2410-2424.
    • (1995) J. Bacteriol. , vol.177 , pp. 2410-2424
    • Cavicchioli, R.1    Schröder, I.2    Constanti, M.3    Gunsalus, R.P.4
  • 10
    • 0020070412 scopus 로고
    • Characterization of a gene, glnL, the product of which is involved in the regulation of nitrogen utilization in Escherichia coli
    • Chen, Y.-M., K. Backman, and B. Magasanik. 1982. Characterization of a gene, glnL, the product of which is involved in the regulation of nitrogen utilization in Escherichia coli. J. Bacteriol. 150:214-220.
    • (1982) J. Bacteriol. , vol.150 , pp. 214-220
    • Chen, Y.-M.1    Backman, K.2    Magasanik, B.3
  • 11
    • 0026740927 scopus 로고
    • Identification and characterization of narQ, a second nitrate sensor for nitrate-dependent gene regulation in Escherichia coli
    • Chiang, R. C., R. Cavicchioli, and R. P. Gunsalus. 1992. Identification and characterization of narQ, a second nitrate sensor for nitrate-dependent gene regulation in Escherichia coli. Mol. Microbiol. 6:1913-1923.
    • (1992) Mol. Microbiol. , vol.6 , pp. 1913-1923
    • Chiang, R.C.1    Cavicchioli, R.2    Gunsalus, R.P.3
  • 12
    • 0026470916 scopus 로고
    • Physical map location of the narQ gene of Escherichia coli
    • Chiang, R. C., R. Cavicchioli, and R. P. Gunsalus. 1992. Physical map location of the narQ gene of Escherichia coli. J. Bacteriol. 174:7882.
    • (1992) J. Bacteriol. , vol.174 , pp. 7882
    • Chiang, R.C.1    Cavicchioli, R.2    Gunsalus, R.P.3
  • 13
    • 0026056114 scopus 로고
    • Anacrobically expressed Escherichia coli genes identified by operon fusion techniques
    • Choe, M., and W. S. Reznikoff. 1991. Anacrobically expressed Escherichia coli genes identified by operon fusion techniques. J. Bacteriol. 173:6139-6146.
    • (1991) J. Bacteriol. , vol.173 , pp. 6139-6146
    • Choe, M.1    Reznikoff, W.S.2
  • 14
    • 0023656201 scopus 로고
    • Nucleotide sequence and comparative analysis of the frd operon encoding the fumarate reductase of Proteus vulgaris: Extensive sequence divergence of the membrane anchors and absence of a frd-linked ampC cephalosporinase gene
    • Cole, S. T. 1987. Nucleotide sequence and comparative analysis of the frd operon encoding the fumarate reductase of Proteus vulgaris: extensive sequence divergence of the membrane anchors and absence of a frd-linked ampC cephalosporinase gene. Eur. J. Biochem. 167:481-488.
    • (1987) Eur. J. Biochem. , vol.167 , pp. 481-488
    • Cole, S.T.1
  • 15
    • 0026813814 scopus 로고
    • Contribution of the fnr and arcA gene products in coordinate regulation of the cytochrome o (cvoABCDE) and d cydAB] oxidase genes in Escherichia coli
    • Cotter, P. A., and R. P. Gunsalus. 1992. Contribution of the fnr and arcA gene products in coordinate regulation of the cytochrome o (cvoABCDE) and d (cydAB] oxidase genes in Escherichia coli. FEMS Microbiol. Lett. 91:31-36.
    • (1992) FEMS Microbiol. Lett. , vol.91 , pp. 31-36
    • Cotter, P.A.1    Gunsalus, R.P.2
  • 16
    • 0029030757 scopus 로고
    • Expression of the narX, narL, narP, and nurQ genes of Escherichia coli K-12: Regulation of the regulators
    • Darwin, A. J., and V. Stewart. 1995. Expression of the narX, narL, narP, and nurQ genes of Escherichia coli K-12: regulation of the regulators. J. Bacteriol. 177:3865-3869.
    • (1995) J. Bacteriol. , vol.177 , pp. 3865-3869
    • Darwin, A.J.1    Stewart, V.2
  • 17
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereux, J., P. Haeberli. and O. Smithies. 1984. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 12:387-395.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 387-395
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3
  • 18
    • 0025265852 scopus 로고
    • Rubredoxin reductase of Pseudomonas oleovorans: Structural relationship to other flavoprotein oxidoreductases based on one NAD and two FAD fingerprints
    • Eggink, G., H. Engel, G. Vriend, P. Terpstra, and B. Witholt. 1990. Rubredoxin reductase of Pseudomonas oleovorans: structural relationship to other flavoprotein oxidoreductases based on one NAD and two FAD fingerprints. J. Mol. Biol. 212:135-142.
    • (1990) J. Mol. Biol. , vol.212 , pp. 135-142
    • Eggink, G.1    Engel, H.2    Vriend, G.3    Terpstra, P.4    Witholt, B.5
  • 19
    • 0025954526 scopus 로고
    • 2 evolution system of Rhodospirillum rubrum: Role of a 22-kDa iron-sulfur protein in mediating electron transfer between carbon monoxide dehydrogenase and hydrogenase
    • 2 evolution system of Rhodospirillum rubrum: role of a 22-kDa iron-sulfur protein in mediating electron transfer between carbon monoxide dehydrogenase and hydrogenase. J. Biol. Chem. 266:18395-18403.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18395-18403
    • Ensign, S.A.1    Ludden, P.W.2
  • 20
    • 0027369102 scopus 로고
    • Regulation of the gltBDF operon of Escherichia coli: How is a leucine-insensitive operon regulated by the leucine-responsive regulatory protein?
    • Ernsting, B. R., J. W. Denninger, R. M. Blumenthal, and R. G. Matthews. 1993. Regulation of the gltBDF operon of Escherichia coli: how is a leucine-insensitive operon regulated by the leucine-responsive regulatory protein? J. Bacteriol. 175:7160-7169.
    • (1993) J. Bacteriol. , vol.175 , pp. 7160-7169
    • Ernsting, B.R.1    Denninger, J.W.2    Blumenthal, R.M.3    Matthews, R.G.4
  • 21
    • 0027550316 scopus 로고
    • Molecular characterization of NADH-dependent glutamate synthase from Alfalfa nodules
    • Gregerson, R. G., S. S. Miller, S. N. Twary, S. J. Gantt, and C. P. Vance. 1993. Molecular characterization of NADH-dependent glutamate synthase from Alfalfa nodules. Plant Cell 5:215-226.
    • (1993) Plant Cell , vol.5 , pp. 215-226
    • Gregerson, R.G.1    Miller, S.S.2    Twary, S.N.3    Gantt, S.J.4    Vance, C.P.5
  • 22
    • 0030028140 scopus 로고    scopus 로고
    • Repression of the Escherichia coli modABCD (molybdate transport) operon by ModE
    • Grunden, A. M., R. M. Ray, J. K. Rosentel, F. G. Healy, and K. T. Shan- mugam. 1996. Repression of the Escherichia coli modABCD (molybdate transport) operon by ModE. J. Bacteriol. 178:735-744.
    • (1996) J. Bacteriol. , vol.178 , pp. 735-744
    • Grunden, A.M.1    Ray, R.M.2    Rosentel, J.K.3    Healy, F.G.4    Mugam, K.T.5
  • 23
    • 0027989421 scopus 로고
    • Aerobic-anaerobic gene regulation in Escherichia coli: Control by the ArcAB and Fnr regulons
    • Gunsalus, R. P., and S.-J. Park. 1994. Aerobic-anaerobic gene regulation in Escherichia coli: control by the ArcAB and Fnr regulons. Res. Microbiol. 145:437-450.
    • (1994) Res. Microbiol. , vol.145 , pp. 437-450
    • Gunsalus, R.P.1    Park, S.-J.2
  • 24
    • 0024340114 scopus 로고
    • New method for generating deletions and rearrangements in Escherichia coli
    • Hamilton, C. M., M. Aldea, B. K. Washburn, P. Babitzke, and S. R. Kushner. 1989. New method for generating deletions and rearrangements in Escherichia coli. J Bacteriol. 171:4617-4622.
    • (1989) J Bacteriol. , vol.171 , pp. 4617-4622
    • Hamilton, C.M.1    Aldea, M.2    Washburn, B.K.3    Babitzke, P.4    Kushner, S.R.5
  • 26
    • 0023272628 scopus 로고
    • Cloning and nucleotide sequence of the chID locus
    • Johann, S., and S. M. Hinton. 1987. Cloning and nucleotide sequence of the chID locus. J. Bacteriol. 169:1911-1916.
    • (1987) J. Bacteriol. , vol.169 , pp. 1911-1916
    • Johann, S.1    Hinton, S.M.2
  • 27
    • 0025606276 scopus 로고
    • Nitrate- And molybdenum-independent signal transduction mutations in narX that alter regulation of anaerobic respiratory genes in Escherichia coli
    • Kalman, L. V., and R. P. Gunsalus. 1990. Nitrate- and molybdenum-independent signal transduction mutations in narX that alter regulation of anaerobic respiratory genes in Escherichia coli. J. Bacteriol. 172:7049-7056.
    • (1990) J. Bacteriol. , vol.172 , pp. 7049-7056
    • Kalman, L.V.1    Gunsalus, R.P.2
  • 28
    • 0026649571 scopus 로고
    • Genetic and physiological characterization of the Rhodospirillum rubrum carbon monoxide dehydrogenase system
    • Kerby, R. L., S. S. Hong, S. A. Ensign, L, J. Coppoc, P. W. Ludden, and G. P. Roberts. 1992. Genetic and physiological characterization of the Rhodospirillum rubrum carbon monoxide dehydrogenase system. J. Bacteriol. 174: 5284-5294.
    • (1992) J. Bacteriol. , vol.174 , pp. 5284-5294
    • Kerby, R.L.1    Hong, S.S.2    Ensign, S.A.3    Coppoc, L.J.4    Ludden, P.W.5    Roberts, G.P.6
  • 29
    • 85035183771 scopus 로고    scopus 로고
    • Personal communication
    • 28a.Kolesnikow, T. Personal communication.
    • Kolesnikow, T.1
  • 30
    • 85035188874 scopus 로고    scopus 로고
    • Unpublished data
    • 28b.Kolesnikow, T. Unpublished data.
    • Kolesnikow, T.1
  • 31
    • 0026545675 scopus 로고
    • Regulation of narK gene expression in Escherichia coli in response to anaerobiosis, nitrate, iron, and molybdenum
    • Kolesnikow, T., I. Schröder, and R. P. Gunsalus. 1992. Regulation of narK gene expression in Escherichia coli in response to anaerobiosis, nitrate, iron, and molybdenum. J. Bacteriol. 174:7104-7111.
    • (1992) J. Bacteriol. , vol.174 , pp. 7104-7111
    • Kolesnikow, T.1    Schröder, I.2    Gunsalus, R.P.3
  • 32
    • 85035187275 scopus 로고    scopus 로고
    • Personal communication
    • 29a.Low, D. Personal communication.
    • Low, D.1
  • 34
    • 0025353046 scopus 로고
    • Identification of phosphate starvatkm-inducible genes in Escherichia coli K-12 by DNA sequence analysis of psi::lacZ(Mu d1) transcriptional fusions
    • Metcalf, W. W., P. M. Steed, and B. L. Wanner, 1990. Identification of phosphate starvatkm-inducible genes in Escherichia coli K-12 by DNA sequence analysis of psi::lacZ(Mu d1) transcriptional fusions. J. Bacteriol. 172:3191-3200.
    • (1990) J. Bacteriol. , vol.172 , pp. 3191-3200
    • Metcalf, W.W.1    Steed, P.M.2    Wanner, B.L.3
  • 36
    • 0027412184 scopus 로고
    • Glutamate synthase geres of the diazotroph Azospirillum brasilense: Cloning, sequencing, and analysis of functional domains
    • Pelanda, R., M. A. Vanoni, M. Perego, L. Poubelli, A. Galizzi, B. Curti. and G. Zanetti. 1993. Glutamate synthase geres of the diazotroph Azospirillum brasilense: cloning, sequencing, and analysis of functional domains. J. Biol. Chem. 268:3099-3106.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3099-3106
    • Pelanda, R.1    Vanoni, M.A.2    Perego, M.3    Poubelli, L.4    Galizzi, A.5    Curti, B.6    Zanetti, G.7
  • 37
    • 0026705854 scopus 로고
    • Either of two functionally redundant sensor proteins, NarX and NarQ, is sufficient for nitrate regulation in Escherichia coli K-12
    • Rabin, R. S., and V. J. Stewart. 1992. Either of two functionally redundant sensor proteins, NarX and NarQ, is sufficient for nitrate regulation in Escherichia coli K-12. Proc. Natl. Acad. Sci. USA 89:8419-8423.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 8419-8423
    • Rabin, R.S.1    Stewart, V.J.2
  • 38
    • 0000060736 scopus 로고
    • Ammonia assimilation and the biosynthesis of glutamine, glutamate, aspartate, asparagine. L-alanine, and D-alanine
    • F. C. Neidhardt, J. L. Ingraham, K. B. Low, B. Magasanik, M. Schaechter, and H. E. Umbarger (ed.), American Society for Microbiology, Washington, D.C
    • Reitzer, L. J., and B. Magasanik. 1987. Ammonia assimilation and the biosynthesis of glutamine, glutamate, aspartate, asparagine. L-alanine, and D-alanine, p. 302-320. In F. C. Neidhardt, J. L. Ingraham, K. B. Low, B. Magasanik, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella typhimurium: cellular and molecular biology. American Society for Microbiology, Washington, D.C.
    • (1987) Escherichia Coli and Salmonella Typhimurium: Cellular and Molecular Biology , pp. 302-320
    • Reitzer, L.J.1    Magasanik, B.2
  • 39
    • 0025930768 scopus 로고
    • Mechanism of regulation of the formate-hydrogenlyase pathway by oxygen, nitrate, and pH: Definition of the formate regulon
    • Rossmann, R., G. Sawers, and A. Böck. 1991. Mechanism of regulation of the formate-hydrogenlyase pathway by oxygen, nitrate, and pH: definition of the formate regulon. Mol. Microbiol. 5:2807-2814.
    • (1991) Mol. Microbiol. , vol.5 , pp. 2807-2814
    • Rossmann, R.1    Sawers, G.2    Böck, A.3
  • 40
    • 0026009206 scopus 로고
    • Alteration of the iron-sulfur cluster composition of Escherichia coli dimethyl sulfoxide reductase by site-directed mutagenesis
    • Rothery, R. A., and J. H. Weiner. 1991. Alteration of the iron-sulfur cluster composition of Escherichia coli dimethyl sulfoxide reductase by site-directed mutagenesis. Biochemistry 30:8296-8305.
    • (1991) Biochemistry , vol.30 , pp. 8296-8305
    • Rothery, R.A.1    Weiner, J.H.2
  • 42
    • 0026356524 scopus 로고
    • Expression and operon structure of the sel genes of Escherichia coli and identification of a third selenium-containing formate dehydrogenase isoenzyme
    • Sawers, G., J. Heider, E. Zehelein, and A. Böck. 1991 Expression and operon structure of the sel genes of Escherichia coli and identification of a third selenium-containing formate dehydrogenase isoenzyme. J. Bacteriol. 173: 4983-4993.
    • (1991) J. Bacteriol. , vol.173 , pp. 4983-4993
    • Sawers, G.1    Heider, J.2    Zehelein, E.3    Böck, A.4
  • 43
    • 0027452546 scopus 로고
    • Nitrate dependent activation of the Escherichia coli nitrate reductase narGHJI] operon by NarL and FNR requires integration host factor protein
    • Schröder, L., S. Daire, and R. P. Gunsalus. 1993. Nitrate dependent activation of the Escherichia coli nitrate reductase (narGHJI] operon by NarL and FNR requires integration host factor protein. J. Biol. Chem. 268:771-774.
    • (1993) J. Biol. Chem. , vol.268 , pp. 771-774
    • Schröder, L.1    Daire, S.2    Gunsalus, R.P.3
  • 44
    • 0027499561 scopus 로고
    • The nac (nitrogen assimilation control) gene from Klebsiella aerogenes
    • Schwacha, A., and R. A. Bender. 1993. The nac (nitrogen assimilation control) gene from Klebsiella aerogenes. J. Bacteriol. 175:2107-2115.
    • (1993) J. Bacteriol. , vol.175 , pp. 2107-2115
    • Schwacha, A.1    Bender, R.A.2
  • 45
    • 0025019734 scopus 로고
    • Redesign of the coenzyme specificities of a dehydrogenase by protein engineering
    • Scrutton, N. S., A. Berry, and R. N. Perham. 1990. Redesign of the coenzyme specificities of a dehydrogenase by protein engineering. Nature (London) 343:38-43.
    • (1990) Nature (London) , vol.343 , pp. 38-43
    • Scrutton, N.S.1    Berry, A.2    Perham, R.N.3
  • 47
    • 0023255472 scopus 로고
    • Improved single and multicopy lac-based cloning vectors for protein and operon fusions
    • Simons, R. W., R. Houman, and N. Kleckner. 1987. Improved single and multicopy lac-based cloning vectors for protein and operon fusions. Gene 53:85-96.
    • (1987) Gene , vol.53 , pp. 85-96
    • Simons, R.W.1    Houman, R.2    Kleckner, N.3
  • 48
    • 0024989737 scopus 로고
    • FNR and its role in oxygen-regulated gene expression in Escherichia coli
    • Spino, S., and J. R. Guest. 1990. FNR and its role in oxygen-regulated gene expression in Escherichia coli. FEMS Microbiol. Rev. 75:399-428.
    • (1990) FEMS Microbiol. Rev. , vol.75 , pp. 399-428
    • Spino, S.1    Guest, J.R.2
  • 49
    • 0027321764 scopus 로고
    • Nitrate regulation of anaerobic respiratory gene expression in Escherichia coli
    • Stewart, V. 1993. Nitrate regulation of anaerobic respiratory gene expression in Escherichia coli. Mol. Microbiol. 9:425-434.
    • (1993) Mol. Microbiol. , vol.9 , pp. 425-434
    • Stewart, V.1
  • 50
    • 0026659227 scopus 로고
    • Characterization of the flavins and the iron-sulfur centers of glutamate synthase from Azospirillum brasilence by adsorption, circular dichroism, and electron paramagnetic resonance spectroscopies
    • Vanoni, M. A., D. E. Edmondson, G. Zanetti, and B. Curti. 1992. Characterization of the flavins and the iron-sulfur centers of glutamate synthase from Azospirillum brasilence by adsorption, circular dichroism, and electron paramagnetic resonance spectroscopies. Biochemistry 31:4613-4623.
    • (1992) Biochemistry , vol.31 , pp. 4613-4623
    • Vanoni, M.A.1    Edmondson, D.E.2    Zanetti, G.3    Curti, B.4
  • 51
    • 33845318295 scopus 로고
    • Interaction of pyrophosphate moieties with α-helixes in dinucleotide binding proteins
    • Wierenga, R. K., M. C. H. De Maeyer, and W. G. J. Hol. 1985. Interaction of pyrophosphate moieties with α-helixes in dinucleotide binding proteins. Biochemistry 24:1346-1357.
    • (1985) Biochemistry , vol.24 , pp. 1346-1357
    • Wierenga, R.K.1    De Maeyer, M.C.H.2    Hol, W.G.J.3
  • 52
    • 0022460634 scopus 로고
    • Anaerobically induced genes of Escherichia coli
    • Winkelman, J. W., and D. P. Clark. 1986. Anaerobically induced genes of Escherichia coli. J. Bacteriol. 167:362-367.
    • (1986) J. Bacteriol. , vol.167 , pp. 362-367
    • Winkelman, J.W.1    Clark, D.P.2
  • 53
    • 0026652126 scopus 로고
    • Nucleotide sequence, function, activation and evolution of the cryptic use operon of Escherichia coli K-12
    • Xu, L., and B. Hall. 1992. Nucleotide sequence, function, activation and evolution of the cryptic use operon of Escherichia coli K-12. Mol. Biol. Evol. 9:688-706.
    • (1992) Mol. Biol. Evol. , vol.9 , pp. 688-706
    • Xu, L.1    Hall, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.