메뉴 건너뛰기




Volumn 189, Issue 11, 2007, Pages 3935-3944

Transcription of all amoC copies is associated with recovery of Nitrosomonas europaea from ammonia starvation

Author keywords

[No Author keywords available]

Indexed keywords

AMMONIA; HOLOENZYME; NUCLEASE S1; PROLINE;

EID: 34249801778     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.01861-06     Document Type: Article
Times cited : (37)

References (54)
  • 1
    • 0033568606 scopus 로고    scopus 로고
    • The Escherichia coli sigma(E)-dependent extracytoplasmic stress response is controlled by the regulated proteolysis of an anti-sigma factor
    • Ades, S. E., L. E. Connolly, B. M. Alba, and C. A. Gross. 1999. The Escherichia coli sigma(E)-dependent extracytoplasmic stress response is controlled by the regulated proteolysis of an anti-sigma factor. Gene Dev. 13:2449-2461.
    • (1999) Gene Dev , vol.13 , pp. 2449-2461
    • Ades, S.E.1    Connolly, L.E.2    Alba, B.M.3    Gross, C.A.4
  • 2
    • 0028177036 scopus 로고
    • Effects of starvation for exogenous carbon on functional messenger RNA stability and rate of peptide chain elongation in Escherichia coli
    • Albertson, N. H., and T. Nystrom. 1994. Effects of starvation for exogenous carbon on functional messenger RNA stability and rate of peptide chain elongation in Escherichia coli. FEMS Microbiol. Lett. 117:181-188.
    • (1994) FEMS Microbiol. Lett , vol.117 , pp. 181-188
    • Albertson, N.H.1    Nystrom, T.2
  • 3
    • 0025088796 scopus 로고
    • Functional messenger RNA half-lives in the marine Vibrio sp S14 during starvation and recovery
    • Albertson, N. H., T. Nystrom, and S. Kjelleberg. 1990. Functional messenger RNA half-lives in the marine Vibrio sp S14 during starvation and recovery. J. Gen. Microbiol. 136:2195-2199.
    • (1990) J. Gen. Microbiol , vol.136 , pp. 2195-2199
    • Albertson, N.H.1    Nystrom, T.2    Kjelleberg, S.3
  • 4
    • 0036038187 scopus 로고    scopus 로고
    • Molecular biology and biochemistry of ammonia oxidation by Nitrosomonas europaea
    • Arp, D. J., L. A. Sayavedra-Soto, and N. G. Hommes. 2002. Molecular biology and biochemistry of ammonia oxidation by Nitrosomonas europaea. Arch. Microbiol. 178:250-255.
    • (2002) Arch. Microbiol , vol.178 , pp. 250-255
    • Arp, D.J.1    Sayavedra-Soto, L.A.2    Hommes, N.G.3
  • 5
    • 0028924092 scopus 로고
    • Overlapping promoters for two different RNA polymerase holoenzymes control Bradyrhizohium japonicum nifA expression
    • Barrios, H., H. M. Fischer, H. Hennecke, and E. Morett. 1995. Overlapping promoters for two different RNA polymerase holoenzymes control Bradyrhizohium japonicum nifA expression. J. Bacteriol. 177:1760-1765.
    • (1995) J. Bacteriol , vol.177 , pp. 1760-1765
    • Barrios, H.1    Fischer, H.M.2    Hennecke, H.3    Morett, E.4
  • 6
    • 15444372598 scopus 로고    scopus 로고
    • Influence of starvation on potential ammonia-oxidizing activity and amoA mRNA levels of Nitrosospira briensis
    • Bollmann, A., I. Schmidt, A. M. Saunders, and M. H. Nicolaisen. 2005. Influence of starvation on potential ammonia-oxidizing activity and amoA mRNA levels of Nitrosospira briensis. Appl. Environ. Microbiol. 71:1276-1282.
    • (2005) Appl. Environ. Microbiol , vol.71 , pp. 1276-1282
    • Bollmann, A.1    Schmidt, I.2    Saunders, A.M.3    Nicolaisen, M.H.4
  • 7
    • 0026492668 scopus 로고
    • Control of Rnase E mediated RNA degradation by 5′-terminal base pairing in Escherichia coli
    • Bouvet, P., and J. G. Belasco. 1992. Control of Rnase E mediated RNA degradation by 5′-terminal base pairing in Escherichia coli. Nature 360:488-491.
    • (1992) Nature , vol.360 , pp. 488-491
    • Bouvet, P.1    Belasco, J.G.2
  • 9
    • 0032617132 scopus 로고    scopus 로고
    • Degradation of mRNA in Escherichia coli: An old problem with some new twists
    • Coburn, G. A., and G. A. Mackie. 1999. Degradation of mRNA in Escherichia coli: An old problem with some new twists. Prog. Nucleic Acid Res. 62:55-108.
    • (1999) Prog. Nucleic Acid Res , vol.62 , pp. 55-108
    • Coburn, G.A.1    Mackie, G.A.2
  • 10
    • 0025612734 scopus 로고
    • Characterization of three different nitrogen-regulated promoter regions for the expression of glnB and glnA in Azospirillum brasilense
    • de Zamaroczy, M., F. Delorme, and C. Elmerich. 1990. Characterization of three different nitrogen-regulated promoter regions for the expression of glnB and glnA in Azospirillum brasilense. Mol. Gen. Genet. 224:421-430.
    • (1990) Mol. Gen. Genet , vol.224 , pp. 421-430
    • de Zamaroczy, M.1    Delorme, F.2    Elmerich, C.3
  • 11
    • 0026602761 scopus 로고
    • A 5′-terminal stem loop structure can stabilize messenger RNA in Escherichia coli
    • Emory, S. A., P. Bouvet, and J. G. Belasco. 1992. A 5′-terminal stem loop structure can stabilize messenger RNA in Escherichia coli. Gene Dev. 6:135-148.
    • (1992) Gene Dev , vol.6 , pp. 135-148
    • Emory, S.A.1    Bouvet, P.2    Belasco, J.G.3
  • 12
    • 0033781828 scopus 로고    scopus 로고
    • Oxygen regulation of the Escherichia coli cytochrome d oxidase (cydAB) operon: Roles of multiple promoters and the Fnr-1 and Fnr-2 binding sites
    • Govantes, F., J. A. Albrecht, and R. P. Gunsalus. 2000. Oxygen regulation of the Escherichia coli cytochrome d oxidase (cydAB) operon: roles of multiple promoters and the Fnr-1 and Fnr-2 binding sites. Mol. Microbiol. 37:1456-1469.
    • (2000) Mol. Microbiol , vol.37 , pp. 1456-1469
    • Govantes, F.1    Albrecht, J.A.2    Gunsalus, R.P.3
  • 13
    • 0029888893 scopus 로고    scopus 로고
    • Structural dissection and functional analysis of the complex promoter of the streptokinase gene from Streptococcus equisimilis H46A
    • Grafe, S., T. Ellinger, and H. Malke. 1996. Structural dissection and functional analysis of the complex promoter of the streptokinase gene from Streptococcus equisimilis H46A. Med. Microbiol. Immunol. 185:11-17.
    • (1996) Med. Microbiol. Immunol , vol.185 , pp. 11-17
    • Grafe, S.1    Ellinger, T.2    Malke, H.3
  • 14
    • 0029946715 scopus 로고    scopus 로고
    • Effect of the pufQ-pufB intercistronic region on puf mRNA stability in Rhodobacter capsulatus
    • Heck, C., R. Rothfuchs, A. Jager, R. Rauhut, and G. Klug. 1996. Effect of the pufQ-pufB intercistronic region on puf mRNA stability in Rhodobacter capsulatus. Mol. Microbiol. 20:1165-1178.
    • (1996) Mol. Microbiol , vol.20 , pp. 1165-1178
    • Heck, C.1    Rothfuchs, R.2    Jager, A.3    Rauhut, R.4    Klug, G.5
  • 15
    • 15644373219 scopus 로고    scopus 로고
    • Mutagenesis and expression of amo, which codes for ammonia monooxygenase in Nitrosomonas europaea
    • Hommes, N. G., L. A. Sayavedra-Soto, and D. J. Arp. 1998. Mutagenesis and expression of amo, which codes for ammonia monooxygenase in Nitrosomonas europaea. J. Bacteriol. 180:3353-3359.
    • (1998) J. Bacteriol , vol.180 , pp. 3353-3359
    • Hommes, N.G.1    Sayavedra-Soto, L.A.2    Arp, D.J.3
  • 16
    • 0035152075 scopus 로고    scopus 로고
    • Transcript analysis of multiple copies of amo (encoding ammonia monooxygenase) and hao (encoding hydroxylamine oxidoreductase) in Nitrosomonas europaea
    • Hommes, N. G., L. A. Sayavedra-Soto, and D. J. Arp. 2001. Transcript analysis of multiple copies of amo (encoding ammonia monooxygenase) and hao (encoding hydroxylamine oxidoreductase) in Nitrosomonas europaea. J. Bacteriol. 183:1096-1100.
    • (2001) J. Bacteriol , vol.183 , pp. 1096-1100
    • Hommes, N.G.1    Sayavedra-Soto, L.A.2    Arp, D.J.3
  • 17
    • 0037073077 scopus 로고    scopus 로고
    • Promoter clearance and escape in prokaryotes
    • Hsu, L. M. 2002. Promoter clearance and escape in prokaryotes. Biochim. Biophys. Acta 1577:191-207.
    • (2002) Biochim. Biophys. Acta , vol.1577 , pp. 191-207
    • Hsu, L.M.1
  • 18
    • 21444448763 scopus 로고    scopus 로고
    • PROTINFO: New algorithms for enhanced protein structure predictions
    • Hung, L. H., S. C. Ngan, T. Y. Liu, and R. Samudrala. 2005. PROTINFO: new algorithms for enhanced protein structure predictions. Nucleic Acids Res. 33:W77-W80.
    • (2005) Nucleic Acids Res , vol.33
    • Hung, L.H.1    Ngan, S.C.2    Liu, T.Y.3    Samudrala, R.4
  • 19
    • 0042622449 scopus 로고    scopus 로고
    • PROTINFO: Secondary and tertiary protein structure prediction
    • Hung, L. H., and R. Samudrala. 2003. PROTINFO: secondary and tertiary protein structure prediction. Nucleic Acids Res. 31:3296-3299.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3296-3299
    • Hung, L.H.1    Samudrala, R.2
  • 20
    • 0034333387 scopus 로고    scopus 로고
    • Glutamine synthetase gene expression at elevated hydrostatic pressure in a deep-sea piezophilic Shewanella violacea
    • Ikegami, A., K. Nakasone, C. Kato, Y. Nakamura, I. Yoshikawa, R. Usami, and K. Horikoshi. 2000. Glutamine synthetase gene expression at elevated hydrostatic pressure in a deep-sea piezophilic Shewanella violacea. FEMS Microbiol. Lett. 192:91-95.
    • (2000) FEMS Microbiol. Lett , vol.192 , pp. 91-95
    • Ikegami, A.1    Nakasone, K.2    Kato, C.3    Nakamura, Y.4    Yoshikawa, I.5    Usami, R.6    Horikoshi, K.7
  • 21
    • 0001127120 scopus 로고
    • Physiological-effects of long-term energy-source deprivation on the survival of a marine chemolithotrophic ammonium-oxidizing bacterium
    • Johnstone, B. H., and R. D. Jones. 1988. Physiological-effects of long-term energy-source deprivation on the survival of a marine chemolithotrophic ammonium-oxidizing bacterium. Mar. Ecol. Prog. Ser. 49:295-303.
    • (1988) Mar. Ecol. Prog. Ser , vol.49 , pp. 295-303
    • Johnstone, B.H.1    Jones, R.D.2
  • 22
    • 0008648375 scopus 로고
    • Recovery of a marine chemolithotrophic ammonium-oxidizing bacterium from long-term energy-source deprivation
    • Johnstone, B. H., and R. D. Jones. 1988. Recovery of a marine chemolithotrophic ammonium-oxidizing bacterium from long-term energy-source deprivation. Can. J. Microbiol. 34:1347-1350.
    • (1988) Can. J. Microbiol , vol.34 , pp. 1347-1350
    • Johnstone, B.H.1    Jones, R.D.2
  • 23
    • 34249794698 scopus 로고    scopus 로고
    • Kenney, D. R., and D. W. Nelson. 1982. Nitrogen - inorganic forms, p. 643-693. In A. L. Page (ed.), Methods of soil analysis, part 2. American Society of Agronomy, Madison, WI.
    • Kenney, D. R., and D. W. Nelson. 1982. Nitrogen - inorganic forms, p. 643-693. In A. L. Page (ed.), Methods of soil analysis, part 2. American Society of Agronomy, Madison, WI.
  • 25
    • 0031007617 scopus 로고    scopus 로고
    • A gene encoding a membrane protein exists upstream of the amoA/amoB genes in ammonia oxidizing bacteria: A third member of the amo operon?
    • Klotz, M. G., J. Alzerreca, and J. M. Norton. 1997. A gene encoding a membrane protein exists upstream of the amoA/amoB genes in ammonia oxidizing bacteria: A third member of the amo operon? FEMS Microbiol. Lett. 150:65-73.
    • (1997) FEMS Microbiol. Lett , vol.150 , pp. 65-73
    • Klotz, M.G.1    Alzerreca, J.2    Norton, J.M.3
  • 26
    • 0034868585 scopus 로고    scopus 로고
    • Distribution and ecophysiology of the nitrifying bacteria emphasizing cultured species
    • Koops, H. P., and A. Pommerening-Roser. 2001. Distribution and ecophysiology of the nitrifying bacteria emphasizing cultured species. FEMS Microbiol. Ecol. 37:1-9.
    • (2001) FEMS Microbiol. Ecol , vol.37 , pp. 1-9
    • Koops, H.P.1    Pommerening-Roser, A.2
  • 27
    • 0031883229 scopus 로고    scopus 로고
    • Stationary phase, amino acid limitation and recovery from stationary phase modulate the stability and translation of chloramphenicol acetyltransferase mRNA and total mRNA in Escherichia coli
    • Kuzj, A. E., P. S. Medberry, and J. L. Schottel. 1998. Stationary phase, amino acid limitation and recovery from stationary phase modulate the stability and translation of chloramphenicol acetyltransferase mRNA and total mRNA in Escherichia coli. Microbiology 144(Pt 3):739-750.
    • (1998) Microbiology , vol.144 , Issue.PART 3 , pp. 739-750
    • Kuzj, A.E.1    Medberry, P.S.2    Schottel, J.L.3
  • 28
    • 15044356424 scopus 로고    scopus 로고
    • Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methane
    • Lieberman, R. L., and A. C. Rosenzweig. 2005. Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methane. Nature 434:177-182.
    • (2005) Nature , vol.434 , pp. 177-182
    • Lieberman, R.L.1    Rosenzweig, A.C.2
  • 29
    • 27744520845 scopus 로고    scopus 로고
    • The quest for the particulate methane monooxygenase active site
    • Lieberman, R. L., and A. C. Rosenzweig. 2005. The quest for the particulate methane monooxygenase active site. Dalton Trans. 3390-3396.
    • (2005) Dalton Trans , pp. 3390-3396
    • Lieberman, R.L.1    Rosenzweig, A.C.2
  • 30
    • 0028019587 scopus 로고
    • The role of the sigma-factor sigma(S) (Katf) in bacterial global regulation
    • Loewen, P. C., and R. Henggearonis. 1994. The role of the sigma-factor sigma(S) (Katf) in bacterial global regulation. Annu. Rev. Microbiol. 48:53-80.
    • (1994) Annu. Rev. Microbiol , vol.48 , pp. 53-80
    • Loewen, P.C.1    Henggearonis, R.2
  • 31
    • 0036841380 scopus 로고    scopus 로고
    • Broad-host-range cre-lox system for antibiotic marker recycling in gram-negative bacteria
    • Marx, C. J., and M. E. Lidstrom. 2002. Broad-host-range cre-lox system for antibiotic marker recycling in gram-negative bacteria. BioTechniques 33:1062-1067.
    • (2002) BioTechniques , vol.33 , pp. 1062-1067
    • Marx, C.J.1    Lidstrom, M.E.2
  • 32
    • 0033591465 scopus 로고    scopus 로고
    • Expanded sequence dependence of thermodynamic parameters improves prediction of RNA secondary structure
    • Mathews, D. H., J. Sabina, M. Zuker, and D. H. Turner. 1999. Expanded sequence dependence of thermodynamic parameters improves prediction of RNA secondary structure. J. Mol. Biol. 288:911-940.
    • (1999) J. Mol. Biol , vol.288 , pp. 911-940
    • Mathews, D.H.1    Sabina, J.2    Zuker, M.3    Turner, D.H.4
  • 33
    • 0027153142 scopus 로고
    • Sequence of the gene coding for ammonia monooxygenase in Nitrosomonas europaea
    • McTavish, H., J. A. Fuchs, and A. B. Hooper. 1993. Sequence of the gene coding for ammonia monooxygenase in Nitrosomonas europaea. J. Bacteriol. 175:2436-2444.
    • (1993) J. Bacteriol , vol.175 , pp. 2436-2444
    • McTavish, H.1    Fuchs, J.A.2    Hooper, A.B.3
  • 34
    • 6744243693 scopus 로고    scopus 로고
    • Shortage of nutrients in bacteria: The stringent response
    • Mukherjee, T. K., A. Raghavan, and D. Chatterji. 1998. Shortage of nutrients in bacteria: the stringent response. Curr. Sci. India 75:684-689.
    • (1998) Curr. Sci. India , vol.75 , pp. 684-689
    • Mukherjee, T.K.1    Raghavan, A.2    Chatterji, D.3
  • 35
    • 2942538872 scopus 로고    scopus 로고
    • Unique roles of the rrn P2 rRNA promoters in Escherichia coli
    • Murray, H. D., and R. L. Gourse. 2004. Unique roles of the rrn P2 rRNA promoters in Escherichia coli. Mol. Microbiol. 52:1375-1387.
    • (2004) Mol. Microbiol , vol.52 , pp. 1375-1387
    • Murray, H.D.1    Gourse, R.L.2
  • 36
    • 0037084067 scopus 로고    scopus 로고
    • Transcriptional regulation of fis operon involves a module of multiple coupled promoters
    • Nasser, W., M. Rochman, and G. Muskhelishvili. 2002. Transcriptional regulation of fis operon involves a module of multiple coupled promoters. EMBO J. 21:715-724.
    • (2002) EMBO J , vol.21 , pp. 715-724
    • Nasser, W.1    Rochman, M.2    Muskhelishvili, G.3
  • 37
    • 0036167265 scopus 로고    scopus 로고
    • Diversity of ammonia monooxygenase operon in autotrophic ammonia-oxidizing bacteria
    • Norton, J. M., J. J. Alzerreca, Y. Suwa, and M. G. Klotz. 2002. Diversity of ammonia monooxygenase operon in autotrophic ammonia-oxidizing bacteria. Arch. Microbiol. 177:139-149.
    • (2002) Arch. Microbiol , vol.177 , pp. 139-149
    • Norton, J.M.1    Alzerreca, J.J.2    Suwa, Y.3    Klotz, M.G.4
  • 38
    • 0035166777 scopus 로고    scopus 로고
    • Polyclonal antibodies recognizing the AmoB protein of ammonia oxidizers of the beta-subclass of the class Proteobacteria
    • Pinck, C., C. Coeur, P. Potier, and E. Bock. 2001. Polyclonal antibodies recognizing the AmoB protein of ammonia oxidizers of the beta-subclass of the class Proteobacteria. Appl. Environ. Microbiol. 67:118-124.
    • (2001) Appl. Environ. Microbiol , vol.67 , pp. 118-124
    • Pinck, C.1    Coeur, C.2    Potier, P.3    Bock, E.4
  • 40
    • 3342936478 scopus 로고    scopus 로고
    • A comprehensive analysis of 40 blind protein structure predictions
    • Samudrala, R., and M. Levitt. 2002. A comprehensive analysis of 40 blind protein structure predictions. BMC Struct. Biol. 2:3.
    • (2002) BMC Struct. Biol , vol.2 , pp. 3
    • Samudrala, R.1    Levitt, M.2
  • 41
    • 0032577270 scopus 로고    scopus 로고
    • A graph-theoretic algorithm for comparative modeling of protein structure
    • Samudrala, R., and J. Moult. 1998. A graph-theoretic algorithm for comparative modeling of protein structure. J. Mol. Biol. 279:287-302.
    • (1998) J. Mol. Biol , vol.279 , pp. 287-302
    • Samudrala, R.1    Moult, J.2
  • 42
    • 0032488962 scopus 로고    scopus 로고
    • An all-atom distance-dependent conditional probability discriminatory function for protein structure prediction
    • Samudrala, R., and J. Moult. 1998. An all-atom distance-dependent conditional probability discriminatory function for protein structure prediction. J. Mol. Biol. 275:895-916.
    • (1998) J. Mol. Biol , vol.275 , pp. 895-916
    • Samudrala, R.1    Moult, J.2
  • 44
    • 0032923140 scopus 로고    scopus 로고
    • Role of multiple gene copies in particulate methane monooxygenase activity in the methane-oxidizing bacterium Methylococcus capsulatus Bath
    • Stolyar, S., A. M. Costello, T. L. Peeples, and M. E. Lidstrom. 1999. Role of multiple gene copies in particulate methane monooxygenase activity in the methane-oxidizing bacterium Methylococcus capsulatus Bath. Microbiology 145(Pt 5):1235-1244.
    • (1999) Microbiology , vol.145 , Issue.PART 5 , pp. 1235-1244
    • Stolyar, S.1    Costello, A.M.2    Peeples, T.L.3    Lidstrom, M.E.4
  • 45
    • 0037115871 scopus 로고    scopus 로고
    • A hairpin near the 5′ end stabilises the DNA gyrase mRNA in Mycobacterium smegmatis
    • Unniraman, S., M. Chatterji, and V. Nagaraja. 2002. A hairpin near the 5′ end stabilises the DNA gyrase mRNA in Mycobacterium smegmatis. Nucleic Acids Res. 30:5376-5381.
    • (2002) Nucleic Acids Res , vol.30 , pp. 5376-5381
    • Unniraman, S.1    Chatterji, M.2    Nagaraja, V.3
  • 46
    • 0035834664 scopus 로고    scopus 로고
    • Alternate paradigm for intrinsic transcription termination in eubacteria
    • Unniraman, S., R. Prakash, and V. Nagaraja. 2001. Alternate paradigm for intrinsic transcription termination in eubacteria. J. Biol. Chem. 276:41850-41855.
    • (2001) J. Biol. Chem , vol.276 , pp. 41850-41855
    • Unniraman, S.1    Prakash, R.2    Nagaraja, V.3
  • 47
    • 0025919586 scopus 로고
    • Competition for ammonium between nitrifying and heterotrophic bacteria in dual energy-limited chemostats
    • Verhagen, F. J., and H. J. Laanbroek. 1991. Competition for ammonium between nitrifying and heterotrophic bacteria in dual energy-limited chemostats. Appl. Environ. Microbiol. 57:3255-3263.
    • (1991) Appl. Environ. Microbiol , vol.57 , pp. 3255-3263
    • Verhagen, F.J.1    Laanbroek, H.J.2
  • 48
    • 0028993835 scopus 로고
    • Competition for ammonium between plant roots and nitrifying and heterotrophic bacteria and the effects of protozoan grazing
    • Verhagen, F. J. M., H. J. Laanbroek, and J. W. Woldendorp. 1995. Competition for ammonium between plant roots and nitrifying and heterotrophic bacteria and the effects of protozoan grazing. Plant Soil 170:241-250.
    • (1995) Plant Soil , vol.170 , pp. 241-250
    • Verhagen, F.J.M.1    Laanbroek, H.J.2    Woldendorp, J.W.3
  • 49
    • 0028000994 scopus 로고
    • Coaxial stacking of helixes enhances binding of oligoribonucleotides and improves predictions of RNA folding
    • Walter, A. E., D. H. Turner, J. Kim, M. H. Lyttle, P. Muller, D. H. Mathews, and M. Zuker. 1994. Coaxial stacking of helixes enhances binding of oligoribonucleotides and improves predictions of RNA folding. Proc. Natl. Acad. Sci. USA 91:9218-9222.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9218-9222
    • Walter, A.E.1    Turner, D.H.2    Kim, J.3    Lyttle, M.H.4    Muller, P.5    Mathews, D.H.6    Zuker, M.7
  • 50
    • 3142678008 scopus 로고    scopus 로고
    • The transcription of the cbb operon in Nitrosomonas europaea
    • Wei, X. M., L. A. Sayavedra-Soto, and D. J. Arp. 2004. The transcription of the cbb operon in Nitrosomonas europaea. Microbiology 150:1869-1879.
    • (2004) Microbiology , vol.150 , pp. 1869-1879
    • Wei, X.M.1    Sayavedra-Soto, L.A.2    Arp, D.J.3
  • 51
    • 0031768533 scopus 로고    scopus 로고
    • Effect of long-term ammonia starvation on the oxidation of ammonia and hydroxylamine by Nitrosomonas europaea
    • Wilhelm, R., A. Abeliovich, and A. Nejidat. 1998. Effect of long-term ammonia starvation on the oxidation of ammonia and hydroxylamine by Nitrosomonas europaea. J. Biochem. 124:811-515.
    • (1998) J. Biochem , vol.124 , pp. 811-515
    • Wilhelm, R.1    Abeliovich, A.2    Nejidat, A.3
  • 52
    • 0003140215 scopus 로고
    • Nitrification as a bacterial energy source
    • J. I. Prosser ed, IRL Press, Oxford, United Kingdom
    • Wood, P. M. 1986. Nitrification as a bacterial energy source, p. 39-62. In J. I. Prosser (ed.), Nitrification. IRL Press, Oxford, United Kingdom.
    • (1986) Nitrification , pp. 39-62
    • Wood, P.M.1
  • 53
    • 0039820099 scopus 로고    scopus 로고
    • Eubacterial sigma-factors
    • Wösten, M. 1998. Eubacterial sigma-factors. FEMS Microbiol. Rev. 22:127-150.
    • (1998) FEMS Microbiol. Rev , vol.22 , pp. 127-150
    • Wösten, M.1
  • 54
    • 0002287019 scopus 로고    scopus 로고
    • Algorithms and thermodynamics for RNA secondary structure prediction: A practical guide
    • B. F. C. Clark ed, Kluwer Academic Publishers, Boston, MA
    • Zuker, M., D. H. Mathews, and D. H. Turner. 1999. Algorithms and thermodynamics for RNA secondary structure prediction: a practical guide, p. 11-43. In B. F. C. Clark (ed.), RNA biochemistry and biotechnology. Kluwer Academic Publishers, Boston, MA.
    • (1999) RNA biochemistry and biotechnology , pp. 11-43
    • Zuker, M.1    Mathews, D.H.2    Turner, D.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.