메뉴 건너뛰기




Volumn 10, Issue 4, 2010, Pages 3562-3584

Potential for development of an Escherichia coli-based biosensor for assessing bioavailable methionine: A review

Author keywords

Bioavailability; Escherichia coli; Methionine; Microbial biosensors

Indexed keywords

ACCURATE QUANTIFICATIONS; BIOAVAILABILITY; ENVIRONMENTAL POLLUTIONS; GOVERNMENTAL REGULATIONS; METHIONINE; METHIONINE BIOSYNTHESIS; MICROBIAL BIOSENSOR; MICROBIOLOGICAL ASSAYS;

EID: 77951717588     PISSN: 14248220     EISSN: None     Source Type: Journal    
DOI: 10.3390/s100403562     Document Type: Review
Times cited : (8)

References (133)
  • 1
    • 0001861438 scopus 로고    scopus 로고
    • Rumen-protected amino acids for dairy cattle: Progress towards determining lysine and methionine requirements
    • Schwab, C.G. Rumen-protected amino acids for dairy cattle: Progress towards determining lysine and methionine requirements. Anim. Feed Sci. Technol. 1996, 59, 87-101.
    • (1996) Anim. Feed Sci. Technol , vol.59 , pp. 87-101
    • Schwab, C.G.1
  • 2
    • 0034074915 scopus 로고    scopus 로고
    • Ideal amino acid profiles as a basis for feed protein evaluation
    • Boisen, S.; Hvelplund, T.; Weisbjerg, M.R. Ideal amino acid profiles as a basis for feed protein evaluation. Livest Prod. Sci. 2000, 64, 239-251.
    • (2000) Livest Prod. Sci , vol.64 , pp. 239-251
    • Boisen, S.1    Hvelplund, T.2    Weisbjerg, M.R.3
  • 3
    • 0033119957 scopus 로고    scopus 로고
    • Cystine is the first limiting amino acid for utilization of endogenous amino acids in chicks fed a protein-free diet
    • Webel, D.M.; Baker, D.H. Cystine is the first limiting amino acid for utilization of endogenous amino acids in chicks fed a protein-free diet. Nutr. Res. 1999, 19, 569-577.
    • (1999) Nutr. Res , vol.19 , pp. 569-577
    • Webel, D.M.1    Baker, D.H.2
  • 4
    • 71449112528 scopus 로고    scopus 로고
    • Role of dietary methionine in poultry production
    • Bunchasak, C. Role of dietary methionine in poultry production. J. Poult. Sci. 2009, 46, 169-179.
    • (2009) J. Poult. Sci , vol.46 , pp. 169-179
    • Bunchasak, C.1
  • 5
    • 33646809781 scopus 로고    scopus 로고
    • The sulfur-containing amino acids: An overview
    • Brosnan, J.T.; Brosnan, M.E. The sulfur-containing amino acids: an overview. J. Nutr. 2006, 136, 1636S-1640.
    • (2006) J. Nutr , vol.136
    • Brosnan, J.T.1    Brosnan, M.E.2
  • 7
    • 34548067938 scopus 로고    scopus 로고
    • 2-Keto-4-(Methylthio) butyric acid (keto analog of methionine) is a safe and efficacious precursor of L-methionine in chicks
    • Dilger, R.N.; Kobler, C.; Weckbecker, C.; Hoehler, D.; Baker, D.H. 2-Keto-4-(Methylthio) butyric acid (keto analog of methionine) is a safe and efficacious precursor of L-methionine in chicks. J. Nutr. 2007, 137, 1868-1873.
    • (2007) J. Nutr , vol.137 , pp. 1868-1873
    • Dilger, R.N.1    Kobler, C.2    Weckbecker, C.3    Hoehler, D.4    Baker, D.H.5
  • 8
    • 0042706516 scopus 로고    scopus 로고
    • Influence of supplementation with liquid DL-methionine hydroxy analogue-free acid (alimet) or DL-methionine on performance of broilers
    • Daenner, E.; Bessei, W. Influence of supplementation with liquid DL-methionine hydroxy analogue-free acid (alimet) or DL-methionine on performance of broilers. J. Appl. Poult. Res. 2003, 12, 101-105.
    • (2003) J. Appl. Poult. Res , vol.12 , pp. 101-105
    • Daenner, E.1    Bessei, W.2
  • 9
    • 33746267340 scopus 로고    scopus 로고
    • The potential to reduce poultry nitrogen emissions with dietary methionine or methionine analogues supplementation
    • Kim, W.K.; Froelich Jr., C.A.; Patterson, P.H.; Ricke, S.C. The potential to reduce poultry nitrogen emissions with dietary methionine or methionine analogues supplementation. World Poult. Sci. J. 2006, 62, 338-353.
    • (2006) World Poult. Sci. J , vol.62 , pp. 338-353
    • Kim, W.K.1    Froelich, C.A.2    Patterson, P.H.3    Ricke, S.C.4
  • 10
    • 19944371054 scopus 로고    scopus 로고
    • In Nutritional diseases
    • Saif, Y.M., Ed.; Iowa State Press: Ames, IA, USA
    • Klasing, K.C.; Austic, R.E. In Nutritional diseases. In Diseases of Poultry; Saif, Y.M., Ed.; Iowa State Press: Ames, IA, USA, 2003; p. 1027.
    • (2003) Diseases of Poultry , pp. 1027
    • Klasing, K.C.1    Austic, R.E.2
  • 11
    • 33646788078 scopus 로고    scopus 로고
    • Comparative species utilization and toxicity of sulfur amino acids
    • Baker, D.H. Comparative species utilization and toxicity of sulfur amino acids. J. Nutr. 2006, 136, 1670S-1675.
    • (2006) J. Nutr , vol.136
    • Baker, D.H.1
  • 12
    • 0019525072 scopus 로고
    • The effects of high dietary protein and nitrogen levels on the preformed methyl group requirement and methionine-induced growth depression in chicks
    • Pesti, G.M.; Benevenga, N.J.; Harper, A.E.; Sunde, M.L. The effects of high dietary protein and nitrogen levels on the preformed methyl group requirement and methionine-induced growth depression in chicks. Poult. Sci. 1981, 60, 425-432.
    • (1981) Poult. Sci , vol.60 , pp. 425-432
    • Pesti, G.M.1    Benevenga, N.J.2    Harper, A.E.3    Sunde, M.L.4
  • 14
    • 0003538477 scopus 로고    scopus 로고
    • Aspen Production: Gaithersburg, MD, USA
    • Nielson, S.S. In Food analysis; Aspen Production: Gaithersburg, MD, USA, 1998.
    • (1998) Food Analysis
    • Nielson, S.S.1
  • 15
    • 0031065998 scopus 로고    scopus 로고
    • Protein and amino acid quality of meat and bone meal
    • Parsons, C.M.; Castanon, F.; Han, Y. Protein and amino acid quality of meat and bone meal. Poult. Sci. 1997, 76, 361-368.
    • (1997) Poult. Sci , vol.76 , pp. 361-368
    • Parsons, C.M.1    Castanon, F.2    Han, Y.3
  • 16
    • 33644983153 scopus 로고    scopus 로고
    • Response of growing poultry to amino acids
    • D'Mello, J.P.F., Ed.; CABI Publishing: Wallingford, CT, USA
    • D'Mello, J.P.F. Response of growing poultry to amino acids. In Amino Acids in Animal Nutrition; D'Mello, J.P.F., Ed.; CABI Publishing: Wallingford, CT, USA, 2003; p. 237.
    • (2003) Amino Acids In Animal Nutrition , pp. 237
    • D'mello, J.P.F.1
  • 18
    • 20544455118 scopus 로고    scopus 로고
    • Rapid bacterial-based bioassays for quantifying methionine bioavailability in animal feeds: A review
    • Froelich, C.A.; Ricke, S.C. Rapid bacterial-based bioassays for quantifying methionine bioavailability in animal feeds: a review. J. Rapid Meth. Autom. Microbiol. 2005, 13, 1-10.
    • (2005) J. Rapid Meth. Autom. Microbiol , vol.13 , pp. 1-10
    • Froelich, C.A.1    Ricke, S.C.2
  • 19
    • 34547641724 scopus 로고    scopus 로고
    • Quantification of total and bioavailable lysine in feed protein sources by a whole-cell green fluorescent protein growth-based Escherichia coli biosensor
    • Chalova, V.I.; Kim, W.K.; Woodward, C.L.; Ricke, S.C. Quantification of total and bioavailable lysine in feed protein sources by a whole-cell green fluorescent protein growth-based Escherichia coli biosensor. Appl. Microbiol. Biotechnol. 2007, 76, 91-99.
    • (2007) Appl. Microbiol. Biotechnol , vol.76 , pp. 91-99
    • Chalova, V.I.1    Kim, W.K.2    Woodward, C.L.3    Ricke, S.C.4
  • 20
    • 0034910570 scopus 로고    scopus 로고
    • Microbial biosensors
    • D'Souza, S.F. Microbial biosensors. Bios. Bioelectr. 2001, 16, 337-353.
    • (2001) Bios. Bioelectr , vol.16 , pp. 337-353
    • D'Souza, S.F.1
  • 22
    • 0036096757 scopus 로고    scopus 로고
    • Review of the use of biosensors as analytical tools in the food and drink industries
    • Mello, L.D.; Kubota, L.T. Review of the use of biosensors as analytical tools in the food and drink industries. Food Chem. 2002, 77, 237-256.
    • (2002) Food Chem , vol.77 , pp. 237-256
    • Mello, L.D.1    Kubota, L.T.2
  • 23
    • 61849171142 scopus 로고    scopus 로고
    • A microbial biosensor based on bacterial cells immobilized on chitosan matrix
    • Odaci, D.; Timur, S.; Telefoncua, A. A microbial biosensor based on bacterial cells immobilized on chitosan matrix. Bioelectrochemistry 2009, 75, 77-82.
    • (2009) Bioelectrochemistry , vol.75 , pp. 77-82
    • Odaci, D.1    Timur, S.2    Telefoncua, A.3
  • 25
    • 33646548225 scopus 로고    scopus 로고
    • Microbial biosensor for direct determination of nitrophenyl-substituted organophosphate nerve agents using genetically engineered Moraxella sp
    • Mulchandani, P.; Chen, W.; Mulchandani, A. Microbial biosensor for direct determination of nitrophenyl-substituted organophosphate nerve agents using genetically engineered Moraxella sp. Anal. Chim. Acta 2006, 568, 217-221.
    • (2006) Anal. Chim. Acta , vol.568 , pp. 217-221
    • Mulchandani, P.1    Chen, W.2    Mulchandani, A.3
  • 26
    • 33645848492 scopus 로고    scopus 로고
    • Optical microbial biosensor for detection of methyl parathion pesticide using Flavobacterium sp. whole cells adsorbed on glass fiber filters as disposable biocomponent
    • Kumar, J.; Jha, S.K.; D'Souza, S.F. Optical microbial biosensor for detection of methyl parathion pesticide using Flavobacterium sp. whole cells adsorbed on glass fiber filters as disposable biocomponent. Biosen. Bioel. 2006, 21, 2105-2100.
    • (2006) Biosen. Bioel , vol.21 , pp. 2105-2100
    • Kumar, J.1    Jha, S.K.2    D'Souza, S.F.3
  • 27
    • 48749119961 scopus 로고    scopus 로고
    • Bacterial biosensors for measuring availability of environmental pollutants
    • Tecon, R.; van der Meer, J.R. Bacterial biosensors for measuring availability of environmental pollutants. Sensors 2008, 8, 4062-4080.
    • (2008) Sensors , vol.8 , pp. 4062-4080
    • Tecon, R.1    van der Meer, J.R.2
  • 29
    • 2442447146 scopus 로고    scopus 로고
    • New potentiometric microbial biosensor for ethanol determination in alcoholic beverages
    • Rotariu, L.; Bala, C.; Magearu, V. New potentiometric microbial biosensor for ethanol determination in alcoholic beverages. Anal. Chim. Acta 2004, 513, 119-123.
    • (2004) Anal. Chim. Acta , vol.513 , pp. 119-123
    • Rotariu, L.1    Bala, C.2    Magearu, V.3
  • 30
    • 0024678426 scopus 로고
    • The development of an amperometric microbial biosensor using Acetobacter pasteurianus for lactic acid
    • Luong, J.H.T.; Mulchandani, A.; Groom, C.A. The development of an amperometric microbial biosensor using Acetobacter pasteurianus for lactic acid. J. Biotechnol. 1989, 10, 241-252.
    • (1989) J. Biotechnol , vol.10 , pp. 241-252
    • Luong, J.H.T.1    Mulchandani, A.2    Groom, C.A.3
  • 31
    • 0010300838 scopus 로고
    • A novel method for the determination of lactic acid. Comparison of lactic acid content of English and North European wines
    • Buglass, A.J.; Garnham, S.C. A novel method for the determination of lactic acid. Comparison of lactic acid content of English and North European wines. Am. J. Enol. Vitic. 1991, 42, 63-66.
    • (1991) Am. J. Enol. Vitic , vol.42 , pp. 63-66
    • Buglass, A.J.1    Garnham, S.C.2
  • 32
    • 0004413342 scopus 로고    scopus 로고
    • Microbial biosensors based on oxygen electrodes
    • Mulchandani, A., Rogers, K.R., Eds.; Humanae Press: Totowa, NJ, USA
    • Riedel, K. Microbial biosensors based on oxygen electrodes. In Enzyme and Microbial Biosensors: Techniques and Protocols; Mulchandani, A., Rogers, K.R., Eds.; Humanae Press: Totowa, NJ, USA, 1998; p. 199.
    • (1998) Enzyme and Microbial Biosensors: Techniques and Protocols , pp. 199
    • Riedel, K.1
  • 33
    • 0030877280 scopus 로고    scopus 로고
    • A tryptophan-2-monooxygenase based amperometric biosensor for L-tryptophan determination: Use of a competitive inhibitor as a tool for selectivity increase
    • Simonian, A.L.; Rainina, E.I.; Fitzpatrick, P.F.; Wild, J.R. A tryptophan-2-monooxygenase based amperometric biosensor for L-tryptophan determination: use of a competitive inhibitor as a tool for selectivity increase. Bios. Bioel. 1997, 12, 363-371.
    • (1997) Bios. Bioel , vol.12 , pp. 363-371
    • Simonian, A.L.1    Rainina, E.I.2    Fitzpatrick, P.F.3    Wild, J.R.4
  • 35
    • 15444350252 scopus 로고    scopus 로고
    • The complete genome sequence of Escherichia coli K-12
    • Blattner, F.R. The complete genome sequence of Escherichia coli K-12. Science 1997, 277, 1453-1462.
    • (1997) Science , vol.277 , pp. 1453-1462
    • Blattner, F.R.1
  • 36
    • 0030712223 scopus 로고    scopus 로고
    • A biosensor for environmental genotoxin screening based on an SOS lux assay in recombinant Escherichia coli cells
    • Ptitsyn, L.R.; Horneck, G.; Komova, O.; Kozubek, S.; Krasavin, E.A.; Bonev, M.; Rettberg, P. A biosensor for environmental genotoxin screening based on an SOS lux assay in recombinant Escherichia coli cells. Appl. Environ. Microbiol. 1997, 63, 4377-4384.
    • (1997) Appl. Environ. Microbiol , vol.63 , pp. 4377-4384
    • Ptitsyn, L.R.1    Horneck, G.2    Komova, O.3    Kozubek, S.4    Krasavin, E.A.5    Bonev, M.6    Rettberg, P.7
  • 37
    • 58549118980 scopus 로고    scopus 로고
    • A novel E. coli biosensor for detecting aromatic aldehydes based on a responsive inducible archaeal promoter fused to the green fluorescent protein
    • Fiorentino, G.; Ronca, R.; Bartolucci, S. A novel E. coli biosensor for detecting aromatic aldehydes based on a responsive inducible archaeal promoter fused to the green fluorescent protein. Appl. Microbiol. Biotechnol. 2009, 82, 67-77.
    • (2009) Appl. Microbiol. Biotechnol , vol.82 , pp. 67-77
    • Fiorentino, G.1    Ronca, R.2    Bartolucci, S.3
  • 40
    • 0142027136 scopus 로고    scopus 로고
    • Development of a set of simple bacterial biosensors for quantitative and rapid measurements of arsenite and arsenate in potable water
    • Stocker, J.; Balluch, D.; Gsell, M.; Harms, H.; Feliciano, J.; Daunert, S.; Malik, K.A.; van der Meer, J. R. Development of a set of simple bacterial biosensors for quantitative and rapid measurements of arsenite and arsenate in potable water. Environ. Sci. Technol. 2003, 37, 4743-4750.
    • (2003) Environ. Sci. Technol , vol.37 , pp. 4743-4750
    • Stocker, J.1    Balluch, D.2    Gsell, M.3    Harms, H.4    Feliciano, J.5    Daunert, S.6    Malik, K.A.7    van der Meer, J.R.8
  • 41
    • 42149154825 scopus 로고    scopus 로고
    • GFP expressing bacterial biosensor to measure lead contamination in aquatic environment
    • Chakraborty, T.; Babu, P.G.; Alam, A.; Chaudhari, A. GFP expressing bacterial biosensor to measure lead contamination in aquatic environment. Curr. Sci. 2008, 94, 800-805.
    • (2008) Curr. Sci , vol.94 , pp. 800-805
    • Chakraborty, T.1    Babu, P.G.2    Alam, A.3    Chaudhari, A.4
  • 42
    • 0034276747 scopus 로고    scopus 로고
    • A three-cascaded-enzymes biosensor to determine lactose concentration in raw milk
    • Eshkenazi, I.; Maltz, E.; Zion, B.; Rishpon, J. A three-cascaded-enzymes biosensor to determine lactose concentration in raw milk. J. Dairy Sci. 2000, 83, 1939-1945.
    • (2000) J. Dairy Sci , vol.83 , pp. 1939-1945
    • Eshkenazi, I.1    Maltz, E.2    Zion, B.3    Rishpon, J.A.4
  • 43
    • 0036883710 scopus 로고    scopus 로고
    • Microbial biosensor array with transport mutants of Escherichia coli K12 for the simultaneous determination of mono-and disaccharides
    • Held, M.; Schuhmann, W.; Jahreisc, K.; Schmidt, H. Microbial biosensor array with transport mutants of Escherichia coli K12 for the simultaneous determination of mono-and disaccharides. Biosen. Bioel. 2002, 17, 1089-1094.
    • (2002) Biosen. Bioel , vol.17 , pp. 1089-1094
    • Held, M.1    Schuhmann, W.2    Jahreisc, K.3    Schmidt, H.4
  • 44
    • 0019259093 scopus 로고
    • A microbiological assay based on ampicillin-induced lysis of Escherichia coli auxotrophs
    • Krapf, G.; Bode, W. A microbiological assay based on ampicillin-induced lysis of Escherichia coli auxotrophs. Zbl. Bakt. Hyg., I Abt. Orig. C 1980, 1, 314-319.
    • (1980) Zbl. Bakt. Hyg., I Abt. Orig. C , vol.1 , pp. 314-319
    • Krapf, G.1    Bode, W.2
  • 45
    • 0024531192 scopus 로고
    • The use of Escherichia coli mutants to measure the bioavailability of essential amino acids in foods. Plant Foods Hum
    • Hitchins, A.D.; McDonough, F.E.; Wells, P.A. The use of Escherichia coli mutants to measure the bioavailability of essential amino acids in foods. Plant Foods Hum. Nutr. 1989, 39, 109-120.
    • (1989) Nutr , vol.39 , pp. 109-120
    • Hitchins, A.D.1    McDonough, F.E.2    Wells, P.A.3
  • 46
    • 0343619433 scopus 로고    scopus 로고
    • A bioluminescent Escherichia coli auxotroph for use in an in vitro lysine availability assay
    • Erickson, A.M.; Diaz, I.B.Z.; Kwon, Y.M.; Ricke, S.C. A bioluminescent Escherichia coli auxotroph for use in an in vitro lysine availability assay. J. Microbiol. Meth. 2000, 40, 207-212.
    • (2000) J. Microbiol. Meth , vol.40 , pp. 207-212
    • Erickson, A.M.1    Diaz, I.B.Z.2    Kwon, Y.M.3    Ricke, S.C.4
  • 47
    • 70350029395 scopus 로고    scopus 로고
    • Escherichia coli, an intestinal microorganism, as a biosensor for quantification of amino acid bioavailability
    • Chalova, V.I.; Sirsat, S.A.; O'Bryan, C.A.; Crandall, P.; Ricke, S.C. Escherichia coli, an intestinal microorganism, as a biosensor for quantification of amino acid bioavailability. Sensors 2009, 9, 7038-7057.
    • (2009) Sensors , vol.9 , pp. 7038-7057
    • Chalova, V.I.1    Sirsat, S.A.2    O'Bryan, C.A.3    Crandall, P.4    Ricke, S.C.5
  • 48
    • 0032846457 scopus 로고    scopus 로고
    • Optimisation of enzyme treatment for the degradation of feed proteins for an Escherichia coli auxotroph lysine availability assay
    • Erickson, A.M.; Li, X.; Woodward, C.L.; Ricke, S.C. Optimisation of enzyme treatment for the degradation of feed proteins for an Escherichia coli auxotroph lysine availability assay. J. Sci. Food Agric. 1999, 79, 1929-1935.
    • (1999) J. Sci. Food Agric , vol.79 , pp. 1929-1935
    • Erickson, A.M.1    Li, X.2    Woodward, C.L.3    Ricke, S.C.4
  • 49
    • 8444221544 scopus 로고    scopus 로고
    • Assessment of an Escherichia coli methionine auxotroph growth assay for quantifying crystalline methionine supplemented in poultry feeds
    • Zabala-Díaz, I.B.; Carreon, F.O.C.; Ellis, W.C.; Ricke, S.C. Assessment of an Escherichia coli methionine auxotroph growth assay for quantifying crystalline methionine supplemented in poultry feeds. J. Rapid Methods Auto. Micro. 2004, 12, 155-167.
    • (2004) J. Rapid Methods Auto. Micro , vol.12 , pp. 155-167
    • Zabala-Díaz, I.B.1    Carreon, F.O.C.2    Ellis, W.C.3    Ricke, S.C.4
  • 50
    • 0036968175 scopus 로고    scopus 로고
    • Adaptation of a methionine auxotroph Escherichia coli growth assay to microtiter plates for quantitating methionine
    • Zabala-Díaz, I.B.; Froelich, C.A.; Ricke, S.C. Adaptation of a methionine auxotroph Escherichia coli growth assay to microtiter plates for quantitating methionine. J. Rapid Methods Auto. Micro. 2003, 10, 217-229.
    • (2003) J. Rapid Methods Auto. Micro , vol.10 , pp. 217-229
    • Zabala-Díaz, I.B.1    Froelich, C.A.2    Ricke, S.C.3
  • 51
    • 0001101003 scopus 로고
    • Optimal conditions for mutagenesis by N-methyl-N'-nitro-N-nitrosoguanidine in Escherichia coli K12
    • Adelberg, E.A.; Mandel, M.; Chein, C.C.G. Optimal conditions for mutagenesis by N-methyl-N'-nitro-N-nitrosoguanidine in Escherichia coli K12. Biochem. Biophys. Res. Commun. 1965, 18, 788-795.
    • (1965) Biochem. Biophys. Res. Commun , vol.18 , pp. 788-795
    • Adelberg, E.A.1    Mandel, M.2    Chein, C.C.G.3
  • 53
    • 0030748518 scopus 로고    scopus 로고
    • Creating auxotrophic mutants in Methylophilus methylotrophus AS1 by combining electroporation and chemical mutagenesis
    • Kim, C.S.; Wood, T.K. Creating auxotrophic mutants in Methylophilus methylotrophus AS1 by combining electroporation and chemical mutagenesis. Appl. Microbiol. Biotechnol. 1997, 48, 105-108.
    • (1997) Appl. Microbiol. Biotechnol , vol.48 , pp. 105-108
    • Kim, C.S.1    Wood, T.K.2
  • 54
    • 0030974929 scopus 로고    scopus 로고
    • Reversion rates in a leuB auxotroph of Escherichia coli K-12 correlate with ppGpp levels during exponential growth
    • Wright, B.E.; Minnick, M.F. Reversion rates in a leuB auxotroph of Escherichia coli K-12 correlate with ppGpp levels during exponential growth. Microbiology 1997, 143, 847-854.
    • (1997) Microbiology , vol.143 , pp. 847-854
    • Wright, B.E.1    Minnick, M.F.2
  • 55
    • 0020374667 scopus 로고
    • Mutations affecting regulation of methionine biosynthetic genes isolated by use of met-lac fusions
    • Mulligan, J.T.; Margolin, W.; Krueger, J.H.; Walker, G.C. Mutations affecting regulation of methionine biosynthetic genes isolated by use of met-lac fusions. J. Bacteriol. 1982, 151, 609-619.
    • (1982) J. Bacteriol , vol.151 , pp. 609-619
    • Mulligan, J.T.1    Margolin, W.2    Krueger, J.H.3    Walker, G.C.4
  • 56
    • 0036815194 scopus 로고    scopus 로고
    • Potential rapid bioassay for Alimet® using a methionine Escherichia coli auxotroph
    • Froelich, C.A.; Zabala-Díaz, I.B.; Ricke, S.C. Potential rapid bioassay for Alimet® using a methionine Escherichia coli auxotroph. J. Rapid Methods Auto. Micro. 2002, 10, 161-172.
    • (2002) J. Rapid Methods Auto. Micro , vol.10 , pp. 161-172
    • Froelich, C.A.1    Zabala-Díaz, I.B.2    Ricke, S.C.3
  • 57
    • 84888283213 scopus 로고    scopus 로고
    • Methionine-hydroxy analogue was found to be significantly less bioavailable compared to DL-methionine for protein deposition in growing pigs
    • Shoveller, A.K.; Moehn, S.; Rademacher, M.; Htoo, J.K.; Ball, R.O. Methionine-hydroxy analogue was found to be significantly less bioavailable compared to DL-methionine for protein deposition in growing pigs. Animal 2009, 77, 427-439.
    • (2009) Animal , vol.77 , pp. 427-439
    • Shoveller, A.K.1    Moehn, S.2    Rademacher, M.3    Htoo, J.K.4    Ball, R.O.5
  • 58
    • 77951720855 scopus 로고    scopus 로고
    • Efficacy of methionine hydroxy analog and DL-methionine as methionine sources for growing pigs
    • Feng, Z.; Qiao, S.; Ma, Y.; Wang, X.; Li, X.; Thacker, P.A. Efficacy of methionine hydroxy analog and DL-methionine as methionine sources for growing pigs. J. Anim. Veter. Adv. 2006, 5, 135-142.
    • (2006) J. Anim. Veter. Adv , vol.5 , pp. 135-142
    • Feng, Z.1    Qiao, S.2    Ma, Y.3    Wang, X.4    Li, X.5    Thacker, P.A.6
  • 59
    • 0021685462 scopus 로고
    • Regulatory region of the metA gene of Escherichia coli K-12
    • Michaeli, S.; Mevarech, M.; Ron, E.Z. Regulatory region of the metA gene of Escherichia coli K-12. J. Bacteriol. 1984, 160, 1158-1162.
    • (1984) J. Bacteriol , vol.160 , pp. 1158-1162
    • Michaeli, S.1    Mevarech, M.2    Ron, E.Z.3
  • 60
    • 0015858738 scopus 로고
    • Mechanism of repression of methionine biosynthesis in Escherichia coli
    • Ahmed, A. Mechanism of repression of methionine biosynthesis in Escherichia coli. Mol. Gen. Genet. 1973, 123, 299-324.
    • (1973) Mol. Gen. Genet , vol.123 , pp. 299-324
    • Ahmed, A.1
  • 63
    • 33745160404 scopus 로고    scopus 로고
    • Large-scale identification of protein-protein interaction of Escherichia coli K-12
    • Arifuzzaman, M., et al Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res. 2006, 16, 686-691.
    • (2006) Genome Res , vol.16 , pp. 686-691
    • Arifuzzaman, M.1
  • 64
    • 0141456354 scopus 로고    scopus 로고
    • Escherichia coli cystathionine?-synthase does not obey ping-pong kinetics. Novel continuous assays for the elimination and substitution reactions
    • Aitken, S.M.; Kim, D.H.; Kirsch, J.F. Escherichia coli cystathionine?-synthase does not obey ping-pong kinetics. Novel continuous assays for the elimination and substitution reactions. Biochemistry 2003, 42, 11297-11306.
    • (2003) Biochemistry , vol.42 , pp. 11297-11306
    • Aitken, S.M.1    Kim, D.H.2    Kirsch, J.F.3
  • 65
    • 0041661883 scopus 로고    scopus 로고
    • Effect of cysteine desulfhydrase gene disruption on L-cysteine overproduction in Escherichia coli
    • Awano, N.; Wada, M.; Kohdoh, A.; Oikawa, T.; Takagi, H.; Nakamori, S. Effect of cysteine desulfhydrase gene disruption on L-cysteine overproduction in Escherichia coli. Appl. Microbiol. Biotechnol. 2003, 62, 239-243.
    • (2003) Appl. Microbiol. Biotechnol , vol.62 , pp. 239-243
    • Awano, N.1    Wada, M.2    Kohdoh, A.3    Oikawa, T.4    Takagi, H.5    Nakamori, S.6
  • 66
    • 0024364303 scopus 로고
    • Datta, Prasanta Matthew, Rowena G. Cloning and sequence analysis of the Escherichia coli metH gene encoding cobalamin-dependent methionine synthase and isolation of a tryptic fragment containing the cobalamin-binding domain
    • Banerjee, R.V.; Johnston, N.L.; Sobeski, J.K.; Datta, Prasanta Matthew, Rowena G. Cloning and sequence analysis of the Escherichia coli metH gene encoding cobalamin-dependent methionine synthase and isolation of a tryptic fragment containing the cobalamin-binding domain. J. Biol. Chem. 1989, 264, 13888-13895.
    • (1989) J. Biol. Chem , vol.264 , pp. 13888-13895
    • Banerjee, R.V.1    Johnston, N.L.2    Sobeski, J.K.3
  • 67
    • 0026754531 scopus 로고
    • Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes
    • 771-8.-778
    • Daniels, D.L.; Plunkett, G.I.; Burland, V.; Blattner, F.R. Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes. Science 1992, 257, 771-8.-778.
    • (1992) Science , vol.257
    • Daniels, D.L.1    Plunkett, G.I.2    Burland, V.3    Blattner, F.R.4
  • 68
    • 0032924516 scopus 로고    scopus 로고
    • S-methylmethionine metabolism in Escherichia coli
    • Thanbichler, M.; Neuhierl, B.; Bock, A. S-methylmethionine metabolism in Escherichia coli. J. Bacteriol. 1999, 181, 662-665.
    • (1999) J. Bacteriol , vol.181 , pp. 662-665
    • Thanbichler, M.1    Neuhierl, B.2    Bock, A.3
  • 69
    • 0021101228 scopus 로고
    • Nucleotide sequence of metF, the E. coli structural gene for 5-10 methylene tetrahydrofolate reductase and of its control region
    • Saint-Girons, I.; Duchange, N.; Zakin, M.M.; Park, I.; Margarita, D.; Ferrara, P.; Cohen, G.N. Nucleotide sequence of metF, the E. coli structural gene for 5-10 methylene tetrahydrofolate reductase and of its control region. Nucl. Acids Res. 1983, 11, 6723-6732.
    • (1983) Nucl. Acids Res , vol.11 , pp. 6723-6732
    • Saint-Girons, I.1    Duchange, N.2    Zakin, M.M.3    Park, I.4    Margarita, D.5    Ferrara, P.6    Cohen, G.N.7
  • 70
    • 33646760287 scopus 로고    scopus 로고
    • In vivo hydrolysis of S-adenosylmethionine induces the met regulon of Escherichia coli
    • LaMonte, B.L.; Hughes, J.A. In vivo hydrolysis of S-adenosylmethionine induces the met regulon of Escherichia coli. Microbiology 2006, 152, 1451-1459.
    • (2006) Microbiology , vol.152 , pp. 1451-1459
    • Lamonte, B.L.1    Hughes, J.A.2
  • 71
    • 0025036629 scopus 로고
    • Structure-function studies on Escherichia coli MetR protein, a putative prokaryotic leucine zipper protein
    • Maxon, M.E.; Wigboldus, J.; Brot, N.; Weissbach, H. Structure-function studies on Escherichia coli MetR protein, a putative prokaryotic leucine zipper protein. PNAS 1990, 87, 7076-7079.
    • (1990) PNAS , vol.87 , pp. 7076-7079
    • Maxon, M.E.1    Wigboldus, J.2    Brot, N.3    Weissbach, H.4
  • 72
    • 0024368031 scopus 로고
    • The Escherichia coli regulatory protein MetJ binds to a tandemly repeated 8bp palindrome
    • Davidson, B.E.; Girons, I.S. The Escherichia coli regulatory protein MetJ binds to a tandemly repeated 8bp palindrome. Mol. Microbiol. 1989, 3, 1639-1648.
    • (1989) Mol. Microbiol , vol.3 , pp. 1639-1648
    • Davidson, B.E.1    Girons, I.S.2
  • 73
    • 0023202474 scopus 로고
    • A new methionine locus, metR, that encodes a trans-acting protein required for activation of metE and metH in Escherichia coli and Salmonella typhimurium
    • Urbanowski, M.L.; Stauffer, L.T.; Plamann, L.S.; Stauffer, G.V. A new methionine locus, metR, that encodes a trans-acting protein required for activation of metE and metH in Escherichia coli and Salmonella typhimurium. J. Bacteriol. 1987, 169, 1391-1397.
    • (1987) J. Bacteriol , vol.169 , pp. 1391-1397
    • Urbanowski, M.L.1    Stauffer, L.T.2    Plamann, L.S.3    Stauffer, G.V.4
  • 75
    • 0026500535 scopus 로고
    • Role of the metF and metJ genes on the vitamin B12 regulation of methionine gene expression: Involvement of N5-methyltetrahydrofolic acid
    • Cai, X.; Jakubowski, H.; Redfield, B.; Zaleski, B.; Brot, N.; Weissbach, H. Role of the metF and metJ genes on the vitamin B12 regulation of methionine gene expression: involvement of N5-methyltetrahydrofolic acid. Biochem. Biophys. Res. Commun. 1992, 182, 651-658.
    • (1992) Biochem. Biophys. Res. Commun , vol.182 , pp. 651-658
    • Cai, X.1    Jakubowski, H.2    Redfield, B.3    Zaleski, B.4    Brot, N.5    Weissbach, H.6
  • 76
    • 0016755610 scopus 로고
    • Genetic characterization of the metK locus in Escherichia coli K-12
    • Hunter, J.S.; Greene, R.C.; Su, C.H. Genetic characterization of the metK locus in Escherichia coli K-12. J. Bacteriol. 1975, 122, 1144-1152.
    • (1975) J. Bacteriol , vol.122 , pp. 1144-1152
    • Hunter, J.S.1    Greene, R.C.2    Su, C.H.3
  • 77
    • 0024500829 scopus 로고
    • Regulation of methionine synthesis in Escherichia coli: Effect of the MetR protein on the expression of the metE and metR genes
    • Maxon, M.E.; Redfield, B.; Cai, X.Y.; Shoeman, R.; Fujita, K.; Fisher, W.; Stauffer, G.; Weissbach, H.; Brot, N. Regulation of methionine synthesis in Escherichia coli: effect of the MetR protein on the expression of the metE and metR genes. PNAS 1989, 86, 85-89.
    • (1989) PNAS , vol.86 , pp. 85-89
    • Maxon, M.E.1    Redfield, B.2    Cai, X.Y.3    Shoeman, R.4    Fujita, K.5    Fisher, W.6    Stauffer, G.7    Weissbach, H.8    Brot, N.9
  • 78
    • 0024311293 scopus 로고
    • Methionine synthesis in Escherichia coli: Effect of the MetR protein on metE and metH expression
    • Cai, X.Y.; Maxon, M.E.; Redfield, B.; Glass, R.; Brot, N.; Weissbach, H. Methionine synthesis in Escherichia coli: effect of the MetR protein on metE and metH expression. PNAS 1989, 86, 4407-4411.
    • (1989) PNAS , vol.86 , pp. 4407-4411
    • Cai, X.Y.1    Maxon, M.E.2    Redfield, B.3    Glass, R.4    Brot, N.5    Weissbach, H.6
  • 79
    • 0033770817 scopus 로고    scopus 로고
    • Control of methionine biosynthesis in Escherichia coli by proteolysis
    • Biran, D.; Gur, E.; Gollan, L.; Ron, E.Z. Control of methionine biosynthesis in Escherichia coli by proteolysis. Mol. Microbiol. 2000, 37, 1436-1443.
    • (2000) Mol. Microbiol , vol.37 , pp. 1436-1443
    • Biran, D.1    Gur, E.2    Gollan, L.3    Ron, E.Z.4
  • 80
    • 0033607238 scopus 로고    scopus 로고
    • Enzyme-catalyzed acylation of homoserine: Mechanistic characterization of the Escherichia coli metA-encoded homoserine transsuccinylase
    • Born, T.L.; Blanchard, J.S. Enzyme-catalyzed acylation of homoserine: Mechanistic characterization of the Escherichia coli metA-encoded homoserine transsuccinylase. Biochemistry 1999, 38, 14416-14423.
    • (1999) Biochemistry , vol.38 , pp. 14416-14423
    • Born, T.L.1    Blanchard, J.S.2
  • 81
    • 0025127113 scopus 로고
    • Adaptation of Escherichia coli to elevated temperatures: The metA gene product is a heat shock protein
    • Ron, EZ.; Alajem, S.; Biran, D.; Grossman, N. Adaptation of Escherichia coli to elevated temperatures: the metA gene product is a heat shock protein. Antonie Van Leeuwenhoek 1990, 58, 169-174.
    • (1990) Antonie Van Leeuwenhoek , vol.58 , pp. 169-174
    • Ron, E.Z.1    Alajem, S.2    Biran, D.3    Grossman, N.4
  • 82
    • 57449100055 scopus 로고    scopus 로고
    • Improved thermostability and acetic acid tolerance of Escherichia coli via directed evolution of homoserine O-succinyltransferase
    • Mordukhova, E.A.; Lee, H.; Pan, J. Improved thermostability and acetic acid tolerance of Escherichia coli via directed evolution of homoserine O-succinyltransferase. Appl. Environ. Microbiol. 2008, 74, 7660-7668.
    • (2008) Appl. Environ. Microbiol , vol.74 , pp. 7660-7668
    • Mordukhova, E.A.1    Lee, H.2    Pan, J.3
  • 83
    • 0028935282 scopus 로고
    • Heat shock-dependent transcriptional activation of the metA gene of Escherichia coli
    • Biran, D.; Brot, N.; Weissbach, H.; Ron, E.Z. Heat shock-dependent transcriptional activation of the metA gene of Escherichia coli. J. Bacteriol. 1995, 177, 1374-1379.
    • (1995) J. Bacteriol , vol.177 , pp. 1374-1379
    • Biran, D.1    Brot, N.2    Weissbach, H.3    Ron, E.Z.4
  • 84
    • 0026728876 scopus 로고
    • Role of the MetR regulatory system in vitamin B12-mediated repression of the Salmonella typhimurium metE gene
    • Wu, W.F.; Urbanowski, M.L.; Stauffer, G.V. Role of the MetR regulatory system in vitamin B12-mediated repression of the Salmonella typhimurium metE gene. J. Bacteriol. 1992, 174, 4833-4837.
    • (1992) J. Bacteriol , vol.174 , pp. 4833-4837
    • Wu, W.F.1    Urbanowski, M.L.2    Stauffer, G.V.3
  • 85
    • 0029760593 scopus 로고    scopus 로고
    • Cobalamin-independent methionine synthase from Escherichia coli: A zinc metalloenzyme
    • González, J.C.; Peariso, K.; Penner-Hahn, J.E.; Matthews, R.G. Cobalamin-independent methionine synthase from Escherichia coli: A zinc metalloenzyme. Biochemistry 1996, 35, 12228-12234.
    • (1996) Biochemistry , vol.35 , pp. 12228-12234
    • González, J.C.1    Peariso, K.2    Penner-Hahn, J.E.3    Matthews, R.G.4
  • 86
    • 0016671558 scopus 로고
    • Regulation of methionine transport activity in Escherichia coli
    • Kadner, R.J. Regulation of methionine transport activity in Escherichia coli. J. Bacteriol. 1975, 122, 110-119.
    • (1975) J. Bacteriol , vol.122 , pp. 110-119
    • Kadner, R.J.1
  • 87
    • 0036776777 scopus 로고    scopus 로고
    • The Escherichia coli metD locus encodes an ABC transporter which includes Abc (MetN), YaeE (MetI), and YaeC (MetQ)
    • Merlin, C.; Gardiner, G.; Durand, S.; Masters, M. The Escherichia coli metD locus encodes an ABC transporter which includes Abc (MetN), YaeE (MetI), and YaeC (MetQ). J. Bacteriol. 2002, 184, 5513-5517.
    • (2002) J. Bacteriol , vol.184 , pp. 5513-5517
    • Merlin, C.1    Gardiner, G.2    Durand, S.3    Masters, M.4
  • 88
    • 0017337388 scopus 로고
    • Transport and utilization of D-methionine and other methionine sources in Escherichia coli
    • Kadner, R.J. Transport and utilization of D-methionine and other methionine sources in Escherichia coli. J. Bacteriol. 1977, 129, 207-216.
    • (1977) J. Bacteriol , vol.129 , pp. 207-216
    • Kadner, R.J.1
  • 89
    • 0016796768 scopus 로고
    • Energy coupling for methionine transport in Escherichia coli
    • Kadner, R.J.; Winkler, H.H. Energy coupling for methionine transport in Escherichia coli. J. Bacteriol. 1975, 123, 985-991.
    • (1975) J. Bacteriol , vol.123 , pp. 985-991
    • Kadner, R.J.1    Winkler, H.H.2
  • 90
    • 0036720127 scopus 로고    scopus 로고
    • The metD D-methionine transporter locus of Escherichia coli is an ABC transporter gene cluster
    • Gál, J.; Szvetnik, A.; Róbert Schnell, R.; Kálmán, M. The metD D-methionine transporter locus of Escherichia coli is an ABC transporter gene cluster. J. Bacteriol. 2002, 184, 4930-4932.
    • (2002) J. Bacteriol , vol.184 , pp. 4930-4932
    • Gál, J.1    Szvetnik, A.2    Róbert Schnell, R.3    Kálmán, M.4
  • 91
    • 0015947712 scopus 로고
    • Transport systems for L-methionine in Escherichia coli
    • Kadner, R.J. Transport systems for L-methionine in Escherichia coli. J. Bacteriol. 1974, 117, 232-241.
    • (1974) J. Bacteriol , vol.117 , pp. 232-241
    • Kadner, R.J.1
  • 92
    • 0028358260 scopus 로고
    • Analysis and construction of stable phenotypes in gram-negative bacteria with Tn5- and Tn10-derived minitransposons
    • de Lorenzo, V.; Timmis, K.N. Analysis and construction of stable phenotypes in gram-negative bacteria with Tn5- and Tn10-derived minitransposons. Meth. Enzymol. 1994, 235, 386-405.
    • (1994) Meth. Enzymol , vol.235 , pp. 386-405
    • de Lorenzo, V.1    Timmis, K.N.2
  • 93
    • 0028923695 scopus 로고
    • In vivo growth characteristics of leucine and methionine auxotrophic mutants of Mycobacterium bovis BCG generated by transposon mutagenesis
    • McAdam, R.A.; Weisbrod, T.R.; Martin, J.; Scuderi, J.D.; Brown, A.M.; Cirillo, J.D.B.; Jacobs, J.W.R. In vivo growth characteristics of leucine and methionine auxotrophic mutants of Mycobacterium bovis BCG generated by transposon mutagenesis. Infect Immun. 1995, 63, 1004-1012.
    • (1995) Infect Immun , vol.63 , pp. 1004-1012
    • McAdam, R.A.1    Weisbrod, T.R.2    Martin, J.3    Scuderi, J.D.4    Brown, A.M.5    Cirillo, J.D.B.6    Jacobs, J.W.R.7
  • 94
    • 0025822841 scopus 로고
    • Auxotrophs produced by transposon mutagenesis in Streptomyces tendae ATCC 31160
    • Engel, P.; Wright, M.S. Auxotrophs produced by transposon mutagenesis in Streptomyces tendae ATCC 31160. Lett. Appl. Microbiol. 1991, 13, 51-54.
    • (1991) Lett. Appl. Microbiol , vol.13 , pp. 51-54
    • Engel, P.1    Wright, M.S.2
  • 95
    • 0033846629 scopus 로고    scopus 로고
    • Efficient amplification of multiple transposon-flanking sequences
    • Kwon, Y.M.; Ricke, S.C. Efficient amplification of multiple transposon-flanking sequences. J. Microbiol. Meth. 2000, 41, 195-199.
    • (2000) J. Microbiol. Meth , vol.41 , pp. 195-199
    • Kwon, Y.M.1    Ricke, S.C.2
  • 96
    • 0036436704 scopus 로고    scopus 로고
    • Functional screening of bacterial genome for virulence genes by transposon footprinting
    • Kwon, Y.M.; Kubena, L.F.; Nisbet, D.J.; Ricke, S.C. Functional screening of bacterial genome for virulence genes by transposon footprinting. Methods Enzymol. 2002, 358, 141-152.
    • (2002) Methods Enzymol , vol.358 , pp. 141-152
    • Kwon, Y.M.1    Kubena, L.F.2    Nisbet, D.J.3    Ricke, S.C.4
  • 97
    • 33750479870 scopus 로고    scopus 로고
    • Protection elicited by two glutamine auxotrophs of Mycobacterium tuberculosis and in vivo growth phenotypes of the four unique glutamine synthetase mutants in a murine model
    • Lee, S.; Jeon, B.; Bardarov, S.; Chen, M.; Morris, S.L.; Jacobs, W.R., Jr. Protection elicited by two glutamine auxotrophs of Mycobacterium tuberculosis and in vivo growth phenotypes of the four unique glutamine synthetase mutants in a murine model. Infect. Immun. 2006, 74, 6491-6495.
    • (2006) Infect. Immun , vol.74 , pp. 6491-6495
    • Lee, S.1    Jeon, B.2    Bardarov, S.3    Chen, M.4    Morris, S.L.5    Jacobs Jr., W.R.6
  • 98
    • 0037352557 scopus 로고    scopus 로고
    • Construction and complementation of the first auxotrophic mutant in the spirochaete Leptospira meyeri
    • Bauby, H.; Saint Girons, I.; Picardeau, M. Construction and complementation of the first auxotrophic mutant in the spirochaete Leptospira meyeri. Microbiology 2003, 149, 689-693.
    • (2003) Microbiology , vol.149 , pp. 689-693
    • Bauby, H.1    Saint Girons, I.2    Picardeau, M.3
  • 99
    • 0346887118 scopus 로고    scopus 로고
    • Generation of an Escherichia coli lysA targeted deletion mutant by double cross-over recombination for potential use in a bacterial growth-based lysine assay
    • Li, X.; Ricke, S.C. Generation of an Escherichia coli lysA targeted deletion mutant by double cross-over recombination for potential use in a bacterial growth-based lysine assay. Lett. Appl. Microbiol. 2003, 37, 458-462.
    • (2003) Lett. Appl. Microbiol , vol.37 , pp. 458-462
    • Li, X.1    Ricke, S.C.2
  • 100
    • 0021054334 scopus 로고
    • Regulatory pattern of the Escherichia coli lysA gene: Expression of chromosomal lysA-lacZ fusions
    • Stragier, P.; Borne, F.; Richaud, F.; Richaud, C.; Patte, J.C. Regulatory pattern of the Escherichia coli lysA gene: expression of chromosomal lysA-lacZ fusions. J. Bacteriol. 1983, 156, 1198-1203.
    • (1983) J. Bacteriol , vol.156 , pp. 1198-1203
    • Stragier, P.1    Borne, F.2    Richaud, F.3    Richaud, C.4    Patte, J.C.5
  • 101
    • 0021131990 scopus 로고
    • Insertion mutagenesis of the metJBLF gene cluster of Escherichia coli K-12: Evidence for an metBL operon
    • Greene, R.C.; Smith, A.A. Insertion mutagenesis of the metJBLF gene cluster of Escherichia coli K-12: evidence for an metBL operon. J. Bacteriol. 1984, 159, 767-769.
    • (1984) J. Bacteriol , vol.159 , pp. 767-769
    • Greene, R.C.1    Smith, A.A.2
  • 102
    • 0031953244 scopus 로고    scopus 로고
    • The folate branch of the methionine biosynthesis pathway in Streptomyces lividans: Disruption of the 5,10-methylenetetrahydrofolate reductase gene leads to methionine auxotrophy
    • Blanco, J.; Coque, J.J.R.; Martin, J.F. The folate branch of the methionine biosynthesis pathway in Streptomyces lividans: Disruption of the 5,10-methylenetetrahydrofolate reductase gene leads to methionine auxotrophy. J. Bacteriol. 1998, 180, 1586-1591.
    • (1998) J. Bacteriol , vol.180 , pp. 1586-1591
    • Blanco, J.1    Coque, J.J.R.2    Martin, J.F.3
  • 103
    • 0015136105 scopus 로고
    • Mutant strains of Escherichia coli K12 that use D-amino acids
    • Kuhn, J.; Somerville, R.L. Mutant strains of Escherichia coli K12 that use D-amino acids. PNAS 1966, 68, 2484-2487.
    • (1966) PNAS , vol.68 , pp. 2484-2487
    • Kuhn, J.1    Somerville, R.L.2
  • 104
    • 0020686355 scopus 로고
    • Biochemistry of sulfur-containing amino acids
    • Cooper, A.J.L. Biochemistry of sulfur-containing amino acids. Annu. Rev. Biochem. 1983, 52, 187-222.
    • (1983) Annu. Rev. Biochem , vol.52 , pp. 187-222
    • Cooper, A.J.L.1
  • 105
    • 0000993972 scopus 로고
    • Utilization of D-methionine by Escherichia coli
    • Cooper, S. Utilization of D-methionine by Escherichia coli. J. Bacteriol. 1966, 92, 328-332.
    • (1966) J. Bacteriol , vol.92 , pp. 328-332
    • Cooper, S.1
  • 106
    • 47249084799 scopus 로고    scopus 로고
    • The high-affinity E. coli methionine ABC transporter: Structure and allosteric regulation
    • Kadaba, N.S.; Kaiser, J.T.; Johnson, E.; Lee, A.; Rees, D.C. The high-affinity E. coli methionine ABC transporter: Structure and allosteric regulation. Science 2008, 321, 250-253.
    • (2008) Science , vol.321 , pp. 250-253
    • Kadaba, N.S.1    Kaiser, J.T.2    Johnson, E.3    Lee, A.4    Rees, D.C.5
  • 107
    • 77951720156 scopus 로고    scopus 로고
    • In Environmental assessment: Bioreporter systems
    • Osborn, A.M., Smith, C.S., Eds.; Taylor & Francis Group: New York, NY, USA
    • Ripp, S.A.; Sayler, G.S. In Environmental assessment: bioreporter systems. In Molecular Microbial Ecology; Osborn, A.M., Smith, C.S., Eds.; Taylor & Francis Group: New York, NY, USA, 2005; p. 321.
    • (2005) Molecular Microbial Ecology , pp. 321
    • Ripp, S.A.1    Sayler, G.S.2
  • 108
    • 0021912163 scopus 로고
    • A colorimetric enzyme assay using Escherichia coli to determine nutritionally available lysine in biological materials
    • Tuffnell, J.M.; Payne, J.W. A colorimetric enzyme assay using Escherichia coli to determine nutritionally available lysine in biological materials. J. Appl. Bact. 1985, 58, 333-341.
    • (1985) J. Appl. Bact , vol.58 , pp. 333-341
    • Tuffnell, J.M.1    Payne, J.W.2
  • 112
    • 0032793005 scopus 로고    scopus 로고
    • Antibiotic amendment for suppression of indigenous microflora in feed sources for an Escherichia coli auxotroph lysine assay
    • Erickson, A.M.; Zabala-Díaz, I.B.; Ricke, S.C. Antibiotic amendment for suppression of indigenous microflora in feed sources for an Escherichia coli auxotroph lysine assay. J. Appl. Microbiol. 1999, 87, 125-130.
    • (1999) J. Appl. Microbiol , vol.87 , pp. 125-130
    • Erickson, A.M.1    Zabala-Díaz, I.B.2    Ricke, S.C.3
  • 113
    • 0036378014 scopus 로고    scopus 로고
    • Methionine auxotroph Escherichia coli growth assay kinetics in antibiotic and antifungal amended selective media
    • Froelich, C.A.; Zabala-Díaz, I.B.; Ricke, S.C. Methionine auxotroph Escherichia coli growth assay kinetics in antibiotic and antifungal amended selective media. J. Environ. Sci. Health. 2002, B37, 485-492.
    • (2002) J. Environ. Sci. Health , vol.B37 , pp. 485-492
    • Froelich, C.A.1    Zabala-Díaz, I.B.2    Ricke, S.C.3
  • 114
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory Press: New York, NY, USA
    • Miller, J.H. In Experiments in Molecular Genetics; Cold Spring Harbor Laboratory Press: New York, NY, USA, 1972.
    • (1972) Experiments In Molecular Genetics
    • Miller, J.H.1
  • 115
    • 0000071066 scopus 로고    scopus 로고
    • Dissimilatory pathways for sugars, polyols, and carboxylates
    • Neidhardt, F.C., Curtiss III, R., Ingraham, J.L., Lin, E.C.C., Low, K.B., Magasanik, B., Reznikoff, W.S., Riley, M., Schaechter, M., Umbarger, H.E., Eds.; ASM Press: Washington, DC, USA
    • Lin, E.C.C. Dissimilatory pathways for sugars, polyols, and carboxylates. In Escherichia coli and Salmonella: Cellular and Molecular Biology; Neidhardt, F.C., Curtiss III, R., Ingraham, J.L., Lin, E.C.C., Low, K.B., Magasanik, B., Reznikoff, W.S., Riley, M., Schaechter, M., Umbarger, H.E., Eds.; ASM Press: Washington, DC, USA, 1996; Volume 1, p. 307.
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology , vol.1 , pp. 307
    • Lin, E.C.C.1
  • 116
    • 0024692881 scopus 로고
    • The complete nucleotide sequence of the lux regulon of Vibrio fischeri and the luxABN region of Photobacterium legiognathi and the mechanism of control of bacterial bioluminescence
    • Baldwin, T.O.; Devine, J.H.; Heckel, R.C.; Lin, J.W.; Shadel, G.S. The complete nucleotide sequence of the lux regulon of Vibrio fischeri and the luxABN region of Photobacterium legiognathi and the mechanism of control of bacterial bioluminescence. J. Biolumin. Chemilum. 1989, 4, 326-341.
    • (1989) J. Biolumin. Chemilum , vol.4 , pp. 326-341
    • Baldwin, T.O.1    Devine, J.H.2    Heckel, R.C.3    Lin, J.W.4    Shadel, G.S.5
  • 117
    • 0023968084 scopus 로고
    • Expression of the firefly luciferase gene in vaccinia virus: A highly sensitive gene marker to follow virus dissemination in tissues of infected animals
    • Rodriguez, J.F.; Rodriguez, D.; Rodriguez, J.R.; McGowan, E.B.; Esteban, M. Expression of the firefly luciferase gene in vaccinia virus: a highly sensitive gene marker to follow virus dissemination in tissues of infected animals. PNAS 1988, 85, 1667-1671.
    • (1988) PNAS , vol.85 , pp. 1667-1671
    • Rodriguez, J.F.1    Rodriguez, D.2    Rodriguez, J.R.3    McGowan, E.B.4    Esteban, M.5
  • 118
    • 84963796102 scopus 로고
    • Bacterial bioluminescence: Application in food microbiology
    • Baker, J.M.; Griffiths, M.W.; Collins-Thompson, D.L. Bacterial bioluminescence: application in food microbiology. J. Food Prot. 1992, 55, 62-70.
    • (1992) J. Food Prot , vol.55 , pp. 62-70
    • Baker, J.M.1    Griffiths, M.W.2    Collins-Thompson, D.L.3
  • 120
    • 0036672212 scopus 로고    scopus 로고
    • Construction and growth kinetics of a bioluminescent methionine auxotroph Escherichia coli strain for potential use in a methionine bioassay
    • Froelich, C.A.; Zabala-Díaz, I.B.; Ricke, S.C. Construction and growth kinetics of a bioluminescent methionine auxotroph Escherichia coli strain for potential use in a methionine bioassay. J. Rapid Methods Auto. Micro. 2002, 10, 69-82.
    • (2002) J. Rapid Methods Auto. Micro , vol.10 , pp. 69-82
    • Froelich, C.A.1    Zabala-Díaz, I.B.2    Ricke, S.C.3
  • 121
    • 0028247407 scopus 로고
    • Intensive techniques for measuring [Ca2+]i changes using a photomultiplier tube
    • Robinson, K.R.; Keating, T.J.; Cork, R.J. Intensive techniques for measuring [Ca2+]i changes using a photomultiplier tube. Meth. Cell Biol. 1994, 40, 287-303.
    • (1994) Meth. Cell Biol , vol.40 , pp. 287-303
    • Robinson, K.R.1    Keating, T.J.2    Cork, R.J.3
  • 122
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescent protein
    • Tsien, R.Y. The green fluorescent protein. Annu. Rev. Biochem. 1998, 67, 509-544.
    • (1998) Annu. Rev. Biochem , vol.67 , pp. 509-544
    • Tsien, R.Y.1
  • 123
    • 0029843338 scopus 로고    scopus 로고
    • Bacterial genetics by flow cytometry: Rapid isolation of Salmonella typhimurium acid-inducible promoters by differential fluorescence induction
    • Valdivia, R.H.; Falkow, S. Bacterial genetics by flow cytometry: rapid isolation of Salmonella typhimurium acid-inducible promoters by differential fluorescence induction. Mol. Microbiol. 1996, 22, 367-378.
    • (1996) Mol. Microbiol , vol.22 , pp. 367-378
    • Valdivia, R.H.1    Falkow, S.2
  • 125
    • 34548576414 scopus 로고
    • Extraction, purification and properties of aequorin, a bioluminescent protein from the Luminous Hydromedusan, Aequorea
    • Shimomura, O.; Johnson, F.H.; Saiga, Y. Extraction, purification and properties of aequorin, a bioluminescent protein from the Luminous Hydromedusan, Aequorea. J. Cell. Comp. Physiol. 1962, 59, 223-239.
    • (1962) J. Cell. Comp. Physiol , vol.59 , pp. 223-239
    • Shimomura, O.1    Johnson, F.H.2    Saiga, Y.3
  • 126
    • 0002123598 scopus 로고    scopus 로고
    • Emerging technologies: Bioreporters, biosensors, and microprobes
    • Hurst, C.J., Knudsen, G.R., McInerny, M.J., Stetzenbach, L.D., Walter, M.V., Eds.; ASM Press: Washington, DC
    • Burlage, R.S. Emerging technologies: bioreporters, biosensors, and microprobes. In Manual of Environmental Microbiology; Hurst, C.J., Knudsen, G.R., McInerny, M.J., Stetzenbach, L.D., Walter, M.V., Eds.; ASM Press: Washington, DC, 1997; p. 115.
    • (1997) Manual of Environmental Microbiology , pp. 115
    • Burlage, R.S.1
  • 128
    • 0035871239 scopus 로고    scopus 로고
    • Seeing the wood through the trees: A review of techniques for distinguishing green fluorescent protein from endogenous autofluorescence
    • Billinton, N.; Knight, A.W. Seeing the wood through the trees: a review of techniques for distinguishing green fluorescent protein from endogenous autofluorescence. Anal. Biochem. 2001, 291, 175-197.
    • (2001) Anal. Biochem , vol.291 , pp. 175-197
    • Billinton, N.1    Knight, A.W.2
  • 129
    • 0030087710 scopus 로고    scopus 로고
    • Engineering green fluorescent protein for improved brightness, longer wavelengths, and fluorescence resonance transfer
    • Heim, R.; Tsien, R.Y. Engineering green fluorescent protein for improved brightness, longer wavelengths, and fluorescence resonance transfer. Current Biol. 1996, 6, 178-182.
    • (1996) Current Biol , vol.6 , pp. 178-182
    • Heim, R.1    Tsien, R.Y.2
  • 130
    • 0029670330 scopus 로고    scopus 로고
    • Improved green fluorescent protein by molecular evolution using DNA shuffling
    • Crameri, A.; Whitehorn, E.A.; Tate, E.; Stemmer, W.P.C. Improved green fluorescent protein by molecular evolution using DNA shuffling. Nature Biotech. 1996, 14, 315-319.
    • (1996) Nature Biotech , vol.14 , pp. 315-319
    • Crameri, A.1    Whitehorn, E.A.2    Tate, E.3    Stemmer, W.P.C.4
  • 131
    • 0030784698 scopus 로고    scopus 로고
    • Use of the green fluorescent protein and its mutants in quantitative fluorescence microscopy
    • Patterson, G.H.; Knobel, S.M.; Sharif, W.D.; Kain, S.R.; Piston, D.W. Use of the green fluorescent protein and its mutants in quantitative fluorescence microscopy. Biophys. J. 1997, 73, 2782-2790.
    • (1997) Biophys. J , vol.73 , pp. 2782-2790
    • Patterson, G.H.1    Knobel, S.M.2    Sharif, W.D.3    Kain, S.R.4    Piston, D.W.5
  • 132
    • 33645235472 scopus 로고    scopus 로고
    • Application of an Escherichia coli green fluorescent protein-based biosensor under nonsterile conditions and autofluorescence background
    • Chalova, V.; Woodward, C.L.; Ricke, S.C. Application of an Escherichia coli green fluorescent protein-based biosensor under nonsterile conditions and autofluorescence background. Lett. Appl. Microbiol. 2006, 42, 265-270.
    • (2006) Lett. Appl. Microbiol , vol.42 , pp. 265-270
    • Chalova, V.1    Woodward, C.L.2    Ricke, S.C.3
  • 133
    • 0031746834 scopus 로고    scopus 로고
    • New unstable variants of green fluorescent protein for studies of transient gene expression in bacteria
    • Andersen, J.B.; Sternberg, C.; Poulsen, L.K.; Bjørn, S.P.; Givskov, M.; Molin, S. New unstable variants of green fluorescent protein for studies of transient gene expression in bacteria. Appl. Environ. Microbiol. 1998, 64, 2240-2246.
    • (1998) Appl. Environ. Microbiol , vol.64 , pp. 2240-2246
    • Andersen, J.B.1    Sternberg, C.2    Poulsen, L.K.3    Bjørn, S.P.4    Givskov, M.5    Molin, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.