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Volumn 255, Issue 3, 1998, Pages 628-637

Purification and characterization of recombinant Thermotoga maritima dihydrofolate reductase

Author keywords

Dihydrofolate reductase; Expression in Escherichia coli; Purification; Thermal stability; Thermotoga maritima

Indexed keywords

DIHYDROFOLATE REDUCTASE; RECOMBINANT PROTEIN;

EID: 0032145626     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2550628.x     Document Type: Article
Times cited : (29)

References (66)
  • 1
    • 0022522022 scopus 로고
    • Thermotoga maritima sp.nov. represents a new genus of unique extremely thermophilic eubacteria growing up to 90°C
    • Huber, R., Langworthy, T. A., König, H., Thomm, M., Woese, C. R., Sleytr, U. B. & Stetter, K. O. (1986) Thermotoga maritima sp.nov. represents a new genus of unique extremely thermophilic eubacteria growing up to 90°C, Arch. Microbiol. 144, 324-333.
    • (1986) Arch. Microbiol. , vol.144 , pp. 324-333
    • Huber, R.1    Langworthy, T.A.2    König, H.3    Thomm, M.4    Woese, C.R.5    Sleytr, U.B.6    Stetter, K.O.7
  • 2
    • 0002416323 scopus 로고
    • The Thermotogales
    • Kristjansson, J. K., ed. CRC Press, Inc., London
    • Huber, R. & Stetter, K. O. (1992) The Thermotogales, in Thermophilic bacteria (Kristjansson, J. K., ed.) pp. 185-194, CRC Press, Inc., London.
    • (1992) Thermophilic Bacteria , pp. 185-194
    • Huber, R.1    Stetter, K.O.2
  • 4
    • 0026648514 scopus 로고
    • Stability and reconstitution of D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic eubacterium Thermotoga maritima
    • Rehaber, V. & Jaenicke, R. (1992) Stability and reconstitution of D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic eubacterium Thermotoga maritima, J. Biol. Chem. 267, 10 999-11 006.
    • (1992) J. Biol. Chem. , vol.267 , pp. 10999-11006
    • Rehaber, V.1    Jaenicke, R.2
  • 5
    • 0028073909 scopus 로고
    • Cloning, sequencing, and expression of RecA proteins from three distantly related thermophilic eubacteria
    • Wetmur, J. G., Wong, D. M., Ortiz, B., Tong, J., Reichert, F. & Gelfand, D. H. (1994) Cloning, sequencing, and expression of RecA proteins from three distantly related thermophilic eubacteria, J. Biol. Chem. 269, 25 928-25 935.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25928-25935
    • Wetmur, J.G.1    Wong, D.M.2    Ortiz, B.3    Tong, J.4    Reichert, F.5    Gelfand, D.H.6
  • 6
    • 0029008857 scopus 로고
    • Two extremely thermostable xylanases of the hyperthermophilic bacterium Thermotoga maritima MSB8
    • Winterhalter, C. & Liebl, W. (1995) Two extremely thermostable xylanases of the hyperthermophilic bacterium Thermotoga maritima MSB8, Appl. Env. Microbiol. 61, 1810-1815.
    • (1995) Appl. Env. Microbiol. , vol.61 , pp. 1810-1815
    • Winterhalter, C.1    Liebl, W.2
  • 7
    • 0028031585 scopus 로고
    • Properties of a thermostable 4Fe-ferredoxin from the hyperthermophilic bacterium Thermotoga maritima
    • Blamey, J. M., Mukund, S. & Adams, M. W. (1994) Properties of a thermostable 4Fe-ferredoxin from the hyperthermophilic bacterium Thermotoga maritima, FEMS Microbiol. Lett. 121, 165-169.
    • (1994) FEMS Microbiol. Lett. , vol.121 , pp. 165-169
    • Blamey, J.M.1    Mukund, S.2    Adams, M.W.3
  • 8
    • 0028085225 scopus 로고
    • Characterization of an ancestral type of pyruvate ferredoxin oxidoreductase from the hyperthermophilic bacterium. Thermotoga maritima
    • Blamey, J. M. & Adams, M. W. (1994) Characterization of an ancestral type of pyruvate ferredoxin oxidoreductase from the hyperthermophilic bacterium. Thermotoga maritima, Biochemistry 33, 1000-1007.
    • (1994) Biochemistry , vol.33 , pp. 1000-1007
    • Blamey, J.M.1    Adams, M.W.2
  • 9
    • 0000899457 scopus 로고
    • Chemistry and biochemistry of folate
    • (Blakley, R. L. & Benkovic, S. L., eds) John Wiley & Sons, New York
    • Blakley, R. L. (1984) Chemistry and biochemistry of folate in Folates and pterins (Blakley, R. L. & Benkovic, S. L., eds) vol. 1, pp. 191-253, John Wiley & Sons, New York.
    • (1984) Folates and Pterins , vol.1 , pp. 191-253
    • Blakley, R.L.1
  • 10
    • 0029944197 scopus 로고    scopus 로고
    • In search of dihydrofolate reductase
    • Huennekens, F. M. (1996) In search of dihydrofolate reductase, Protein Sci. 5, 1201-1208.
    • (1996) Protein Sci. , vol.5 , pp. 1201-1208
    • Huennekens, F.M.1
  • 13
    • 0027737508 scopus 로고
    • Molecular aspects and mechanism of action of dihydrofolate reductase inhibitors
    • Hartman, P. G. (1993) Molecular aspects and mechanism of action of dihydrofolate reductase inhibitors, J. Chemotherapy 5, 369-376.
    • (1993) J. Chemotherapy , vol.5 , pp. 369-376
    • Hartman, P.G.1
  • 14
    • 0028315470 scopus 로고
    • The methotrexate story: A paradigm for development of cancer chemotherapeutic agents
    • Huennekens, F. M. (1994) The methotrexate story: a paradigm for development of cancer chemotherapeutic agents, Adv. Enzyme Regul. 34, 397-419.
    • (1994) Adv. Enzyme Regul. , vol.34 , pp. 397-419
    • Huennekens, F.M.1
  • 16
    • 0027457707 scopus 로고
    • Cloning, expression, and characterization of Cryptococcus neoformans dihydrofolate reductase
    • Sirawaraporn, W., Cao, M., Santi, D. V. & Edman, J. C. (1993) Cloning, expression, and characterization of Cryptococcus neoformans dihydrofolate reductase, J. Biol. Chem. 268, 8888-8892.
    • (1993) J. Biol. Chem. , vol.268 , pp. 8888-8892
    • Sirawaraporn, W.1    Cao, M.2    Santi, D.V.3    Edman, J.C.4
  • 17
    • 0027230113 scopus 로고
    • Dexamethasone negatively regulates the activity of a chimeric dihydrofolate reductase/glucocorticoid receptor protein
    • Israel, D. I. & Kaufman, R. J. (1993) Dexamethasone negatively regulates the activity of a chimeric dihydrofolate reductase/glucocorticoid receptor protein, Proc. Natl Acad. Sci. USA 90, 4290-4294.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 4290-4294
    • Israel, D.I.1    Kaufman, R.J.2
  • 18
    • 0027136119 scopus 로고
    • Stable molecular transformation of Toxoplasma gondii: A selectable dihydrofolate reductase-thymidylate synthase marker based on drug-resistance mutations in malaria
    • Donald, R. G. K. & Roos, D. S. (1993) Stable molecular transformation of Toxoplasma gondii: a selectable dihydrofolate reductase-thymidylate synthase marker based on drug-resistance mutations in malaria, Proc. Natl Acad. Sci. USA 90, 11703-11707.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 11703-11707
    • Donald, R.G.K.1    Roos, D.S.2
  • 19
    • 0031029554 scopus 로고    scopus 로고
    • Discrimination of a single base change in a ribozyme using the gene for dihydrofolate reductase as a selective marker in Escherichia coli
    • Fujita, S., Koguma, T., Ohkawa, J., Mori, K., Kohda, T., Kise, H., Nishikawa, S., Iwakura, M. & Taira, K. (1997) Discrimination of a single base change in a ribozyme using the gene for dihydrofolate reductase as a selective marker in Escherichia coli, Proc. Natl Acad. Sci. USA 94, 391-396.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 391-396
    • Fujita, S.1    Koguma, T.2    Ohkawa, J.3    Mori, K.4    Kohda, T.5    Kise, H.6    Nishikawa, S.7    Iwakura, M.8    Taira, K.9
  • 20
    • 0028851168 scopus 로고
    • Cloning and molecular analysis of the dihydrofolate reductase gene from Lactococcus lactis
    • Leszczynska, K., Bolhuis, A., Leenhouts, K., Venema, G. & Ceglowski, P. (1995) Cloning and molecular analysis of the dihydrofolate reductase gene from Lactococcus lactis, Appl. Env. Micobiol. 61, 561-566.
    • (1995) Appl. Env. Micobiol. , vol.61 , pp. 561-566
    • Leszczynska, K.1    Bolhuis, A.2    Leenhouts, K.3    Venema, G.4    Ceglowski, P.5
  • 21
    • 0027479899 scopus 로고
    • Primary structure of the dihydrofolate reductase-thymidylate synthase gene from Toxoplasma gondii
    • Roos, D. S. (1993) Primary structure of the dihydrofolate reductase-thymidylate synthase gene from Toxoplasma gondii, J. Biol. Chem. 268, 6269-6280.
    • (1993) J. Biol. Chem. , vol.268 , pp. 6269-6280
    • Roos, D.S.1
  • 22
    • 0024971668 scopus 로고
    • Dihydrofolate reductase of the extremely halophilic archaebacterium Halobacterium volcanii
    • Zusman, T., Rosenshine, I., Boehm, G., Jaenicke, R., Leskiw, B. & Mevarech, M. (1989) Dihydrofolate reductase of the extremely halophilic archaebacterium Halobacterium volcanii, J. Biol. Chem. 264, 18878-18883.
    • (1989) J. Biol. Chem. , vol.264 , pp. 18878-18883
    • Zusman, T.1    Rosenshine, I.2    Boehm, G.3    Jaenicke, R.4    Leskiw, B.5    Mevarech, M.6
  • 23
    • 0029053960 scopus 로고
    • The dihydrofolate reductase-encoding gene dyrA of the hyperthermophilic bacterium Thermotoga maritima
    • Van de Casteele, M., Legrain, C., Wilquet, V. & Glansdorff, N. (1995) The dihydrofolate reductase-encoding gene dyrA of the hyperthermophilic bacterium Thermotoga maritima, Gene (Amst.) 158, 101-105.
    • (1995) Gene (Amst.) , vol.158 , pp. 101-105
    • Van De Casteele, M.1    Legrain, C.2    Wilquet, V.3    Glansdorff, N.4
  • 24
    • 0029011953 scopus 로고
    • Characterization of the gene for the chromosomal dihydrofolate reductase (DHFR) of Staphylococcus epidermidis ATCC 14990: The origin of the trimethoprim-resistant S1 DHFR from Staphylococcus aureus?
    • Dale, G., Broger, C., Hartman, P. G., Langen, H., Page, M. G. P., Then, R. L. & Stüber, D. (1995) Characterization of the gene for the chromosomal dihydrofolate reductase (DHFR) of Staphylococcus epidermidis ATCC 14990: the origin of the trimethoprim-resistant S1 DHFR from Staphylococcus aureus? J. Bacteriol. 177, 2965-2970.
    • (1995) J. Bacteriol. , vol.177 , pp. 2965-2970
    • Dale, G.1    Broger, C.2    Hartman, P.G.3    Langen, H.4    Page, M.G.P.5    Then, R.L.6    Stüber, D.7
  • 25
    • 0023668190 scopus 로고
    • Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coli
    • Fierke, C. A., Johnson, K. A. & Benkovic, S. J. (1987) Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coli, Biochemistry 26, 4085-4092.
    • (1987) Biochemistry , vol.26 , pp. 4085-4092
    • Fierke, C.A.1    Johnson, K.A.2    Benkovic, S.J.3
  • 26
    • 0027202812 scopus 로고
    • Dihydrofolate reductase from the pathogenic fungus Pneumocystis carinii: Catalytic properties and interaction with antifolates
    • Margosiak, S. A., Appleman, J. R., Santi, D. V. & Blakley, R. L. (1993) Dihydrofolate reductase from the pathogenic fungus Pneumocystis carinii: catalytic properties and interaction with antifolates, Arch. Biochem. Biophys. 305, 499-509.
    • (1993) Arch. Biochem. Biophys. , vol.305 , pp. 499-509
    • Margosiak, S.A.1    Appleman, J.R.2    Santi, D.V.3    Blakley, R.L.4
  • 27
    • 0025336884 scopus 로고
    • The kinetic mechanism of wild-type and mutant mouse dihydrofolate reductases
    • Thillet, J., Adams, J. A. & Benkovic, S. J. (1990) The kinetic mechanism of wild-type and mutant mouse dihydrofolate reductases, Biochemistry 29, 5195-5202.
    • (1990) Biochemistry , vol.29 , pp. 5195-5202
    • Thillet, J.1    Adams, J.A.2    Benkovic, S.J.3
  • 28
    • 0025325955 scopus 로고
    • Unusual transient- and steady-state kinetic behaviour is predicted by the kinetic scheme operational for recombinant human dihydrofolate reductase
    • Appleman, J. R., Beard, W. A., Delcamp, T. J., Prendergast, N. J., Freisheim, J. H. & Blakley, R. L. (1990) Unusual transient- and steady-state kinetic behaviour is predicted by the kinetic scheme operational for recombinant human dihydrofolate reductase, J. Biol. Chem. 265, 2740-2748.
    • (1990) J. Biol. Chem. , vol.265 , pp. 2740-2748
    • Appleman, J.R.1    Beard, W.A.2    Delcamp, T.J.3    Prendergast, N.J.4    Freisheim, J.H.5    Blakley, R.L.6
  • 29
    • 0023665334 scopus 로고
    • Kinetic analysis of the mechanism of Escherichia coli dihydrofolate reductase
    • Penner, M. H. & Frieden, C. (1987) Kinetic analysis of the mechanism of Escherichia coli dihydrofolate reductase, J. Biol. Chem. 262, 15 908-15 914.
    • (1987) J. Biol. Chem. , vol.262 , pp. 15908-15914
    • Penner, M.H.1    Frieden, C.2
  • 30
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • Studier, F. W. & Moffatt, B. A. (1986) Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes, J. Mol. Biol. 189, 113-130.
    • (1986) J. Mol. Biol. , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 32
    • 0001572474 scopus 로고
    • Topography of cotransducible arginine mutations in Escherichia coli K-12
    • Glansdorff, N. (1965) Topography of cotransducible arginine mutations in Escherichia coli K-12, Genetics 51, 167-179.
    • (1965) Genetics , vol.51 , pp. 167-179
    • Glansdorff, N.1
  • 33
    • 0001030631 scopus 로고
    • Regulation of ribosomal RNA promoters with a synthetic lac operator
    • Brosius, J. & Holy, A. (1984) Regulation of ribosomal RNA promoters with a synthetic lac operator, Proc. Natl Acad. Sci. USA 81, 6929-6933.
    • (1984) Proc. Natl Acad. Sci. USA , vol.81 , pp. 6929-6933
    • Brosius, J.1    Holy, A.2
  • 37
    • 0002436379 scopus 로고
    • Particle size analysis: Number distributions by dynamic light scattering
    • Hallett, F. R., Craig, T., Marsh, J. & Nickel, B. (1988) Particle size analysis: number distributions by dynamic light scattering, Can. J. Spect. 34, 63-70.
    • (1988) Can. J. Spect. , vol.34 , pp. 63-70
    • Hallett, F.R.1    Craig, T.2    Marsh, J.3    Nickel, B.4
  • 38
    • 0027190754 scopus 로고
    • Evaluation of secondary structure of proteins from UV circular dichroism using an unsupervised learning neural network
    • Andrade, M. A., Chacòn, P., Merelo, J. J. & Morán, F. (1993) Evaluation of secondary structure of proteins from UV circular dichroism using an unsupervised learning neural network, Prot. Eng. 6, 383-390.
    • (1993) Prot. Eng. , vol.6 , pp. 383-390
    • Andrade, M.A.1    Chacòn, P.2    Merelo, J.J.3    Morán, F.4
  • 40
    • 0020442184 scopus 로고
    • Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 Å resolution
    • Filman, D. J., Bolin, J. T., Matthews, D. A. & Kraut, J. (1982) Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 Å resolution, J. Biol. Chem. 257, 13 663-13 672.
    • (1982) J. Biol. Chem. , vol.257 , pp. 13663-13672
    • Filman, D.J.1    Bolin, J.T.2    Matthews, D.A.3    Kraut, J.4
  • 41
    • 0023931977 scopus 로고
    • Crystal structure of human dihydrofolate reductase complexed with folate
    • Oefner, C., D'Arcy, A. & Winkler, F. K. (1988) Crystal structure of human dihydrofolate reductase complexed with folate, Eur. J. Biochem. 174, 377-385.
    • (1988) Eur. J. Biochem. , vol.174 , pp. 377-385
    • Oefner, C.1    D'Arcy, A.2    Winkler, F.K.3
  • 42
    • 0025037428 scopus 로고
    • Crystal structures of recombinant human dihydrofolate reductase complexed with folate and 5-deazafolate
    • Davies, J. R. II, Delcamp, T. J., Prendergast, N. J., Ashford, V. A., Freisheim, J. H. & Kraut, J. (1990) Crystal structures of recombinant human dihydrofolate reductase complexed with folate and 5-deazafolate, Biochemistry 29, 9467-9479.
    • (1990) Biochemistry , vol.29 , pp. 9467-9479
    • Davies II, J.R.1    Delcamp, T.J.2    Prendergast, N.J.3    Ashford, V.A.4    Freisheim, J.H.5    Kraut, J.6
  • 45
    • 0026005997 scopus 로고
    • Transient intermediates in the folding of dihydrofolate reductase as detected by far-ultraviolet circular dichroism spectroscopy
    • Kuwajima, K., Garvey, E. P., Finn, B. E., Matthews, C. R. & Sugai, S. (1991) Transient intermediates in the folding of dihydrofolate reductase as detected by far-ultraviolet circular dichroism spectroscopy, Biochemistry 30, 7693-7703.
    • (1991) Biochemistry , vol.30 , pp. 7693-7703
    • Kuwajima, K.1    Garvey, E.P.2    Finn, B.E.3    Matthews, C.R.4    Sugai, S.5
  • 46
    • 0017803126 scopus 로고
    • Effect of temperature on fluorescence and circular dichroism of Escherichia coli dihydrofolate reductase and its complexes
    • Kitchell, B. B. & Henkens, R. W. (1978) Effect of temperature on fluorescence and circular dichroism of Escherichia coli dihydrofolate reductase and its complexes, Biochim. Biophys. Acta 534, 89-98.
    • (1978) Biochim. Biophys. Acta , vol.534 , pp. 89-98
    • Kitchell, B.B.1    Henkens, R.W.2
  • 47
    • 0018436389 scopus 로고
    • Circular-dichroism studies of ligand binding to dihydrofolate reductase from Lactobacillus casei MTX/R
    • Hood, K., Bayley, P. M. & Roberts, C. K. (1979) Circular-dichroism studies of ligand binding to dihydrofolate reductase from Lactobacillus casei MTX/R, Biochem. J. 177, 425-432.
    • (1979) Biochem. J. , vol.177 , pp. 425-432
    • Hood, K.1    Bayley, P.M.2    Roberts, C.K.3
  • 48
    • 0017330326 scopus 로고
    • Characterization of chicken liver dihydrofolate reductase after purification by affinity chromatography and isoelectric focusing
    • Kaufman, B. T. & Kemerer, V. F. (1977) Characterization of chicken liver dihydrofolate reductase after purification by affinity chromatography and isoelectric focusing, Arch. Biochem. Biophys. 179, 420-431.
    • (1977) Arch. Biochem. Biophys. , vol.179 , pp. 420-431
    • Kaufman, B.T.1    Kemerer, V.F.2
  • 49
    • 0019891857 scopus 로고
    • Dihydrofolate reductase hysteresis and its effect on inhibitor binding analyses
    • Baccanari, D. P. & Joyner, S. S. (1981) Dihydrofolate reductase hysteresis and its effect on inhibitor binding analyses, Biochem. 20, 1710-1716.
    • (1981) Biochem. , vol.20 , pp. 1710-1716
    • Baccanari, D.P.1    Joyner, S.S.2
  • 50
    • 0021872251 scopus 로고
    • Substrate-induced hysteresis in the activity of Escherichia coli dihydrofolate reductase
    • Penner, M. H. & Frieden, C. (1985) Substrate-induced hysteresis in the activity of Escherichia coli dihydrofolate reductase, J. Biol. Chem. 260, 5366-5369.
    • (1985) J. Biol. Chem. , vol.260 , pp. 5366-5369
    • Penner, M.H.1    Frieden, C.2
  • 51
    • 0029886547 scopus 로고    scopus 로고
    • Heterologous expression and characterization of the bifunctional dihydrofolate reductase-thymidylate synthase enzyme of Toxoplasma gondii
    • Trujillo, M., Donald, R. G. K., Roos, D. S., Greene, P. J. & Santi, D. V. (1996) Heterologous expression and characterization of the bifunctional dihydrofolate reductase-thymidylate synthase enzyme of Toxoplasma gondii, Biochemistry 35, 6366-6374.
    • (1996) Biochemistry , vol.35 , pp. 6366-6374
    • Trujillo, M.1    Donald, R.G.K.2    Roos, D.S.3    Greene, P.J.4    Santi, D.V.5
  • 52
    • 0027546782 scopus 로고
    • Refolding of recombinant Pneumocystis carinii dihydrofolate reductase and characterization of the enzyme
    • Delves, C. J., Ballantine, S. P., Tansik, R. L., Baccanari, D. P. & Stammers, D. K. (1993) Refolding of recombinant Pneumocystis carinii dihydrofolate reductase and characterization of the enzyme, Protein Expr. Purif. 4, 16-23.
    • (1993) Protein Expr. Purif. , vol.4 , pp. 16-23
    • Delves, C.J.1    Ballantine, S.P.2    Tansik, R.L.3    Baccanari, D.P.4    Stammers, D.K.5
  • 55
    • 7344221897 scopus 로고
    • Purification and characterization of dihydrofolate reductase from methotrexate-resistant human lymphoblastoid cells
    • Delcamp, T. J., Susten, S. S., Blankenship, D. T. & Freisheim, J. H. (1983) Purification and characterization of dihydrofolate reductase from methotrexate-resistant human lymphoblastoid cells, Arch. Biochem. Biophys. 179, 420-431.
    • (1983) Arch. Biochem. Biophys. , vol.179 , pp. 420-431
    • Delcamp, T.J.1    Susten, S.S.2    Blankenship, D.T.3    Freisheim, J.H.4
  • 56
    • 0013820394 scopus 로고
    • Inhibition of folate biosynthesis and function as a basis for chemotherapy
    • Hitchings, G. H. & Burchall, J. J. (1965) Inhibition of folate biosynthesis and function as a basis for chemotherapy, Adv. Enzymol. 27, 417-468.
    • (1965) Adv. Enzymol. , vol.27 , pp. 417-468
    • Hitchings, G.H.1    Burchall, J.J.2
  • 58
    • 0017403997 scopus 로고
    • Escherichia coli dihydrofolate reductase: Isolation and characterization of two isozymes
    • Baccanari, D. P., Averett, D., Briggs, C. & Burchall, J. (1977) Escherichia coli dihydrofolate reductase: isolation and characterization of two isozymes, Biochemistry 16, 3566-3572.
    • (1977) Biochemistry , vol.16 , pp. 3566-3572
    • Baccanari, D.P.1    Averett, D.2    Briggs, C.3    Burchall, J.4
  • 59
    • 0029917031 scopus 로고    scopus 로고
    • Activation of chicken liver dihydrofolate reductase by urea and guanidine hydrochloride is accompanied by conformational change at the active site
    • Fan, Y. X., Ju, M., Zhou, J. M. & Tsou, C. L. (1996) Activation of chicken liver dihydrofolate reductase by urea and guanidine hydrochloride is accompanied by conformational change at the active site, Biochem. J. 315, 97-102.
    • (1996) Biochem. J. , vol.315 , pp. 97-102
    • Fan, Y.X.1    Ju, M.2    Zhou, J.M.3    Tsou, C.L.4
  • 61
    • 0029786277 scopus 로고    scopus 로고
    • Structure and stability of hyperstable proteins: Glycolytic enzymes from hyperthermophilic bacterium Thermotoga maritima
    • Jaenicke, R., Schurig, H., Beaucamp, N. & Ostendorp, R. (1996) Structure and stability of hyperstable proteins: glycolytic enzymes from hyperthermophilic bacterium Thermotoga maritima, Adv. Protein Chem. 48, 181-269.
    • (1996) Adv. Protein Chem. , vol.48 , pp. 181-269
    • Jaenicke, R.1    Schurig, H.2    Beaucamp, N.3    Ostendorp, R.4
  • 62
    • 0032539795 scopus 로고    scopus 로고
    • The crystal structure of Pyrococcus furiosus ornithine carbamoyltransferase reveals a key role for oligomerization in enzyme stability at extremely high temperatures
    • Villeret, V., Clantin, B., Tricot, C., Legrain, C., Roovers, M., Stalon, V., Glansdorff, N. & Van Beeumen, J. (1998) The crystal structure of Pyrococcus furiosus ornithine carbamoyltransferase reveals a key role for oligomerization in enzyme stability at extremely high temperatures, Proc. Natl Acad. Sci. USA 95, 2801-2806.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 2801-2806
    • Villeret, V.1    Clantin, B.2    Tricot, C.3    Legrain, C.4    Roovers, M.5    Stalon, V.6    Glansdorff, N.7    Van Beeumen, J.8
  • 63
    • 0027291015 scopus 로고
    • Prediction of protein secondary structure at better than 70% accuracy
    • Rost, B. & Sander, C. (1993) Prediction of protein secondary structure at better than 70% accuracy, J. Mol. Biol. 232, 584-599.
    • (1993) J. Mol. Biol. , vol.232 , pp. 584-599
    • Rost, B.1    Sander, C.2
  • 64
    • 0028300741 scopus 로고
    • Combining evolutionary information and neural networks to predict protein secondary structure
    • Rost, B. & Sander, C. (1994) Combining evolutionary information and neural networks to predict protein secondary structure, Prot. Struct. Funct. Genet. 19, 55-77.
    • (1994) Prot. Struct. Funct. Genet. , vol.19 , pp. 55-77
    • Rost, B.1    Sander, C.2
  • 65
    • 0014940726 scopus 로고
    • Kinetic aspects of regulation of metabolic processes
    • Frieden, C. (1970) Kinetic aspects of regulation of metabolic processes, J. Biol. Chem. 245, 5788-5799.
    • (1970) J. Biol. Chem. , vol.245 , pp. 5788-5799
    • Frieden, C.1
  • 66
    • 0026065644 scopus 로고
    • Crystal structure of unliganded Escherichia coli dihydrofolate reductase. Ligand-induced conformational changes and cooperativity in binding
    • Bystroff, C. & Kraut, J. (1991) Crystal structure of unliganded Escherichia coli dihydrofolate reductase. Ligand-induced conformational changes and cooperativity in binding, Biochemistry 30, 2227-2239.
    • (1991) Biochemistry , vol.30 , pp. 2227-2239
    • Bystroff, C.1    Kraut, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.