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Volumn 69, Issue 1, 1999, Pages 77-85

Light activates reduction of methotrexate by NADPH in the ternary complex with Escherichia coli dihydrofolate reductase

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ESCHERICHIA COLI;

EID: 0032603483     PISSN: 00318655     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1751-1097.1999.tb05309.x     Document Type: Article
Times cited : (5)

References (57)
  • 1
    • 0017380464 scopus 로고
    • High-dose methotrexate with citrovorum factor rescue: Predictive value of serum methotrexate concentrations and corrective measures to avert toxicity
    • Nirenberg, A., C. Mosende, B. M. Mehta, A. L. Gisolfi and G. Rosen (1977) High-dose methotrexate with citrovorum factor rescue: predictive value of serum methotrexate concentrations and corrective measures to avert toxicity. Cancer Treat. Rep. 61, 779-783.
    • (1977) Cancer Treat. Rep. , vol.61 , pp. 779-783
    • Nirenberg, A.1    Mosende, C.2    Mehta, B.M.3    Gisolfi, A.L.4    Rosen, G.5
  • 2
    • 0017713675 scopus 로고
    • Incidence of drug-related deaths secondary to high-dose methotrexate and citrovorum factor administration
    • Von Hoff, D. D., J. S. Penta, L. J. Helman and M. Slavik (1977) Incidence of drug-related deaths secondary to high-dose methotrexate and citrovorum factor administration. Cancer Treat. Rep. 61, 745-748.
    • (1977) Cancer Treat. Rep. , vol.61 , pp. 745-748
    • Von Hoff, D.D.1    Penta, J.S.2    Helman, L.J.3    Slavik, M.4
  • 3
    • 0023278781 scopus 로고
    • Effects on dihydrofolate reductase of methotrexate metabolites and intracellular folates formed following methotrexate exposure of human breast cancer cells
    • Drake, J. C., C. J. Allegra, J. Baram, B. T. Kaufman and B. A. Chabner (1987) Effects on dihydrofolate reductase of methotrexate metabolites and intracellular folates formed following methotrexate exposure of human breast cancer cells. Biochem. Pharmacol. 36, 2416-2418.
    • (1987) Biochem. Pharmacol. , vol.36 , pp. 2416-2418
    • Drake, J.C.1    Allegra, C.J.2    Baram, J.3    Kaufman, B.T.4    Chabner, B.A.5
  • 4
    • 0027160427 scopus 로고
    • Effect of chemotherapy on the energy and protein metabolism of children near the end of treatment for acute lymphoblastic leukemia
    • Vaisman, N., V. A. Stallings, H. Chan, S. S. Weitzman, R. Clarke and P. B. Pencharz (1993) Effect of chemotherapy on the energy and protein metabolism of children near the end of treatment for acute lymphoblastic leukemia. Am. J. Clin. Nutr. 57, 679-684.
    • (1993) Am. J. Clin. Nutr. , vol.57 , pp. 679-684
    • Vaisman, N.1    Stallings, V.A.2    Chan, H.3    Weitzman, S.S.4    Clarke, R.5    Pencharz, P.B.6
  • 7
    • 0026596946 scopus 로고
    • Methotrexate for juevenile rheumatoid arthritis
    • White, P. H. and B. M. Ansell (1992) Methotrexate for juevenile rheumatoid arthritis. N. Engl. J. Med. 326, 1077-1078.
    • (1992) N. Engl. J. Med. , vol.326 , pp. 1077-1078
    • White, P.H.1    Ansell, B.M.2
  • 9
    • 0016356713 scopus 로고
    • Dihydrofolate reductase from a methotrexate resisitant strain of Escherichia coli: Binding of several folates and pteridines as monitored by ultraviolet difference spectroscopy
    • Poe, M., N. J. Greenfield, J. M. Hirshfield and K. Hoogsteen (1974) Dihydrofolate reductase from a methotrexate resisitant strain of Escherichia coli: binding of several folates and pteridines as monitored by ultraviolet difference spectroscopy. Cancer Biochem. Biophys. 1, 7-11.
    • (1974) Cancer Biochem. Biophys. , vol.1 , pp. 7-11
    • Poe, M.1    Greenfield, N.J.2    Hirshfield, J.M.3    Hoogsteen, K.4
  • 10
    • 0017648237 scopus 로고
    • Dihydrofolate reductase from a resistant subline of the L1210 lymphoma. Purification by affinity chromatography and ultraviolet difference spectrophotometric and circular dichroic studies
    • Gupta, S. V., F. J. Greenfield, M. Poe, D. R. Makulu, M. N. Williams, B. A. Moroson and J. R. Bertino (1977) Dihydrofolate reductase from a resistant subline of the L1210 lymphoma. Purification by affinity chromatography and ultraviolet difference spectrophotometric and circular dichroic studies. Biochemistry 16, 3073-3079.
    • (1977) Biochemistry , vol.16 , pp. 3073-3079
    • Gupta, S.V.1    Greenfield, F.J.2    Poe, M.3    Makulu, D.R.4    Williams, M.N.5    Moroson, B.A.6    Bertino, J.R.7
  • 11
    • 0017807624 scopus 로고
    • Ultraviolet difference spectroscopic studies of substrate and inhibitor binding to Lactobacillus casei dihydrofolate reductase
    • Hood, K. and G. C. K. Roberts (1978) Ultraviolet difference spectroscopic studies of substrate and inhibitor binding to Lactobacillus casei dihydrofolate reductase. Biochem. J. 171, 357-366.
    • (1978) Biochem. J. , vol.171 , pp. 357-366
    • Hood, K.1    Roberts, G.C.K.2
  • 12
    • 0018102220 scopus 로고
    • Interaction of methotrexate, folates, and pyridine nucleotides with dihydrofolate reductase: Calorimetric and spectroscopic binding studies
    • Subramanian, S. and B. T. Kaufman (1978) Interaction of methotrexate, folates, and pyridine nucleotides with dihydrofolate reductase: calorimetric and spectroscopic binding studies. Proc. Natl. Acad. Sci. USA 75, 3201-3205.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 3201-3205
    • Subramanian, S.1    Kaufman, B.T.2
  • 13
    • 0019820721 scopus 로고
    • Protonation of methotrexate bound to the catalytic site of dihydrofolate reductase from Lactobacillus casei
    • Cocco, L., C. J. Temple, J. A. Montgomery, R. E. London and R. L. Blakley (1981) Protonation of methotrexate bound to the catalytic site of dihydrofolate reductase from Lactobacillus casei. Biochem. Biophys. Res. Commun. 100, 413-419.
    • (1981) Biochem. Biophys. Res. Commun. , vol.100 , pp. 413-419
    • Cocco, L.1    Temple, C.J.2    Montgomery, J.A.3    London, R.E.4    Blakley, R.L.5
  • 14
    • 0020619163 scopus 로고
    • The pH dependence of the binding of dihydrofolate and substate analogues to dihydrofolate reductase from Escherichia coli
    • Stone, S. R. and J. F. Morrison (1983) The pH dependence of the binding of dihydrofolate and substate analogues to dihydrofolate reductase from Escherichia coli. Biochim. Biophys. Acta 745, 247-258.
    • (1983) Biochim. Biophys. Acta , vol.745 , pp. 247-258
    • Stone, S.R.1    Morrison, J.F.2
  • 15
    • 0015495443 scopus 로고
    • Circular dichroism studies of dihydrofolate reductase from a methotrexate-resistant strain of escherichia coli
    • Greenfield, N. J., M. N. Williams, M. Poe and K. Hoogsteen (1972) Circular dichroism studies of dihydrofolate reductase from a methotrexate-resistant strain of Escherichia coli. Biochemistry 11, 4706-4711.
    • (1972) Biochemistry , vol.11 , pp. 4706-4711
    • Greenfield, N.J.1    Williams, M.N.2    Poe, M.3    Hoogsteen, K.4
  • 16
    • 0016703410 scopus 로고
    • Circular dichroism studies of dihydrofolate reductase from a methotrexate-resistant strain of Escherichia coli B, MB 1428: Ternary complexes
    • Greenfield, N. J. (1975) Circular dichroism studies of dihydrofolate reductase from a methotrexate-resistant strain of Escherichia coli B, MB 1428: ternary complexes. Biochim. Biophys. Acta 403, 32-46.
    • (1975) Biochim. Biophys. Acta , vol.403 , pp. 32-46
    • Greenfield, N.J.1
  • 17
    • 0026326486 scopus 로고
    • Analysis of hydride transfer and cofactor fluorescence decay in mutants of dihydrofolate reductase: Possible evidence for participation of enzyme molecular motions in catalysis
    • Farnum, M. F., D. Magde, E. E. Howell, J. T. Hirai and M. S. Warren (1991) Analysis of hydride transfer and cofactor fluorescence decay in mutants of dihydrofolate reductase: possible evidence for participation of enzyme molecular motions in catalysis. Biochemistry 30, 11567-11579.
    • (1991) Biochemistry , vol.30 , pp. 11567-11579
    • Farnum, M.F.1    Magde, D.2    Howell, E.E.3    Hirai, J.T.4    Warren, M.S.5
  • 18
    • 0017841237 scopus 로고
    • Binding of methotrexate to Escherichia coli dihydrofolate reductase as measured by visible and ultraviolet resonance Raman spectroscopy
    • Saperstein, D. D., A. J. Rein, M. Poe and M. F. Leahy (1978) Binding of methotrexate to Escherichia coli dihydrofolate reductase as measured by visible and ultraviolet resonance Raman spectroscopy. J. Am. Chem. Soc. 100, 4296-4300.
    • (1978) J. Am. Chem. Soc. , vol.100 , pp. 4296-4300
    • Saperstein, D.D.1    Rein, A.J.2    Poe, M.3    Leahy, M.F.4
  • 19
    • 0019506732 scopus 로고
    • Methotrexate and folate binding to dihydrofolate reductase. Separate characterization of the pteridine and p-aminobenzoyl binding sites by resonance Raman spectroscopy
    • Ozaki, Y., R. W. King and P. R. Carey (1981) Methotrexate and folate binding to dihydrofolate reductase. Separate characterization of the pteridine and p-aminobenzoyl binding sites by resonance Raman spectroscopy. Biochemistry 20, 3219-3225.
    • (1981) Biochemistry , vol.20 , pp. 3219-3225
    • Ozaki, Y.1    King, R.W.2    Carey, P.R.3
  • 20
    • 0027261328 scopus 로고
    • A study of the binding of NADP coenzymes to dihydrofolate reductase by Raman difference spectroscopy
    • Zheng, J., Y. Q. Chen and R. Callender (1993) A study of the binding of NADP coenzymes to dihydrofolate reductase by Raman difference spectroscopy. Eur. J. Biochem. 215, 9-16.
    • (1993) Eur. J. Biochem. , vol.215 , pp. 9-16
    • Zheng, J.1    Chen, Y.Q.2    Callender, R.3
  • 21
    • 0031030973 scopus 로고    scopus 로고
    • pH-dependent conformational changes in Escherichia coli dihydrofolate reductase revealed by Raman difference spectroscopy
    • Chen, Y. Q., J. Kraut and R. Callender (1997) pH-Dependent conformational changes in Escherichia coli dihydrofolate reductase revealed by Raman difference spectroscopy. Biophys. J. 72, 936-941.
    • (1997) Biophys. J. , vol.72 , pp. 936-941
    • Chen, Y.Q.1    Kraut, J.2    Callender, R.3
  • 22
    • 0019490836 scopus 로고
    • Carbon-13 nuclear magnetic resonance study of protonation of methotrexate and aminopterin bound to dihydrofolate reductase
    • Cocco, L., J. P. Groff, C. J. Temple, J. A. Montgomery, R. E. London, N. A. Matwiyoff and R. L. Blakley (1981) Carbon-13 nuclear magnetic resonance study of protonation of methotrexate and aminopterin bound to dihydrofolate reductase. Biochemistry 20, 3972-3978.
    • (1981) Biochemistry , vol.20 , pp. 3972-3978
    • Cocco, L.1    Groff, J.P.2    Temple, C.J.3    Montgomery, J.A.4    London, R.E.5    Matwiyoff, N.A.6    Blakley, R.L.7
  • 23
  • 25
    • 0025923765 scopus 로고
    • 15N NMR studies of the conformation of E. coli dihydrofolate reductase in complex with folate or methotrexate
    • 15N NMR studies of the conformation of E. coli dihydrofolate reductase in complex with folate or methotrexate. FEBS Lett. 289, 231-234.
    • (1991) FEBS Lett. , vol.289 , pp. 231-234
    • Huang, F.Y.1    Yang, Q.X.2    Huang, T.H.3
  • 26
    • 0026613993 scopus 로고
    • 13C NMR studies of complexes of Escherichia coli dihydrofolate reductase formed with methotrexate and with folic acid
    • 13C NMR studies of complexes of Escherichia coli dihydrofolate reductase formed with methotrexate and with folic acid. FEBS Lett. 312, 147-151.
    • (1992) FEBS Lett. , vol.312 , pp. 147-151
    • Cheung, H.T.1    Birdsall, B.2    Feeney, J.3
  • 27
    • 0027338123 scopus 로고
    • 13C NMR determination of the tautaomeric and ionizations states of folate in its complexes with Lactobacillus casei dihydrofolate reductase
    • 13C NMR determination of the tautaomeric and ionizations states of folate in its complexes with Lactobacillus casei dihydrofolate reductase. Biochemistry 32, 6846-6854.
    • (1993) Biochemistry , vol.32 , pp. 6846-6854
    • Cheung, H.T.1    Birdsall, B.2    Frenkiel, T.A.3    Chau, D.D.4    Feeney, J.5
  • 29
    • 0026652129 scopus 로고
    • Nuclear magnetic resonance detection of bound water molecules in the active site of Lactobacillus casei dihydrofolate reductase in aqueous solution
    • Gerothanassis, I. P., B. Birdsall, C. J. Bauer, T. A. Frenkiel and J. Feeney (1992) Nuclear magnetic resonance detection of bound water molecules in the active site of Lactobacillus casei dihydrofolate reductase in aqueous solution. J. Mol. Biol. 226, 549-554.
    • (1992) J. Mol. Biol. , vol.226 , pp. 549-554
    • Gerothanassis, I.P.1    Birdsall, B.2    Bauer, C.J.3    Frenkiel, T.A.4    Feeney, J.5
  • 30
    • 0028172371 scopus 로고
    • 3H-NMR studies of multiple conformations and dynamic processes in complexes of folate and methotrexate with Lactobacillus casei dihydrofolate reductase
    • 3H-NMR studies of multiple conformations and dynamic processes in complexes of folate and methotrexate with Lactobacillus casei dihydrofolate reductase. Biochem. J. 303, 401-405.
    • (1994) Biochem. J. , vol.303 , pp. 401-405
    • Curtis, N.1    Moore, S.2    Birdsall, B.3    Bloxsidge, J.4    Gibson, C.L.5    Jones, J.R.6    Feeney, J.7
  • 34
    • 0020441466 scopus 로고
    • Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 A resolution
    • Bolin, J. T., D. J. Filman, D. A. Matthews, R. C. Hamlin and J. Kraut (1982) Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 A resolution. J. Biol. Chem. 257, 13650-13662.
    • (1982) J. Biol. Chem. , vol.257 , pp. 13650-13662
    • Bolin, J.T.1    Filman, D.J.2    Matthews, D.A.3    Hamlin, R.C.4    Kraut, J.5
  • 35
    • 0027080589 scopus 로고
    • Crystal structure determination at 2.3 A of recombinant human dihydrofolate reductase ternary complex with NADPH and bethotrexate-gamma-tetrazole
    • Cody, V., J. R. Luft, E. Ciszak, T. I. Kalman and J. H. Freisheim (1992) Crystal structure determination at 2.3 A of recombinant human dihydrofolate reductase ternary complex with NADPH and bethotrexate-gamma-tetrazole. Anticancer Drug Des. 7, 483-491.
    • (1992) Anticancer Drug Des. , vol.7 , pp. 483-491
    • Cody, V.1    Luft, J.R.2    Ciszak, E.3    Kalman, T.I.4    Freisheim, J.H.5
  • 36
    • 0031015737 scopus 로고    scopus 로고
    • Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: Crystallographic evidence
    • Sawaya, M. R. and J. Kraut (1997) Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence. Biochemistry 36, 586-603.
    • (1997) Biochemistry , vol.36 , pp. 586-603
    • Sawaya, M.R.1    Kraut, J.2
  • 37
    • 0025270551 scopus 로고
    • + ternary complex. Substrate binding and a model for the transition state
    • + ternary complex. Substrate binding and a model for the transition state. Biochemistry 29, 3263-3277.
    • (1990) Biochemistry , vol.29 , pp. 3263-3277
    • Bystroff, C.1    Oatley, S.J.2    Kraut, J.3
  • 38
    • 0008067386 scopus 로고
    • 13C-enriched methotrexate for NMR studies of drug-enzyme interactions
    • 13C-enriched methotrexate for NMR studies of drug-enzyme interactions. Heterocycles 25, 507-514.
    • (1987) Heterocycles , vol.25 , pp. 507-514
    • Cheung, H.T.A.1    Smal, M.2    Chau, D.D.3
  • 39
    • 0023668190 scopus 로고
    • Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coli
    • J. K. A.
    • Fierke, C. A., J. K. A. and S. J. Benkovic (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    Benkovic, S.J.2
  • 40
    • 0001174968 scopus 로고
    • Analogs of pteroylglutamic acid. III. 4-amino derivatives
    • Seeger, D. R., D. B. Cosulich and M. E. Hultquist (1949) Analogs of pteroylglutamic acid. III. 4-amino derivatives. J. Am. Chem. Soc. 71, 1753.
    • (1949) J. Am. Chem. Soc. , vol.71 , pp. 1753
    • Seeger, D.R.1    Cosulich, D.B.2    Hultquist, M.E.3
  • 41
    • 0028290484 scopus 로고
    • Nonresonance raman difference spectroscopy: A general probe of protein structure, ligand binding, enymatic catalysis, and the structures of other biomacromolecules
    • Callender, R. and H. Deng (1994) Nonresonance raman difference spectroscopy: a general probe of protein structure, ligand binding, enymatic catalysis, and the structures of other biomacromolecules. Annu. Rev. Biophys. Biomol. Struct. 23, 215-245.
    • (1994) Annu. Rev. Biophys. Biomol. Struct. , vol.23 , pp. 215-245
    • Callender, R.1    Deng, H.2
  • 43
    • 84986840440 scopus 로고
    • Fluorescence-free resonance Raman spectra of reduced nicotinamide adenine dinucleotide via ultraviolet excitation
    • Bowman, W. D. and T. G. Spiro (1980) Fluorescence-free resonance Raman spectra of reduced nicotinamide adenine dinucleotide via ultraviolet excitation. J. Raman Spectrosc. 9, 369-371.
    • (1980) J. Raman Spectrosc. , vol.9 , pp. 369-371
    • Bowman, W.D.1    Spiro, T.G.2
  • 44
    • 0022551940 scopus 로고
    • Raman spectroscopy of oxidized and reduced nicotinamide adenine dinucleotides
    • Yue, K. T., C. L. Martin, D. Chen, P. Nelson, D. L. Sloan and R. Callender (1986) Raman spectroscopy of oxidized and reduced nicotinamide adenine dinucleotides. Biochemistry 25, 4941-4947.
    • (1986) Biochemistry , vol.25 , pp. 4941-4947
    • Yue, K.T.1    Martin, C.L.2    Chen, D.3    Nelson, P.4    Sloan, D.L.5    Callender, R.6
  • 45
    • 0001502874 scopus 로고
    • Raman spectroscopic studies of the effects of substrate binding on coenzymes bound to lactate dehydrogenase
    • Deng, H., J. Burgner and R. Callender (1992) Raman spectroscopic studies of the effects of substrate binding on coenzymes bound to lactate dehydrogenase. J. Am. Chem. Soc. 114, 7997-8003.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 7997-8003
    • Deng, H.1    Burgner, J.2    Callender, R.3
  • 46
    • 0028305058 scopus 로고
    • Determination by raman spectroscopy of the pKa of N5 of dihydrofolate bound to dihydrofolate reductase: Mechanistic implications
    • Chen, Y. Q., J. Kraut, R. L. Blakley and R. Callender (1994) Determination by Raman spectroscopy of the pKa of N5 of dihydrofolate bound to dihydrofolate reductase: mechanistic implications. Biochemistry 33, 7021-7026.
    • (1994) Biochemistry , vol.33 , pp. 7021-7026
    • Chen, Y.Q.1    Kraut, J.2    Blakley, R.L.3    Callender, R.4
  • 47
    • 0022408542 scopus 로고
    • Theoretical studies on the activation of the pterin cofactor in the catalytic mechanism of dihydrofolate reductase
    • Gready, J. E. (1985) Theoretical studies on the activation of the pterin cofactor in the catalytic mechanism of dihydrofolate reductase. Biochemistry 24, 4761-4766.
    • (1985) Biochemistry , vol.24 , pp. 4761-4766
    • Gready, J.E.1
  • 48
    • 0018759051 scopus 로고
    • Methotrexate, a high-affinity pseudosubstrate of dihydrofolate reductase
    • Williams, J. W., J. F. Morrison and R. G. Duggleby (1979) Methotrexate, a high-affinity pseudosubstrate of dihydrofolate reductase. Biochemistry 18, 2567-2573.
    • (1979) Biochemistry , vol.18 , pp. 2567-2573
    • Williams, J.W.1    Morrison, J.F.2    Duggleby, R.G.3
  • 49
    • 0021345608 scopus 로고
    • Inhibition of dihydrofolate reductase from bacterial and vertebrate sources by folate, aminopterin, methotrexate and their 5-deaza analogs
    • Stone, S. R., J. A. Montgomery and J. F. Morrison (1984) Inhibition of dihydrofolate reductase from bacterial and vertebrate sources by folate, aminopterin, methotrexate and their 5-deaza analogs. Biochem. Pharmacol. 33, 175-179.
    • (1984) Biochem. Pharmacol. , vol.33 , pp. 175-179
    • Stone, S.R.1    Montgomery, J.A.2    Morrison, J.F.3
  • 50
    • 0023891809 scopus 로고
    • Role of aspartate 27 in the binding of methotrexate to dihydrofolate reductase from Escherichia coli
    • Appleman, J. R., E. E. Howell, J. Kraut, M. Kuhl and R. L. Blakley (1988) Role of aspartate 27 in the binding of methotrexate to dihydrofolate reductase from Escherichia coli. J. Biol. Chem. 263, 9187-9198.
    • (1988) J. Biol. Chem. , vol.263 , pp. 9187-9198
    • Appleman, J.R.1    Howell, E.E.2    Kraut, J.3    Kuhl, M.4    Blakley, R.L.5
  • 51
    • 0023730578 scopus 로고
    • Kinetics of the formation and isomerization of methotrexate complexes of recombinant human dihydrofolate reductase
    • Appleman, J. R., N. Prendergast, T. J. Delcamp, J. H. Freisheim and R. L. Blakley (1988) Kinetics of the formation and isomerization of methotrexate complexes of recombinant human dihydrofolate reductase. J. Biol. Chem. 263, 10304-10313.
    • (1988) J. Biol. Chem. , vol.263 , pp. 10304-10313
    • Appleman, J.R.1    Prendergast, N.2    Delcamp, T.J.3    Freisheim, J.H.4    Blakley, R.L.5
  • 52
    • 3242770330 scopus 로고
    • Hypochromism in polynucleotides
    • Tinoco, I., Jr. (1960) Hypochromism in polynucleotides. J. Am. Chem. Soc. 84, 4785-4790.
    • (1960) J. Am. Chem. Soc. , vol.84 , pp. 4785-4790
    • Tinoco I., Jr.1
  • 53
    • 0014946591 scopus 로고
    • Conformational dependence of Raman scattering intensities in polyadenylic acid
    • Tomlinson, B. L. and W. L. Peticolas (1970) Conformational dependence of Raman scattering intensities in polyadenylic acid. J. Chem. Phys. 52, 2154-2156.
    • (1970) J. Chem. Phys. , vol.52 , pp. 2154-2156
    • Tomlinson, B.L.1    Peticolas, W.L.2
  • 54
    • 0014995585 scopus 로고
    • Conformational dependence of the Raman scattering intensities from polynucleotides. III. Order-disorder changes in helical structures
    • Small, E. W. and W. L. Peticolas (1971) Conformational dependence of the Raman scattering intensities from polynucleotides. III. Order-disorder changes in helical structures. Biopolymers 10, 1377-1416.
    • (1971) Biopolymers , vol.10 , pp. 1377-1416
    • Small, E.W.1    Peticolas, W.L.2
  • 55
    • 0022546047 scopus 로고
    • Functional role of aspartic acid-27 in dihydrofolate reductase revealed by mutagenesis
    • Howell, E. E., J. E. Villafranca, M. S. Warren, S. J. Oatley and J. Kraut (1986) Functional role of aspartic acid-27 in dihydrofolate reductase revealed by mutagenesis. Science 231, 1123-1128.
    • (1986) Science , vol.231 , pp. 1123-1128
    • Howell, E.E.1    Villafranca, J.E.2    Warren, M.S.3    Oatley, S.J.4    Kraut, J.5
  • 56
    • 0021266280 scopus 로고
    • Enzymatic synthesis of polyglutamate derivatives of 7-hydroxymethotrexate
    • McGuire, J. J., P. Hsieh and J. R. Bertino (1984) Enzymatic synthesis of polyglutamate derivatives of 7-hydroxymethotrexate. Biochem. Pharmacol. 33, 1355-1361.
    • (1984) Biochem. Pharmacol. , vol.33 , pp. 1355-1361
    • McGuire, J.J.1    Hsieh, P.2    Bertino, J.R.3
  • 57
    • 0021356277 scopus 로고
    • Synthesis and properties of 7-hydroxymethotrexate polyglutamyl derivatives in Ehrlich ascites tumor cells in vitro
    • Fabre, G., I. Fabre, L. H. Matherly, J. P. Cano and I. D. Goldman (1984) Synthesis and properties of 7-hydroxymethotrexate polyglutamyl derivatives in Ehrlich ascites tumor cells in vitro. J. Biol. Chem. 259, 5066-5072.
    • (1984) J. Biol. Chem. , vol.259 , pp. 5066-5072
    • Fabre, G.1    Fabre, I.2    Matherly, L.H.3    Cano, J.P.4    Goldman, I.D.5


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