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Volumn 13, Issue 12, 2006, Pages 1339-1347

An Inhibitor of Human Asparagine Synthetase Suppresses Proliferation of an L-Asparaginase-Resistant Leukemia Cell Line

Author keywords

CELLCYCLE; CHEMBIOL

Indexed keywords

ANTINEOPLASTIC AGENT; ASPARAGINASE; ASPARTATE AMMONIA LIGASE; ENZYME INHIBITOR; SULFUR AMINO ACID;

EID: 33845591794     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2006.10.010     Document Type: Article
Times cited : (42)

References (70)
  • 1
    • 0035873421 scopus 로고    scopus 로고
    • Structural basis for the activity and substrate specificity of Erwinia chrysanthemi L-asparaginase
    • Aghaiypour K., Wlodawer A., and Lubkowski J. Structural basis for the activity and substrate specificity of Erwinia chrysanthemi L-asparaginase. Biochemistry 40 (2001) 5655-5664
    • (2001) Biochemistry , vol.40 , pp. 5655-5664
    • Aghaiypour, K.1    Wlodawer, A.2    Lubkowski, J.3
  • 3
    • 0018704340 scopus 로고
    • Effective dose of L-asparaginase for induction of remission in previously untreated children with acute lymphocytic leukemia: a report from the childrens cancer study group
    • Ertel I.J., Nesbit M.G., Hammon D., Weiner J., and Sather H. Effective dose of L-asparaginase for induction of remission in previously untreated children with acute lymphocytic leukemia: a report from the childrens cancer study group. Cancer Res. 39 (1979) 3893-3896
    • (1979) Cancer Res. , vol.39 , pp. 3893-3896
    • Ertel, I.J.1    Nesbit, M.G.2    Hammon, D.3    Weiner, J.4    Sather, H.5
  • 7
    • 0035397709 scopus 로고    scopus 로고
    • Asparagine synthetase expression alone is sufficient to induce L-asparaginase resistance in MOLT-4 human leukemia cells
    • Aslanian A.M., and Kilberg M.S. Asparagine synthetase expression alone is sufficient to induce L-asparaginase resistance in MOLT-4 human leukemia cells. Biochem. J. 357 (2001) 321-328
    • (2001) Biochem. J. , vol.357 , pp. 321-328
    • Aslanian, A.M.1    Kilberg, M.S.2
  • 8
    • 0024520077 scopus 로고
    • Biochemical characterization of U937 cells resistant to L-asparaginase: the role of asparagine synthetase
    • Kiriyama Y., Kubota M., Takimoto T., Kitoh J., Tanizawa A., Akiyama Y., and Mikawa H. Biochemical characterization of U937 cells resistant to L-asparaginase: the role of asparagine synthetase. Leukemia 3 (1989) 294-297
    • (1989) Leukemia , vol.3 , pp. 294-297
    • Kiriyama, Y.1    Kubota, M.2    Takimoto, T.3    Kitoh, J.4    Tanizawa, A.5    Akiyama, Y.6    Mikawa, H.7
  • 9
    • 0031408593 scopus 로고    scopus 로고
    • L-asparaginase: perspectives on the mechanisms of action and resistance
    • Chakrabarti R., and Schuster S.M. L-asparaginase: perspectives on the mechanisms of action and resistance. J. Pediatr. Hematol. Oncol. 4 (1997) 597-611
    • (1997) J. Pediatr. Hematol. Oncol. , vol.4 , pp. 597-611
    • Chakrabarti, R.1    Schuster, S.M.2
  • 10
    • 0014588094 scopus 로고
    • L-asparaginase resistance in human leukemia-asparagine synthetase
    • Haskell C.M., and Canellos G.P. L-asparaginase resistance in human leukemia-asparagine synthetase. Biochem. Pharmacol. 18 (1969) 2578-2580
    • (1969) Biochem. Pharmacol. , vol.18 , pp. 2578-2580
    • Haskell, C.M.1    Canellos, G.P.2
  • 11
    • 0042999388 scopus 로고    scopus 로고
    • Pegaspargase: a review of clinical studies
    • Graham M.L. Pegaspargase: a review of clinical studies. Adv. Drug Deliv. Rev. 55 (2003) 1293-1302
    • (2003) Adv. Drug Deliv. Rev. , vol.55 , pp. 1293-1302
    • Graham, M.L.1
  • 13
    • 33744497255 scopus 로고    scopus 로고
    • Up-regulation of asparagine synthetase expression is not linked to the clinical response to L-asparaginase in pediatric acute lymphoblastic leukemia
    • Appel I.M., den Boer M.L., Meijerink J.P.P., Veerman A.J.P., Reniers N.C.M., and Pieters R. Up-regulation of asparagine synthetase expression is not linked to the clinical response to L-asparaginase in pediatric acute lymphoblastic leukemia. Blood 106 (2006) 4244-4249
    • (2006) Blood , vol.106 , pp. 4244-4249
    • Appel, I.M.1    den Boer, M.L.2    Meijerink, J.P.P.3    Veerman, A.J.P.4    Reniers, N.C.M.5    Pieters, R.6
  • 14
    • 11244314360 scopus 로고    scopus 로고
    • A genome-wide view of the in vitro response to L-asparaginase in acute lymphoblastic leukemia
    • Fine B.M., Kaspers G.J., Ho M., Loonen A.H., and Boxer L.M. A genome-wide view of the in vitro response to L-asparaginase in acute lymphoblastic leukemia. Cancer Res. 65 (2005) 291-299
    • (2005) Cancer Res. , vol.65 , pp. 291-299
    • Fine, B.M.1    Kaspers, G.J.2    Ho, M.3    Loonen, A.H.4    Boxer, L.M.5
  • 15
    • 19344377657 scopus 로고    scopus 로고
    • Asparagine synthetase expression is linked with L-asparaginase resistance in TEL-AML1-negative but not TEL-AML1-positive pediatric acute lymphoblastic leukemia
    • Stams W.A.G., den Boer M.L., Holleman A., Appel I.M., Beverloo H.B., van Wering E.R., Janka-Schaub G.E., Evans W.E., and Pieters R. Asparagine synthetase expression is linked with L-asparaginase resistance in TEL-AML1-negative but not TEL-AML1-positive pediatric acute lymphoblastic leukemia. Blood 105 (2005) 4223-4225
    • (2005) Blood , vol.105 , pp. 4223-4225
    • Stams, W.A.G.1    den Boer, M.L.2    Holleman, A.3    Appel, I.M.4    Beverloo, H.B.5    van Wering, E.R.6    Janka-Schaub, G.E.7    Evans, W.E.8    Pieters, R.9
  • 16
    • 0018690292 scopus 로고
    • Analogs of L-aspartic acid in chemotherapy for cancer
    • Jayaram H.N., and Cooney D.A. Analogs of L-aspartic acid in chemotherapy for cancer. Cancer Treat. Rep. 63 (1979) 1095-1108
    • (1979) Cancer Treat. Rep. , vol.63 , pp. 1095-1108
    • Jayaram, H.N.1    Cooney, D.A.2
  • 18
    • 0033534161 scopus 로고    scopus 로고
    • Three-dimensional structure of Escherichia coli asparagine synthetase B: a short journey from substrate to product
    • Larsen T.M., Boehlein S.K., Schuster S.M., Richards N.G.J., Thoden J.B., Holden H.M., and Rayment I. Three-dimensional structure of Escherichia coli asparagine synthetase B: a short journey from substrate to product. Biochemistry 38 (1999) 16146-16157
    • (1999) Biochemistry , vol.38 , pp. 16146-16157
    • Larsen, T.M.1    Boehlein, S.K.2    Schuster, S.M.3    Richards, N.G.J.4    Thoden, J.B.5    Holden, H.M.6    Rayment, I.7
  • 20
    • 0022033084 scopus 로고
    • Purification and characterization of beef pancreatic asparagine synthetase
    • Luehr C.A., and Schuster S.M. Purification and characterization of beef pancreatic asparagine synthetase. Arch. Biochem. Biophys. 237 (1985) 335-346
    • (1985) Arch. Biochem. Biophys. , vol.237 , pp. 335-346
    • Luehr, C.A.1    Schuster, S.M.2
  • 21
    • 0034919604 scopus 로고    scopus 로고
    • Channeling of substrates and intermediates in enzyme-catalyzed reactions
    • Huang X., Holden H.M., and Raushel F. Channeling of substrates and intermediates in enzyme-catalyzed reactions. Annu. Rev. Biochem. 70 (2001) 149-180
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 149-180
    • Huang, X.1    Holden, H.M.2    Raushel, F.3
  • 22
    • 0037404142 scopus 로고    scopus 로고
    • Revisiting the steady-state kinetic mechanism of glutamine-dependent asparagine synthetase from Escherichia coli
    • Tesson A.R., Soper T.S., Ciustea M., and Richards N.G.J. Revisiting the steady-state kinetic mechanism of glutamine-dependent asparagine synthetase from Escherichia coli. Arch. Biochem. Biophys. 413 (2003) 23-31
    • (2003) Arch. Biochem. Biophys. , vol.413 , pp. 23-31
    • Tesson, A.R.1    Soper, T.S.2    Ciustea, M.3    Richards, N.G.J.4
  • 23
    • 0141742572 scopus 로고    scopus 로고
    • Synthesis and characterization of an N-acylsulfonamide inhibitor of human asparagine synthetase
    • Koroniak L., Ciustea M., Gutierrez J.A., and Richards N.G.J. Synthesis and characterization of an N-acylsulfonamide inhibitor of human asparagine synthetase. Org. Lett. 5 (2003) 2033-2036
    • (2003) Org. Lett. , vol.5 , pp. 2033-2036
    • Koroniak, L.1    Ciustea, M.2    Gutierrez, J.A.3    Richards, N.G.J.4
  • 24
    • 0033597605 scopus 로고    scopus 로고
    • A potent transition-state analogue inhibitor of Escherichia coli asparagine synthetase A
    • Koizumi M., Hiratake J., Nakatsu T., Kato H., and Oda J. A potent transition-state analogue inhibitor of Escherichia coli asparagine synthetase A. J. Am. Chem. Soc. 121 (1999) 5799-5800
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 5799-5800
    • Koizumi, M.1    Hiratake, J.2    Nakatsu, T.3    Kato, H.4    Oda, J.5
  • 25
    • 0015912061 scopus 로고
    • Terminal deoxynucleotidyl transferase-activity in a cell line (MOLT-4) derived from peripheral blood of a patient with acute lymphoblastic leukemia
    • Srivasta B.I., and Minowada J. Terminal deoxynucleotidyl transferase-activity in a cell line (MOLT-4) derived from peripheral blood of a patient with acute lymphoblastic leukemia. Biochem. Biophys. Res. Commun. 51 (1973) 529-535
    • (1973) Biochem. Biophys. Res. Commun. , vol.51 , pp. 529-535
    • Srivasta, B.I.1    Minowada, J.2
  • 26
    • 0014670438 scopus 로고
    • The asparagine synthetase of Escherichia coli I: biosynthetic role of the enzyme, purification and characterization of the reaction products
    • Cedar H., and Schwartz J.H. The asparagine synthetase of Escherichia coli I: biosynthetic role of the enzyme, purification and characterization of the reaction products. J. Biol. Chem. 244 (1969) 4112-4121
    • (1969) J. Biol. Chem. , vol.244 , pp. 4112-4121
    • Cedar, H.1    Schwartz, J.H.2
  • 27
    • 0031984643 scopus 로고    scopus 로고
    • Crystal structure of asparagine synthetase reveals a close evolutionary relationship to class II aminoacyl tRNA synthetase
    • Nakatsu T., Kato H., and Oda J. Crystal structure of asparagine synthetase reveals a close evolutionary relationship to class II aminoacyl tRNA synthetase. Nat. Struct. Biol. 5 (1998) 15-19
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 15-19
    • Nakatsu, T.1    Kato, H.2    Oda, J.3
  • 29
    • 84988129057 scopus 로고
    • Optimization of parameters for semiempirical methods I: method
    • Stewart J.J.P. Optimization of parameters for semiempirical methods I: method. J. Comput. Chem. 10 (1989) 209-220
    • (1989) J. Comput. Chem. , vol.10 , pp. 209-220
    • Stewart, J.J.P.1
  • 30
    • 33751157086 scopus 로고
    • Conductor-like screening model for real solvents: a new approach to the quantitative calculation of solvation phenomena
    • Klamt A. Conductor-like screening model for real solvents: a new approach to the quantitative calculation of solvation phenomena. J. Phys. Chem. 99 (1995) 2224-2235
    • (1995) J. Phys. Chem. , vol.99 , pp. 2224-2235
    • Klamt, A.1
  • 31
    • 84961981091 scopus 로고    scopus 로고
    • Implicit solvation models: equilibria, structure, spectra, and dynamics
    • Cramer C.J., and Truhlar D.G. Implicit solvation models: equilibria, structure, spectra, and dynamics. Chem. Rev. 99 (1999) 2161-2200
    • (1999) Chem. Rev. , vol.99 , pp. 2161-2200
    • Cramer, C.J.1    Truhlar, D.G.2
  • 32
    • 22744438689 scopus 로고    scopus 로고
    • Efficient expression, purification and characterization of C-terminally tagged, recombinant human asparagine synthetase
    • Ciustea M., Gutierrez J.A., Abbatiello S.E., Eyler J.R., and Richards N.G.J. Efficient expression, purification and characterization of C-terminally tagged, recombinant human asparagine synthetase. Arch. Biochem. Biophys. 440 (2005) 18-27
    • (2005) Arch. Biochem. Biophys. , vol.440 , pp. 18-27
    • Ciustea, M.1    Gutierrez, J.A.2    Abbatiello, S.E.3    Eyler, J.R.4    Richards, N.G.J.5
  • 33
    • 0017171832 scopus 로고
    • A continuous spectrophotometric assay for argininosuccinate synthetase based on pyrophosphate formation
    • O'Brien W.E. A continuous spectrophotometric assay for argininosuccinate synthetase based on pyrophosphate formation. Anal. Biochem. 76 (1976) 423-430
    • (1976) Anal. Biochem. , vol.76 , pp. 423-430
    • O'Brien, W.E.1
  • 34
    • 0015523863 scopus 로고
    • Glutamine-dependent asparagine synthetase from leukemia cells
    • Horowitz B., and Meister A. Glutamine-dependent asparagine synthetase from leukemia cells. J. Biol. Chem. 247 (1972) 6708-6719
    • (1972) J. Biol. Chem. , vol.247 , pp. 6708-6719
    • Horowitz, B.1    Meister, A.2
  • 36
    • 0023728105 scopus 로고
    • The behavior and significance of slow-binding enzyme inhibitors
    • Morrison J.F., and Walsh C.T. The behavior and significance of slow-binding enzyme inhibitors. Adv. Enzymol. Relat. Areas Mol. Biol. 61 (1988) 201-301
    • (1988) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.61 , pp. 201-301
    • Morrison, J.F.1    Walsh, C.T.2
  • 37
    • 0031755549 scopus 로고    scopus 로고
    • Design, synthesis and evaluation of transition-state analogue inhibitors of Escherichia coli γ-glutamylcysteine synthetase
    • Tokutake N., Hiratake J., Katoh M., Irie T., Kato H., and Oda J. Design, synthesis and evaluation of transition-state analogue inhibitors of Escherichia coli γ-glutamylcysteine synthetase. Bioorg. Med. Chem. 6 (1998) 1935-1953
    • (1998) Bioorg. Med. Chem. , vol.6 , pp. 1935-1953
    • Tokutake, N.1    Hiratake, J.2    Katoh, M.3    Irie, T.4    Kato, H.5    Oda, J.6
  • 38
    • 0014526454 scopus 로고
    • Identification of L-methionine S-sulfoximine as the diastereoisomer of L-methionine SR-sulfoximine that inhibits glutamine synthetase
    • Manning J.M., Moore S., Rowe W.B., and Meister A. Identification of L-methionine S-sulfoximine as the diastereoisomer of L-methionine SR-sulfoximine that inhibits glutamine synthetase. Biochemistry 8 (1969) 2681-2685
    • (1969) Biochemistry , vol.8 , pp. 2681-2685
    • Manning, J.M.1    Moore, S.2    Rowe, W.B.3    Meister, A.4
  • 39
    • 0025758343 scopus 로고
    • Analytical and preparative separation of the diastereoisomers of L-buthionine (SR)-sulfoximine, a potent inhibitor of glutathione biosynthesis
    • Campbell E.B., Hayward M.L., and Griffith O.W. Analytical and preparative separation of the diastereoisomers of L-buthionine (SR)-sulfoximine, a potent inhibitor of glutathione biosynthesis. Anal. Biochem. 194 (1991) 268-277
    • (1991) Anal. Biochem. , vol.194 , pp. 268-277
    • Campbell, E.B.1    Hayward, M.L.2    Griffith, O.W.3
  • 41
    • 0023100286 scopus 로고
    • Effect of the presence of a reversible inhibitor on the time course of slow-binding inhibition
    • Weiss P.M., and Cleland W.W. Effect of the presence of a reversible inhibitor on the time course of slow-binding inhibition. Anal. Biochem. 161 (1987) 438-441
    • (1987) Anal. Biochem. , vol.161 , pp. 438-441
    • Weiss, P.M.1    Cleland, W.W.2
  • 42
    • 0016700753 scopus 로고
    • Tight-binding inhibitors. I: kinetics
    • Cha S. Tight-binding inhibitors. I: kinetics. Biochem. Pharmacol. 24 (1975) 2177-2185
    • (1975) Biochem. Pharmacol. , vol.24 , pp. 2177-2185
    • Cha, S.1
  • 44
    • 0025867099 scopus 로고
    • Investigation of the mechanism of phosphinothricin inactivation of Escherichia coli glutamine synthetase using rapid quench techniques
    • Abell L.M., and Villafranca J.J. Investigation of the mechanism of phosphinothricin inactivation of Escherichia coli glutamine synthetase using rapid quench techniques. Biochemistry 30 (1991) 6135-6141
    • (1991) Biochemistry , vol.30 , pp. 6135-6141
    • Abell, L.M.1    Villafranca, J.J.2
  • 45
    • 0028082017 scopus 로고
    • Structural model for the reaction mechanism of glutamine synthetase, based on 5 crystal structures of enzyme-substrate complexes
    • Liaw S.H., and Eisenberg D. Structural model for the reaction mechanism of glutamine synthetase, based on 5 crystal structures of enzyme-substrate complexes. Biochemistry 33 (1994) 675-681
    • (1994) Biochemistry , vol.33 , pp. 675-681
    • Liaw, S.H.1    Eisenberg, D.2
  • 46
    • 0014526454 scopus 로고
    • Identification of L-methionine S-sulfoximine as diastereoisomer of L-methionine SR-sulfoximine that inhibits glutamine synthetase
    • Manning J.M., Moore S., Rowe W.B., and Meister A. Identification of L-methionine S-sulfoximine as diastereoisomer of L-methionine SR-sulfoximine that inhibits glutamine synthetase. Biochemistry 8 (1969) 2681-2685
    • (1969) Biochemistry , vol.8 , pp. 2681-2685
    • Manning, J.M.1    Moore, S.2    Rowe, W.B.3    Meister, A.4
  • 47
    • 0015919826 scopus 로고
    • Studies on glutamine synthetase from Escherichia coli: formation of pyrrolidone carboxylate and inhibtion by methionine sulfoximine
    • Weisbrod R.E., and Meister A. Studies on glutamine synthetase from Escherichia coli: formation of pyrrolidone carboxylate and inhibtion by methionine sulfoximine. J. Biol. Chem. 248 (1973) 3997-4002
    • (1973) J. Biol. Chem. , vol.248 , pp. 3997-4002
    • Weisbrod, R.E.1    Meister, A.2
  • 48
    • 0036405237 scopus 로고    scopus 로고
    • The γ-glutamyl thioester covalent intermediate in the glutaminase reaction catalyzed by Escherichia coli asparagine synthetase B
    • Schnizer H.G., Boehlein S.K., Stewart J.D., Schuster S.M., and Richards N.G.J. The γ-glutamyl thioester covalent intermediate in the glutaminase reaction catalyzed by Escherichia coli asparagine synthetase B. Methods Enzymol. 354 (2002) 260-271
    • (2002) Methods Enzymol. , vol.354 , pp. 260-271
    • Schnizer, H.G.1    Boehlein, S.K.2    Stewart, J.D.3    Schuster, S.M.4    Richards, N.G.J.5
  • 49
    • 0033596863 scopus 로고    scopus 로고
    • Formation and isolation of a covalent intermediate during the glutaminase reaction of a class II amidotransferase
    • Schnizer H.G., Boehlein S.K., Stewart J.D., Richards N.G.J., and Schuster S.M. Formation and isolation of a covalent intermediate during the glutaminase reaction of a class II amidotransferase. Biochemistry 38 (1999) 3677-3682
    • (1999) Biochemistry , vol.38 , pp. 3677-3682
    • Schnizer, H.G.1    Boehlein, S.K.2    Stewart, J.D.3    Richards, N.G.J.4    Schuster, S.M.5
  • 50
    • 0000620845 scopus 로고
    • L-Glutamate UV assay with glutamate dehydrogenase and NAD
    • Bergmeyer H.U. (Ed), Academic Press, New York
    • Bernt E., and Bergmeyer H.U. L-Glutamate UV assay with glutamate dehydrogenase and NAD. In: Bergmeyer H.U. (Ed). Methods of Enzymatic Analysis (1974), Academic Press, New York 1704-1708
    • (1974) Methods of Enzymatic Analysis , pp. 1704-1708
    • Bernt, E.1    Bergmeyer, H.U.2
  • 51
    • 0028246266 scopus 로고
    • Glutamine-dependent nitrogen transfer in Escherichia coli asparagine synthetase B: searching for the catalytic triad
    • Boehlein S.K., Richards N.G.J., and Schuster S.M. Glutamine-dependent nitrogen transfer in Escherichia coli asparagine synthetase B: searching for the catalytic triad. J. Biol. Chem. 269 (1994) 7450-7457
    • (1994) J. Biol. Chem. , vol.269 , pp. 7450-7457
    • Boehlein, S.K.1    Richards, N.G.J.2    Schuster, S.M.3
  • 52
    • 0027985441 scopus 로고
    • Arginine 30 and asparagine 74 have functional roles in the glutamine dependent activities of Escherichia coli asparagine synthetase B
    • Boehlein S.K., Richards N.G.J., and Schuster S.M. Arginine 30 and asparagine 74 have functional roles in the glutamine dependent activities of Escherichia coli asparagine synthetase B. J. Biol. Chem. 269 (1994) 26789-26795
    • (1994) J. Biol. Chem. , vol.269 , pp. 26789-26795
    • Boehlein, S.K.1    Richards, N.G.J.2    Schuster, S.M.3
  • 55
    • 0034678025 scopus 로고    scopus 로고
    • Dual role for the glutamine phosphoribosyl-phosphate amidotransferase ammonia channel: interdomain signaling and intermediate channeling
    • Bera A.K., Smith J.L., and Zalkin H. Dual role for the glutamine phosphoribosyl-phosphate amidotransferase ammonia channel: interdomain signaling and intermediate channeling. J. Biol. Chem. 275 (2000) 7975-7979
    • (2000) J. Biol. Chem. , vol.275 , pp. 7975-7979
    • Bera, A.K.1    Smith, J.L.2    Zalkin, H.3
  • 56
    • 0001083651 scopus 로고
    • Mechanistic investigations on glucosamine-6-phosphate synthase
    • Badet-Denisot M.A., René L., and Badet B. Mechanistic investigations on glucosamine-6-phosphate synthase. Bull. Soc. Chim. Fr. 130 (1993) 249-255
    • (1993) Bull. Soc. Chim. Fr. , vol.130 , pp. 249-255
    • Badet-Denisot, M.A.1    René, L.2    Badet, B.3
  • 57
    • 0030966193 scopus 로고    scopus 로고
    • Amino acid control of asparagine synthetase: relation to asparaginase resistance in human leukemia cells
    • Hutson R.G., Kitoh T., Moraga-Amador D., Cosic S., Schuster S.M., and Kilberg M.S. Amino acid control of asparagine synthetase: relation to asparaginase resistance in human leukemia cells. Am. J. Physiol. 272 (1997) C1691-C1699
    • (1997) Am. J. Physiol. , vol.272
    • Hutson, R.G.1    Kitoh, T.2    Moraga-Amador, D.3    Cosic, S.4    Schuster, S.M.5    Kilberg, M.S.6
  • 58
    • 0035881515 scopus 로고    scopus 로고
    • Multiple adaptive mechanisms affect asparagine synthetase substrate availability in asparaginase-resistant MOLT-4 human leukemia cells
    • Aslanian A.M., and Kilberg M.S. Multiple adaptive mechanisms affect asparagine synthetase substrate availability in asparaginase-resistant MOLT-4 human leukemia cells. Biochem. J. 357 (2001) 58-67
    • (2001) Biochem. J. , vol.357 , pp. 58-67
    • Aslanian, A.M.1    Kilberg, M.S.2
  • 59
    • 0029803056 scopus 로고    scopus 로고
    • A combined assay of cell viability and in vitro cytotoxicity with a highly water-soluble tetrazolium salt, neutral red and crystal violet
    • Ishiyama M., Tominaga H., Shiga M., Sasamoto K., Ohkura Y., and Ueno K. A combined assay of cell viability and in vitro cytotoxicity with a highly water-soluble tetrazolium salt, neutral red and crystal violet. Biol. Pharm. Bull. 19 (1996) 1518-1520
    • (1996) Biol. Pharm. Bull. , vol.19 , pp. 1518-1520
    • Ishiyama, M.1    Tominaga, H.2    Shiga, M.3    Sasamoto, K.4    Ohkura, Y.5    Ueno, K.6
  • 60
    • 33644908481 scopus 로고    scopus 로고
    • Expression levels of asparagine synthetase in blasts from children and adults with acute lymphoblastic leukemia
    • Leslie M., Case M.C., Hall A.G., and Coulthard S.A. Expression levels of asparagine synthetase in blasts from children and adults with acute lymphoblastic leukemia. Br. J. Haematol. 132 (2006) 740-742
    • (2006) Br. J. Haematol. , vol.132 , pp. 740-742
    • Leslie, M.1    Case, M.C.2    Hall, A.G.3    Coulthard, S.A.4
  • 61
    • 0031024171 scopus 로고    scopus 로고
    • Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings
    • Lipinski C.A., Lombardo F., Dominy B.W., and Feeney P.J. Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings. Adv. Drug Deliv. Rev. 23 (1997) 3-25
    • (1997) Adv. Drug Deliv. Rev. , vol.23 , pp. 3-25
    • Lipinski, C.A.1    Lombardo, F.2    Dominy, B.W.3    Feeney, P.J.4
  • 62
    • 13444292249 scopus 로고    scopus 로고
    • Using genome-wide transcriptional profiling to elucidate small molecule mechanisms
    • Butcher R.A., and Schreiber S.L. Using genome-wide transcriptional profiling to elucidate small molecule mechanisms. Curr. Opin. Chem. Biol. 9 (2005) 25-30
    • (2005) Curr. Opin. Chem. Biol. , vol.9 , pp. 25-30
    • Butcher, R.A.1    Schreiber, S.L.2
  • 64
    • 0017184389 scopus 로고
    • Rapid and sensitive method for quantitation of microgram quantities of protein utilizing principle of protein-dye binding
    • Bradford M.M. Rapid and sensitive method for quantitation of microgram quantities of protein utilizing principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 65
    • 0018861395 scopus 로고
    • Safety aspects of handling the potent allergen FDNB
    • Thompson J.S., and Edmonds O.P. Safety aspects of handling the potent allergen FDNB. Ann. Occup. Hyg. 23 (1980) 27-33
    • (1980) Ann. Occup. Hyg. , vol.23 , pp. 27-33
    • Thompson, J.S.1    Edmonds, O.P.2
  • 66
    • 0035367791 scopus 로고    scopus 로고
    • HPLC determination of taurine in sports drinks
    • Orth D.L. HPLC determination of taurine in sports drinks. J. Chem. Educ. 78 (2001) 791-792
    • (2001) J. Chem. Educ. , vol.78 , pp. 791-792
    • Orth, D.L.1
  • 67
    • 0023926514 scopus 로고
    • Amino acid analysis by dinitrophenylation and reverse-phase high-pressure liquid chromatography
    • Morton R.C., and Gerber G.E. Amino acid analysis by dinitrophenylation and reverse-phase high-pressure liquid chromatography. Anal. Biochem. 170 (1988) 220-227
    • (1988) Anal. Biochem. , vol.170 , pp. 220-227
    • Morton, R.C.1    Gerber, G.E.2
  • 68
    • 0018735516 scopus 로고
    • Statistical analysis of enzyme kinetic data
    • Cleland W.W. Statistical analysis of enzyme kinetic data. Methods Enzymol. 63 (1979) 103-138
    • (1979) Methods Enzymol. , vol.63 , pp. 103-138
    • Cleland, W.W.1
  • 69
    • 0025390935 scopus 로고
    • MOPAC: a semiempirical molecular orbital program
    • Stewart J.J.P. MOPAC: a semiempirical molecular orbital program. J. Comput. Aided Mol. Des. 4 (1990) 1-45
    • (1990) J. Comput. Aided Mol. Des. , vol.4 , pp. 1-45
    • Stewart, J.J.P.1
  • 70
    • 0026112194 scopus 로고
    • On the use of isovalued surfaces to determine molecular shape and reaction pathways
    • Purvis III G.D. On the use of isovalued surfaces to determine molecular shape and reaction pathways. J. Comput. Aided Mol. Des. 5 (1991) 55-80
    • (1991) J. Comput. Aided Mol. Des. , vol.5 , pp. 55-80
    • Purvis III, G.D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.