메뉴 건너뛰기




Volumn 17, Issue 20, 2010, Pages 2183-2195

Structure-function relationships and clinical applications of L-Asparaginases

Author keywords

Acute lymphoblastic leukemia; Catalytic mechanism protein crystallography; L asparaginase; Protein drug

Indexed keywords

AGAROSE; AMINO ACID; AMMONIA; ANTINEOPLASTIC AGENT; ASPARAGINASE MACROGOL; ASPARAGINE; BLEOMYCIN; CISPLATIN; CORTICOSTEROID; CYCLOPHOSPHAMIDE; CYTOSINE; DOXORUBICIN; ENZYME ANTIBODY; GLUTAMINASE; LIPOSOME; METHOTREXATE; MONOMER; POLYACRYLAMIDE; VINCRISTINE; ASPARAGINASE;

EID: 77955602245     PISSN: 09298673     EISSN: None     Source Type: Journal    
DOI: 10.2174/092986710791299920     Document Type: Erratum
Times cited : (35)

References (88)
  • 1
    • 84965111634 scopus 로고
    • Regression of transplanted lymphomas induced in vivo by means of normal guinea pig serum. I. Course of transplanted cancers of various kinds in mice and rats given guinea pig serum, horse serum, or rabbit serum
    • Kidd, J.G. Regression of transplanted lymphomas induced in vivo by means of normal guinea pig serum. I. Course of transplanted cancers of various kinds in mice and rats given guinea pig serum, horse serum, or rabbit serum. J. Exp. Med., 1953, 98, 565-582.
    • (1953) J. Exp. Med. , vol.98 , pp. 565-582
    • Kidd, J.G.1
  • 2
    • 36949081498 scopus 로고
    • Evidence that the L-Asparaginase activity of guinea pig serum is responsible for its antilymphoma effects
    • Broome, J.D. Evidence that the L-Asparaginase activity of guinea pig serum is responsible for its antilymphoma effects. Nature, 1961, 191, 1114-1115.
    • (1961) Nature , vol.191 , pp. 1114-1115
    • Broome, J.D.1
  • 3
    • 75449125982 scopus 로고
    • Evidence that the L-asparaginase of guinea pig serum is responsible for its antilymphoma effects. II. Lymphoma6C3HED cells cultured in a medium devoid of L-asparagine lose their susceptibility to the effects of guinea pig serum in vivo
    • Broome, J.D. Evidence that the L-asparaginase of guinea pig serum is responsible for its antilymphoma effects. II. Lymphoma6C3HED cells cultured in a medium devoid of L-asparagine lose their susceptibility to the effects of guinea pig serum in vivo. J.Exp. Med., 1963, 118, 121-148.
    • (1963) J.Exp. Med. , vol.118 , pp. 121-148
    • Broome, J.D.1
  • 4
    • 0013990505 scopus 로고
    • Toxic and antineoplastic effects of L-asparaginase. Study of mice with lymphoma and normal monkeys and report on a child with leukemia
    • Dolowy, W.C.; Henson, D.; Cornet, J.; Sellin, H. Toxic and antineoplastic effects of L-asparaginase. Study of mice with lymphoma and normal monkeys and report on a child with leukemia. Cancer, 1966, 19, 1813-1819.
    • (1966) Cancer , vol.19 , pp. 1813-1819
    • Dolowy, W.C.1    Henson, D.2    Cornet, J.3    Sellin, H.4
  • 7
    • 35048824745 scopus 로고    scopus 로고
    • Treatment of acute lymphoblastic leukaemia: A new era
    • Apostolidou, E.; Swords, R.; Alvarado, Y.; Giles, F.J. Treatment of acute lymphoblastic leukaemia: a new era. Drugs, 2007, 67, 2153-2171.
    • (2007) Drugs , vol.67 , pp. 2153-2171
    • Apostolidou, E.1    Swords, R.2    Alvarado, Y.3    Giles, F.J.4
  • 8
    • 33644798329 scopus 로고    scopus 로고
    • Childhood acute lymphoblastic leukaemia and relapse
    • Gaynon, P.S. Childhood acute lymphoblastic leukaemia and relapse. Br. J. Haematol., 2005, 131, 579-587.
    • (2005) Br. J. Haematol. , vol.131 , pp. 579-587
    • Gaynon, P.S.1
  • 9
    • 18644364984 scopus 로고    scopus 로고
    • Pharmacokinetic/pharmacodynamic relationships of asparaginase formulations: The past, the present and recommendations for the future
    • Avramis, V.I.; Panosyan, E.H. Pharmacokinetic/pharmacodynamic relationships of asparaginase formulations: the past, the present and recommendations for the future. Clin. Pharmacokinet., 2005, 44, 367-393.
    • (2005) Clin. Pharmacokinet. , vol.44 , pp. 367-393
    • Avramis, V.I.1    Panosyan, E.H.2
  • 11
    • 0032145202 scopus 로고    scopus 로고
    • Use of L-asparaginase in childhood ALL
    • Muller, H.J.; Boos, J. Use of L-asparaginase in childhood ALL. Crit. Rev. Oncol. Hematol., 1998, 28, 97-113.
    • (1998) Crit. Rev. Oncol. Hematol. , vol.28 , pp. 97-113
    • Muller, H.J.1    Boos, J.2
  • 13
    • 0035672697 scopus 로고    scopus 로고
    • Comparison of intramuscular therapy with Erwinia asparaginase and asparaginase Medac: Pharmacokinetics,pharmacodynamics, formation of antibodies and influence on the coagulation system
    • Albertsen, B.K.; Schrøder, H.; Ingerslev, J.; Jakobsen, P.; Avramis, V.I.; Müller, H.J.; Carlsen, N.T.; Schmiegelow, K. Comparison of intramuscular therapy with Erwinia asparaginase and asparaginase Medac: pharmacokinetics,pharmacodynamics, formation of antibodies and influence on the coagulation system. Br. J. Haematol., 2001, 115, 983-990.
    • (2001) Br. J. Haematol. , vol.115 , pp. 983-990
    • Albertsen, B.K.1    Schrøder, H.2    Ingerslev, J.3    Jakobsen, P.4    Avramis, V.I.5    Müller, H.J.6    Carlsen, N.T.7    Schmiegelow, K.8
  • 14
    • 51649107776 scopus 로고    scopus 로고
    • Pharmacokinetic, pharmacodynamic and intracellular effects of PEGasparaginase in newly diagnosed childhood acute lymphoblastic leukemia: Results from a single agent window study
    • Appel, I.M.; Kazemier, K.M.; Boos, J. Lanvers, C.; Huijmans, J.; Veerman, A.J.; van Wering, E.; den Boer M.L.; Pieters, R. Pharmacokinetic, pharmacodynamic and intracellular effects of PEGasparaginase in newly diagnosed childhood acute lymphoblastic leukemia: results from a single agent window study. Leukemia, 2008, 22, 1665-1679.
    • (2008) Leukemia , vol.22 , pp. 1665-1679
    • Appel, I.M.1    Kazemier, K.M.2    Boos, J.3    Lanvers, C.4    Huijmans, J.5    Veerman, A.J.6    van Wering, E.7    den Boer, M.L.8    Pieters, R.9
  • 15
    • 34548776939 scopus 로고    scopus 로고
    • Asparaginase (native ASNase or pegylated ASNase) in the treatment of acute lymphoblastic leukemia
    • Avramis, V.I.; Tiwari, P.N. Asparaginase (native ASNase or pegylated ASNase) in the treatment of acute lymphoblastic leukemia. Int. J. Nanomed., 2006, 1, 241-254.
    • (2006) Int. J. Nanomed. , vol.1 , pp. 241-254
    • Avramis, V.I.1    Tiwari, P.N.2
  • 16
    • 34547811078 scopus 로고    scopus 로고
    • Pharmacoanalytical assays of Erwinia asparaginase (erwinase) and pharmacokinetic results in high-risk acute lymphoblastic leukemia (HR ALL) patients: Simulations of erwinase population PK-PD models
    • Avramis, V.I.; Martin-Aragon, S.; Avramis, E.V.; Asselin, B.L. Pharmacoanalytical assays of Erwinia asparaginase (erwinase) and pharmacokinetic results in high-risk acute lymphoblastic leukemia (HR ALL) patients: simulations of erwinase population PK-PD models. Anticancer Res., 2007, 27, 2561-2572.
    • (2007) Anticancer Res. , vol.27 , pp. 2561-2572
    • Avramis, V.I.1    Martin-Aragon, S.2    Avramis, E.V.3    Asselin, B.L.4
  • 17
  • 18
    • 0015568726 scopus 로고
    • L-asparaginase: A review
    • Wriston, J.J.; Yellin, T. L-asparaginase: a review. Adv. Enzymol., 1973, 39, 185-200.
    • (1973) Adv. Enzymol. , vol.39 , pp. 185-200
    • Wriston, J.J.1    Yellin, T.2
  • 19
    • 0021103897 scopus 로고
    • On the distribution of plasma Lasparaginase
    • Yurel, E.; Peru, D.; Wriston, J.J. On the distribution of plasma Lasparaginase. Experientia, 1983, 39, 383-385.
    • (1983) Experientia , vol.39 , pp. 383-385
    • Yurel, E.1    Peru, D.2    Wriston, J.J.3
  • 20
    • 0014958405 scopus 로고
    • Multiple forms of L-asparaginase
    • Ho, P.P.; Milikin, E.B. Multiple forms of L-asparaginase. Biochim. Biophys. Acta, 1970, 206, 196-198.
    • (1970) Biochim. Biophys. Acta , vol.206 , pp. 196-198
    • Ho, P.P.1    Milikin, E.B.2
  • 21
    • 33846167401 scopus 로고    scopus 로고
    • Structural aspects of L-asparaginases, their friends and relations
    • Michalska, K.; Jaskolski, M. Structural aspects of L-asparaginases, their friends and relations. Acta Biochim. Pol., 2006, 53, 627-640.
    • (2006) Acta Biochim. Pol. , vol.53 , pp. 627-640
    • Michalska, K.1    Jaskolski, M.2
  • 22
    • 0028015804 scopus 로고
    • Structural characterization of Pseudomonas 7A glutaminase-asparaginase
    • Lubkowski, J.; Wlodawer, A.; Ammon, H.L.; Copeland, T.D.; Swain, A.L. Structural characterization of Pseudomonas 7A glutaminase-asparaginase. Biochemistry, 1994, 33, 10257-10265.
    • (1994) Biochemistry , vol.33 , pp. 10257-10265
    • Lubkowski, J.1    Wlodawer, A.2    Ammon, H.L.3    Copeland, T.D.4    Swain, A.L.5
  • 24
    • 0039637861 scopus 로고
    • The purification and properties of asparaginase from Lupinus species
    • Lea, P.J.; Farnden, L.; Miflin, B.J. The purification and properties of asparaginase from Lupinus species. Phytochemistry, 1979, 17, 217-222.
    • (1979) Phytochemistry , vol.17 , pp. 217-222
    • Lea, P.J.1    Farnden, L.2    Miflin, B.J.3
  • 29
    • 0026878310 scopus 로고
    • The isolation and characterisation of a cDNA clone encoding L-asparaginase from developing seeds of lupin (Lupinus arboreus)
    • Lough, T.J.; Reddington, B.D.; Grant, M.R.; Hill, D.F.; Reynolds, P.H. Farnden, K.J. The isolation and characterisation of a cDNA clone encoding L-asparaginase from developing seeds of lupin (Lupinus arboreus). Plant Mol. Biol., 1992, 19, 391-399.
    • (1992) Plant Mol. Biol. , vol.19 , pp. 391-399
    • Lough, T.J.1    Reddington, B.D.2    Grant, M.R.3    Hill, D.F.4    Reynolds, P.H.5    Farnden, K.J.6
  • 30
    • 33745271363 scopus 로고    scopus 로고
    • Crystal structure of plant asparaginase
    • Mishalska, M.; Bujacz, G.; Jaskolski, M. Crystal structure of plant asparaginase. J. Mol. Biol., 2006, 360, 105-16.
    • (2006) J. Mol. Biol. , vol.360 , pp. 105-116
    • Mishalska, M.1    Bujacz, G.2    Jaskolski, M.3
  • 31
    • 0014481842 scopus 로고
    • The purification and properties of a beta-aspartyl N-acetylglucosylamine amidohydrolase from hen oviduct
    • Tarentino, A.L.; Maley, F. The purification and properties of a beta-aspartyl N-acetylglucosylamine amidohydrolase from hen oviduct. Arch. Biochem. Biophys., 1969, 130, 295-303.
    • (1969) Arch. Biochem. Biophys. , vol.130 , pp. 295-303
    • Tarentino, A.L.1    Maley, F.2
  • 32
    • 0342646916 scopus 로고    scopus 로고
    • The L-asparagine operon of Rhizobium etli contains a gene encoding an atypical asparaginase
    • Ortuño-Olea, L.; Durán-Vargas, S. The L-asparagine operon of Rhizobium etli contains a gene encoding an atypical asparaginase. FEMS Microbiol. Lett., 2000, 189, 177-182.
    • (2000) FEMS Microbiol. Lett. , vol.189 , pp. 177-182
    • Ortuño-Olea, L.1    Durán-Vargas, S.2
  • 34
    • 0027530947 scopus 로고
    • Crystal structure of Escherichia coli L-asparaginase, an enzyme used in cancer therapy
    • USA
    • Swain, A.L.; Jaskólski, M.; Housset, D.; Rao, J.K.; Wlodawer, A., Crystal structure of Escherichia coli L-asparaginase, an enzyme used in cancer therapy. Proc. Natl. Acad. Sci. USA, 1993, 90, 1474-1478.
    • (1993) Proc. Natl. Acad. Sci. , vol.90 , pp. 1474-1478
    • Swain, A.L.1    Jaskólski, M.2    Housset, D.3    Rao, J.K.4    Wlodawer, A.5
  • 35
    • 0035873421 scopus 로고    scopus 로고
    • Structural basis for the activity and substrate specificity of Erwinia chrysanthemi Lasparaginase
    • Aghaiypour, K.; Wlodawer, A.; Lubkowski, J. Structural basis for the activity and substrate specificity of Erwinia chrysanthemi Lasparaginase. Biochemistry, 2001, 40, 5655-5664.
    • (2001) Biochemistry , vol.40 , pp. 5655-5664
    • Aghaiypour, K.1    Wlodawer, A.2    Lubkowski, J.3
  • 40
    • 24044549361 scopus 로고    scopus 로고
    • Structure of the type I L-asparaginase from the hyperthermophilic archaeon Pyrococcus horikoshii at 2.16 angstroms resolution
    • Yao, M.; Yasutake, Y.; Morita, H.; Tanaka, I. Structure of the type I L-asparaginase from the hyperthermophilic archaeon Pyrococcus horikoshii at 2.16 angstroms resolution. Acta Crystallogr. D 2005, 61, 294-301.
    • (2005) Acta Crystallogr. D , vol.61 , pp. 294-301
    • Yao, M.1    Yasutake, Y.2    Morita, H.3    Tanaka, I.4
  • 41
    • 34248232994 scopus 로고    scopus 로고
    • Crystal structure and allosteric regulation of the cytoplasmic Escherichia coli L-asparaginase I
    • Yun, M-K.; Nourse, A.; White, S.W.; Rock, C; Richard J. Crystal structure and allosteric regulation of the cytoplasmic Escherichia coli L-asparaginase I. J. Mol. Biol., 2007, 369, 794-811.
    • (2007) J. Mol. Biol. , vol.369 , pp. 794-811
    • Yun, M.-K.1    Nourse, A.2    White, S.W.3    Rock, C.4    Richard, J.5
  • 42
    • 0027255527 scopus 로고
    • A left-handed crossover involved in amidohydrolase catalysis. Crystal structure of Erwinia chrysanthemi L-asparaginase with bound L-aspartate
    • Miller, M.; Rao, J.; Wlodawer, A.; Gribskov, M., A left-handed crossover involved in amidohydrolase catalysis. Crystal structure of Erwinia chrysanthemi L-asparaginase with bound L-aspartate. FEBS Lett., 1993, 328, 275-279.
    • (1993) FEBS Lett. , vol.328 , pp. 275-279
    • Miller, M.1    Rao, J.2    Wlodawer, A.3    Gribskov, M.4
  • 43
    • 0034673170 scopus 로고    scopus 로고
    • Reactions of Pseudomonas 7A glutaminase-asparaginase with diazo analogues of glutamine and asparagine result in unexpected covalent inhibitions and suggests an unusual catalytic triad Thr-Tyr-Glu
    • Ortlund, E.; Lacount, M.W.; Lewinski, K.; Lebioda, L. Reactions of Pseudomonas 7A glutaminase-asparaginase with diazo analogues of glutamine and asparagine result in unexpected covalent inhibitions and suggests an unusual catalytic triad Thr-Tyr-Glu. Biochemistry, 2000, 39, 1199-1204.
    • (2000) Biochemistry , vol.39 , pp. 1199-1204
    • Ortlund, E.1    Lacount, M.W.2    Lewinski, K.3    Lebioda, L.4
  • 44
    • 0030597979 scopus 로고    scopus 로고
    • A covalently bound catalytic intermediate in Escherichia coli asparaginase: Crystal structure of a Thr-89-Val mutant
    • Palm, G.J.; Lubkowski, J.; Derst, C.; Schleper, S.; Rohm, K.H.; Wlodawer, A. A covalently bound catalytic intermediate in Escherichia coli asparaginase: crystal structure of a Thr-89-Val mutant. FEBS Lett., 1996, 390, 211-216.
    • (1996) FEBS Lett. , vol.390 , pp. 211-216
    • Palm, G.J.1    Lubkowski, J.2    Derst, C.3    Schleper, S.4    Rohm, K.H.5    Wlodawer, A.6
  • 45
    • 0032168569 scopus 로고    scopus 로고
    • Catalytic triads and their relatives
    • Dodson, G.; Wlodawer, A. Catalytic triads and their relatives. Trends Biochem. Sci., 1998, 23, 347-352.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 347-352
    • Dodson, G.1    Wlodawer, A.2
  • 48
    • 24944555774 scopus 로고    scopus 로고
    • Cloning, expression and characterization of Erwinia carotovora L-asparaginase
    • Kotzia, G.A.; Labrou, N.E. Cloning, expression and characterization of Erwinia carotovora L-asparaginase. J. Biotechnol., 2005, 119, 309-323.
    • (2005) J. Biotechnol. , vol.119 , pp. 309-323
    • Kotzia, G.A.1    Labrou, N.E.2
  • 49
    • 0033773575 scopus 로고    scopus 로고
    • Engineering the substrate specificity of Escherichia coli asparaginase II. Selective reduction of glutaminase activity by amino acid replacements at position 248
    • Derst, C.; Henseling, J.; Röhm, K.H. Engineering the substrate specificity of Escherichia coli asparaginase II. Selective reduction of glutaminase activity by amino acid replacements at position 248. Protein Sci., 2000, 9, 2009-2017.
    • (2000) Protein Sci. , vol.9 , pp. 2009-2017
    • Derst, C.1    Henseling, J.2    Röhm, K.H.3
  • 50
    • 1942536596 scopus 로고    scopus 로고
    • One-step purification and kinetic properties of the recombinant Lasparaginase from Erwinia carotovora
    • Krasotkina, J.; Borisova, A.A.; Gervaziev, Y.V.; Sokolov, N.N. One-step purification and kinetic properties of the recombinant Lasparaginase from Erwinia carotovora. Biotechnol. Appl. Biochem., 2004, 39, 215-221.
    • (2004) Biotechnol. Appl. Biochem. , vol.39 , pp. 215-221
    • Krasotkina, J.1    Borisova, A.A.2    Gervaziev, Y.V.3    Sokolov, N.N.4
  • 51
    • 33845649780 scopus 로고    scopus 로고
    • L-Asparaginase from Erwinia Chrysanthemi 3937: Cloning, expression and characterization
    • Kotzia, G.A.; Labrou, N.E. L-Asparaginase from Erwinia Chrysanthemi 3937: cloning, expression and characterization. J. Biotechnol., 2007, 127, 657-669.
    • (2007) J. Biotechnol. , vol.127 , pp. 657-669
    • Kotzia, G.A.1    Labrou, N.E.2
  • 52
    • 0028136892 scopus 로고
    • Erwinia chrysanthemi L-asparaginase: Epitope mapping and production of antigenically modified enzymes
    • Moola, Z.B.; Scawen, M.D.; Atkinson, T.; Nicholls, D.J. Erwinia chrysanthemi L-asparaginase: epitope mapping and production of antigenically modified enzymes. Biochem. J., 1994, 302, 921-927.
    • (1994) Biochem. J. , vol.302 , pp. 921-927
    • Moola, Z.B.1    Scawen, M.D.2    Atkinson, T.3    Nicholls, D.J.4
  • 53
    • 33644499478 scopus 로고    scopus 로고
    • Monitoring protein aggregation during thermal unfolding in circular dichroism experiments
    • Benjwal, S.; Verma, S.; Röhm, K.H.; Gursky, O. Monitoring protein aggregation during thermal unfolding in circular dichroism experiments. Protein Sci., 2006, 15, 635-639.
    • (2006) Protein Sci. , vol.15 , pp. 635-639
    • Benjwal, S.1    Verma, S.2    Röhm, K.H.3    Gursky, O.4
  • 54
    • 0031807838 scopus 로고    scopus 로고
    • Increased serum trypsin and elastase-1 levels in patients undergoing L-asparaginase therapy
    • Shimizu, T.; Yamashiro, Y.; Igarashi, J.; Fujita, H.; Ishimoto, K. Increased serum trypsin and elastase-1 levels in patients undergoing L-asparaginase therapy. Eur. J. Pediatr., 1998, 157, 561-563.
    • (1998) Eur. J. Pediatr. , vol.157 , pp. 561-563
    • Shimizu, T.1    Yamashiro, Y.2    Igarashi, J.3    Fujita, H.4    Ishimoto, K.5
  • 55
    • 0034694204 scopus 로고    scopus 로고
    • Construction and structural modeling of a single-chain Fv-asparaginase fusion protein resistant to proteolysis
    • Guo, L.; Wang, J.; Qian, S.; Yan, X.; Chen, R.; Meng, G. Construction and structural modeling of a single-chain Fv-asparaginase fusion protein resistant to proteolysis. Biotechnol. Bioeng., 2000, 70, 456-463.
    • (2000) Biotechnol. Bioeng. , vol.70 , pp. 456-463
    • Guo, L.1    Wang, J.2    Qian, S.3    Yan, X.4    Chen, R.5    Meng, G.6
  • 57
    • 33847323097 scopus 로고    scopus 로고
    • Pharmacological and clinical evaluation of L-asparaginase in the treatment of leukemia
    • Narta, U.K.; Kanwar, S.S.; Azmi, W. Pharmacological and clinical evaluation of L-asparaginase in the treatment of leukemia. Crit. Rev. Oncol. Hematol., 2007, 61, 208-221.
    • (2007) Crit. Rev. Oncol. Hematol. , vol.61 , pp. 208-221
    • Narta, U.K.1    Kanwar, S.S.2    Azmi, W.3
  • 58
    • 34249812940 scopus 로고    scopus 로고
    • Tailoring structure-function properties of L-asparaginase: Engineering resistance to trypsin cleavage
    • Kotzia, G.A.; Lappa, K.; Labrou, N.E. Tailoring structure-function properties of L-asparaginase: engineering resistance to trypsin cleavage. Biochem. J., 2007, 404, 337-343.
    • (2007) Biochem. J. , vol.404 , pp. 337-343
    • Kotzia, G.A.1    Lappa, K.2    Labrou, N.E.3
  • 59
    • 34447096370 scopus 로고    scopus 로고
    • Enhancing the thermostability of Escherichia coli L-asparaginase II by substitution with Pro in predicted hydrogen-bonded turn structures
    • Li, L.-Z.; Xie, T.-H.; Li, H.-J.; Qing, C.; Zhang, G.-H. Suna, M.-S. Enhancing the thermostability of Escherichia coli L-asparaginase II by substitution with Pro in predicted hydrogen-bonded turn structures. Enz. Microb. Technol., 2007, 41, 523-527.
    • (2007) Enz. Microb. Technol. , vol.41 , pp. 523-527
    • Li, L.-Z.1    Xie, T.-H.2    Li, H.-J.3    Qing, C.4    Zhang, G.-H.5    Suna, M.-S.6
  • 60
    • 61349130050 scopus 로고    scopus 로고
    • Engineering thermal stability of Lasparaginase by in vtiro directed evolution
    • Kotzia, G.A.; Labrou, N.E. Engineering thermal stability of Lasparaginase by in vtiro directed evolution. FEBS J., 2009, 276, 1750-1761.
    • (2009) FEBS J. , vol.276 , pp. 1750-1761
    • Kotzia, G.A.1    Labrou, N.E.2
  • 61
    • 0036973847 scopus 로고    scopus 로고
    • In vivo half life of nanoencapsulated L-asparaginase
    • Baran, E.T.; Ozer, N.; Hasirci, V. In vivo half life of nanoencapsulated L-asparaginase. J. Mater. Sci. Mater. Med., 2002, 13, 1113-1121.
    • (2002) J. Mater. Sci. Mater. Med. , vol.13 , pp. 1113-1121
    • Baran, E.T.1    Ozer, N.2    Hasirci, V.3
  • 62
    • 0030842264 scopus 로고    scopus 로고
    • Immobilization of L-asparaginase into a biocompatible poly(ethylene glycol)-albumin hydrogel: Evaluation of performance in vivo
    • Jean-Francois, J.; Fortier, G. Immobilization of L-asparaginase into a biocompatible poly(ethylene glycol)-albumin hydrogel: evaluation of performance in vivo. Biotechnol. Appl. Biochem., 1997, 26,203-212.
    • (1997) Biotechnol. Appl.Biochem. , vol.26 , pp. 203-212
    • Jean-Francois, J.1    Fortier, G.2
  • 63
    • 0025003462 scopus 로고
    • Erythrocytes as carriers for L-asparaginase. Methodological and mouse in-vivo studies
    • Kravtzoff, R.; Ropars, C.; Laguerre, M.; Muh, J.P.; Chassaigne, M. Erythrocytes as carriers for L-asparaginase. Methodological and mouse in-vivo studies. J. Pharm. Pharmacol., 1990, 42, 473-476.
    • (1990) J. Pharm. Pharmacol. , vol.42 , pp. 473-476
    • Kravtzoff, R.1    Ropars, C.2    Laguerre, M.3    Muh, J.P.4    Chassaigne, M.5
  • 65
    • 84857778627 scopus 로고    scopus 로고
    • EMEA, Public summary of positive opinion for orphan designation of L-asparaginase encapsulated in erythrocytes for the treatment of pancreatic cancer (Doc. Ref.: EMEA/COMP/218226/2009)
    • EMEA, Committee for Orphan Medicinal Products, Public summary of positive opinion for orphan designation of L-asparaginase encapsulated in erythrocytes for the treatment of pancreatic cancer (Doc. Ref.: EMEA/COMP/218226/2009). http://www.emea.europa.eu/
    • Committee for Orphan Medicinal Products
  • 66
    • 0022622276 scopus 로고
    • Soluble asparaginasedextran conjugates show increased circulatory persistence and lowered antigen reactivity
    • Wileman, T.E.; Foster, R.L.; Elliott, P.N. Soluble asparaginasedextran conjugates show increased circulatory persistence and lowered antigen reactivity. J. Pharm. Pharmacol., 1986, 38, 264-271.
    • (1986) J. Pharm. Pharmacol. , vol.38 , pp. 264-271
    • Wileman, T.E.1    Foster, R.L.2    Elliott, P.N.3
  • 67
    • 34250091274 scopus 로고
    • Immobilization of the enzyme Lasparaginase of E. coli on polysaccharides. V. Preparation and properties of polymeric conjugates based on water-soluble CMcellulose differing by the quantitative amounts of polymer
    • Karsakevich, A. S.; Kinstler, O. B.; Vina, I. A.; Kashkin, A. P.; Putilova, N.E.; Merengova, L. F. Immobilization of the enzyme Lasparaginase of E. coli on polysaccharides. V. Preparation and properties of polymeric conjugates based on water-soluble CMcellulose differing by the quantitative amounts of polymer. Chem. Nat. Compd., 1987, 23, 488-492.
    • (1987) Chem. Nat. Compd. , vol.23 , pp. 488-492
    • Karsakevich, A.S.1    Kinstler, O.B.2    Vina, I.A.3    Kashkin, A.P.4    Putilova, N.E.5    Merengova, L.F.6
  • 68
    • 0020050329 scopus 로고
    • Advantages in the use of L-asparaginase-albumin polymer as an antitumor agent
    • Poznansky, M.J.; Shandling, M.; Salkie, M.A.; Elliott, J.F.; Lau, E. Advantages in the use of L-asparaginase-albumin polymer as an antitumor agent. Cancer Res., 1982, 42, 1020-1025.
    • (1982) Cancer Res. , vol.42 , pp. 1020-1025
    • Poznansky, M.J.1    Shandling, M.2    Salkie, M.A.3    Elliott, J.F.4    Lau, E.5
  • 69
    • 0019996289 scopus 로고
    • Increased antitumor activity of Escherichia coli. Lasparaginase by modification with monomethoxypolyethylene glycol
    • Kamisaki, Y.; Wada, H.; Yagura, T.; Nishimura, H.; Matsushima, A.; Inada, Y. Increased antitumor activity of Escherichia coli. Lasparaginase by modification with monomethoxypolyethylene glycol. Gann, 1982, 73, 470-474.
    • (1982) Gann , vol.73 , pp. 470-474
    • Kamisaki, Y.1    Wada, H.2    Yagura, T.3    Nishimura, H.4    Matsushima, A.5    Inada, Y.6
  • 70
    • 0020440676 scopus 로고
    • Immunological and pharmacological characterization of poly-DL-alanyl-modified Erwinia carotovora L-asparaginase
    • Uren, J.R.B.; Hargis, J.; Beardsley, P. Immunological and pharmacological characterization of poly-DL-alanyl-modified Erwinia carotovora L-asparaginase. Cancer Res., 1982, 42, 4068-4071.
    • (1982) Cancer Res. , vol.42 , pp. 4068-4071
    • Uren, J.R.B.1    Hargis, J.2    Beardsley, P.3
  • 71
    • 0029150904 scopus 로고
    • Engineering resistance to trypsin inactivation into LAsparaginase through the production of a chimeric protein between the enzyme and a protective single-chain antibody
    • Newsted, W. J.; Ramjeesingh, M.; Zywulko, M.; Rothstein, S.J.; Shami, E. Y. Engineering resistance to trypsin inactivation into LAsparaginase through the production of a chimeric protein between the enzyme and a protective single-chain antibody. Enz. Microb. Technol., 1995, 17, 757-764.
    • (1995) Enz. Microb. Technol. , vol.17 , pp. 757-764
    • Newsted, W.J.1    Ramjeesingh, M.2    Zywulko, M.3    Rothstein, S.J.4    Shami, E.Y.5
  • 72
    • 27544480064 scopus 로고    scopus 로고
    • Synthesis, characterization and immunogenicity of silk fibroin-L-asparaginase bioconjugates
    • Zhang, Y.Q.; Zhou, W.L.; Shen, W.D.; Chen, Y.H.; Zha, X.M.; Shirai, K.; Kiguchi, K. Synthesis, characterization and immunogenicity of silk fibroin-L-asparaginase bioconjugates. J. Biotechnol., 2005, 120, 315-326.
    • (2005) J. Biotechnol. , vol.120 , pp. 315-326
    • Zhang, Y.Q.1    Zhou, W.L.2    Shen, W.D.3    Chen, Y.H.4    Zha, X.M.5    Shirai, K.6    Kiguchi, K.7
  • 73
    • 31744440204 scopus 로고    scopus 로고
    • Synthesis of silk sericin peptides-L-asparaginase (SS-ASNase) bioconjugates and their characterization
    • Zhang, Y.Q.; Tao, M.L.; Shen, W.D.; Mao, J.P.; Chen, Y.H. Synthesis of silk sericin peptides-L-asparaginase (SS-ASNase) bioconjugates and their characterization. J. Chem. Technol.Biotechnol., 2006, 81, 136-145.
    • (2006) J. Chem. Technol.Biotechnol. , vol.81 , pp. 136-145
    • Zhang, Y.Q.1    Tao, M.L.2    Shen, W.D.3    Mao, J.P.4    Chen, Y.H.5
  • 74
    • 0030835335 scopus 로고    scopus 로고
    • Polysialylated asparaginase: Preparation, activity and pharmacokinetics
    • Fernandes, A.I.; Gregoriadis, G. Polysialylated asparaginase: preparation, activity and pharmacokinetics. Biochemica et Biophysica Acta., 1997, 1341, 26-34.
    • (1997) Biochemica et Biophysica Acta. , vol.1341 , pp. 26-34
    • Fernandes, A.I.1    Gregoriadis, G.2
  • 76
    • 0020584360 scopus 로고
    • Use of immobilized Lasparaginase in acrylic microparticles in an extracorporeal hollowfiber dialyzer
    • Edman, P.; Nylen, U.; Sjoholm, I. Use of immobilized Lasparaginase in acrylic microparticles in an extracorporeal hollowfiber dialyzer. J. Pharmacol. Exper. Therap., 1983, 225, 164-167.
    • (1983) J. Pharmacol. Exper. Therap. , vol.225 , pp. 164-167
    • Edman, P.1    Nylen, U.2    Sjoholm, I.3
  • 77
    • 35649000945 scopus 로고    scopus 로고
    • Nitrogen metabolism of asparagines and glutamate in Vero cells studied by (1)H/(15)N NMR spectroscopy
    • Huang H.; Yu, Y.; Yi, X.; Zhang, Y. Nitrogen metabolism of asparagines and glutamate in Vero cells studied by (1)H/(15)N NMR spectroscopy. Appl. Microbiol. Biotechnol., 2007, 77, 427-436.
    • (2007) Appl. Microbiol. Biotechnol. , vol.77 , pp. 427-436
    • Huang, H.1    Yu, Y.2    Yi, X.3    Zhang, Y.4
  • 78
    • 4143063669 scopus 로고    scopus 로고
    • Asparaginase pharmacokinetics after intensive polyethylene glycol-conjugated Lasparaginase therapy for children with relapsed acute lymphoblastic leukemia
    • Hawkins, D.S.; Park, J.R.; Thomson, B.G.; Felgenhauer, J.L.; Holcenberg, J.S.; Panosyan, E.H.; Avramis, V.I. Asparaginase pharmacokinetics after intensive polyethylene glycol-conjugated Lasparaginase therapy for children with relapsed acute lymphoblastic leukemia. Clin. Cancer Res., 2004, 10, 5335-5341.
    • (2004) Clin. Cancer Res. , vol.10 , pp. 5335-5341
    • Hawkins, D.S.1    Park, J.R.2    Thomson, B.G.3    Felgenhauer, J.L.4    Holcenberg, J.S.5    Panosyan, E.H.6    Avramis, V.I.7
  • 79
    • 33745765204 scopus 로고    scopus 로고
    • Asparagine depletion after pegylated E. coli asparaginase treatment and induction outcome in children with acute lymphoblastic leukemia in first bone marrow relapse: A Children's Oncology Group study (CCG-1941)
    • Jarrar, M.; Gaynon, P.S.; Periclou, A.P.; Fu, C.; Harris, R.E.; Stram, D.; Altman, A.; Bostrom, B.; Breneman, J.; Steele, D.; Trigg, M.; Zipf, T.; Avramis, V.I. Asparagine depletion after pegylated E. coli asparaginase treatment and induction outcome in children with acute lymphoblastic leukemia in first bone marrow relapse: a Children's Oncology Group study (CCG-1941). Pediatr Blood Cancer, 2006, 47, 141-146.
    • (2006) Pediatr Blood Cancer , vol.47 , pp. 141-146
    • Jarrar, M.1    Gaynon, P.S.2    Periclou, A.P.3    Fu, C.4    Harris, R.E.5    Stram, D.6    Altman, A.7    Bostrom, B.8    Breneman, J.9    Steele, D.10    Trigg, M.11    Zipf, T.12    Avramis, V.I.13
  • 80
    • 33947600985 scopus 로고    scopus 로고
    • Pharmacodynamics and safety of intravenous Pegaspargase during remission induction in adultsaged 55 years or younger with newly diagnosed acute lymphoblastic leukemia
    • Douer, D.; Yampolsky, H.; Cohen, L.J.; Watkins, K.; Levine, A.M.; Periclou, A.P.; Avramis, V.I. Pharmacodynamics and safety of intravenous Pegaspargase during remission induction in adultsaged 55 years or younger with newly diagnosed acute lymphoblastic leukemia. Blood, 2007, 109, 2744-2750.
    • (2007) Blood , vol.109 , pp. 2744-2750
    • Douer, D.1    Yampolsky, H.2    Cohen, L.J.3    Watkins, K.4    Levine, A.M.5    Periclou, A.P.6    Avramis, V.I.7
  • 84
    • 63449112670 scopus 로고    scopus 로고
    • Diagnosis and management of hypersensitivity reactions related to common cancer chemotherapy agents
    • Lee, C.; Gianos, M.; Klaustermeyer, W.B. Diagnosis and management of hypersensitivity reactions related to common cancer chemotherapy agents. Ann. Allergy Asthma Immunol. 2009, 102, 179-187.
    • (2009) Ann. Allergy Asthma Immunol , vol.102 , pp. 179-187
    • Lee, C.1    Gianos, M.2    Klaustermeyer, W.B.3
  • 85
    • 0020336534 scopus 로고
    • Hypersensitivity reaction to cancer chemotherapy
    • Weiss, R.B. Hypersensitivity reaction to cancer chemotherapy. Semin. Oncol., 1982, 9, 5-12.
    • (1982) Semin. Oncol. , vol.9 , pp. 5-12
    • Weiss, R.B.1
  • 86
    • 26844525474 scopus 로고    scopus 로고
    • Mapping of B-cell epitopes in E. coli asparaginase II, an enzyme used in leukemia treatment
    • Werner, A.; Röhm, K.-H.; M􀀃ller, H.-J. Mapping of B-cell epitopes in E. coli asparaginase II, an enzyme used in leukemia treatment. Biol. Chem., 2005, 386, 535-540,
    • (2005) Biol. Chem. , vol.386 , pp. 535-540
    • Werner, A.1    Röhm, K.-H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.