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Volumn 35, Issue C, 1997, Pages 207-252

6. prune/Killar of prune: A Conditional Dominant Lethal Interaction in Drosophila

Author keywords

[No Author keywords available]

Indexed keywords

ABNORMAL WING DISCS PROTEIN, DROSOPHILA; DROSOPHILA PROTEIN; DROSOPTERIN; INSECT PROTEIN; NUCLEOSIDE DIPHOSPHATE KINASE; PRUNE PROTEIN, DROSOPHILA; PTERIDINE DERIVATIVE;

EID: 0030624791     PISSN: 00652660     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0065-2660(08)60451-4     Document Type: Article
Times cited : (16)

References (166)
  • 1
    • 0017869256 scopus 로고
    • Guanylate kinases from human erythrocytes, hog brain, and rat liver
    • Agarwal K.C., Miech R.P., and Parks Jr. R.E. Guanylate kinases from human erythrocytes, hog brain, and rat liver. Methods Enzymol. 51 (1978) 483-490
    • (1978) Methods Enzymol. , vol.51 , pp. 483-490
    • Agarwal, K.C.1    Miech, R.P.2    Parks Jr., R.E.3
  • 2
    • 0028820545 scopus 로고
    • Evidence of the phenylalanine hydroxylase involvement in biosynthesis of pteridines and hydroxylation of tryptophan in Drosophila melanogaster
    • Alcathiz S., Ruiz-Vazquez P., and Silva F.J. Evidence of the phenylalanine hydroxylase involvement in biosynthesis of pteridines and hydroxylation of tryptophan in Drosophila melanogaster. Ptridines 6 (1995) 135-137
    • (1995) Ptridines , vol.6 , pp. 135-137
    • Alcathiz, S.1    Ruiz-Vazquez, P.2    Silva, F.J.3
  • 3
  • 4
    • 0025143109 scopus 로고
    • Proteolytic conversion of xanthine dehydrogenase from the NAD-dependent type to the O2-dependent type: Amino acid sequence of rat liver xanthine dehydrogenase and identification of the cleavage sites of the enzyme protein during irreversible conversion by trypsin
    • Amaya Y., Yamazaki K., Sato M., Noda K., Nishino T., and Nishino T. Proteolytic conversion of xanthine dehydrogenase from the NAD-dependent type to the O2-dependent type: Amino acid sequence of rat liver xanthine dehydrogenase and identification of the cleavage sites of the enzyme protein during irreversible conversion by trypsin. J. Biol. Chem. 265 24 (1990) 14170-14175
    • (1990) J. Biol. Chem. , vol.265 , Issue.24 , pp. 14170-14175
    • Amaya, Y.1    Yamazaki, K.2    Sato, M.3    Noda, K.4    Nishino, T.5    Nishino, T.6
  • 7
    • 0001323401 scopus 로고
    • The differentiation of eye pigments in Drosophila as studied by transplantation
    • Beadle G.W., and Ephrussi B. The differentiation of eye pigments in Drosophila as studied by transplantation. Genetics 21 (1936) 225-247
    • (1936) Genetics , vol.21 , pp. 225-247
    • Beadle, G.W.1    Ephrussi, B.2
  • 8
    • 0001061237 scopus 로고
    • Development of eye colors in Drosophila: Fat bodies and Malpighian tubes as sources of diffusible substances
    • Beadle G.W. Development of eye colors in Drosophila: Fat bodies and Malpighian tubes as sources of diffusible substances. Genetics 22 (1937) 587-611
    • (1937) Genetics , vol.22 , pp. 587-611
    • Beadle, G.W.1
  • 9
    • 0018088353 scopus 로고
    • Regulation of purine biosynthesis in cultured Drosophila melanogaster cells: I.-Conditional activity of hypoxanthine-guanine-phosphoribosyltransferase and 5′ nucleotidase
    • Becker J.L. Regulation of purine biosynthesis in cultured Drosophila melanogaster cells: I.-Conditional activity of hypoxanthine-guanine-phosphoribosyltransferase and 5′ nucleotidase. Biochemie 60 (1978) 619-625
    • (1978) Biochemie , vol.60 , pp. 619-625
    • Becker, J.L.1
  • 10
    • 0019265866 scopus 로고
    • Regulation of purine biosynthesis in cultured Drosophila melanogaster cells: II. Relationships between hypoxanthine-guanine-phosphoribosyltransferase and 5′ nucleotidase
    • Becker J.L. Regulation of purine biosynthesis in cultured Drosophila melanogaster cells: II. Relationships between hypoxanthine-guanine-phosphoribosyltransferase and 5′ nucleotidase. Biochemie 62 (1980) 665-670
    • (1980) Biochemie , vol.62 , pp. 665-670
    • Becker, J.L.1
  • 11
    • 0024971293 scopus 로고
    • Guanylate kinase from Saccharomyces cerevisiae: Isolation and characterization, crystallization and preliminary X-ray analysis, amino acid sequence and comparison with adenylate kinases
    • Berger A., Schiltz E., and Schulz G.E. Guanylate kinase from Saccharomyces cerevisiae: Isolation and characterization, crystallization and preliminary X-ray analysis, amino acid sequence and comparison with adenylate kinases. Eur. J. Biochem. 184 2 (1989) 433-443
    • (1989) Eur. J. Biochem. , vol.184 , Issue.2 , pp. 433-443
    • Berger, A.1    Schiltz, E.2    Schulz, G.E.3
  • 12
    • 0024416273 scopus 로고
    • Association of low nm23 RNA levels in human primary infiltrating ductal breast carcinomas with lymph node involvement and other histopathological indicators of high metastatic potential
    • Bevilacqua G., Sobel M.E., Liotta L.A., and Steeg P.S. Association of low nm23 RNA levels in human primary infiltrating ductal breast carcinomas with lymph node involvement and other histopathological indicators of high metastatic potential. Cancer Res. 49 (1989) 5185-5190
    • (1989) Cancer Res. , vol.49 , pp. 5185-5190
    • Bevilacqua, G.1    Sobel, M.E.2    Liotta, L.A.3    Steeg, P.S.4
  • 13
    • 0024103455 scopus 로고
    • Analysis of the lethal interaction between the prune and Killer of prune mutations of Drosophila
    • Biggs J., Tripoulas N., Hersperger E., Dearolf C., and Shearn A. Analysis of the lethal interaction between the prune and Killer of prune mutations of Drosophila. Genes Dev. 2 (1988) 1333-1343
    • (1988) Genes Dev. , vol.2 , pp. 1333-1343
    • Biggs, J.1    Tripoulas, N.2    Hersperger, E.3    Dearolf, C.4    Shearn, A.5
  • 14
    • 0025612249 scopus 로고
    • A Drosophila gene that is homologous to a mammalian gene associated with tumor metastasis codes for a nucleoside diphosphate kinase
    • Biggs J., Hersperger E., Steeg P.S., Liotta L.A., and Shearn A. A Drosophila gene that is homologous to a mammalian gene associated with tumor metastasis codes for a nucleoside diphosphate kinase. Cell 63 5 (1990) 933-940
    • (1990) Cell , vol.63 , Issue.5 , pp. 933-940
    • Biggs, J.1    Hersperger, E.2    Steeg, P.S.3    Liotta, L.A.4    Shearn, A.5
  • 15
    • 0027160708 scopus 로고
    • Targeted gene expression as a means of altering cell fates and generating dominant phenotypes
    • Brand A.M., and Perrimon N. Targeted gene expression as a means of altering cell fates and generating dominant phenotypes. Development 118 (1993) 401-415
    • (1993) Development , vol.118 , pp. 401-415
    • Brand, A.M.1    Perrimon, N.2
  • 17
    • 77956733874 scopus 로고    scopus 로고
    • Guanine monophosphate synthetase and the burgundy locus in Drosophila melanogaster
    • Chomey E., and Nash D. Guanine monophosphate synthetase and the burgundy locus in Drosophila melanogaster. In A. Conf. Dros. Res. Num. 37 (1996) 378
    • (1996) In A. Conf. Dros. Res. Num. , vol.37 , pp. 378
    • Chomey, E.1    Nash, D.2
  • 19
    • 0027979186 scopus 로고
    • Molecular and genetic analyses of Drosophila Prat, which encodes the first enzyme of de novo purine biosynthesis
    • Clark D.V. Molecular and genetic analyses of Drosophila Prat, which encodes the first enzyme of de novo purine biosynthesis. Genetics 136 (1994) 547-557
    • (1994) Genetics , vol.136 , pp. 547-557
    • Clark, D.V.1
  • 20
    • 0021888931 scopus 로고
    • Tetrahydrobiopterin biosynthesis: Studies with specifically labeled (2H)NAD(P)H and 2H2O and of the enzymes involved
    • Curtius H.C., Heintel D., Ghisla S., Kuster T., Leimbacher W., and Niederwieser A. Tetrahydrobiopterin biosynthesis: Studies with specifically labeled (2H)NAD(P)H and 2H2O and of the enzymes involved. Eur. J. Biochem. 148 (1985) 413-419
    • (1985) Eur. J. Biochem. , vol.148 , pp. 413-419
    • Curtius, H.C.1    Heintel, D.2    Ghisla, S.3    Kuster, T.4    Leimbacher, W.5    Niederwieser, A.6
  • 22
    • 0025847645 scopus 로고
    • 7-Tetrahydrobiopterin is an uncoupled cofactor for rat hepatic phenylalanine hydroxylase
    • Davis M.D., and Kaufman S. 7-Tetrahydrobiopterin is an uncoupled cofactor for rat hepatic phenylalanine hydroxylase. FEBS Lett. 285 (1991) 17-20
    • (1991) FEBS Lett. , vol.285 , pp. 17-20
    • Davis, M.D.1    Kaufman, S.2
  • 23
    • 0026025853 scopus 로고
    • Conversion of 6-substituted tetrahydropterins to 7-isomers via phenylalanine hydroxylase-generated intermediates
    • Davis M.D., Kaufman S., and Milstien S. Conversion of 6-substituted tetrahydropterins to 7-isomers via phenylalanine hydroxylase-generated intermediates. Proc. Natl. Acad. Sci. USA 88 (1991) 385-389
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 385-389
    • Davis, M.D.1    Kaufman, S.2    Milstien, S.3
  • 24
    • 0026448115 scopus 로고
    • "7-Tetrahydrobiopterin," a naturally occurring analogue of tetrahydrobiopterin, is a cofactor for and a potential inhibitor of the aromatic amino acid hydroxylases
    • Davis M.D., Ribeiro P., Tipper J., and Kaufman S. "7-Tetrahydrobiopterin," a naturally occurring analogue of tetrahydrobiopterin, is a cofactor for and a potential inhibitor of the aromatic amino acid hydroxylases. Proc. Natl. Acad. Sci. USA 89 (1992) 10109-10113
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10109-10113
    • Davis, M.D.1    Ribeiro, P.2    Tipper, J.3    Kaufman, S.4
  • 25
    • 0023820539 scopus 로고
    • b3, a cell-autonomous lethal mutation of Drosophila induced by hybrid dysgenesis
    • b3, a cell-autonomous lethal mutation of Drosophila induced by hybrid dysgenesis. Dev. Biol. 129 (1988) 159-168
    • (1988) Dev. Biol. , vol.129 , pp. 159-168
    • Dearolf, C.R.1    Hersperger, E.2    Shearn, A.3
  • 26
    • 0023820541 scopus 로고
    • b3, a cell-autonomous lethal mutation of Drosophila induced by hybrid dysgenesis
    • b3, a cell-autonomous lethal mutation of Drosophila induced by hybrid dysgenesis. Dev. Biol. 129 (1988) 169-178
    • (1988) Dev. Biol. , vol.129 , pp. 169-178
    • Dearolf, C.R.1    Tripoulas, N.2    Biggs, J.3    Shearn, A.4
  • 27
    • 0018788768 scopus 로고
    • Biosynthesis of "drosopterins" by an enzyme system from Drosophila melanogaster
    • Dorsett D., Yim J.J., and Jacobson K.B. Biosynthesis of "drosopterins" by an enzyme system from Drosophila melanogaster. Biochemistry 18 (1979) 2596-2600
    • (1979) Biochemistry , vol.18 , pp. 2596-2600
    • Dorsett, D.1    Yim, J.J.2    Jacobson, K.B.3
  • 28
    • 0020484774 scopus 로고
    • Purification and biosynthesis of quench spot, a drosopterin precursor in Drosophila melanogaster
    • Dorsett D., and Jacobson K.B. Purification and biosynthesis of quench spot, a drosopterin precursor in Drosophila melanogaster. Biochemistry 21 6 (1982) 1238-1243
    • (1982) Biochemistry , vol.21 , Issue.6 , pp. 1238-1243
    • Dorsett, D.1    Jacobson, K.B.2
  • 31
    • 0017818003 scopus 로고
    • Control of drosopterin synthesis in Drosophila melanogaster: Mutants showing an altered pattern of GTP cyclohydrolase activity during development
    • Evans B.A., and Howells A.J. Control of drosopterin synthesis in Drosophila melanogaster: Mutants showing an altered pattern of GTP cyclohydrolase activity during development. Biochem. Genet. 16 (1978) 13-25
    • (1978) Biochem. Genet. , vol.16 , pp. 13-25
    • Evans, B.A.1    Howells, A.J.2
  • 32
    • 0018388350 scopus 로고
    • Partial purification and some properties of biopterin synthase and dihydropterin oxidase from Drosophila melanogaster
    • Fan C.L., and Brown G.M. Partial purification and some properties of biopterin synthase and dihydropterin oxidase from Drosophila melanogaster. Biochem. Genet 17 (1979) 351-369
    • (1979) Biochem. Genet , vol.17 , pp. 351-369
    • Fan, C.L.1    Brown, G.M.2
  • 33
    • 0022500201 scopus 로고
    • Pigment patterns in mutants affecting the biosynthesis of pteridines and xanthommatin in Drosophila melanogaster
    • Ferre J., Silva F.J., Real M.D., and Mensua J.L. Pigment patterns in mutants affecting the biosynthesis of pteridines and xanthommatin in Drosophila melanogaster. Biochem. Genet. 24 (1986) 545-569
    • (1986) Biochem. Genet. , vol.24 , pp. 545-569
    • Ferre, J.1    Silva, F.J.2    Real, M.D.3    Mensua, J.L.4
  • 34
    • 0026457964 scopus 로고
    • Levels of nm23 mRNA in metastatic malignant melanomas/Inverse correlation to disease progression
    • Florenes V.A., Aamdal S., Myklebost O., Maelandsmo G.M., Bruland O.S., and Fodstad O. Levels of nm23 mRNA in metastatic malignant melanomas/Inverse correlation to disease progression. Cancer Res. 52 (1992) 6088-6091
    • (1992) Cancer Res. , vol.52 , pp. 6088-6091
    • Florenes, V.A.1    Aamdal, S.2    Myklebost, O.3    Maelandsmo, G.M.4    Bruland, O.S.5    Fodstad, O.6
  • 35
    • 0001210403 scopus 로고
    • Conversion of 2-amino 3,4 dihydro-4-oxopteridine to isoxanthopterin in Drosophila melanogaster
    • Forrest H.S., Glassman E., and Mitchell H.K. Conversion of 2-amino 3,4 dihydro-4-oxopteridine to isoxanthopterin in Drosophila melanogaster. Science 124 (1956) 725-726
    • (1956) Science , vol.124 , pp. 725-726
    • Forrest, H.S.1    Glassman, E.2    Mitchell, H.K.3
  • 36
    • 0028100733 scopus 로고
    • Cluster of cytochrome P450 genes on the X chromosome of Drosophila melanogaster
    • Frolov M.V., and Alatortsev V.E. Cluster of cytochrome P450 genes on the X chromosome of Drosophila melanogaster. DNA Cell Biol. 13 (1994) 663-668
    • (1994) DNA Cell Biol. , vol.13 , pp. 663-668
    • Frolov, M.V.1    Alatortsev, V.E.2
  • 37
    • 0028226497 scopus 로고
    • The mRNA product of the Drosophila gene prune is spliced and encodes a protein containing a putative transmembrane domain
    • Frolov M.V., Zverlov V.V., and Alatortzev V.E. The mRNA product of the Drosophila gene prune is spliced and encodes a protein containing a putative transmembrane domain. Mol. Gen. Genet. 242 (1994) 478-483
    • (1994) Mol. Gen. Genet. , vol.242 , pp. 478-483
    • Frolov, M.V.1    Zverlov, V.V.2    Alatortzev, V.E.3
  • 38
    • 0016217820 scopus 로고
    • Developmental capacities of benign and malignant neoplasms of Drosophila
    • Gateff E., and Schneiderman H.A. Developmental capacities of benign and malignant neoplasms of Drosophila. Roux Arch. Dev. Biol. 176 (1974) 23-65
    • (1974) Roux Arch. Dev. Biol. , vol.176 , pp. 23-65
    • Gateff, E.1    Schneiderman, H.A.2
  • 39
    • 0027252959 scopus 로고
    • Guanylate kinase of Escherichia coli K-12
    • Gentry D., Bengra C., Ikehara K., and Cashel M. Guanylate kinase of Escherichia coli K-12. J. Biol. Chem. 268 19 (1993) 14316-14321
    • (1993) J. Biol. Chem. , vol.268 , Issue.19 , pp. 14316-14321
    • Gentry, D.1    Bengra, C.2    Ikehara, K.3    Cashel, M.4
  • 40
    • 0026759740 scopus 로고
    • Molecular analysis of a cytochrome P450 gene of family-4 on the Drosophila X-chromosome
    • Ghandi R., Varak E., and Goldberg M.L. Molecular analysis of a cytochrome P450 gene of family-4 on the Drosophila X-chromosome. DNA Cell Biol. 11 (1992) 397-404
    • (1992) DNA Cell Biol. , vol.11 , pp. 397-404
    • Ghandi, R.1    Varak, E.2    Goldberg, M.L.3
  • 41
    • 0025914104 scopus 로고
    • Nucleoside diphosphate kinase from human erythrocytes: Structural characterization of the two polypeptide chains responsible for heterogeneity of the hexameric enzyme
    • Gilles A.M., Presecan E., Vonica A., and Lascu I. Nucleoside diphosphate kinase from human erythrocytes: Structural characterization of the two polypeptide chains responsible for heterogeneity of the hexameric enzyme. J. Biol. Chem. 266 (1991) 8784-8789
    • (1991) J. Biol. Chem. , vol.266 , pp. 8784-8789
    • Gilles, A.M.1    Presecan, E.2    Vonica, A.3    Lascu, I.4
  • 43
    • 73849161247 scopus 로고
    • + on xanthine dehydrogenase of Drosophila melanogaster. II. Xanthine dehydrogenase activity during development
    • + on xanthine dehydrogenase of Drosophila melanogaster. II. Xanthine dehydrogenase activity during development. Proc. Natl. Acad. Sci. USA 48 (1962) 1712-1718
    • (1962) Proc. Natl. Acad. Sci. USA , vol.48 , pp. 1712-1718
    • Glassman, E.1    McLean, J.2
  • 44
    • 77956716318 scopus 로고
    • The autonomy of reciprocal eye transplant between pn and Kpn
    • Grell E.H. The autonomy of reciprocal eye transplant between pn and Kpn. Drosophila Information Service 32 (1958) 123-124
    • (1958) Drosophila Information Service , vol.32 , pp. 123-124
    • Grell, E.H.1
  • 45
    • 12644290138 scopus 로고
    • "Prune"/"Killer-of-Prune": A complementary lethal system in Drosophila melanogaster affecting pteridine metabolism
    • Pfleiderer W. (Ed), Walter de Gruyter, Berlin
    • Hackstein J.H.P. "Prune"/"Killer-of-Prune": A complementary lethal system in Drosophila melanogaster affecting pteridine metabolism. In: Pfleiderer W. (Ed). Chemistry and Biology of Pteridines (1975), Walter de Gruyter, Berlin 429-436
    • (1975) Chemistry and Biology of Pteridines , pp. 429-436
    • Hackstein, J.H.P.1
  • 46
    • 0026699218 scopus 로고
    • The lethal prune/Killer of prune interaction of Drosophila causes a syndrome resembling human neurofibromatosis (NF1
    • Hackstein J.H.P. The lethal prune/Killer of prune interaction of Drosophila causes a syndrome resembling human neurofibromatosis (NF1. Eur. J. Cell. Biol. 58 (1992) 429-444
    • (1992) Eur. J. Cell. Biol. , vol.58 , pp. 429-444
    • Hackstein, J.H.P.1
  • 47
    • 0008702445 scopus 로고
    • Properties of mutants of Drosophila melanogaster and changes during development as revealed by paper chromatography
    • Hadorn E., and Mitchell H.K. Properties of mutants of Drosophila melanogaster and changes during development as revealed by paper chromatography. Proc. Natl. Acad. Sci. USA 37 (1951) 650-665
    • (1951) Proc. Natl. Acad. Sci. USA , vol.37 , pp. 650-665
    • Hadorn, E.1    Mitchell, H.K.2
  • 48
    • 0003803253 scopus 로고
    • Analysis of a Drosophila Neuroblastoma Gene
    • Ph.D. Thesis, University of Virginia, Charlottesville, VA
    • Hankins, G. R. (1991). "Analysis of a Drosophila Neuroblastoma Gene." Ph.D. Thesis, University of Virginia, Charlottesville, VA
    • (1991)
    • Hankins, G.R.1
  • 49
    • 0028362406 scopus 로고
    • Dihydrofolate reductase of Drosophila: Cloning and expression of a gene with a rare transcript
    • Hao H., Tyshenko M.G., and Walker V.K. Dihydrofolate reductase of Drosophila: Cloning and expression of a gene with a rare transcript. J. Biol. Chem. 269 (1994) 15179-15185
    • (1994) J. Biol. Chem. , vol.269 , pp. 15179-15185
    • Hao, H.1    Tyshenko, M.G.2    Walker, V.K.3
  • 50
    • 0027251094 scopus 로고
    • Feedback regulation mechanisms for the control of GTP cyclohydrolase I activity
    • Harada T., Kagamiyama H., and Hatakeyama K. Feedback regulation mechanisms for the control of GTP cyclohydrolase I activity. Science 260 (1993) 1507-1510
    • (1993) Science , vol.260 , pp. 1507-1510
    • Harada, T.1    Kagamiyama, H.2    Hatakeyama, K.3
  • 51
    • 0026428162 scopus 로고
    • Expression of the anti-metastatic gene nm23 in human breast cancer; association with good prognosis
    • Hennesy C., Henry J.A., May F.E.B., Westly B.R., Angus B., and Lennard T.W.J. Expression of the anti-metastatic gene nm23 in human breast cancer; association with good prognosis. J. Natl. Cancer Inst. 83 (1991) 281-285
    • (1991) J. Natl. Cancer Inst. , vol.83 , pp. 281-285
    • Hennesy, C.1    Henry, J.A.2    May, F.E.B.3    Westly, B.R.4    Angus, B.5    Lennard, T.W.J.6
  • 52
    • 0028787696 scopus 로고
    • A human NDP-kinase B specifically binds single-stranded poly-pyrimidine sequences
    • Hildebrandt M., Lacombe M.-L., Mesnildrey S., and Veron M. A human NDP-kinase B specifically binds single-stranded poly-pyrimidine sequences. Nucleic Acids Res. 23 19 (1995) 3858-3864
    • (1995) Nucleic Acids Res. , vol.23 , Issue.19 , pp. 3858-3864
    • Hildebrandt, M.1    Lacombe, M.-L.2    Mesnildrey, S.3    Veron, M.4
  • 53
    • 0026009463 scopus 로고
    • Positive relationship between expression of anti-metastatic factor (nm23 gene product or nucleoside diphosphate kinase) and good prognosis in human breast cancer
    • Hirayama R., Sawai S., Takagi Y., Mishima Y., Kimura N., Shimada N., Esaki Y., Kurashima C., Utsuyama M., and Hirokawa K. Positive relationship between expression of anti-metastatic factor (nm23 gene product or nucleoside diphosphate kinase) and good prognosis in human breast cancer. J. Natl. Cancer Inst. 83 (1991) 1249-1250
    • (1991) J. Natl. Cancer Inst. , vol.83 , pp. 1249-1250
    • Hirayama, R.1    Sawai, S.2    Takagi, Y.3    Mishima, Y.4    Kimura, N.5    Shimada, N.6    Esaki, Y.7    Kurashima, C.8    Utsuyama, M.9    Hirokawa, K.10
  • 55
    • 0342823334 scopus 로고
    • Report of new mutants: Drosophila melanogaster
    • Ilyina O.V. Report of new mutants: Drosophila melanogaster. Drosophila Information Service 55 (1980) 205
    • (1980) Drosophila Information Service , vol.55 , pp. 205
    • Ilyina, O.V.1
  • 56
    • 0027154954 scopus 로고
    • Adenine phosphoribosyltransferase genes in two Drosophila species: Dosage compensation, a nuclear matrix attachment site, and a novel intron position
    • Johnson D.H. Adenine phosphoribosyltransferase genes in two Drosophila species: Dosage compensation, a nuclear matrix attachment site, and a novel intron position. Mol. Gen. Genet. 238 (1993) 383-389
    • (1993) Mol. Gen. Genet. , vol.238 , pp. 383-389
    • Johnson, D.H.1
  • 57
    • 0023513844 scopus 로고
    • Cloning of a Drosophila melanogaster adenine phosphoribosyltransferase structural gene and deduced amino acid sequence of the enzyme
    • Johnson D.H., Edstrom J.E., Burnett J.B., and Friedman T.B. Cloning of a Drosophila melanogaster adenine phosphoribosyltransferase structural gene and deduced amino acid sequence of the enzyme. Gene 59 (1987) 77-86
    • (1987) Gene , vol.59 , pp. 77-86
    • Johnson, D.H.1    Edstrom, J.E.2    Burnett, J.B.3    Friedman, T.B.4
  • 58
    • 49149142930 scopus 로고
    • Metabolism of guanine and guanosine in larvae of Drosophila melanogaster
    • Johnson M.M., Nash D., and Henderson J.F. Metabolism of guanine and guanosine in larvae of Drosophila melanogaster. Comp. Biochem. Physiol. 66 (1980) 563-567
    • (1980) Comp. Biochem. Physiol. , vol.66 , pp. 563-567
    • Johnson, M.M.1    Nash, D.2    Henderson, J.F.3
  • 59
    • 0021972904 scopus 로고
    • Three purine auxotrophic loci on the second chromosome of Drosophila melanogaster
    • Johnstone M.E., Nash D., and Naguib F.N. Three purine auxotrophic loci on the second chromosome of Drosophila melanogaster. Biochem. Genet 23 (1985) 7-8
    • (1985) Biochem. Genet , vol.23 , pp. 7-8
    • Johnstone, M.E.1    Nash, D.2    Naguib, F.N.3
  • 60
    • 0028174952 scopus 로고
    • The Drosophila molybdenum cofactor gene cinnamon is homologous to three E. coli cofactor proteins and to the rat gephyrin
    • Kamdar K.P., Shelton M.E., and Finnerty V. The Drosophila molybdenum cofactor gene cinnamon is homologous to three E. coli cofactor proteins and to the rat gephyrin. Genetics 137 (1994) 791-801
    • (1994) Genetics , vol.137 , pp. 791-801
    • Kamdar, K.P.1    Shelton, M.E.2    Finnerty, V.3
  • 61
    • 0029786302 scopus 로고    scopus 로고
    • Nucleoside diphosphate kinase: Investigation of the intersubunit contacts by site directed mutagenesis and crystallography
    • in press
    • Karlsson A., Mesnildrey S., Xu Y., Morera S., Janin J., and Veron M. Nucleoside diphosphate kinase: Investigation of the intersubunit contacts by site directed mutagenesis and crystallography. J. Biol. Chem. (1996) in press
    • (1996) J. Biol. Chem.
    • Karlsson, A.1    Mesnildrey, S.2    Xu, Y.3    Morera, S.4    Janin, J.5    Veron, M.6
  • 62
    • 77956772593 scopus 로고
    • Tumor invasion and metastasis in the central nervous system
    • Katz D.A., and Liotta L.A. Tumor invasion and metastasis in the central nervous system. Prog. Neuropathol. 6 (1986) 119-131
    • (1986) Prog. Neuropathol. , vol.6 , pp. 119-131
    • Katz, D.A.1    Liotta, L.A.2
  • 65
    • 0023333651 scopus 로고
    • Sequence of the structural gene for xanthine dehydrogenase (rosy locus) in Drosophila melanogaster
    • Keith T.P., Riley M.A., Kreitman M.E., Lewontin R.C., Curtis D., and Chambers G. Sequence of the structural gene for xanthine dehydrogenase (rosy locus) in Drosophila melanogaster. Genetics 116 (1987) 67-73
    • (1987) Genetics , vol.116 , pp. 67-73
    • Keith, T.P.1    Riley, M.A.2    Kreitman, M.E.3    Lewontin, R.C.4    Curtis, D.5    Chambers, G.6
  • 66
    • 0028844343 scopus 로고
    • Cloning of Drosophila purple gene and expression in E. coli: purple gene encodes PTP synthase
    • Kim N., and Yim J. Cloning of Drosophila purple gene and expression in E. coli: purple gene encodes PTP synthase. Pteridines 6 3 (1995) 119-122
    • (1995) Pteridines , vol.6 , Issue.3 , pp. 119-122
    • Kim, N.1    Yim, J.2
  • 67
    • 0025181057 scopus 로고
    • Isolation and characterization of a cDNA clone encoding rat nucleoside diphosphate kinase
    • Kimura N., Shimada N., Nomura K., and Watanabe K. Isolation and characterization of a cDNA clone encoding rat nucleoside diphosphate kinase. J. Biol. Chem. 265 (1990) 15744-15749
    • (1990) J. Biol. Chem. , vol.265 , pp. 15744-15749
    • Kimura, N.1    Shimada, N.2    Nomura, K.3    Watanabe, K.4
  • 69
    • 0027050284 scopus 로고
    • Cloning and expression of the essential gene for guanylate kinase from yeast
    • Konrad M. Cloning and expression of the essential gene for guanylate kinase from yeast. J. Biol. Chem. 267 36 (1992) 25652-25655
    • (1992) J. Biol. Chem. , vol.267 , Issue.36 , pp. 25652-25655
    • Konrad, M.1
  • 70
    • 0018407854 scopus 로고
    • Purification and properties of the enzymes from Drosophila melanogaster that catalyze the synthesis of sepiapterin from dihydroneopterin triphosphate
    • Krivi G.G., and Brown G.M. Purification and properties of the enzymes from Drosophila melanogaster that catalyze the synthesis of sepiapterin from dihydroneopterin triphosphate. Biochem. Genet. 17 (1979) 371-390
    • (1979) Biochem. Genet. , vol.17 , pp. 371-390
    • Krivi, G.G.1    Brown, G.M.2
  • 71
    • 0025287814 scopus 로고
    • Functional cloning of a nucleoside diphosphate kinase from Dictyostelium discoideum
    • Lacombe M.L., Wallet V., Troll H., and Veron M. Functional cloning of a nucleoside diphosphate kinase from Dictyostelium discoideum. J. Biol. Chem. 265 (1990) 10012-10018
    • (1990) J. Biol. Chem. , vol.265 , pp. 10012-10018
    • Lacombe, M.L.1    Wallet, V.2    Troll, H.3    Veron, M.4
  • 72
    • 0026708128 scopus 로고
    • A Pro/Ser substitution in nucleoside diphosphate kinase of Drosophila melanogaster (mutation Killer of prune) affects stability but not catalytic efficiency of the enzyme
    • Lascu I., Chaffotte A., Limbourg-Bouchon B., and Veron M. A Pro/Ser substitution in nucleoside diphosphate kinase of Drosophila melanogaster (mutation Killer of prune) affects stability but not catalytic efficiency of the enzyme. J. Biol. Chem. 267 (1992) 12775-12781
    • (1992) J. Biol. Chem. , vol.267 , pp. 12775-12781
    • Lascu, I.1    Chaffotte, A.2    Limbourg-Bouchon, B.3    Veron, M.4
  • 73
    • 0025753514 scopus 로고
    • Reduced tumor incidence, metastatic potential, and cytokine responsiveness of nm23-transfected melanoma cells
    • Leone A., Flatow U., King C.R., Sandeen M.A., Margulies I.M., Liotta L.A., and Steeg P.S. Reduced tumor incidence, metastatic potential, and cytokine responsiveness of nm23-transfected melanoma cells. Cell 65 (1991) 25-35
    • (1991) Cell , vol.65 , pp. 25-35
    • Leone, A.1    Flatow, U.2    King, C.R.3    Sandeen, M.A.4    Margulies, I.M.5    Liotta, L.A.6    Steeg, P.S.7
  • 74
    • 0027304816 scopus 로고
    • Transfection of human nm23-H1 into the human MDA-MB-435 breast carcinoma cell line: Effects on tumor metastatic potential, colonization and enzymatic activity
    • Leone A., Flatow U., VanHoutte K., and Steeg P.S. Transfection of human nm23-H1 into the human MDA-MB-435 breast carcinoma cell line: Effects on tumor metastatic potential, colonization and enzymatic activity. Oncogene 8 (1993) 2325-2333
    • (1993) Oncogene , vol.8 , pp. 2325-2333
    • Leone, A.1    Flatow, U.2    VanHoutte, K.3    Steeg, P.S.4
  • 76
    • 0029438051 scopus 로고
    • Remembering Sturtevant
    • Lewis E. Remembering Sturtevant. Genetics 141 (1995) 1227-1230
    • (1995) Genetics , vol.141 , pp. 1227-1230
    • Lewis, E.1
  • 77
    • 77956767578 scopus 로고
    • A new system for fine structure analysis of genes in Drosophila
    • Lifschytz E., and Falk R. A new system for fine structure analysis of genes in Drosophila. Drosophila Information Service 43 (1968) 131
    • (1968) Drosophila Information Service , vol.43 , pp. 131
    • Lifschytz, E.1    Falk, R.2
  • 78
    • 0014554672 scopus 로고
    • The action of the gene prune (pn) in Drosophila melanogaster
    • Lifschytz E., and Falk R. The action of the gene prune (pn) in Drosophila melanogaster. Genet. Res. Camb. 14 (1969) 53-61
    • (1969) Genet. Res. Camb. , vol.14 , pp. 53-61
    • Lifschytz, E.1    Falk, R.2
  • 79
    • 0014522427 scopus 로고
    • A genetic analysis of the Killer-prune (K-pn) locus of Drosophila melanogaster
    • Lifschytz E., and Falk R. A genetic analysis of the Killer-prune (K-pn) locus of Drosophila melanogaster. Genetics 62 (1969) 353-358
    • (1969) Genetics , vol.62 , pp. 353-358
    • Lifschytz, E.1    Falk, R.2
  • 80
    • 0028797125 scopus 로고
    • Nucleoside diphosphate kinase from pea chloroplasts: Purification, cDNA cloning and import into chloroplasts
    • Lubeck J., and Soll J. Nucleoside diphosphate kinase from pea chloroplasts: Purification, cDNA cloning and import into chloroplasts. Planta 196 (1995) 668-673
    • (1995) Planta , vol.196 , pp. 668-673
    • Lubeck, J.1    Soll, J.2
  • 81
    • 0029819176 scopus 로고    scopus 로고
    • Site directed mutagenesis of nm23-H1: Mutation of proline 96 or serine 120 abrogates its motility inhibitory activity upon transfection into human breast carcinoma cells
    • in press
    • MacDonald N.J., Freije J.M.P., Stracke M.L., Manrow R.E., and Steeg P.S. Site directed mutagenesis of nm23-H1: Mutation of proline 96 or serine 120 abrogates its motility inhibitory activity upon transfection into human breast carcinoma cells. J. Biol. Chem. (1996) in press
    • (1996) J. Biol. Chem.
    • MacDonald, N.J.1    Freije, J.M.P.2    Stracke, M.L.3    Manrow, R.E.4    Steeg, P.S.5
  • 82
    • 0020827102 scopus 로고
    • A genetic analysis of the pteridine biosynthetic enzyme, guanosine triphosphate cyclohydrolase, in Drosophila melanogaster
    • Mackay W.J., and Donnell O.'J.M. A genetic analysis of the pteridine biosynthetic enzyme, guanosine triphosphate cyclohydrolase, in Drosophila melanogaster. Genetics 105 (1983) 35-53
    • (1983) Genetics , vol.105 , pp. 35-53
    • Mackay, W.J.1    Donnell, O.'J.M.2
  • 83
    • 0025848403 scopus 로고
    • Brain nitric oxide synthase is a biopterin- and flavin-containing multi-functional oxido-reductase
    • Mayer B., John M., Heinzel B., Werner E.R., Wachter H., Schultz G., and Bohme E. Brain nitric oxide synthase is a biopterin- and flavin-containing multi-functional oxido-reductase. FEBS Lett. 288 (1991) 187-191
    • (1991) FEBS Lett. , vol.288 , pp. 187-191
    • Mayer, B.1    John, M.2    Heinzel, B.3    Werner, E.R.4    Wachter, H.5    Schultz, G.6    Bohme, E.7
  • 85
    • 77956740951 scopus 로고
    • The absence of hypoxanthine-guanine phosphoribosyl-transferase in extracts of Drosophila melanogaster and established embryonic diploid cell lines
    • Moiseenko E.V., and Kakpakov V.T. The absence of hypoxanthine-guanine phosphoribosyl-transferase in extracts of Drosophila melanogaster and established embryonic diploid cell lines. Dros. Info. Serv. 51 (1974) 44-45
    • (1974) Dros. Info. Serv. , vol.51 , pp. 44-45
    • Moiseenko, E.V.1    Kakpakov, V.T.2
  • 86
  • 87
    • 0028063891 scopus 로고
    • Adenosine 5′-diphosphate binding and the active site of nucleoside diphosphate kinase
    • Morera S., Lascu I., Dumas C., LeBras G., Briozzo P., Veron M., and Janin J. Adenosine 5′-diphosphate binding and the active site of nucleoside diphosphate kinase. Biochemistry 33 (1994) 459-467
    • (1994) Biochemistry , vol.33 , pp. 459-467
    • Morera, S.1    Lascu, I.2    Dumas, C.3    LeBras, G.4    Briozzo, P.5    Veron, M.6    Janin, J.7
  • 88
    • 0028091859 scopus 로고
    • Refined X-ray structure of Dictyostelium discoideum nucleoside diphosphate kinase at 1.8 A resolution
    • Morera S., LeBras G., Lascu I., Lacombe M.L., Veron M., and Janin J. Refined X-ray structure of Dictyostelium discoideum nucleoside diphosphate kinase at 1.8 A resolution. J. Mol. Biol. 243 5 (1994) 873-890
    • (1994) J. Mol. Biol. , vol.243 , Issue.5 , pp. 873-890
    • Morera, S.1    LeBras, G.2    Lascu, I.3    Lacombe, M.L.4    Veron, M.5    Janin, J.6
  • 89
    • 0019879440 scopus 로고
    • Purification and properties of guanylate kinase from baker's yeast
    • Mariguchi M., Kohno H., Kamei M., and Tochikura T. Purification and properties of guanylate kinase from baker's yeast. Biochim. Biophys. Acta 662 1 (1981) 165-167
    • (1981) Biochim. Biophys. Acta , vol.662 , Issue.1 , pp. 165-167
    • Mariguchi, M.1    Kohno, H.2    Kamei, M.3    Tochikura, T.4
  • 90
    • 0028264849 scopus 로고
    • Three-dimensional structure of 6-pyruvoyl tetrahydropterin synthase, an enzyme involved in tetrahydrobiopterin biosynthesis
    • Nar H., Huber R., Heizmann C.W., Thony B., and Burgisser D. Three-dimensional structure of 6-pyruvoyl tetrahydropterin synthase, an enzyme involved in tetrahydrobiopterin biosynthesis. EMBO J. 13 6 (1994) 1255-1262
    • (1994) EMBO J. , vol.13 , Issue.6 , pp. 1255-1262
    • Nar, H.1    Huber, R.2    Heizmann, C.W.3    Thony, B.4    Burgisser, D.5
  • 91
    • 77956727995 scopus 로고
    • Paper chromatography of pteridines of prune and clot stocks of Drosophila melanogaster
    • Narayanan Y., and Weir J.A. Paper chromatography of pteridines of prune and clot stocks of Drosophila melanogaster. Genetics 50 (1964) 387-392
    • (1964) Genetics , vol.50 , pp. 387-392
    • Narayanan, Y.1    Weir, J.A.2
  • 92
    • 0028408088 scopus 로고
    • The raspberry locus of Drosophila melanogaster includes an inosine monophosphate dehydrogenase like coding sequence
    • Nash D., Hu S., Leonard N.J., Tiong S.Y., and Fillips D. The raspberry locus of Drosophila melanogaster includes an inosine monophosphate dehydrogenase like coding sequence. Genome 37 (1994) 333-344
    • (1994) Genome , vol.37 , pp. 333-344
    • Nash, D.1    Hu, S.2    Leonard, N.J.3    Tiong, S.Y.4    Fillips, D.5
  • 93
    • 0023061373 scopus 로고
    • P450 genes: Structure, evolution, and regulation
    • Richardson C.C., Boyer P.D., Bawid I.B., and Meister A. (Eds), Annual Reviews Inc., Palo Alto, CA
    • Nebert D.W., and Gonzalez F.J. P450 genes: Structure, evolution, and regulation. In: Richardson C.C., Boyer P.D., Bawid I.B., and Meister A. (Eds). Annual Review of Biochemistry (1987), Annual Reviews Inc., Palo Alto, CA 945-993
    • (1987) Annual Review of Biochemistry , pp. 945-993
    • Nebert, D.W.1    Gonzalez, F.J.2
  • 94
    • 0026759586 scopus 로고
    • A single locus encodes both phenylalanine hydroxylase and tryptophan hydroxylase activities in Drosophila
    • Neckameyer W.S., and White K. A single locus encodes both phenylalanine hydroxylase and tryptophan hydroxylase activities in Drosophila. J. Biol. Chem. 267 (1992) 4199-4206
    • (1992) J. Biol. Chem. , vol.267 , pp. 4199-4206
    • Neckameyer, W.S.1    White, K.2
  • 96
    • 0021142850 scopus 로고
    • The microtubule-associated nucleoside diphosphate kinase
    • Nickerson J.A., and Wells W.W. The microtubule-associated nucleoside diphosphate kinase. J. Biol. Chem. 18 (1984) 11297-11304
    • (1984) J. Biol. Chem. , vol.18 , pp. 11297-11304
    • Nickerson, J.A.1    Wells, W.W.2
  • 98
    • 0024577957 scopus 로고
    • Molecular and developmental genetics of the Punch locus, a pterin biosynthesis gene in Drosophila melanogaster
    • O'Donnell J.M., McLean J.R., and Reynolds E.R. Molecular and developmental genetics of the Punch locus, a pterin biosynthesis gene in Drosophila melanogaster. Dev. Genet 10 (1989) 273-286
    • (1989) Dev. Genet , vol.10 , pp. 273-286
    • O'Donnell, J.M.1    McLean, J.R.2    Reynolds, E.R.3
  • 99
    • 0016679085 scopus 로고
    • Temperature-sensitive prune (pn) mutations of Drosophila melanogaster
    • Orevi N., and Falk R. Temperature-sensitive prune (pn) mutations of Drosophila melanogaster. Mutat. Res 33 (1975) 193-200
    • (1975) Mutat. Res , vol.33 , pp. 193-200
    • Orevi, N.1    Falk, R.2
  • 101
    • 0025264874 scopus 로고
    • Purification and characterization of 6-pyruvoyl-tetrahydropterin synthase from Drosophila melanogaster
    • Park Y.S., Kim J.H., Jacobson K.B., and Yim J.J. Purification and characterization of 6-pyruvoyl-tetrahydropterin synthase from Drosophila melanogaster. Biochim. Biophys. Acta 1038 (1990) 186-194
    • (1990) Biochim. Biophys. Acta , vol.1038 , pp. 186-194
    • Park, Y.S.1    Kim, J.H.2    Jacobson, K.B.3    Yim, J.J.4
  • 102
    • 77956920094 scopus 로고
    • Nucleoside diphosphokinase
    • Boyer P.D. (Ed), Academic Press, New York
    • Parks R., and Agarwal R. Nucleoside diphosphokinase. In: Boyer P.D. (Ed). The Enzymes (1973), Academic Press, New York 307-344
    • (1973) The Enzymes , pp. 307-344
    • Parks, R.1    Agarwal, R.2
  • 103
    • 0000845787 scopus 로고
    • Ommochromes and pteridines
    • Ashburner M., and Wright T.R.F. (Eds), Academic Press, London
    • Phillips J.S., and Forrest H.S. Ommochromes and pteridines. In: Ashburner M., and Wright T.R.F. (Eds). The Genetics and Biology of Drosophila (1980), Academic Press, London 541-623
    • (1980) The Genetics and Biology of Drosophila , pp. 541-623
    • Phillips, J.S.1    Forrest, H.S.2
  • 104
    • 0027293728 scopus 로고
    • Human c-myc transcription factor PuF identified as nm23-H2 nucleoside diphosphate kinase, a candidate suppressor of tumor metastasis
    • Postel E.H., Berberich S.J., Flint S.J., and Ferrone C.A. Human c-myc transcription factor PuF identified as nm23-H2 nucleoside diphosphate kinase, a candidate suppressor of tumor metastasis. Science 261 (1993) 478-480
    • (1993) Science , vol.261 , pp. 478-480
    • Postel, E.H.1    Berberich, S.J.2    Flint, S.J.3    Ferrone, C.A.4
  • 105
    • 0028518725 scopus 로고
    • Sepiapterin reductase and the biosynthesis of tetrahydro-biopterin in Drosophila melanogaster
    • Primus J.P., and Brown G.M. Sepiapterin reductase and the biosynthesis of tetrahydro-biopterin in Drosophila melanogaster. Insect Biochem. Mol. Biol 24 (1994) 907-918
    • (1994) Insect Biochem. Mol. Biol , vol.24 , pp. 907-918
    • Primus, J.P.1    Brown, G.M.2
  • 107
    • 0026669725 scopus 로고
    • The pterin molybdenum cofactors
    • Rajagopalan K.V., and Johnson J.L. The pterin molybdenum cofactors. J. Biol. Chem. 267 15 (1992) 10199-10202
    • (1992) J. Biol. Chem. , vol.267 , Issue.15 , pp. 10199-10202
    • Rajagopalan, K.V.1    Johnson, J.L.2
  • 108
    • 0025701665 scopus 로고
    • The purification of dihydrofolate reductase from Drosophila melanogaster
    • Rancourt S.L., and Walker V.K. The purification of dihydrofolate reductase from Drosophila melanogaster. Biochim. Biophys. Acta 1039 (1990) 261-268
    • (1990) Biochim. Biophys. Acta , vol.1039 , pp. 261-268
    • Rancourt, S.L.1    Walker, V.K.2
  • 109
    • 0024313577 scopus 로고
    • Xanthine dehydrogenase is transported to the Drosophila eye
    • Reaume A.G., Clark S.H., and Chovnik A. Xanthine dehydrogenase is transported to the Drosophila eye. Genetics 123 (1989) 503-509
    • (1989) Genetics , vol.123 , pp. 503-509
    • Reaume, A.G.1    Clark, S.H.2    Chovnik, A.3
  • 110
    • 0029048213 scopus 로고
    • Molecular and biochemical characterization of dNOS: A Drosophila Ca[2+] calmodulin-dependent nitric oxide synthase
    • Regulski M., and Tully T. Molecular and biochemical characterization of dNOS: A Drosophila Ca[2+] calmodulin-dependent nitric oxide synthase. Proc. Natl. Acad. Sci. USA 92 (1995) 9072-9076
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9072-9076
    • Regulski, M.1    Tully, T.2
  • 111
    • 0014409199 scopus 로고
    • 6-Hydroxylation of the pteridine ring by xanthine oxidase
    • Rembold H., and Gutensohn W. 6-Hydroxylation of the pteridine ring by xanthine oxidase. Biochem. Biophys. Res. Commun. 31 (1968) 837-841
    • (1968) Biochem. Biophys. Res. Commun. , vol.31 , pp. 837-841
    • Rembold, H.1    Gutensohn, W.2
  • 114
    • 0026525669 scopus 로고
    • Nucleoside diphosphate kinase/NM23 expression in breast cancer: Lack of correlation with lymph-node metastasis
    • Sastre-Garau X., Lacombe M.L., Jouve M., Veron M., and Magdelenat H. Nucleoside diphosphate kinase/NM23 expression in breast cancer: Lack of correlation with lymph-node metastasis. Int. J. Cancer 50 (1992) 533-538
    • (1992) Int. J. Cancer , vol.50 , pp. 533-538
    • Sastre-Garau, X.1    Lacombe, M.L.2    Jouve, M.3    Veron, M.4    Magdelenat, H.5
  • 116
    • 0026475351 scopus 로고
    • Allosteric characteristics of GTP cyclohydrolase I from Escherichia coli
    • Schoedon G., Redweik U., Frank G., Cotton R.G., and Blau N. Allosteric characteristics of GTP cyclohydrolase I from Escherichia coli. Eur. J. Biochem 210 (1992) 561-568
    • (1992) Eur. J. Biochem , vol.210 , pp. 561-568
    • Schoedon, G.1    Redweik, U.2    Frank, G.3    Cotton, R.G.4    Blau, N.5
  • 117
    • 0022539204 scopus 로고
    • Molybdenum hydroxylases in Drosophila III. Further characterization of the low xanthine dehydroxylase gene
    • Schott D.R., Baldwin M.C., and Finnerty V. Molybdenum hydroxylases in Drosophila III. Further characterization of the low xanthine dehydroxylase gene. Biochem. Genet. 24 (1986) 509-527
    • (1986) Biochem. Genet. , vol.24 , pp. 509-527
    • Schott, D.R.1    Baldwin, M.C.2    Finnerty, V.3
  • 118
    • 4243449579 scopus 로고
    • Aurodrosopterins in eye colour mutants of Drosophila melanogaster
    • Pfleiderer W. (Ed), Walter de Gruyter, Berlin
    • Schwinck I. Aurodrosopterins in eye colour mutants of Drosophila melanogaster. In: Pfleiderer W. (Ed). Chemistry and Biology of Pteridines (1975), Walter de Gruyter, Berlin 919-930
    • (1975) Chemistry and Biology of Pteridines , pp. 919-930
    • Schwinck, I.1
  • 119
    • 0023888075 scopus 로고
    • Inhibition of GTP cyclohydrolase I by pterins
    • Shen R.S., Alam A., and Zhang Y.X. Inhibition of GTP cyclohydrolase I by pterins. Biochim. Biophys. Acta 965 (1988) 9-15
    • (1988) Biochim. Biophys. Acta , vol.965 , pp. 9-15
    • Shen, R.S.1    Alam, A.2    Zhang, Y.X.3
  • 120
    • 0027408957 scopus 로고
    • A second form (beta isoform) of nucleoside diphosphate kinase from rat: Isolation and characterization of complementary genomic DNA and expression
    • Shimada N., Ishikawa N., Munakata Y., Toda T., Watanabe K., and Kimura N. A second form (beta isoform) of nucleoside diphosphate kinase from rat: Isolation and characterization of complementary genomic DNA and expression. J. Biol. Chem. 268 (1993) 2583-2589
    • (1993) J. Biol. Chem. , vol.268 , pp. 2583-2589
    • Shimada, N.1    Ishikawa, N.2    Munakata, Y.3    Toda, T.4    Watanabe, K.5    Kimura, N.6
  • 121
    • 0014430931 scopus 로고
    • Multiple molecular forms of xanthine dehydrogenase and related enzymes. II. Conversion of one form of xanthine dehydrogenase to another by extracts of Drosophila melanogaster
    • Shinoda T., and Glassman E. Multiple molecular forms of xanthine dehydrogenase and related enzymes. II. Conversion of one form of xanthine dehydrogenase to another by extracts of Drosophila melanogaster. Biochim. Biophys. Acta 160 (1968) 178-187
    • (1968) Biochim. Biophys. Acta , vol.160 , pp. 178-187
    • Shinoda, T.1    Glassman, E.2
  • 122
    • 27244462078 scopus 로고
    • Cloning and sequence analysis of a Drosophila melanogaster IMP dehydrogenase
    • Sifri C.D., Wilson K., Smolik S., Forte M., and Ullman B. Cloning and sequence analysis of a Drosophila melanogaster IMP dehydrogenase. Biochim. Biophys. Acta 1217 (1994) 103-106
    • (1994) Biochim. Biophys. Acta , vol.1217 , pp. 103-106
    • Sifri, C.D.1    Wilson, K.2    Smolik, S.3    Forte, M.4    Ullman, B.5
  • 123
    • 0025935083 scopus 로고
    • Genetic and biochemical characterization of little isoxanthopterin (lix), a gene controlling dihydropterin oxidase activity in Drosophila melanogaster
    • Silva F.J., Escriche B., Ordono E., and Ferre J. Genetic and biochemical characterization of little isoxanthopterin (lix), a gene controlling dihydropterin oxidase activity in Drosophila melanogaster. Mol. Gen. Genet 230 (1991) 97-103
    • (1991) Mol. Gen. Genet , vol.230 , pp. 97-103
    • Silva, F.J.1    Escriche, B.2    Ordono, E.3    Ferre, J.4
  • 124
    • 0028867240 scopus 로고
    • The raspberry locus encodes Drosophila inosine monophosphate dehydrogenase
    • Slee R., and Bownes M. The raspberry locus encodes Drosophila inosine monophosphate dehydrogenase. Mol. Gen. Genet. 248 (1995) 755-766
    • (1995) Mol. Gen. Genet. , vol.248 , pp. 755-766
    • Slee, R.1    Bownes, M.2
  • 125
    • 0020674339 scopus 로고
    • Variations in the expression of the gene Pgd due to the effect of chromosomal rearrangements in Drosophila
    • Slobodyanyuk S.Y., and Serov O.L. Variations in the expression of the gene Pgd due to the effect of chromosomal rearrangements in Drosophila. Mol. Gen. Genet 191 (1983) 372-377
    • (1983) Mol. Gen. Genet , vol.191 , pp. 372-377
    • Slobodyanyuk, S.Y.1    Serov, O.L.2
  • 126
    • 0023359653 scopus 로고
    • On the role of sepiapterin reductase in the biosynthesis of tetrahydrobiopterin
    • Smith G.K. On the role of sepiapterin reductase in the biosynthesis of tetrahydrobiopterin. Arch. Biochem. Biophys. 255 (1987) 254-266
    • (1987) Arch. Biochem. Biophys. , vol.255 , pp. 254-266
    • Smith, G.K.1
  • 128
    • 0019967916 scopus 로고
    • Transposition of cloned P elements into Drosophila germ line chromosomes
    • Spradling A.C., and Rubin G.M. Transposition of cloned P elements into Drosophila germ line chromosomes. Science 218 (1982) 341-347
    • (1982) Science , vol.218 , pp. 341-347
    • Spradling, A.C.1    Rubin, G.M.2
  • 131
    • 0023797049 scopus 로고
    • Altered expression of NM23, a gene associated with low tumor metastatic potential, during adenovirus 2 Ela inhibition of experimental metastasis
    • Steeg P.S., Bevilacqua G., Pozzatti R., Liotta L.A., and Sobel M.E. Altered expression of NM23, a gene associated with low tumor metastatic potential, during adenovirus 2 Ela inhibition of experimental metastasis. Cancer Res. 48 (1988) 6550-6554
    • (1988) Cancer Res. , vol.48 , pp. 6550-6554
    • Steeg, P.S.1    Bevilacqua, G.2    Pozzatti, R.3    Liotta, L.A.4    Sobel, M.E.5
  • 132
    • 0026520374 scopus 로고
    • Refined structure of the complex between guanylate kinase and its substrate GMP at 2.0 A resolution
    • Stehle T., and Schulz G.E. Refined structure of the complex between guanylate kinase and its substrate GMP at 2.0 A resolution. J. Mol. Biol. 224 4 (1992) 1127-1141
    • (1992) J. Mol. Biol. , vol.224 , Issue.4 , pp. 1127-1141
    • Stehle, T.1    Schulz, G.E.2
  • 133
    • 0013605216 scopus 로고
    • Molybdoenzymes in Drosophila. IV. Further characterization of the cinnamon phenotype
    • Stilvaletta L.A., Warner C.K., Langley S., and Finnerty V. Molybdoenzymes in Drosophila. IV. Further characterization of the cinnamon phenotype. Mol. Gen. Genet. 213 (1988) 505-512
    • (1988) Mol. Gen. Genet. , vol.213 , pp. 505-512
    • Stilvaletta, L.A.1    Warner, C.K.2    Langley, S.3    Finnerty, V.4
  • 134
    • 0028051486 scopus 로고
    • The Drosophila lethal(2) giant larvae tumor suppressor protein is a component of the cytoskeleton
    • Strand D., Raska I., and Mechler B.M. The Drosophila lethal(2) giant larvae tumor suppressor protein is a component of the cytoskeleton. J. Cell Biol. 27 4 (1994) 1345-1360
    • (1994) J. Cell Biol. , vol.27 , Issue.4 , pp. 1345-1360
    • Strand, D.1    Raska, I.2    Mechler, B.M.3
  • 135
    • 0001758235 scopus 로고
    • A highly specific complementary lethal system in Drosophila melanogaster
    • Sturtevant A.H. A highly specific complementary lethal system in Drosophila melanogaster. Genetics 41 (1956) 118-123
    • (1956) Genetics , vol.41 , pp. 118-123
    • Sturtevant, A.H.1
  • 136
    • 0021765267 scopus 로고
    • Intermediates in the enzymic synthesis of tetrahydrobiopterin in Drosophila melanogaster
    • Switchenko A.C., Primus J.P., and Brown G.M. Intermediates in the enzymic synthesis of tetrahydrobiopterin in Drosophila melanogaster. Biochem. Biophys. Res. Commun 120 (1984) 754-760
    • (1984) Biochem. Biophys. Res. Commun , vol.120 , pp. 754-760
    • Switchenko, A.C.1    Primus, J.P.2    Brown, G.M.3
  • 137
    • 0021953762 scopus 로고
    • The enzymatic conversion of dihydroneopterin triphosphate to tripolyphosphate and 6-pyruvoyl-tetrahydropterin, an intermediate in the biosynthesis of other pterins in Drosophila melanogaster
    • Switchenko A.C., and Brown G.M. The enzymatic conversion of dihydroneopterin triphosphate to tripolyphosphate and 6-pyruvoyl-tetrahydropterin, an intermediate in the biosynthesis of other pterins in Drosophila melanogaster. J. Biol. Chem 260 (1985) 2945-2951
    • (1985) J. Biol. Chem , vol.260 , pp. 2945-2951
    • Switchenko, A.C.1    Brown, G.M.2
  • 138
    • 0026074997 scopus 로고
    • Isolation and characterization of the prune locus of Drosophila melanogaster
    • Teng D.H., Bender L.B., Engele C.M., Tsubota S.I., and Venkatesh T.R. Isolation and characterization of the prune locus of Drosophila melanogaster. Genetics 128 (1991) 373-380
    • (1991) Genetics , vol.128 , pp. 373-380
    • Teng, D.H.1    Bender, L.B.2    Engele, C.M.3    Tsubota, S.I.4    Venkatesh, T.R.5
  • 139
    • 0027283558 scopus 로고
    • The expression of the Drosophila awd gene during normal development and in neoplastic brain tumors caused by Igl mutations
    • Timmons L., Hersperger E., Woodhouse E., Xu J., Liu L.-Z., and Shearn A. The expression of the Drosophila awd gene during normal development and in neoplastic brain tumors caused by Igl mutations. Dev. Biol 158 (1993) 364-379
    • (1993) Dev. Biol , vol.158 , pp. 364-379
    • Timmons, L.1    Hersperger, E.2    Woodhouse, E.3    Xu, J.4    Liu, L.-Z.5    Shearn, A.6
  • 140
    • 0028981364 scopus 로고
    • Kpm which revert the prune/Killer of prune lethal interaction affect conserved residues that are involved in nucleoside diphosphate kinase substrate binding and catalysis
    • Kpm which revert the prune/Killer of prune lethal interaction affect conserved residues that are involved in nucleoside diphosphate kinase substrate binding and catalysis. J. Biol. Chem. 270 (1995) 23021-23030
    • (1995) J. Biol. Chem. , vol.270 , pp. 23021-23030
    • Timmons, L.1    Xu, J.2    Hersperger, G.3    Deng, X.4    Shearn, A.5
  • 141
    • 0030455822 scopus 로고    scopus 로고
    • Germline transformation using a prune cDNA rescues prune/Killer of prune letrality and the prune eye color phenotype
    • in press
    • L. Timmons, A. Shearn (1996). Germline transformation using a prune cDNA rescues prune/Killer of prune letrality and the prune eye color phenotype. Genetics (in press)
    • (1996) Genetics
    • Timmons, L.1    Shearn, A.2
  • 142
    • 0024674250 scopus 로고
    • Drosophila purine auxotrophy: New alleles of adenosine 2 exhibiting a complex visible phenotype
    • Tiong S.Y.K., Keizer C., Nash D., and Patterson D. Drosophila purine auxotrophy: New alleles of adenosine 2 exhibiting a complex visible phenotype. Biochem. Genet. 27 (1989) 333-348
    • (1989) Biochem. Genet. , vol.27 , pp. 333-348
    • Tiong, S.Y.K.1    Keizer, C.2    Nash, D.3    Patterson, D.4
  • 143
    • 0025254083 scopus 로고
    • Genetic analysis of the adenosine3 (Gart) region of the second chromosome of Drosophila melanogaster
    • Tiong S.Y.K., and Nash D. Genetic analysis of the adenosine3 (Gart) region of the second chromosome of Drosophila melanogaster. Genetics 124 (1990) 889-897
    • (1990) Genetics , vol.124 , pp. 889-897
    • Tiong, S.Y.K.1    Nash, D.2
  • 144
    • 0027373195 scopus 로고
    • Separate nuclear genes encode cytosolic and mitochondrial nucleoside diphosphate kinase in Dictyostelium discoideum
    • Troll H., Winckler T., Lascu I., Muller N., Saurin W., Veron M., and Mutzel R. Separate nuclear genes encode cytosolic and mitochondrial nucleoside diphosphate kinase in Dictyostelium discoideum. J. Biol. Chem 268 (1993) 25469-25475
    • (1993) J. Biol. Chem , vol.268 , pp. 25469-25475
    • Troll, H.1    Winckler, T.2    Lascu, I.3    Muller, N.4    Saurin, W.5    Veron, M.6    Mutzel, R.7
  • 145
    • 0020479929 scopus 로고
    • Purification and properties of dihydropterin oxidase from Drosophila melanogaster
    • Unnash T.R., and Brown G.M. Purification and properties of dihydropterin oxidase from Drosophila melanogaster. J. Biol. Chem 257 (1982) 14211-14216
    • (1982) J. Biol. Chem , vol.257 , pp. 14211-14216
    • Unnash, T.R.1    Brown, G.M.2
  • 146
    • 0026660533 scopus 로고
    • Molecular cloning and functional expression of the second mouse nm23/NDP kinase gene, nm23-M2
    • Urano T., Takamiya K., Furukawa K., and Shiku H. Molecular cloning and functional expression of the second mouse nm23/NDP kinase gene, nm23-M2. FEBS Lett 309 (1992) 358-362
    • (1992) FEBS Lett , vol.309 , pp. 358-362
    • Urano, T.1    Takamiya, K.2    Furukawa, K.3    Shiku, H.4
  • 147
    • 0029093085 scopus 로고
    • Overexpression of DR-nm23, a protein encoded by a member of the nm23 gene family, inhibits granulocyte differentiation and induces apoptosis in 32Dc13 myeloid cells
    • Venturelli D., Martinez R., Melotti P., Casella I., Peschle C., Cucco C., Spampinato G., Darzynkiewicz Z., and Calabretta B. Overexpression of DR-nm23, a protein encoded by a member of the nm23 gene family, inhibits granulocyte differentiation and induces apoptosis in 32Dc13 myeloid cells. Proc. Natl. Acad. Sc. USA 92 16 (1995) 7435-7439
    • (1995) Proc. Natl. Acad. Sc. USA , vol.92 , Issue.16 , pp. 7435-7439
    • Venturelli, D.1    Martinez, R.2    Melotti, P.3    Casella, I.4    Peschle, C.5    Cucco, C.6    Spampinato, G.7    Darzynkiewicz, Z.8    Calabretta, B.9
  • 149
    • 0020478852 scopus 로고
    • Drosophila malanogaster ma-I mutants are defective in the sulfuration of desulfo Mo hydroxylases
    • Wahl R.C., Warner C.K., Finnerty V., and Rajagopalan K.V. Drosophila malanogaster ma-I mutants are defective in the sulfuration of desulfo Mo hydroxylases. J. Biol. Chem. 257 (1982) 3958-3962
    • (1982) J. Biol. Chem. , vol.257 , pp. 3958-3962
    • Wahl, R.C.1    Warner, C.K.2    Finnerty, V.3    Rajagopalan, K.V.4
  • 150
  • 151
    • 0021982971 scopus 로고
    • Comparative activity of rat liver dihydrofolate reductase with 7,8-dihydrofolate and other 7,8-dihydropteridines
    • Webber S., and Whiteley J.M. Comparative activity of rat liver dihydrofolate reductase with 7,8-dihydrofolate and other 7,8-dihydropteridines. Arch. Biochem. Biophys. 236 (1985) 681-690
    • (1985) Arch. Biochem. Biophys. , vol.236 , pp. 681-690
    • Webber, S.1    Whiteley, J.M.2
  • 152
    • 0022650158 scopus 로고
    • Purification and characterization of GTP cyclohydrolase I from Drosophila melanogaster
    • Weisberg E.P., and Donnell O.'J.M. Purification and characterization of GTP cyclohydrolase I from Drosophila melanogaster. J. Biol. Chem 261 3 (1986) 1453-1458
    • (1986) J. Biol. Chem , vol.261 , Issue.3 , pp. 1453-1458
    • Weisberg, E.P.1    Donnell, O.'J.M.2
  • 153
    • 0021719829 scopus 로고
    • Purification and properties of the enzymes from Drosophila melanogaster that catalyze the conversion of dihydroneopterin triphosphate to the pyrim-idodiazepine precursor of drosopterins
    • Wiederrecht G.J., and Brown G.M. Purification and properties of the enzymes from Drosophila melanogaster that catalyze the conversion of dihydroneopterin triphosphate to the pyrim-idodiazepine precursor of drosopterins. J. Biol. Chem. 259 (1984) 14121-14127
    • (1984) J. Biol. Chem. , vol.259 , pp. 14121-14127
    • Wiederrecht, G.J.1    Brown, G.M.2
  • 154
    • 0019888486 scopus 로고
    • The isolation and identification of an intermediate involved in the biosynthesis of drosopterin in Drosophila melanogaster
    • Wiederrecht G.J., Paton D.R., and Brown G.M. The isolation and identification of an intermediate involved in the biosynthesis of drosopterin in Drosophila melanogaster. J. Biol. Chem 256 (1981) 10399-10402
    • (1981) J. Biol. Chem , vol.256 , pp. 10399-10402
    • Wiederrecht, G.J.1    Paton, D.R.2    Brown, G.M.3
  • 155
    • 0021341967 scopus 로고
    • Enzymatic conversion of dihydroneopterin triphosphate to the pyrimidodiazepine intermediate involved in the biosynthesis of the drosopterins in Drosophila melanogaster
    • Wiederrecht G.J., Paton D.R., and Brown G.M. Enzymatic conversion of dihydroneopterin triphosphate to the pyrimidodiazepine intermediate involved in the biosynthesis of the drosopterins in Drosophila melanogaster. J. Biol. Chem 259 (1984) 2195-2200
    • (1984) J. Biol. Chem , vol.259 , pp. 2195-2200
    • Wiederrecht, G.J.1    Paton, D.R.2    Brown, G.M.3
  • 156
    • 0026750592 scopus 로고
    • Human dihydrofolate reductase: Reduction of alternative substrates, pH effects, and inhibition by deazafolates
    • Williams E.A., and Morrison J.F. Human dihydrofolate reductase: Reduction of alternative substrates, pH effects, and inhibition by deazafolates. Biochemistry 31 (1992) 6801-6811
    • (1992) Biochemistry , vol.31 , pp. 6801-6811
    • Williams, E.A.1    Morrison, J.F.2
  • 157
    • 0027764466 scopus 로고
    • Crystal structure of Myxococcus xanthus nucleoside diphosphate kinase and its interaction with a nucleotide substrate at 2.0 A resolution
    • Williams R.L., Oren D.A., Munoz-Dorado J., Inouye S., Inouye M., and Arnold E. Crystal structure of Myxococcus xanthus nucleoside diphosphate kinase and its interaction with a nucleotide substrate at 2.0 A resolution. J. Mol. Biol. 234 (1993) 1230-1247
    • (1993) J. Mol. Biol. , vol.234 , pp. 1230-1247
    • Williams, R.L.1    Oren, D.A.2    Munoz-Dorado, J.3    Inouye, S.4    Inouye, M.5    Arnold, E.6
  • 158
    • 0017711753 scopus 로고
    • Mechanism of suppression in Drosophila. V. Localization of the purple mutant of Drosophila melanogaster in the pteridine biosynthetic pathway
    • Wilson T.G., and Jacobson K.B. Mechanism of suppression in Drosophila. V. Localization of the purple mutant of Drosophila melanogaster in the pteridine biosynthetic pathway. Biochem. Genet. 15 (1977) 321-332
    • (1977) Biochem. Genet. , vol.15 , pp. 321-332
    • Wilson, T.G.1    Jacobson, K.B.2
  • 160
    • 0025941465 scopus 로고
    • The discs-large tumor suppressor gene of Drosophila encodes a guanylate kinase homolog localized at septate junctions
    • Woods D., and Bryant P. The discs-large tumor suppressor gene of Drosophila encodes a guanylate kinase homolog localized at septate junctions. Cell 66 3 (1991) 451-464
    • (1991) Cell , vol.66 , Issue.3 , pp. 451-464
    • Woods, D.1    Bryant, P.2
  • 161
    • 0030220853 scopus 로고    scopus 로고
    • The enzymatic activity of Drosophila AWD/NDP kinase is necessary but not sufficient for its biological function
    • Xu J., Liu L.-Z., Deng X., Timmons L., Hersperger E., Steeg P.S., Veron M., and Shearn A. The enzymatic activity of Drosophila AWD/NDP kinase is necessary but not sufficient for its biological function. Dev. Biol. 177 (1996) 544-557
    • (1996) Dev. Biol. , vol.177 , pp. 544-557
    • Xu, J.1    Liu, L.-Z.2    Deng, X.3    Timmons, L.4    Hersperger, E.5    Steeg, P.S.6    Veron, M.7    Shearn, A.8
  • 162
    • 77956770713 scopus 로고
    • Electrophoretic variants of xanthine dehydrogenase in Drosophila melanogaster
    • Yen T.T., and Glassman E. Electrophoretic variants of xanthine dehydrogenase in Drosophila melanogaster. Genetics 54 (1966) 369-370
    • (1966) Genetics , vol.54 , pp. 369-370
    • Yen, T.T.1    Glassman, E.2
  • 163
    • 77956789159 scopus 로고
    • A new enzyme in pteridine metabolism that cleaves the side chain of dihydroneopterin triphosphate
    • Yim J.J., Crummett D.D., and Jacobson K.B. A new enzyme in pteridine metabolism that cleaves the side chain of dihydroneopterin triphosphate. Fed. Proc. 6 (1978) 1344
    • (1978) Fed. Proc. , vol.6 , pp. 1344
    • Yim, J.J.1    Crummett, D.D.2    Jacobson, K.B.3
  • 164
    • 33749026724 scopus 로고
    • Detection and some properties of an enzyme from Drosophila melanogaster that releases the side chain from dihydroneopterin triphosphate
    • Yim J.J., Jacobson K.B., and Crummett D. Detection and some properties of an enzyme from Drosophila melanogaster that releases the side chain from dihydroneopterin triphosphate. Insect Biochem. 11 (1981) 363-370
    • (1981) Insect Biochem. , vol.11 , pp. 363-370
    • Yim, J.J.1    Jacobson, K.B.2    Crummett, D.3
  • 166
    • 77956766972 scopus 로고
    • The biology of pteridines in insects
    • Ziegler I., and Harmsen R. The biology of pteridines in insects. Adv. Insect Physiol. 6 (1969) 139-203
    • (1969) Adv. Insect Physiol. , vol.6 , pp. 139-203
    • Ziegler, I.1    Harmsen, R.2


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