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Volumn 12, Issue 1, 2004, Pages 75-84

Crystal Structure of Human Thymidine Phosphorylase in Complex with a Small Molecule Inhibitor

Author keywords

[No Author keywords available]

Indexed keywords

5 CHLORO 6 [1 (2 IMINOPYRROLIDINYL)METHYL]URACIL; ANTINEOPLASTIC AGENT; CHLORIDE; PHOSPHORYLASE; PLATELET DERIVED ENDOTHELIAL CELL GROWTH FACTOR; PYRIMIDINE NUCLEOTIDE; THYMIDINE PHOSPHORYLASE; UNCLASSIFIED DRUG; URACIL DERIVATIVE;

EID: 1642559369     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2003.11.018     Document Type: Article
Times cited : (84)

References (54)
  • 2
    • 0026656211 scopus 로고
    • Neurotrophic action of gliostatin on cortical neurons. Identity of gliostatin and platelet-derived endothelial cell growth factor
    • Asai K., Nakanishi K., Isobe I., Eksioglu Y.Z., Hirano A., Hama K., Miyamoto T., Kato T. Neurotrophic action of gliostatin on cortical neurons. Identity of gliostatin and platelet-derived endothelial cell growth factor. J. Biol. Chem. 267:1992;20311-20316.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20311-20316
    • Asai, K.1    Nakanishi, K.2    Isobe, I.3    Eksioglu, Y.Z.4    Hirano, A.5    Hama, K.6    Miyamoto, T.7    Kato, T.8
  • 3
    • 0028103275 scopus 로고
    • Collaborative Computational Project 4) the CCP4 suite: Programs for protein crystallography
    • CCP4 Collaborative Computational Project 4) The CCP4 suite. programs for protein crystallography Acta Crystallogr. D. 50:1994;760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 4
    • 0037448395 scopus 로고    scopus 로고
    • Potential tumor-selective nitroimidazolylmethyluracil prodrug derivatives: Inhibitors of the angiogenic enzyme thymidine phosphorylase
    • Cole C., Reigan P., Gbaj A., Edwards P.N., Douglas K.T., Stratford I.J., Freeman S., Jaffar M. Potential tumor-selective nitroimidazolylmethyluracil prodrug derivatives. inhibitors of the angiogenic enzyme thymidine phosphorylase J. Med. Chem. 46:2003;207-209.
    • (2003) J. Med. Chem. , vol.46 , pp. 207-209
    • Cole, C.1    Reigan, P.2    Gbaj, A.3    Edwards, P.N.4    Douglas, K.T.5    Stratford, I.J.6    Freeman, S.7    Jaffar, M.8
  • 5
    • 0031449585 scopus 로고    scopus 로고
    • Overexpression of the angiogenic factor platelet-derived endothelial cell growth factor/thymidine phosphorylase in psoriatic epidermis
    • Creamer D., Jaggar R., Allen M., Bicknell R., Barker J. Overexpression of the angiogenic factor platelet-derived endothelial cell growth factor/thymidine phosphorylase in psoriatic epidermis. Br. J. Dermatol. 137:1997;851-855.
    • (1997) Br. J. Dermatol. , vol.137 , pp. 851-855
    • Creamer, D.1    Jaggar, R.2    Allen, M.3    Bicknell, R.4    Barker, J.5
  • 7
    • 0019404119 scopus 로고
    • Catabolism of thymidine in human blood platelets: Purification and properties of thymidine phosphorylase
    • Desgranges C., Razaka G., Rabaud M., Bricaud H. Catabolism of thymidine in human blood platelets. purification and properties of thymidine phosphorylase Biochim. Biophys. Acta. 654:1981;211-218.
    • (1981) Biochim. Biophys. Acta , vol.654 , pp. 211-218
    • Desgranges, C.1    Razaka, G.2    Rabaud, M.3    Bricaud, H.4
  • 8
    • 0031226772 scopus 로고    scopus 로고
    • Empirical scoring functions.1. The development of a fast empirical scoring function to estimate the binding affinity of ligands in receptor complexes
    • Eldridge M.D., Murray C.W., Auton T.R., Paolini G.V., Mee R.P., Murray C.W. Empirical scoring functions.1. The development of a fast empirical scoring function to estimate the binding affinity of ligands in receptor complexes. J. Comput. Aided Mol. Des. 11:1997;425-445.
    • (1997) J. Comput. Aided Mol. Des. , vol.11 , pp. 425-445
    • Eldridge, M.D.1    Murray, C.W.2    Auton, T.R.3    Paolini, G.V.4    Mee, R.P.5    Murray, C.W.6
  • 9
    • 0033119938 scopus 로고    scopus 로고
    • Further additions to MolScript version 1.4, including reading and contouring of electron-density maps
    • Esnouf R.M. Further additions to MolScript version 1.4, including reading and contouring of electron-density maps. Acta Crystallogr. D. 55:1999;938-940.
    • (1999) Acta Crystallogr. D , vol.55 , pp. 938-940
    • Esnouf, R.M.1
  • 10
    • 0030027519 scopus 로고    scopus 로고
    • The angiogenic factor platelet-derived endothelial cell growth factor/thymidine phosphorylase is up-regulated in breast cancer epithelium and endothelium
    • Fox S.B., Westwood M., Moghaddam A., Comley M., Turley H., Whitehouse R.M., Bicknell R., Gatter K.C., Harris A.L. The angiogenic factor platelet-derived endothelial cell growth factor/thymidine phosphorylase is up-regulated in breast cancer epithelium and endothelium. Br. J. Cancer. 73:1996;275-280.
    • (1996) Br. J. Cancer , vol.73 , pp. 275-280
    • Fox, S.B.1    Westwood, M.2    Moghaddam, A.3    Comley, M.4    Turley, H.5    Whitehouse, R.M.6    Bicknell, R.7    Gatter, K.C.8    Harris, A.L.9
  • 11
    • 0034657004 scopus 로고    scopus 로고
    • Structure and activity of specific inhibitors of thymidine phosphorylase to potentiate the function of antitumor 2′-deoxyribonucleosides
    • Fukushima M., Suzuki N., Emura T., Yano S., Kazuno H., Tada Y., Yamada Y., Asao T. Structure and activity of specific inhibitors of thymidine phosphorylase to potentiate the function of antitumor 2′- deoxyribonucleosides. Biochem. Pharmacol. 59:2000;1227-1236.
    • (2000) Biochem. Pharmacol. , vol.59 , pp. 1227-1236
    • Fukushima, M.1    Suzuki, N.2    Emura, T.3    Yano, S.4    Kazuno, H.5    Tada, Y.6    Yamada, Y.7    Asao, T.8
  • 12
    • 0035971738 scopus 로고    scopus 로고
    • A smooth permittivity function for Poisson-Boltzmann solvation methods
    • Grant J.A., Pickup B.T., Nicholls A. A smooth permittivity function for Poisson-Boltzmann solvation methods. J. Comput. Chem. 22:2001;608-640.
    • (2001) J. Comput. Chem. , vol.22 , pp. 608-640
    • Grant, J.A.1    Pickup, B.T.2    Nicholls, A.3
  • 13
    • 0037571112 scopus 로고    scopus 로고
    • Merck molecular force field.1. Basis, form, scope, parameterization, and performance of mmff94
    • Halgren T.A., Halgren T.A. Merck molecular force field.1. Basis, form, scope, parameterization, and performance of mmff94. J. Comput. Chem. 17:1996;490-519.
    • (1996) J. Comput. Chem. , vol.17 , pp. 490-519
    • Halgren, T.A.1    Halgren, T.A.2
  • 14
    • 0030442990 scopus 로고    scopus 로고
    • Positioning hydrogen atoms by optimizing hydrogen-bond networks in protein structures
    • Hooft R.W.W., Sander C., Vriend G., Hooft R.W.W. Positioning hydrogen atoms by optimizing hydrogen-bond networks in protein structures. Proteins. 26:1996;363-376.
    • (1996) Proteins , vol.26 , pp. 363-376
    • Hooft, R.W.W.1    Sander, C.2    Vriend, G.3    Hooft, R.W.W.4
  • 15
    • 0032857363 scopus 로고    scopus 로고
    • Expression of the angiogenic protein, platelet-derived endothelial cell growth factor, in coronary atherosclerotic plaques: In vivo correlation of lesional microvessel density and constrictive vascular remodeling
    • Ignatescu M.C., Gharehbaghi-Schnell E., Hassan A., Rezaie-Majd S., Korschineck I., Schleef R.R., Glogar H.D., Lang I.M. Expression of the angiogenic protein, platelet-derived endothelial cell growth factor, in coronary atherosclerotic plaques. in vivo correlation of lesional microvessel density and constrictive vascular remodeling Arterioscler. Thromb. Vasc. Biol. 19:1999;2340-2347.
    • (1999) Arterioscler. Thromb. Vasc. Biol. , vol.19 , pp. 2340-2347
    • Ignatescu, M.C.1    Gharehbaghi-Schnell, E.2    Hassan, A.3    Rezaie-Majd, S.4    Korschineck, I.5    Schleef, R.R.6    Glogar, H.D.7    Lang, I.M.8
  • 16
    • 0015217521 scopus 로고
    • Cytoplasmic uridine phosphoryaseft liver. Characterization and kinetics
    • Kraut A., Yamada E.W. Cytoplasmic uridine phosphoryaseft liver. Characterization and kinetics. J. Biol. Chem. 246:1971;2021-2030.
    • (1971) J. Biol. Chem. , vol.246 , pp. 2021-2030
    • Kraut, A.1    Yamada, E.W.2
  • 17
    • 0014409337 scopus 로고
    • Pentosyl transfer mechanisms of the mammalian nucleoside phosphorylases
    • Krenitsky T.A. Pentosyl transfer mechanisms of the mammalian nucleoside phosphorylases. J. Biol. Chem. 243:1968;2871-2875.
    • (1968) J. Biol. Chem. , vol.243 , pp. 2871-2875
    • Krenitsky, T.A.1
  • 18
    • 0020474050 scopus 로고
    • Correlation of substrate-stabilization patterns with proposed mechanisms for three nucleoside phosphorylases
    • Krenitsky T.A., Tuttle J.V. Correlation of substrate-stabilization patterns with proposed mechanisms for three nucleoside phosphorylases. Biochim. Biophys. Acta. 703:1982;247-249.
    • (1982) Biochim. Biophys. Acta , vol.703 , pp. 247-249
    • Krenitsky, T.A.1    Tuttle, J.V.2
  • 19
    • 0001501064 scopus 로고
    • Pyrimidine nucleosidases: Their classification and relationship to uric acid ribonucleoside phosphorylase
    • Krenitsky T.A., Mellors J.W., Barclay R.K. Pyrimidine nucleosidases. their classification and relationship to uric acid ribonucleoside phosphorylase J. Biol. Chem. 240:1965;1281-1286.
    • (1965) J. Biol. Chem. , vol.240 , pp. 1281-1286
    • Krenitsky, T.A.1    Mellors, J.W.2    Barclay, R.K.3
  • 20
    • 0019876093 scopus 로고
    • Purine nucleoside synthesis, an efficient method employing nucleoside phosphorylases
    • Krenitsky T.A., Koszalka G.W., Tuttle J.V. Purine nucleoside synthesis, an efficient method employing nucleoside phosphorylases. Biochemistry. 20:1981;3615-3621.
    • (1981) Biochemistry , vol.20 , pp. 3615-3621
    • Krenitsky, T.A.1    Koszalka, G.W.2    Tuttle, J.V.3
  • 21
    • 0014197030 scopus 로고
    • Inhibition of thymidine phosphorylase by 6-aminothymine and derivatives of 6-aminouracil
    • Langen P., Etzold G., Barwolff D., Preussel B. Inhibition of thymidine phosphorylase by 6-aminothymine and derivatives of 6-aminouracil. Biochem. Pharmacol. 16:1967;1833-1837.
    • (1967) Biochem. Pharmacol. , vol.16 , pp. 1833-1837
    • Langen, P.1    Etzold, G.2    Barwolff, D.3    Preussel, B.4
  • 22
    • 0027169515 scopus 로고
    • Main-chain bond lengths and bond angles in protein structures
    • Laskowski R.A., Moss D.S., Thornton J.M. Main-chain bond lengths and bond angles in protein structures. J. Mol. Biol. 231:1993;1049-1067.
    • (1993) J. Mol. Biol. , vol.231 , pp. 1049-1067
    • Laskowski, R.A.1    Moss, D.S.2    Thornton, J.M.3
  • 24
    • 0034929414 scopus 로고    scopus 로고
    • A new software routine that automates the fitting of protein X-ray crystallographic electron-density maps
    • Levitt D.G. A new software routine that automates the fitting of protein X-ray crystallographic electron-density maps. Acta Crystallogr. D. 57:2001;7-9.
    • (2001) Acta Crystallogr. D , vol.57 , pp. 7-9
    • Levitt, D.G.1
  • 26
    • 0029997353 scopus 로고    scopus 로고
    • Thymidine phosphorylase/platelet-derived endothelial cell growth factor expression associated with hepatic metastasis in gastric carcinoma
    • Maeda K., Chung Y.S., Ogawa Y., Takatsuka S., Kang S.M., Ogawa M., Sawada T., Onoda N., Kato Y., Sowa M. Thymidine phosphorylase/platelet-derived endothelial cell growth factor expression associated with hepatic metastasis in gastric carcinoma. Br. J. Cancer. 73:1996;884-888.
    • (1996) Br. J. Cancer , vol.73 , pp. 884-888
    • Maeda, K.1    Chung, Y.S.2    Ogawa, Y.3    Takatsuka, S.4    Kang, S.M.5    Ogawa, M.6    Sawada, T.7    Onoda, N.8    Kato, Y.9    Sowa, M.10
  • 28
    • 0028057108 scopus 로고    scopus 로고
    • Raster 3D version 2.0 - A program for photorealistic molecular graphics
    • Merrit E.A., Murphy M.E.P. Raster 3D version 2.0 - a program for photorealistic molecular graphics. Acta Crystallogr. D. 50:2003;869-873.
    • (2003) Acta Crystallogr. D , vol.50 , pp. 869-873
    • Merrit, E.A.1    Murphy, M.E.P.2
  • 29
    • 0032127244 scopus 로고    scopus 로고
    • Design of a novel oral fluoropyrimidine carbamate, capecitabine, which generates 5-fluorouracil selectively in tumours by enzymes concentrated in human liver and cancer tissue
    • Miwa M., Ura M., Nishida M., Sawada N., Ishikawa T., Mori K., Shimma N., Umeda I., Ishitsuka H. Design of a novel oral fluoropyrimidine carbamate, capecitabine, which generates 5-fluorouracil selectively in tumours by enzymes concentrated in human liver and cancer tissue. Eur. J. Cancer. 34:1998;1274-1281.
    • (1998) Eur. J. Cancer , vol.34 , pp. 1274-1281
    • Miwa, M.1    Ura, M.2    Nishida, M.3    Sawada, N.4    Ishikawa, T.5    Mori, K.6    Shimma, N.7    Umeda, I.8    Ishitsuka, H.9
  • 30
    • 0028957177 scopus 로고
    • Role of thymidine phosphorylase activity in the angiogenic effect of platelet derived endothelial cell growth factor/thymidine phosphorylase
    • Miyadera K., Sumizawa T., Haraguchi M., Yoshida H., Konstanty W., Yamada Y., Akiyama S. Role of thymidine phosphorylase activity in the angiogenic effect of platelet derived endothelial cell growth factor/thymidine phosphorylase. Cancer Res. 55:1995;1687-1690.
    • (1995) Cancer Res. , vol.55 , pp. 1687-1690
    • Miyadera, K.1    Sumizawa, T.2    Haraguchi, M.3    Yoshida, H.4    Konstanty, W.5    Yamada, Y.6    Akiyama, S.7
  • 31
    • 0023244025 scopus 로고
    • Purification and properties of an endothelial cell growth factor from human platelets
    • Miyazono K., Okabe T., Urabe A., Takaku F., Heldin C.H. Purification and properties of an endothelial cell growth factor from human platelets. J. Biol. Chem. 262:1987;4098-4103.
    • (1987) J. Biol. Chem. , vol.262 , pp. 4098-4103
    • Miyazono, K.1    Okabe, T.2    Urabe, A.3    Takaku, F.4    Heldin, C.H.5
  • 32
    • 0030974548 scopus 로고    scopus 로고
    • Expression of platelet-derived endothelial cell growth factor in bladder carcinoma
    • Mizutani Y., Okada Y., Yoshida O. Expression of platelet-derived endothelial cell growth factor in bladder carcinoma. Cancer. 79:1997;1190-1194.
    • (1997) Cancer , vol.79 , pp. 1190-1194
    • Mizutani, Y.1    Okada, Y.2    Yoshida, O.3
  • 33
    • 0026690144 scopus 로고
    • Expression of platelet-derived endothelial cell growth factor in Escherichia coli and confirmation of its thymidine phosphorylase activity
    • Moghaddam A., Bicknell R. Expression of platelet-derived endothelial cell growth factor in Escherichia coli and confirmation of its thymidine phosphorylase activity. Biochemistry. 31:1992;12141-12146.
    • (1992) Biochemistry , vol.31 , pp. 12141-12146
    • Moghaddam, A.1    Bicknell, R.2
  • 35
    • 0028961523 scopus 로고
    • Different angiogenic pathways characterize superficial and invasive bladder cancer
    • O'Brien T., Cranston D., Fuggle S., Bicknell R., Harris A.L. Different angiogenic pathways characterize superficial and invasive bladder cancer. Cancer Res. 55:1995;510-513.
    • (1995) Cancer Res. , vol.55 , pp. 510-513
    • O'Brien, T.1    Cranston, D.2    Fuggle, S.3    Bicknell, R.4    Harris, A.L.5
  • 36
  • 37
    • 0029100420 scopus 로고
    • Increased sensitivity to the prodrug 5′-deoxy-5-fluorouridine and modulation of 5-fluoro-2′-deoxyuridine sensitivity in MCF-7 cells transfected with thymidine phosphorylase
    • Patterson A.V., Zhang H., Moghaddam A., Bicknell R., Talbot D.C., Stratford I.J., Harris A.L. Increased sensitivity to the prodrug 5′-deoxy-5-fluorouridine and modulation of 5-fluoro-2′-deoxyuridine sensitivity in MCF-7 cells transfected with thymidine phosphorylase. Br. J. Cancer. 72:1995;669-675.
    • (1995) Br. J. Cancer , vol.72 , pp. 669-675
    • Patterson, A.V.1    Zhang, H.2    Moghaddam, A.3    Bicknell, R.4    Talbot, D.C.5    Stratford, I.J.6    Harris, A.L.7
  • 38
    • 0017395846 scopus 로고
    • Identification and comparative analysis of thymidine phosphorylase in the plasma of healthy subjects and cancer patients
    • Pauly J.L., Schuller M.G., Zelcer A.A., Kirss T.A., Gore S.S., Germain M.J. Identification and comparative analysis of thymidine phosphorylase in the plasma of healthy subjects and cancer patients. J. Natl. Cancer Inst. 58:1977;1587-1590.
    • (1977) J. Natl. Cancer Inst. , vol.58 , pp. 1587-1590
    • Pauly, J.L.1    Schuller, M.G.2    Zelcer, A.A.3    Kirss, T.A.4    Gore, S.S.5    Germain, M.J.6
  • 39
    • 1842864743 scopus 로고    scopus 로고
    • Design of novel N-(2,4-dioxo-1,2,3,4-tetrahydro-thieno[3,2-d]pyrimidin-7- yl)-guanidines as thymidine phosphorylase inhibitors, and flexible docking to a homology model
    • Price M.L., Guida W.C., Jackson T.E., Nydick J.A., Gladstone P.L., Juarez J.C., Donate F., Ternansky R.J. Design of novel N-(2,4-dioxo-1,2,3,4- tetrahydro-thieno[3,2-d]pyrimidin-7-yl)-guanidines as thymidine phosphorylase inhibitors, and flexible docking to a homology model. Bioorg. Med. Chem. Lett. 13:2003;107-110.
    • (2003) Bioorg. Med. Chem. Lett. , vol.13 , pp. 107-110
    • Price, M.L.1    Guida, W.C.2    Jackson, T.E.3    Nydick, J.A.4    Gladstone, P.L.5    Juarez, J.C.6    Donate, F.7    Ternansky, R.J.8
  • 40
    • 0032533446 scopus 로고    scopus 로고
    • The crystal structure of pyrimidine nucleoside phosphorylase in a closed conformation
    • Pugmire M.J., Ealick S.E. The crystal structure of pyrimidine nucleoside phosphorylase in a closed conformation. Structure. 6:1998;1467-1479.
    • (1998) Structure , vol.6 , pp. 1467-1479
    • Pugmire, M.J.1    Ealick, S.E.2
  • 41
    • 0036183496 scopus 로고    scopus 로고
    • Structural analyses reveal two distinct families of nucleoside phosphorylases
    • Pugmire M.J., Ealick S.E. Structural analyses reveal two distinct families of nucleoside phosphorylases. Biochem. J. 361:2002;1-25.
    • (2002) Biochem. J. , vol.361 , pp. 1-25
    • Pugmire, M.J.1    Ealick, S.E.2
  • 42
    • 0032516763 scopus 로고    scopus 로고
    • Structural and theoretical studies suggest domain movement produces an active conformation of thymidine phosphorylase
    • Pugmire M.J., Cook W.J., Jasanoff A., Walter M.R., Ealick S.E. Structural and theoretical studies suggest domain movement produces an active conformation of thymidine phosphorylase. J. Mol. Biol. 281:1998;285-299.
    • (1998) J. Mol. Biol. , vol.281 , pp. 285-299
    • Pugmire, M.J.1    Cook, W.J.2    Jasanoff, A.3    Walter, M.R.4    Ealick, S.E.5
  • 44
    • 0015244537 scopus 로고
    • Thymidine phosphorylase from Escherichia coli. Properties and kinetics
    • Schwartz M. Thymidine phosphorylase from Escherichia coli. Properties and kinetics. Eur. J. Biochem. 21:1971;191-198.
    • (1971) Eur. J. Biochem. , vol.21 , pp. 191-198
    • Schwartz, M.1
  • 45
    • 0017833231 scopus 로고
    • Thymidine phosphorylase from Escherichia coli
    • Schwartz M. Thymidine phosphorylase from Escherichia coli. Methods Enzymol. 51:1978;442-445.
    • (1978) Methods Enzymol. , vol.51 , pp. 442-445
    • Schwartz, M.1
  • 46
    • 0027138218 scopus 로고
    • Crystallization and x-ray diffraction study of recombinant platelet-derived endothelial cell growth factor
    • Spraggon M., Stuart D., Ponting C., Finnis C., Sleep D., Jones Y. Crystallization and x-ray diffraction study of recombinant platelet-derived endothelial cell growth factor. J. Mol. Biol. 234:1993;879-880.
    • (1993) J. Mol. Biol. , vol.234 , pp. 879-880
    • Spraggon, M.1    Stuart, D.2    Ponting, C.3    Finnis, C.4    Sleep, D.5    Jones, Y.6
  • 51
    • 0242402001 scopus 로고    scopus 로고
    • A dose-finding, safety and pharmacokinetics study of TAS-102, an antitumor/antiangiogenic agent given orally on a once-daily schedule for five-days every three weeks in patients with solid tumors
    • Thomas M.B., Hoff P.M., Carter S., Bland G., Lassere Y., Wolff R., Xiong H., Hayakawa T., Abbruzzese J. A dose-finding, safety and pharmacokinetics study of TAS-102, an antitumor/antiangiogenic agent given orally on a once-daily schedule for five-days every three weeks in patients with solid tumors. Proc. Am. Assoc. Cancer Res. 43:2002;554.
    • (2002) Proc. Am. Assoc. Cancer Res. , vol.43 , pp. 554
    • Thomas, M.B.1    Hoff, P.M.2    Carter, S.3    Bland, G.4    Lassere, Y.5    Wolff, R.6    Xiong, H.7    Hayakawa, T.8    Abbruzzese, J.9
  • 53
    • 78651153400 scopus 로고
    • Deoxyribosyl transfer. I. Thymidine phosphorylase and nucleoside deoxyribosyltransferase in normal and malignant tissues
    • a
    • Zimmerman M., Seidenberg J. Deoxyribosyl transfer. I. Thymidine phosphorylase and nucleoside deoxyribosyltransferase in normal and malignant tissues. J. Biol. Chem. 239:1964;2618-2621. a.
    • (1964) J. Biol. Chem. , vol.239 , pp. 2618-2621
    • Zimmerman, M.1    Seidenberg, J.2
  • 54
    • 0008473922 scopus 로고
    • Deoxyribosyl transfer. II. Nucleoside: Pyrimidine deoxyribosyltransferase activity of three partially purified thymidine phosphorylases
    • b
    • Zimmerman M., Seidenberg J. Deoxyribosyl transfer. II. Nucleoside. pyrimidine deoxyribosyltransferase activity of three partially purified thymidine phosphorylases J. Biol. Chem. 239:1964;2622-2627. b.
    • (1964) J. Biol. Chem. , vol.239 , pp. 2622-2627
    • Zimmerman, M.1    Seidenberg, J.2


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