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Volumn 579, Issue 6, 2005, Pages 1376-1382

Structure of a type II thymidine kinase with bound dTTP

Author keywords

Antiviral drugs; Cancer; dTTP; Human thymidine kinase; Suicide gene; Zinc finger

Indexed keywords

CYSTEINE; THYMIDINE KINASE; THYMIDINE KINASE 1; THYMIDINE KINASE 2; THYMIDINE KINASE INHIBITOR; THYMIDINE TRIPHOSPHATE; THYMINE; UNCLASSIFIED DRUG; VIRUS ENZYME; ZINC ION;

EID: 14244266842     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2005.01.034     Document Type: Article
Times cited : (47)

References (35)
  • 1
    • 0029162556 scopus 로고
    • Mammalian deoxyribonucleoside kinases
    • E.S. Arner, and S. Eriksson Mammalian deoxyribonucleoside kinases Pharmacol. Ther. 67 1995 155 186
    • (1995) Pharmacol. Ther. , vol.67 , pp. 155-186
    • Arner, E.S.1    Eriksson, S.2
  • 4
    • 0030933350 scopus 로고    scopus 로고
    • Overexpression of a heterologous thymidine kinase delays apoptosis induced by factor deprivation and inhibitors of deoxynucleotide metabolism
    • F.J. Oliver, M.K. Collins, and A. Lopez-Rivas Overexpression of a heterologous thymidine kinase delays apoptosis induced by factor deprivation and inhibitors of deoxynucleotide metabolism J. Biol. Chem. 272 1997 10624 10630
    • (1997) J. Biol. Chem. , vol.272 , pp. 10624-10630
    • Oliver, F.J.1    Collins, M.K.2    Lopez-Rivas, A.3
  • 5
    • 0026668209 scopus 로고
    • Thymidine kinase: A tumor marker with prognostic value for non-Hodgkin's lymphoma and a broad range of potential clinical applications
    • M. Hallek, L. Wanders, S. Strohmeyer, and B. Emmerich Thymidine kinase: a tumor marker with prognostic value for non-Hodgkin's lymphoma and a broad range of potential clinical applications Ann. Hematol. 65 1992 1 5
    • (1992) Ann. Hematol. , vol.65 , pp. 1-5
    • Hallek, M.1    Wanders, L.2    Strohmeyer, S.3    Emmerich, B.4
  • 10
    • 0032505705 scopus 로고    scopus 로고
    • Herpes simplex virus thymidine kinase gene transfer for controlled graft-versus-host disease and graft-versus-leukemia: Clinical follow-up and improved new vectors
    • S. Verzeletti, C. Bonini, S. Marktel, N. Nobili, F. Ciceri, C. Traversari, and C. Bordignon Herpes simplex virus thymidine kinase gene transfer for controlled graft-versus-host disease and graft-versus-leukemia: clinical follow-up and improved new vectors Hum. Gene Ther. 9 1998 2243 2251
    • (1998) Hum. Gene Ther. , vol.9 , pp. 2243-2251
    • Verzeletti, S.1    Bonini, C.2    Marktel, S.3    Nobili, N.4    Ciceri, F.5    Traversari, C.6    Bordignon, C.7
  • 11
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • W. Kabsch Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants J. Appl. Crystallogr. 26 1993 795 800
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 13
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • E. de la Fortelle, and G. Bricogne Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods Meth. Enzymol. 276 1997 472
    • (1997) Meth. Enzymol. , vol.276 , pp. 472
    • De La Fortelle, E.1    Bricogne, G.2
  • 14
    • 0037237545 scopus 로고    scopus 로고
    • Automated main-chain model building by template matching and iterative fragment extension
    • T.C. Terwilliger Automated main-chain model building by template matching and iterative fragment extension Acta Crystallogr. D 59 2003 38
    • (2003) Acta Crystallogr. D , vol.59 , pp. 38
    • Terwilliger, T.C.1
  • 15
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit-A versatile program for manipulating atomic coordinates and electron density
    • D.E. McRee XtalView/Xfit-A versatile program for manipulating atomic coordinates and electron density J. Struct. Biol. 125 1999 156 165
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 16
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project (1994) The CCP4 suite: Programs for protein crystallography. Acta Crystallogr. D 50, 760-763
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 19
    • 0038243196 scopus 로고    scopus 로고
    • POVScript+: A program for model and data visualization using persistence of vision ray-tracing
    • T.D. Fenn, D. Ringe, and G.A. Petsko POVScript+: a program for model and data visualization using persistence of vision ray-tracing J Appl. Crystallogr. 36 2003 944 947
    • (2003) J Appl. Crystallogr. , vol.36 , pp. 944-947
    • Fenn, T.D.1    Ringe, D.2    Petsko, G.A.3
  • 20
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • W. Kabsch, and C. Sander Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features Biopolymers 22 1983 2577 2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 21
    • 0002728647 scopus 로고
    • Proceedings of CCP4 Study Weekend on Isomorphous Replacement and Anomalous Scattering
    • Y. Jones, and D. Stuart Proceedings of CCP4 Study Weekend on Isomorphous Replacement and Anomalous Scattering Proceedings of CCP4 Study Weekend 1991 39 48
    • (1991) Proceedings of CCP4 Study Weekend , pp. 39-48
    • Jones, Y.1    Stuart, D.2
  • 23
    • 0017079647 scopus 로고
    • Human deoxythymidine kinase II: Substrate specificity and kinetic behavior of the cytoplasmic and mitochondrial isozymes derived from blast cells of acute myelocytic leukemia
    • L.S. Lee, and Y. Cheng Human deoxythymidine kinase II: substrate specificity and kinetic behavior of the cytoplasmic and mitochondrial isozymes derived from blast cells of acute myelocytic leukemia Biochemistry 15 1976 3686 3690
    • (1976) Biochemistry , vol.15 , pp. 3686-3690
    • Lee, L.S.1    Cheng, Y.2
  • 24
    • 0029020644 scopus 로고
    • The three-dimensional structure of thymidine kinase from herpes simplex virus type 1
    • K. Wild, T. Bohner, A. Aubry, G. Folkers, and G.E. Schulz The three-dimensional structure of thymidine kinase from herpes simplex virus type 1 FEBS Lett. 368 1995 289
    • (1995) FEBS Lett. , vol.368 , pp. 289
    • Wild, K.1    Bohner, T.2    Aubry, A.3    Folkers, G.4    Schulz, G.E.5
  • 28
    • 0028998836 scopus 로고
    • High-resolution structures of adenylate kinase from yeast ligated with inhibitor Ap5A, showing the pathway of phosphoryl transfer
    • U. Abele, and G.E. Schulz High-resolution structures of adenylate kinase from yeast ligated with inhibitor Ap5A, showing the pathway of phosphoryl transfer Protein Sci. 4 1995 1262 1271
    • (1995) Protein Sci. , vol.4 , pp. 1262-1271
    • Abele, U.1    Schulz, G.E.2
  • 29
    • 0030829025 scopus 로고    scopus 로고
    • The structures of thymidine kinase from herpes simplex virus type 1 in complex with substrates and a substrate analogue.PG - 2097-106
    • K. Wild, T. Bohner, G. Folkers, and G.E. Schulz The structures of thymidine kinase from herpes simplex virus type 1 in complex with substrates and a substrate analogue.PG - 2097-106 Protein Sci. 6 1997 2097 2106
    • (1997) Protein Sci. , vol.6 , pp. 2097-2106
    • Wild, K.1    Bohner, T.2    Folkers, G.3    Schulz, G.E.4
  • 31
    • 0038419639 scopus 로고    scopus 로고
    • Structure of human dCK suggests strategies to improve anticancer and antiviral therapy
    • E. Sabini, S. Ort, C. Monnerjahn, M. Konrad, and A. Lavie Structure of human dCK suggests strategies to improve anticancer and antiviral therapy Nat. Struct. Biol. 10 2003 513 519
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 513-519
    • Sabini, E.1    Ort, S.2    Monnerjahn, C.3    Konrad, M.4    Lavie, A.5
  • 32
    • 2342600247 scopus 로고    scopus 로고
    • Structural basis for the specificity, catalysis, and regulation of human uridine-cytidine kinase
    • N.N. Suzuki, K. Koizumi, M. Fukushima, A. Matsuda, and F. Inagaki Structural basis for the specificity, catalysis, and regulation of human uridine-cytidine kinase Structure 12 2004 751 764
    • (2004) Structure , vol.12 , pp. 751-764
    • Suzuki, N.N.1    Koizumi, K.2    Fukushima, M.3    Matsuda, A.4    Inagaki, F.5
  • 33
    • 0033033332 scopus 로고    scopus 로고
    • Structure to 1.9 a resolution of a complex with herpes simplex virus type-1 thymidine kinase of a novel, non-substrate inhibitor: X-ray crystallographic comparison with binding of aciclovir.PG - 121-5
    • M.S. Bennett, F. Wien, J.N. Champness, T. Batuwangala, T. Rutherford, W.C. Summers, H. Sun, G. Wright, and M.R. Sanderson Structure to 1.9 A resolution of a complex with herpes simplex virus type-1 thymidine kinase of a novel, non-substrate inhibitor: X-ray crystallographic comparison with binding of aciclovir.PG - 121-5 FEBS Lett. 443 1999 121
    • (1999) FEBS Lett. , vol.443 , pp. 121
    • Bennett, M.S.1    Wien, F.2    Champness, J.N.3    Batuwangala, T.4    Rutherford, T.5    Summers, W.C.6    Sun, H.7    Wright, G.8    Sanderson, M.R.9
  • 34
    • 0025793498 scopus 로고
    • Comparison of the substrate specificities of human thymidine kinase 1 and 2 and deoxycytidine kinase toward antiviral and cytostatic nucleoside analogs
    • S. Eriksson, B. Kierdaszuk, B. Munch-Petersen, B. Oberg, and N.G. Johansson Comparison of the substrate specificities of human thymidine kinase 1 and 2 and deoxycytidine kinase toward antiviral and cytostatic nucleoside analogs Biochem. Biophys. Res. Commun. 176 1991 586 592
    • (1991) Biochem. Biophys. Res. Commun. , vol.176 , pp. 586-592
    • Eriksson, S.1    Kierdaszuk, B.2    Munch-Petersen, B.3    Oberg, B.4    Johansson, N.G.5
  • 35
    • 3543041813 scopus 로고    scopus 로고
    • Biochemical and structural characterization of (South)- methanocarbathymidine that specifically inhibits growth of herpes simplex virus type 1 thymidine kinase-transduced osteosarcoma cells
    • P. Schelling, M.T. Claus, R. Johner, V.E. Marquez, G.E. Schulz, and L. Scapozza Biochemical and structural characterization of (South)- methanocarbathymidine that specifically inhibits growth of herpes simplex virus type 1 thymidine kinase-transduced osteosarcoma cells J. Biol. Chem. 279 2004 32832 32838
    • (2004) J. Biol. Chem. , vol.279 , pp. 32832-32838
    • Schelling, P.1    Claus, M.T.2    Johner, R.3    Marquez, V.E.4    Schulz, G.E.5    Scapozza, L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.