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Volumn 278, Issue 5, 1998, Pages 983-997

The three-dimensional structure of shikimate kinase

Author keywords

Drug design; Phosphoryl transfer; Shikimate kinase; Shikimate pathway; X ray analysis

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENYLATE KINASE; BACTERIAL ENZYME; MAGNESIUM ION; PHOSPHOTRANSFERASE; SHIKIMIC ACID;

EID: 0032557708     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.1755     Document Type: Article
Times cited : (74)

References (63)
  • 1
    • 0028998836 scopus 로고
    • 5A, showing the pathway of phosphoryl transfer
    • 5A, 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
  • 3
    • 0019201173 scopus 로고
    • Structure of a complex between yeast hexokinase A and glucose. II. Detailed comparisons of conformation and active site configuration with the native hexokinase B monomer and dimer
    • Bennet W.S., Steitz T.A. Structure of a complex between yeast hexokinase A and glucose. II. Detailed comparisons of conformation and active site configuration with the native hexokinase B monomer and dimer. J. Mol. Biol. 140:1980;211-230
    • (1980) J. Mol. Biol. , vol.140 , pp. 211-230
    • Bennet, W.S.1    Steitz, T.A.2
  • 6
    • 0028338283 scopus 로고
    • The closed conformation of a highly flexible protein: The structure of E. coli adenylate kinase with bound AMP an dAMPPNP
    • Berry M.B., Meador B., Bilderback T., Liang P., Glaser M., Phillips G.N. Jr. The closed conformation of a highly flexible protein The structure of E. coli adenylate kinase with bound AMP an dAMPPNP. Proteins: Struct. Funct. Genet. 19:1994;183-198
    • (1994) Proteins: Struct. Funct. Genet. , vol.19 , pp. 183-198
    • Berry, M.B.1    Meador, B.2    Bilderback, T.3    Liang, P.4    Glaser, M.5    Phillips Jr., G.N.6
  • 7
    • 0023140814 scopus 로고
    • Crystallographic R-factor refinement by molecular dynamics
    • Brünger A.T., Kuriyan J., Karplus M. Crystallographic R-factor refinement by molecular dynamics. Science. 235:1987;458-460
    • (1987) Science , vol.235 , pp. 458-460
    • Brünger, A.T.1    Kuriyan, J.2    Karplus, M.3
  • 8
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • The CCP4 suite programs for protein crystallography. Acta Crystallog. sect. D. 50:1994;760-763
    • (1994) Acta Crystallog. sect. D , vol.50 , pp. 760-763
  • 9
    • 0003164468 scopus 로고
    • The shikimate pathway as a target for herbicides
    • A. Dodge. Cambridge University Press
    • Coggins J.R. The shikimate pathway as a target for herbicides. Dodge A. Herbicides and Plant Metabolism. 1989;97-112 Cambridge University Press
    • (1989) Herbicides and Plant Metabolism , pp. 97-112
    • Coggins, J.R.1
  • 11
    • 0002583957 scopus 로고
    • DM, An automated procedure for phase improvement by density modification
    • Cowtan K. DM, An automated procedure for phase improvement by density modification. Joint CCP4 SF-EACBM Newsletter Protein Crystallog. 31:1994;24-28
    • (1994) Joint CCP4 SF-EACBM Newsletter Protein Crystallog. , vol.31 , pp. 24-28
    • Cowtan, K.1
  • 13
    • 0022483540 scopus 로고
    • Purification and properties of shikimate kinase II from Escherichia coli K-12
    • De Feyter R.C., Pittard J. Purification and properties of shikimate kinase II from Escherichia coli K-12. J. Bacteriol. 165:1986;331-333
    • (1986) J. Bacteriol. , vol.165 , pp. 331-333
    • De Feyter, R.C.1    Pittard, J.2
  • 14
    • 0022548992 scopus 로고
    • Nucleotide sequences of the transcription unit containing the aroL and aroM genes from Escherichia coli K-12
    • De Feyter R.C., Davidson B.E., Pittard J. Nucleotide sequences of the transcription unit containing the aroL and aroM genes from Escherichia coli K-12. J. Bacteriol. 165:1986;233-239
    • (1986) J. Bacteriol. , vol.165 , pp. 233-239
    • De Feyter, R.C.1    Davidson, B.E.2    Pittard, J.3
  • 15
    • 0024996454 scopus 로고
    • Three-dimensional structure of the complex between mitochondrial matrix adenylate kinase and its substrate AMP
    • Diederichs K., Schulz G.E. Three-dimensional structure of the complex between mitochondrial matrix adenylate kinase and its substrate AMP. Biochemistry. 29:1990;8138-8144
    • (1990) Biochemistry , vol.29 , pp. 8138-8144
    • Diederichs, K.1    Schulz, G.E.2
  • 16
    • 0023887425 scopus 로고
    • Refined structure of porcine cytosolic adenylate kinase at 2.1 Å resolution
    • Dreusicke D., Karplus A., Schulz G.E. Refined structure of porcine cytosolic adenylate kinase at 2.1 Å resolution. J. Mol. Biol. 199:1988;359-371
    • (1988) J. Mol. Biol. , vol.199 , pp. 359-371
    • Dreusicke, D.1    Karplus, A.2    Schulz, G.E.3
  • 17
    • 0017288499 scopus 로고
    • Exposure of tryptophanyl residues in proteins. Quantitative determination by fluorescence quenching studies
    • Eftink M.R., Ghiron C.A. Exposure of tryptophanyl residues in proteins. Quantitative determination by fluorescence quenching studies. Biochemistry. 15:1976;672-680
    • (1976) Biochemistry , vol.15 , pp. 672-680
    • Eftink, M.R.1    Ghiron, C.A.2
  • 18
    • 0027609916 scopus 로고
    • Sector: Hardware lighted three-dimensional solid model representations of macromolecules
    • Evans S.V. Sector Hardware lighted three-dimensional solid model representations of macromolecules. J. Mol. Graphics. 11:1993;134-138
    • (1993) J. Mol. Graphics , vol.11 , pp. 134-138
    • Evans, S.V.1
  • 19
    • 0027528934 scopus 로고
    • Domain closure in adenylate kinase: Joints on either side of two helices close like neighbouring fingers
    • Gerstein M., Schulz G.E., Chothia C. Domain closure in adenylate kinase Joints on either side of two helices close like neighbouring fingers. J. Mol. Biol. 229:1993;494-501
    • (1993) J. Mol. Biol. , vol.229 , pp. 494-501
    • Gerstein, M.1    Schulz, G.E.2    Chothia, C.3
  • 20
    • 0026536746 scopus 로고
    • Crystal structure of the binary complex of pig muscle phosphoglycerate kinase and its substrate 3-phospho-D-glycerate
    • Harlos K., Vas M., Blake C.F. Crystal structure of the binary complex of pig muscle phosphoglycerate kinase and its substrate 3-phospho-D-glycerate. Proteins: Struct. Funct. Genet. 12:1992;133-144
    • (1992) Proteins: Struct. Funct. Genet. , vol.12 , pp. 133-144
    • Harlos, K.1    Vas, M.2    Blake, C.F.3
  • 21
    • 0030587517 scopus 로고    scopus 로고
    • The crystal structure of the bifunctional enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase reveals distinct domain homologies
    • Hasemann C.A., Istvan E.S., Uyeda K., Deisenhofer J. The crystal structure of the bifunctional enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase reveals distinct domain homologies. Structure. 4:1996;1017-1029
    • (1996) Structure , vol.4 , pp. 1017-1029
    • Hasemann, C.A.1    Istvan, E.S.2    Uyeda, K.3    Deisenhofer, J.4
  • 23
    • 0016624901 scopus 로고
    • Binding energy, specificity, and enzyme catalysis: The circe effect
    • Jencks W.P. Binding energy, specificity, and enzyme catalysis the circe effect. Advan. Enzymol. 43:1975;219-410
    • (1975) Advan. Enzymol. , vol.43 , pp. 219-410
    • Jencks, W.P.1
  • 24
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.-Y., Cowan S.W., Kjelgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A. 47:1991;110-119
    • (1991) Acta Crystallog. sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjelgaard, M.4
  • 25
    • 0002700643 scopus 로고
    • Halloween. Masks and bones
    • S. Bailey, R. Hubbard, & D. Waller. Warrington, UK: SERC Daresbury Laboratory
    • Kleywegt G.J., Jones T.A. Halloween. Masks and bones. Bailey S., Hubbard R., Waller D. From First Map to Final Model Processing. 1994;59-66 SERC Daresbury Laboratory, Warrington, UK
    • (1994) From First Map to Final Model Processing , pp. 59-66
    • Kleywegt, G.J.1    Jones, T.A.2
  • 26
    • 0001858251 scopus 로고
    • Application of a theory of enzyme specificity to protein synthesis
    • Koshland D.E. Jr. Application of a theory of enzyme specificity to protein synthesis. Proc. Natl Acad. Sci. USA. 44:1958;98-104
    • (1958) Proc. Natl Acad. Sci. USA , vol.44 , pp. 98-104
    • Koshland Jr., D.E.1
  • 27
    • 0026244229 scopus 로고
    • MOLSCRIPT-A program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. MOLSCRIPT-A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950
    • (1991) J. Appl. Crystallog , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 28
    • 0030967854 scopus 로고    scopus 로고
    • Crystallisation and preliminary X-ray crystallographic analysis of shikimate kinase from Erwinia chrysanthemi
    • Krell T., Coyle J.E., Horsburgh M.J., Coggins J.R., Lapthorn A.J. Crystallisation and preliminary X-ray crystallographic analysis of shikimate kinase from Erwinia chrysanthemi. Acta Crystallog. sect. D. 53:1997;612-614
    • (1997) Acta Crystallog. sect. D , vol.53 , pp. 612-614
    • Krell, T.1    Coyle, J.E.2    Horsburgh, M.J.3    Coggins, J.R.4    Lapthorn, A.J.5
  • 30
    • 0011241750 scopus 로고
    • Evaluation of protein coordinate sets
    • S. Bailey, R. Hubbard, & D.A. Waller. Warrington, UK: SERC Daresbury Laboratory
    • Laskowski R.A., MacArthur M.W., Thornton J.M. Evaluation of protein coordinate sets. Bailey S., Hubbard R., Waller D.A. From First Map to Final Model. 1994;149-159 SERC Daresbury Laboratory, Warrington, UK
    • (1994) From First Map to Final Model , pp. 149-159
    • Laskowski, R.A.1    Macarthur, M.W.2    Thornton, J.M.3
  • 31
    • 0014432781 scopus 로고
    • Solvent content of proteins
    • Matthews B.W. Solvent content of proteins. J. Mol. Biol. 33:1968;491-497
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 32
    • 0028579433 scopus 로고
    • Protein structural similarities predicted by a sequence-structure compatibility method
    • Matsuo Y., Nishikawa K. Protein structural similarities predicted by a sequence-structure compatibility method. Protein Sci. 3:1994;2055-2063
    • (1994) Protein Sci. , vol.3 , pp. 2055-2063
    • Matsuo, Y.1    Nishikawa, K.2
  • 33
    • 0022474607 scopus 로고
    • The cloning and expression of the aroL gene from Escherichia coli K-12
    • Millar G., Lewendon A., Hunter M.G., Coggins J.R. The cloning and expression of the aroL gene from Escherichia coli K-12. Biochem. J. 237:1986;427-437
    • (1986) Biochem. J. , vol.237 , pp. 427-437
    • Millar, G.1    Lewendon, A.2    Hunter, M.G.3    Coggins, J.R.4
  • 34
    • 0025996094 scopus 로고
    • Evidence for an ancestral core structure in nucleotide-binding proteins with the type A-motif
    • Milner-White J.E., Coggins J.R., Anton I.A. Evidence for an ancestral core structure in nucleotide-binding proteins with the type A-motif. J. Mol. Biol. 221:1991;751-754
    • (1991) J. Mol. Biol. , vol.221 , pp. 751-754
    • Milner-White, J.E.1    Coggins, J.R.2    Anton, I.A.3
  • 35
    • 18244422353 scopus 로고
    • Nucleotide sequence of an Erwinia chrysanthemi gene encoding shikimate kinase
    • Minton N.P., Whitehead P.J., Atkinson T., Gilbert H.J. Nucleotide sequence of an Erwinia chrysanthemi gene encoding shikimate kinase. Nucl. Acids Res. 17:1989;1769
    • (1989) Nucl. Acids Res. , vol.17 , pp. 1769
    • Minton, N.P.1    Whitehead, P.J.2    Atkinson, T.3    Gilbert, H.J.4
  • 36
    • 0030297640 scopus 로고    scopus 로고
    • Protein recognition of adenylate: An example of a fuzzy recognition template
    • Moodie S.L., Mitchell J.B.O., Thornton J.M. Protein recognition of adenylate An example of a fuzzy recognition template. J. Mol. Biol. 263:1996;486-500
    • (1996) J. Mol. Biol. , vol.263 , pp. 486-500
    • Moodie, S.L.1    Mitchell, J.B.O.2    Thornton, J.M.3
  • 38
    • 0029644168 scopus 로고    scopus 로고
    • Adenylate kinase motions during catalysis: An energetic counterweight balancing substrate binding
    • Müller C.W., Schlauderer G.J., Reinstein J., Schulz G.E. Adenylate kinase motions during catalysis an energetic counterweight balancing substrate binding. Structure. 4:1996;147-156
    • (1996) Structure , vol.4 , pp. 147-156
    • Müller, C.W.1    Schlauderer, G.J.2    Reinstein, J.3    Schulz, G.E.4
  • 39
    • 0028327709 scopus 로고
    • The structure of uridylate kinase with its substrates, showing the transition state geometry
    • Müller-Dieckmann H.-J., Schulz G.E. The structure of uridylate kinase with its substrates, showing the transition state geometry. J. Mol. Biol. 236:1994;361-367
    • (1994) J. Mol. Biol. , vol.236 , pp. 361-367
    • Müller-Dieckmann, H.-J.1    Schulz, G.E.2
  • 40
    • 0001851781 scopus 로고    scopus 로고
    • Application of maximum likelihood methods for macromolecular refinement
    • E. Dodson, M. Moore, & S. Bailey. Warrington, UK: SERC Daresbury Laboratory
    • Murshudov G.N., Dodson E.J., Vagin A.A. Application of maximum likelihood methods for macromolecular refinement. Dodson E., Moore M., Bailey S. Macromolecular Refinement. 1996;93-104 SERC Daresbury Laboratory, Warrington, UK
    • (1996) Macromolecular Refinement , pp. 93-104
    • Murshudov, G.N.1    Dodson, E.J.2    Vagin, A.A.3
  • 41
    • 84920325457 scopus 로고
    • AmoRe-An automated package for molecular replacement
    • Navaza J. AmoRe-An automated package for molecular replacement. Acta Crystallog. sect. A. 50:1994;157-163
    • (1994) Acta Crystallog. sect. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 42
    • 70349640265 scopus 로고
    • Adenylate kinase
    • Boyer P.D. New York: Academic Press Ltd
    • Noda L. Adenylate kinase. Boyer P.D. The Enzymes. vol. 8:1973;279-305 Academic Press Ltd, New York
    • (1973) The Enzymes , vol.8 , pp. 279-305
    • Noda, L.1
  • 43
    • 0002634621 scopus 로고
    • Maximum likelihood refinement of heavy atom parameters
    • W. Wolf, P.R. Evans, & A.G.W. Leslie. Warrington, UK: SERC Daresbury Laboratory
    • Otwinowski Z. Maximum likelihood refinement of heavy atom parameters. Wolf W., Evans P.R., Leslie A.G.W. Isomorphous Replacement and Anomalous Scattering. 1991;80-85 SERC Daresbury Laboratory, Warrington, UK
    • (1991) Isomorphous Replacement and Anomalous Scattering , pp. 80-85
    • Otwinowski, Z.1
  • 44
    • 0002452464 scopus 로고
    • Oscillation data reduction program
    • L. Sawyer, N. Isaacs, & S. Bailey. Warrington, UK: Daresbury Laboratory
    • Otwinowski Z. Oscillation data reduction program. Sawyer L., Isaacs N., Bailey S. Data Collection and Processing. 1993;56-62 Daresbury Laboratory, Warrington, UK
    • (1993) Data Collection and Processing , pp. 56-62
    • Otwinowski, Z.1
  • 45
    • 0025310575 scopus 로고
    • Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 Å resolution: Implications for the mechanism of GTP hydrolysis
    • Pai E.F., Krengel U., Petski G.A., Goody R.S., Kabsch W., Wittinghofer A. Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 Å resolution implications for the mechanism of GTP hydrolysis. EMBO J. 9:1990;2351-2359
    • (1990) EMBO J. , vol.9 , pp. 2351-2359
    • Pai, E.F.1    Krengel, U.2    Petski, G.A.3    Goody, R.S.4    Kabsch, W.5    Wittinghofer, A.6
  • 46
    • 0019873820 scopus 로고
    • Estimation of globular protein secondary structure from circular dichroism
    • Provencher S.W., Glöckner J. Estimation of globular protein secondary structure from circular dichroism. Biochemistry. 20:1981;33-37
    • (1981) Biochemistry , vol.20 , pp. 33-37
    • Provencher, S.W.1    Glöckner, J.2
  • 47
    • 0027291015 scopus 로고
    • Prediction of protein secondary structure at better than 70% accuracy
    • Rost B., Sander C. Prediction of protein secondary structure at better than 70% accuracy. J. Mol. Biol. 232:1993;584-599
    • (1993) J. Mol. Biol. , vol.232 , pp. 584-599
    • Rost, B.1    Sander, C.2
  • 49
    • 0029897810 scopus 로고    scopus 로고
    • The structure of bovine mitochondrial adenylate kinase: Comparison with isoenzymes in other compartments
    • Schlauderer G.J., Schulz G.E. The structure of bovine mitochondrial adenylate kinase Comparison with isoenzymes in other compartments. Protein Sci. 5:1996;434-441
    • (1996) Protein Sci , vol.5 , pp. 434-441
    • Schlauderer, G.J.1    Schulz, G.E.2
  • 50
    • 12944300317 scopus 로고
    • Binding of nucleotides by proteins
    • Schulz G.E. Binding of nucleotides by proteins. Curr. Opin. Struct. Biol. 2:1992;61-67
    • (1992) Curr. Opin. Struct. Biol. , vol.2 , pp. 61-67
    • Schulz, G.E.1
  • 52
    • 0002918520 scopus 로고
    • Heavy atom location using SHELX-90
    • W. Wold, P.R. Evans, & A.G.W. Leslie. Warrington, UK: SERC Daresbury Laboratory
    • Sheldrick G.M. Heavy atom location using SHELX-90. Wold W., Evans P.R., Leslie A.G.W. Isomorphous Replacement and Anomalous Scattering. 1991;80-86 SERC Daresbury Laboratory, Warrington, UK
    • (1991) Isomorphous Replacement and Anomalous Scattering , pp. 80-86
    • Sheldrick, G.M.1
  • 53
    • 0029161763 scopus 로고
    • X-ray structure of the magnesium(II)-pyrophosphate complex of the truncated head of Dictyostellium discoideum myosin to 2.7 Å resolution
    • Smith C.A., Reyment I. X-ray structure of the magnesium(II)-pyrophosphate complex of the truncated head of Dictyostellium discoideum myosin to 2.7 Å resolution. Biochemistry. 34:1995;8973-8981
    • (1995) Biochemistry , vol.34 , pp. 8973-8981
    • Smith, C.A.1    Reyment, I.2
  • 54
    • 0029914905 scopus 로고    scopus 로고
    • Active site comparisons highlight structural similarities between myosin and other P-loop proteins
    • Smith C.A., Rayment I. Active site comparisons highlight structural similarities between myosin and other P-loop proteins. Biophys. J. 70:1996;1590-1602
    • (1996) Biophys. J. , vol.70 , pp. 1590-1602
    • Smith, C.A.1    Rayment, I.2
  • 55
    • 0025012803 scopus 로고
    • Three-dimensional structure of the complex of guanylate kinase from yeast with its substrate GMP
    • Stehle T., Schulz G.E. Three-dimensional structure of the complex of guanylate kinase from yeast with its substrate GMP. J. Mol. Biol. 211:1990;249-254
    • (1990) J. Mol. Biol. , vol.211 , pp. 249-254
    • Stehle, T.1    Schulz, G.E.2
  • 56
    • 0026584599 scopus 로고
    • Structure of the recA protein-ADP complex
    • Story R.M., Steitz T.A. Structure of the recA protein-ADP complex. Nature. 355:1992;374-376
    • (1992) Nature , vol.355 , pp. 374-376
    • Story, R.M.1    Steitz, T.A.2
  • 57
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • Studier F.W., Moffatt B.A. Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J. Mol. Biol. 189:1986;113-130
    • (1986) J. Mol. Biol. , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 58
    • 0029991644 scopus 로고    scopus 로고
    • Mecillinam resistance in Escherichia coli is conferred by loss of a second activity of the aroK protein
    • Vinella D., Gagny B., Joseleau-Petit D., D'Ardi R., Cashel M. Mecillinam resistance in Escherichia coli is conferred by loss of a second activity of the aroK protein. J. Bacteriol. 178:1996;3818-3828
    • (1996) J. Bacteriol. , vol.178 , pp. 3818-3828
    • Vinella, D.1    Gagny, B.2    Joseleau-Petit, D.3    D'ardi, R.4    Cashel, M.5
  • 59
    • 0029644728 scopus 로고
    • Movie of the structural changes during a catalytic cycle of nucleoside monophosphate kinases
    • Vonrhein C., Schlauderer G.J., Schulz G.E. Movie of the structural changes during a catalytic cycle of nucleoside monophosphate kinases. Structure. 3:1995;483-490
    • (1995) Structure , vol.3 , pp. 483-490
    • Vonrhein, C.1    Schlauderer, G.J.2    Schulz, G.E.3
  • 60
    • 0001607723 scopus 로고
    • Distantly related sequences in the α- and β-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker J.E., Saraste M., Runswick M.J., Gay N.J. Distantly related sequences in the α- and β-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1:1982;945-951
    • (1982) EMBO J. , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 62
    • 0028967182 scopus 로고
    • A reassessment of the relationship between aroK- and aroL-encoded shikimate kinase enzymes of Escherichia coli
    • Whipp M.J., Pittard A.J. A reassessment of the relationship between aroK- and aroL-encoded shikimate kinase enzymes of Escherichia coli. J. Bacterial. 177:1995;1627-1629
    • (1995) J. Bacterial. , vol.177 , pp. 1627-1629
    • Whipp, M.J.1    Pittard, A.J.2
  • 63
    • 0029020644 scopus 로고
    • The three-dimensional structure of thymidine kinase from Herpes simplex virus type 1
    • Wild K., Bohner T., Aubry A., Folkers G., Schulz G.E. The three-dimensional structure of thymidine kinase from Herpes simplex virus type 1. FEBS Letters. 368:1995;289-292
    • (1995) FEBS Letters , vol.368 , pp. 289-292
    • Wild, K.1    Bohner, T.2    Aubry, A.3    Folkers, G.4    Schulz, G.E.5


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