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Volumn 5, Issue 12, 1997, Pages 1627-1637

Staurosporine-induced conformational changes of cAMP-dependent protein kinase catalytic subunit explain inhibitory potential

Author keywords

Cancer drug design; Crystal structure enzyme flexibility; Protein kinase; Staurosporine

Indexed keywords

ANIMALIA; BOS TAURUS;

EID: 0031574365     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(97)00310-9     Document Type: Article
Times cited : (166)

References (53)
  • 1
    • 0017395981 scopus 로고
    • New alkaloid AM-2282 of Streptomyces origin - Taxonomy, fermentation, isolation and preliminary characterization
    • Omura, S., et al., & Masuma, R. (1977). New alkaloid AM-2282 of Streptomyces origin - taxonomy, fermentation, isolation and preliminary characterization. J. Antibiot. 30, 275-282.
    • (1977) J. Antibiot. , vol.30 , pp. 275-282
    • Omura, S.1    Masuma, R.2
  • 2
    • 0025998841 scopus 로고
    • Use and specificity of staurosporine, UCN-01, and calphostin C as protein kinase inhibitors
    • Tamaoki, T. (1991). Use and specificity of staurosporine, UCN-01, and calphostin C as protein kinase inhibitors. Methods Enzymol. 201, 340-347.
    • (1991) Methods Enzymol. , vol.201 , pp. 340-347
    • Tamaoki, T.1
  • 5
    • 0025045619 scopus 로고
    • Characterization of specific binding sites for [3H]-staurosporine on various protein kinases
    • Herbert, J.M., Seban, E. & Maffrand, J.P. (1990). Characterization of specific binding sites for [3H]-staurosporine on various protein kinases. Biochem. Biophys. Res. Commun. 171, 189-195.
    • (1990) Biochem. Biophys. Res. Commun. , vol.171 , pp. 189-195
    • Herbert, J.M.1    Seban, E.2    Maffrand, J.P.3
  • 6
    • 0023258497 scopus 로고
    • Staurosporine inhibits tyrosine-specific protein kinase activity of Rous sarcoma virus transforming protein p60
    • Nakano, H., Kobayashi, E., Takahashi, I., Tamaoki, T., Kuzuu, Y. & Iba, H. (1987). Staurosporine inhibits tyrosine-specific protein kinase activity of Rous sarcoma virus transforming protein p60. J. Antibiot. Tokyo 40, 706-708.
    • (1987) J. Antibiot. Tokyo , vol.40 , pp. 706-708
    • Nakano, H.1    Kobayashi, E.2    Takahashi, I.3    Tamaoki, T.4    Kuzuu, Y.5    Iba, H.6
  • 7
    • 0025221139 scopus 로고
    • Preferential inhibition of the platelet-derived growth factor receptor tyrosine kinase by staurosporine
    • Secrist, J.P., Sehgal, I., Powis, G. & Abraham, R.T. (1990). Preferential inhibition of the platelet-derived growth factor receptor tyrosine kinase by staurosporine. J. Biol. Chem. 265, 20394-20400.
    • (1990) J. Biol. Chem. , vol.265 , pp. 20394-20400
    • Secrist, J.P.1    Sehgal, I.2    Powis, G.3    Abraham, R.T.4
  • 8
    • 0024166194 scopus 로고
    • Characterization of receptor tyrosine-specific protein kinases by the use of inhibitors. Staurosporine is a 100-times more potent inhibitor of insulin receptor than IGF-I receptor
    • Fujita-Yamaguchi, Y. & Kathura, S. (1988). Characterization of receptor tyrosine-specific protein kinases by the use of inhibitors. Staurosporine is a 100-times more potent inhibitor of insulin receptor than IGF-I receptor. Biochem. Biophys. Res. Commun. 157, 955-962.
    • (1988) Biochem. Biophys. Res. Commun. , vol.157 , pp. 955-962
    • Fujita-Yamaguchi, Y.1    Kathura, S.2
  • 9
    • 0028903210 scopus 로고
    • Staurosporine causes epidermal growth factor to induce differentiation in PC12 cells via receptor up-regulation
    • Raffioni, S. & Bradshaw, R.A. (1995). Staurosporine causes epidermal growth factor to induce differentiation in PC12 cells via receptor up-regulation. J. Biol. Chem. 270, 7568-7572.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7568-7572
    • Raffioni, S.1    Bradshaw, R.A.2
  • 10
    • 0030013883 scopus 로고    scopus 로고
    • Staurosporine induces a complete program of terminal differentiation in neoplastic mouse keratinocytes via activation of protein kinase C
    • Stanwell, C., Dlugosz, A.A. & Yuspa, S.H. (1996). Staurosporine induces a complete program of terminal differentiation in neoplastic mouse keratinocytes via activation of protein kinase C. Carcinogenesis 17, 1259-1265.
    • (1996) Carcinogenesis , vol.17 , pp. 1259-1265
    • Stanwell, C.1    Dlugosz, A.A.2    Yuspa, S.H.3
  • 11
    • 0029987190 scopus 로고    scopus 로고
    • Staurosporine induces programmed cell death in embryonic neurons and activation of the ceramide pathway
    • Wiesner, D.A. & Dawson, G. (1996). Staurosporine induces programmed cell death in embryonic neurons and activation of the ceramide pathway. J. Neurochem. 66, 1418-1425.
    • (1996) J. Neurochem. , vol.66 , pp. 1418-1425
    • Wiesner, D.A.1    Dawson, G.2
  • 12
    • 0027373764 scopus 로고
    • Programmed cell death and the control of cell survival: Lessons from the nervous system
    • Raff, M.C., et al., & Jacobson, M.D. (1993). Programmed cell death and the control of cell survival: lessons from the nervous system. Science 262, 695-700.
    • (1993) Science , vol.262 , pp. 695-700
    • Raff, M.C.1    Jacobson, M.D.2
  • 13
    • 0028268215 scopus 로고
    • Programmed cell death and Bcl-2 protection in the absence of a nucleus
    • Jacobson, M.D., Burn, J.F. & Raff, M.C. (1994). Programmed cell death and Bcl-2 protection in the absence of a nucleus. EMBO J. 13, 1899-1910.
    • (1994) EMBO J. , vol.13 , pp. 1899-1910
    • Jacobson, M.D.1    Burn, J.F.2    Raff, M.C.3
  • 14
    • 0026425587 scopus 로고
    • Antitumor activity of UCN-01, a selective inhibitor of protein kinase C, in murine and human tumor models
    • Akinaga, S., Gomi, K., Morimoto, M., Tamaoki, T. & Okabe, M. (1991). Antitumor activity of UCN-01, a selective inhibitor of protein kinase C, in murine and human tumor models. Cancer Res. 51, 4888-4892.
    • (1991) Cancer Res. , vol.51 , pp. 4888-4892
    • Akinaga, S.1    Gomi, K.2    Morimoto, M.3    Tamaoki, T.4    Okabe, M.5
  • 15
    • 0024379951 scopus 로고
    • A derivative of staurosporine (CGP 41 251) shows selectivity for protein kinase C inhibition and in vitro anti-proliferative as well as in vivo anti-tumor activity
    • Meyer, T., et al., & Matter, A. (1989). A derivative of staurosporine (CGP 41 251) shows selectivity for protein kinase C inhibition and in vitro anti-proliferative as well as in vivo anti-tumor activity. Int. J. Cancer 43, 851-856.
    • (1989) Int. J. Cancer , vol.43 , pp. 851-856
    • Meyer, T.1    Matter, A.2
  • 17
    • 0028866845 scopus 로고
    • Different susceptibility of protein kinases to staurosporine inhibition. Kinetic studies and molecular bases for the resistance of protein kinase CK2
    • Meggio, F., et al., & Pinna, L.A. (1995). Different susceptibility of protein kinases to staurosporine inhibition. Kinetic studies and molecular bases for the resistance of protein kinase CK2. Eur. J. Biochem. 234, 317-322.
    • (1995) Eur. J. Biochem. , vol.234 , pp. 317-322
    • Meggio, F.1    Pinna, L.A.2
  • 18
    • 0026538078 scopus 로고
    • Inhibitors of protein kinase C. 2. Substituted bisindolylmaleimides with improved potency and selectivity
    • Davis, P.D., et al., & Wilkinson, S.E. (1992). Inhibitors of protein kinase C. 2. Substituted bisindolylmaleimides with improved potency and selectivity. J. Med. Chem. 35, 994-1001.
    • (1992) J. Med. Chem. , vol.35 , pp. 994-1001
    • Davis, P.D.1    Wilkinson, S.E.2
  • 19
    • 0029860018 scopus 로고    scopus 로고
    • Crystal structures of catalytic subunit of cAMP-dependent protein kinase in complex with isoquinolinesulfonyl protein kinase inhibitors H7, H8, and H89 - Structural implications for selectivity
    • Engh, R.A., Girod, A., Kinzel, V., Huber, R. & Bossemeyer, D. (1996). Crystal structures of catalytic subunit of cAMP-dependent protein kinase in complex with isoquinolinesulfonyl protein kinase inhibitors H7, H8, and H89 - structural implications for selectivity. J. Biol. Chem. 271, 26157-26164.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26157-26164
    • Engh, R.A.1    Girod, A.2    Kinzel, V.3    Huber, R.4    Bossemeyer, D.5
  • 20
    • 0029850471 scopus 로고    scopus 로고
    • High-resolution crystal structures of human cyclin-dependent kinase 2 with and without ATP: Bound waters and natural ligand as guides for inhibitor design
    • Schulze-Gahmen, U., De-Bondt, H.L & Kim, S.H. (1996). High-resolution crystal structures of human cyclin-dependent kinase 2 with and without ATP: bound waters and natural ligand as guides for inhibitor design. J. Med. Chem. 39, 4540-4546.
    • (1996) J. Med. Chem. , vol.39 , pp. 4540-4546
    • Schulze-Gahmen, U.1    De-Bondt, H.L.2    Kim, S.H.3
  • 21
    • 0029993339 scopus 로고    scopus 로고
    • Structural basis for specificity and potency of a flavonoid inhibitor of human CDK2, a cell cycle kinase
    • De-Azevedo, W.F., et al., & Kim, S.H. (1996). Structural basis for specificity and potency of a flavonoid inhibitor of human CDK2, a cell cycle kinase. Proc. Natl. Acad. Sci. USA 93, 2735-2740.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2735-2740
    • De-Azevedo, W.F.1    Kim, S.H.2
  • 22
    • 0029982777 scopus 로고    scopus 로고
    • Structural basis for selectivity of the isoquinoline sulfonamide family of protein kinase inhibitors
    • Xu, R.M., Carmel, G., Kuret, J. & Cheng, X. (1996). Structural basis for selectivity of the isoquinoline sulfonamide family of protein kinase inhibitors. Proc. Natl. Acad. Sci. USA 93, 6308-6313.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6308-6313
    • Xu, R.M.1    Carmel, G.2    Kuret, J.3    Cheng, X.4
  • 23
    • 0030945871 scopus 로고    scopus 로고
    • Structures of the tyrosine kinase domain of fibroblast growth factor receptor in complex with inhibitors
    • Mohammadi, M., et al., & Schlessinger, J. (1997). Structures of the tyrosine kinase domain of fibroblast growth factor receptor in complex with inhibitors. Science 276, 955-960.
    • (1997) Science , vol.276 , pp. 955-960
    • Mohammadi, M.1    Schlessinger, J.2
  • 24
    • 0030954172 scopus 로고    scopus 로고
    • A highly specific inhibitor of human p38 MAP kinase binds in the ATP pocket
    • Tong, L., et al., Pargellis, C.A. (1997). A highly specific inhibitor of human p38 MAP kinase binds in the ATP pocket. Nat. Struct. Biol. 4, 311-316.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 311-316
    • Tong, L.1    Pargellis, C.A.2
  • 25
    • 0029440002 scopus 로고
    • Modelling study of protein kinase inhibitors: Binding mode of staurosporine and origin of the selectivity of CGP 52411
    • Furet, P., et al., & Traxler, P. (1995). Modelling study of protein kinase inhibitors: binding mode of staurosporine and origin of the selectivity of CGP 52411. J. Comput. Aided Mol. Des. 9, 465-472.
    • (1995) J. Comput. Aided Mol. Des. , vol.9 , pp. 465-472
    • Furet, P.1    Traxler, P.2
  • 26
    • 0029927387 scopus 로고    scopus 로고
    • Inhibition mechanisms of staurosporine and h7 to cAMP-dependent protein kinase through docking study
    • Takagi, A., Mizutani, M.Y., Tomioka, N. & Itai, A. (1996). Inhibition mechanisms of staurosporine and h7 to cAMP-dependent protein kinase through docking study. Chem. Pharmaceut. Bull. 44, 618-620.
    • (1996) Chem. Pharmaceut. Bull. , vol.44 , pp. 618-620
    • Takagi, A.1    Mizutani, M.Y.2    Tomioka, N.3    Itai, A.4
  • 27
    • 0026476024 scopus 로고
    • Cloning of the C alpha catalytic subunit of the bovine cAMP-dependent protein kinase
    • Wiemann, S., Kinzel, V. & Pyerin, W. (1992). Cloning of the C alpha catalytic subunit of the bovine cAMP-dependent protein kinase. Biochim. Biophys. Acta 1171, 93-96.
    • (1992) Biochim. Biophys. Acta , vol.1171 , pp. 93-96
    • Wiemann, S.1    Kinzel, V.2    Pyerin, W.3
  • 28
    • 0026342401 scopus 로고
    • Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase
    • Knighton, D.R. et al. & Sowadski, J.M. (1991). Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science 253, 407-414.
    • (1991) Science , vol.253 , pp. 407-414
    • Knighton, D.R.1    Sowadski, J.M.2
  • 29
    • 0030932129 scopus 로고    scopus 로고
    • Crystal structure of a polyhistidine-tagged recombinant catalytic subunit of cAMP-dependent protein kinase complexed with the peptide inhibitor PKI(5-24) and adenosine
    • Narayana, N., Cox, S., Shaltiel, S., Taylor, S.S. & Xuong, N.-H. (1997). Crystal structure of a polyhistidine-tagged recombinant catalytic subunit of cAMP-dependent protein kinase complexed with the peptide inhibitor PKI(5-24) and adenosine. Biochemistry 36, 4438-4448.
    • (1997) Biochemistry , vol.36 , pp. 4438-4448
    • Narayana, N.1    Cox, S.2    Shaltiel, S.3    Taylor, S.S.4    Xuong, N.-H.5
  • 30
    • 0027408171 scopus 로고
    • Crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MgATP and peptide inhibitor
    • Zheng, J.H., et al., & Sowadski, J.M. (1993). Crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MgATP and peptide inhibitor. Biochemistry 32, 2154-2161.
    • (1993) Biochemistry , vol.32 , pp. 2154-2161
    • Zheng, J.H.1    Sowadski, J.M.2
  • 32
    • 0001328416 scopus 로고
    • The crystal structure of the mammalian catalytic subunit of cAMP-dependent protein kinase and an inhibitor peptide displays an open conformation
    • Karlsson, R., Zheng, J., Xuong, N.H., Taylor, S.S. & Sowadski, J.M. (1993). The crystal structure of the mammalian catalytic subunit of cAMP-dependent protein kinase and an inhibitor peptide displays an open conformation. Acta Cryst. D 49, 381-388.
    • (1993) Acta Cryst. D , vol.49 , pp. 381-388
    • Karlsson, R.1    Zheng, J.2    Xuong, N.H.3    Taylor, S.S.4    Sowadski, J.M.5
  • 33
    • 0031571091 scopus 로고    scopus 로고
    • A binary complex of the catalytic subunit of cAMP-dependent protein kinase and adenosine further defines conformational flexibility
    • Narayana, N., Cox, S., Xuong, N.-H., Ten Eyck, L.F. & Taylor, S.S. (1997). A binary complex of the catalytic subunit of cAMP-dependent protein kinase and adenosine further defines conformational flexibility. Structure 5, 921-935.
    • (1997) Structure , vol.5 , pp. 921-935
    • Narayana, N.1    Cox, S.2    Xuong, N.-H.3    Ten Eyck, L.F.4    Taylor, S.S.5
  • 34
    • 0027429591 scopus 로고
    • Crystal structures of the myristylated catalytic subunit of cAMP-dependent protein kinase reveal open and closed conformations
    • Zheng, J.H., et al., & Teneyck, L.F. (1993). Crystal structures of the myristylated catalytic subunit of cAMP-dependent protein kinase reveal open and closed conformations. Protein Sci. 2, 1559-1573.
    • (1993) Protein Sci. , vol.2 , pp. 1559-1573
    • Zheng, J.H.1    Teneyck, L.F.2
  • 35
    • 0026345394 scopus 로고
    • Protein kinase catalytic domain sequence database: Identification of conserved features of primary structure and classification of family members
    • Hanks, S.K. & Quinn, A.M. (1991). Protein kinase catalytic domain sequence database: identification of conserved features of primary structure and classification of family members. Methods Enzymol. 200, 38-81.
    • (1991) Methods Enzymol. , vol.200 , pp. 38-81
    • Hanks, S.K.1    Quinn, A.M.2
  • 36
    • 0000915668 scopus 로고
    • 2.0 Å refined crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with a peptide inhibitor and detergent
    • Knighton, D.R., et al., & Sowadski, J.M. (1993). 2.0 Å refined crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with a peptide inhibitor and detergent. Acta Cryst. D 49, 357-361.
    • (1993) Acta Cryst. D , vol.49 , pp. 357-361
    • Knighton, D.R.1    Sowadski, J.M.2
  • 37
    • 0031035585 scopus 로고    scopus 로고
    • Synergistic binding of nucleotides and inhibitors to cAMP-dependent protein kinase examined by acrylodan fluorescence spectroscopy
    • Lew, J., Coruh, N., Tsigelny, I., Garrod, S. & Taylor, S. (1997). Synergistic binding of nucleotides and inhibitors to cAMP-dependent protein kinase examined by acrylodan fluorescence spectroscopy. J. Biol. Chem. 272, 1507-1513.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1507-1513
    • Lew, J.1    Coruh, N.2    Tsigelny, I.3    Garrod, S.4    Taylor, S.5
  • 38
    • 0020587052 scopus 로고
    • Adenosine cyclic 3′,5′-monophosphate dependent protein kinase: Interaction of the catalytic subunit and holoenzyme with linbenzoadenine nucleotides
    • Hartl, F.T., Roskoski, R.J., Rosendahl, M.S. & Leonard, N.J. (1983). Adenosine cyclic 3′,5′-monophosphate dependent protein kinase: interaction of the catalytic subunit and holoenzyme with linbenzoadenine nucleotides. Biochemistry 22, 2347-2352.
    • (1983) Biochemistry , vol.22 , pp. 2347-2352
    • Hartl, F.T.1    Roskoski, R.J.2    Rosendahl, M.S.3    Leonard, N.J.4
  • 39
    • 0029090514 scopus 로고
    • Multiple modes of ligand recognition: Crystal structures of cyclin-dependent protein kinase 2 in complex with ATP and two inhibitors, olomoucine and isopentenyladenine
    • Schulze-Gahmen, U., et al., & Kim, S.H. (1995). Multiple modes of ligand recognition: crystal structures of cyclin-dependent protein kinase 2 in complex with ATP and two inhibitors, olomoucine and isopentenyladenine. Proteins 22, 378-391.
    • (1995) Proteins , vol.22 , pp. 378-391
    • Schulze-Gahmen, U.1    Kim, S.H.2
  • 40
    • 0028341134 scopus 로고
    • The glycine-rich sequence of protein kinases: A multifunctional element
    • Bossemeyer, D. (1994). The glycine-rich sequence of protein kinases: a multifunctional element. Trends Biochem. Sci. 19, 201-205.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 201-205
    • Bossemeyer, D.1
  • 41
    • 0029963896 scopus 로고    scopus 로고
    • Three-dimensional structure of mammalian casein kinase I: Molecular basis for phosphate recognition
    • Longenecker, K.L., Roach, P.J. & Hurley, T.D. (1996). Three-dimensional structure of mammalian casein kinase I: molecular basis for phosphate recognition. J. Mol. Biol. 257, 618-631.
    • (1996) J. Mol. Biol. , vol.257 , pp. 618-631
    • Longenecker, K.L.1    Roach, P.J.2    Hurley, T.D.3
  • 42
    • 0027527937 scopus 로고
    • Expression of the catalytic subunit of cAMP-dependent protein kinase in Escherichia coli- Multiple isozymes reflect different phosphorylation states
    • Herberg, F.W., Bell, S.M. & Taylor, S.S. (1993). Expression of the catalytic subunit of cAMP-dependent protein kinase in Escherichia coli- multiple isozymes reflect different phosphorylation states. Protein Eng. 6, 771-777.
    • (1993) Protein Eng. , vol.6 , pp. 771-777
    • Herberg, F.W.1    Bell, S.M.2    Taylor, S.S.3
  • 43
    • 0030570725 scopus 로고    scopus 로고
    • In vivo activation of recombinant cAPK catalytic subunit active site mutants by coexpression of the wild type enzyme, evidence for intermolecular cotranslational phosphorylation
    • Girod, A., Kinzel, V. & Bossemeyer, D. (1996). In vivo activation of recombinant cAPK catalytic subunit active site mutants by coexpression of the wild type enzyme, evidence for intermolecular cotranslational phosphorylation. FEBS Lett. 391, 121-125.
    • (1996) FEBS Lett. , vol.391 , pp. 121-125
    • Girod, A.1    Kinzel, V.2    Bossemeyer, D.3
  • 45
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project No. 4. (1994). The CCP4 suite: programs for protein crystallography. Acta Cryst. D 50, 760-763.
    • (1994) Acta Cryst. D , vol.50 , pp. 760-763
  • 46
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. (1994). AMoRe: an automated package for molecular replacement. Acta Cryst. A 50, 157-163.
    • (1994) Acta Cryst. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 47
    • 0026597444 scopus 로고
    • Free R-value - A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A.T. (1992). Free R-value - a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 49
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh, R.A. & Huber, R. (1991). Accurate bond and angle parameters for X-ray protein structure refinement. Acta Cryst. A 47, 392-400.
    • (1991) Acta Cryst. A , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 50
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron-density maps and location of errors in these models
    • Jones, T.A., Zou, J.Y., Cowan, S.W. & Kjeldgard, M. (1991). Improved methods for building protein models in electron-density maps and location of errors in these models. Acta Cryst. A 47, 110-119.
    • (1991) Acta Cryst. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgard, M.4
  • 51
    • 37049100024 scopus 로고
    • X-ray crystal-structure of staurosporine - New alkaloid from a Steptomyces strain
    • Furusaki, A., et al., & Omura, S. (1978). X-ray crystal-structure of staurosporine - new alkaloid from a Steptomyces strain. J. Chem. Soc. Chem. Commun. 18, 800-801.
    • (1978) J. Chem. Soc. Chem. Commun. , vol.18 , pp. 800-801
    • Furusaki, A.1    Omura, S.2
  • 52
    • 0028198290 scopus 로고
    • Absolute configuration of staurosporine by X-ray analysis
    • Funato, N., et al., & Omura, S. (1994). Absolute configuration of staurosporine by X-ray analysis. Tetrahedron Lett. 35, 1251-1254.
    • (1994) Tetrahedron Lett. , vol.35 , pp. 1251-1254
    • Funato, N.1    Omura, S.2


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