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Volumn 440, Issue 1, 2011, Pages 43-49

Fluorescence detection of GDP in real time with the reagentless biosensor rhodamine-ParM

Author keywords

Fluorescence; GTPase; Nucleotide exchange factor; Rhodamine stacking; Sensor

Indexed keywords

ADENOSINE DIPHOSPHATE; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATE; TETRAMETHYLRHODAMINE;

EID: 80054920667     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20110349     Document Type: Article
Times cited : (10)

References (50)
  • 1
    • 0025010979 scopus 로고
    • The GTPase superfamily: A conserved switch for diverse cell functions
    • Bourne, H. R., Sanders, D. A. and McCormick, F. (1990) The GTPase superfamily: a conserved switch for diverse cell functions. Nature 348, 125-132
    • (1990) Nature , vol.348 , pp. 125-132
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 2
    • 0742288598 scopus 로고    scopus 로고
    • The dynamin superfamily: Universal membrane tubulation and fission molecules?
    • DOI 10.1038/nrm1313
    • Praefcke, G. J. and McMahon, H. T. (2004) The dynamin superfamily: universal membrane tubulation and fission molecules? Nat. Rev. Mol. Cell Biol. 5, 133-147 (Pubitemid 38160256)
    • (2004) Nature Reviews Molecular Cell Biology , vol.5 , Issue.2 , pp. 133-147
    • Praefcke, G.J.K.1    McMahon, H.T.2
  • 3
    • 37049020693 scopus 로고    scopus 로고
    • Emerging themes in IFN-γ-induced macrophage immunity by the p47 and p65 GTPase families
    • DOI 10.1016/j.imbio.2007.09.018, PII S0171298507001064, Macrophage and Dendritic Cells
    • Shenoy, A. R., Kim, B. H., Choi, H. P., Matsuzawa, T., Tiwari, S. and MacMicking, J. D. (2007) Emerging themes in IFN-γ -induced macrophage immunity by the p47 and p65 GTPase families. Immunobiology 212, 771-784 (Pubitemid 350246255)
    • (2008) Immunobiology , vol.212 , Issue.9-10 , pp. 771-784
    • Shenoy, A.R.1    Kim, B.-H.2    Choi, H.-P.3    Matsuzawa, T.4    Tiwari, S.5    MacMicking, J.D.6
  • 5
    • 0028098798 scopus 로고
    • Direct, real-time measurement of rapid inorganic phosphate release using a novel fluorescent probe and its application to actomyosin subfragment 1 ATPase
    • Brune, M., Hunter, J. L., Corrie, J. E. and Webb, M. R. (1994) Direct, real-time measurement of rapid inorganic phosphate release using a novel fluorescent probe and its application to actomyosin subfragment 1 ATPase. Biochemistry 33, 8262-8271
    • (1994) Biochemistry , vol.33 , pp. 8262-8271
    • Brune, M.1    Hunter, J.L.2    Corrie, J.E.3    Webb, M.R.4
  • 8
    • 59349118696 scopus 로고    scopus 로고
    • A genetically encoded fluorescent reporter of ATP:ADP ratio
    • Berg, J., Hung, Y. P. and Yellen, G. (2009) A genetically encoded fluorescent reporter of ATP:ADP ratio. Nat. Methods 6, 161-166
    • (2009) Nat. Methods , vol.6 , pp. 161-166
    • Berg, J.1    Hung, Y.P.2    Yellen, G.3
  • 9
    • 70349449239 scopus 로고    scopus 로고
    • Visualization of ATP levels inside single living cells with fluorescence resonance energy transfer-based genetically encoded indicators
    • Imamura, H., Nhat, K. P., Togawa, H., Saito, K., Iino, R., Kato-Yamada, Y., Nagai, T. and Noji, H. (2009) Visualization of ATP levels inside single living cells with fluorescence resonance energy transfer-based genetically encoded indicators. Proc. Natl. Acad. Sci. U.S.A. 106, 15651-15656
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 15651-15656
    • Imamura, H.1    Nhat, K.P.2    Togawa, H.3    Saito, K.4    Iino, R.5    Kato-Yamada, Y.6    Nagai, T.7    Noji, H.8
  • 10
    • 55949111485 scopus 로고    scopus 로고
    • Fluorescent single-stranded DNA binding protein as a probe for sensitive, real-time assays of helicase activity
    • Dillingham, M. S., Tibbles, K. L., Hunter, J. L., Bell, J. C., Kowalczykowski, S. C. and Webb, M. R. (2008) Fluorescent single-stranded DNA binding protein as a probe for sensitive, real-time assays of helicase activity. Biophys. J. 95, 3330-3339
    • (2008) Biophys. J. , vol.95 , pp. 3330-3339
    • Dillingham, M.S.1    Tibbles, K.L.2    Hunter, J.L.3    Bell, J.C.4    Kowalczykowski, S.C.5    Webb, M.R.6
  • 11
    • 70450246978 scopus 로고    scopus 로고
    • A biosensor for fluorescent determination of ADP with high time resolution
    • Kunzelmann, S. and Webb, M. R. (2009) A biosensor for fluorescent determination of ADP with high time resolution. J. Biol. Chem. 284, 33130-33138
    • (2009) J. Biol. Chem. , vol.284 , pp. 33130-33138
    • Kunzelmann, S.1    Webb, M.R.2
  • 12
    • 77951139684 scopus 로고    scopus 로고
    • A fluorescent, reagentless biosensor for ADP based on tetramethylrhodamine-labeled ParM
    • Kunzelmann, S. and Webb, M. R. (2010) A fluorescent, reagentless biosensor for ADP based on tetramethylrhodamine-labeled ParM. ACS Chem. Biol. 5, 415-425
    • (2010) ACS Chem. Biol. , vol.5 , pp. 415-425
    • Kunzelmann, S.1    Webb, M.R.2
  • 13
    • 12244298896 scopus 로고    scopus 로고
    • F-actin-like filaments formed by plasmid segregation protein ParM
    • van den Ent, F., Moller-Jensen, J., Amos, L. A., Gerdes, K. and Lowe, J. (2002) F-actin-like filaments formed by plasmid segregation protein ParM. EMBO J. 21, 6935-6943
    • (2002) EMBO J. , vol.21 , pp. 6935-6943
    • Van Den Ent, F.1    Moller-Jensen, J.2    Amos, L.A.3    Gerdes, K.4    Lowe, J.5
  • 15
    • 0000053614 scopus 로고
    • Aggregation of equilibriums of xanthene dyes
    • Selwyn, J. E. and Steinfeld, J. I. (1972) Aggregation of equilibriums of xanthene dyes. J. Phys. Chem. 76, 762-774
    • (1972) J. Phys. Chem. , vol.76 , pp. 762-774
    • Selwyn, J.E.1    Steinfeld, J.I.2
  • 16
    • 49949085338 scopus 로고    scopus 로고
    • Bacterial actin: Architecture of the ParMRC plasmid DNA partitioning complex
    • Salje, J. and Lowe, J. (2008) Bacterial actin: architecture of the ParMRC plasmid DNA partitioning complex. EMBO J. 27, 2230-2238
    • (2008) EMBO J. , vol.27 , pp. 2230-2238
    • Salje, J.1    Lowe, J.2
  • 17
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace, C. N., Vajdos, F., Fee, L., Grimsley, G. and Gray, T. (1995) How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 4, 2411-2423
    • (1995) Protein Sci. , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 18
    • 31144442429 scopus 로고    scopus 로고
    • Optimised synthesis of 6-iodoacetamidotetramethylrhodamine
    • Munasinghe, V. R. N. and Corrie, J. E. T. (2006) Optimised synthesis of 6-iodoacetamidotetramethylrhodamine. ARKIVOC ii, 143-149 (Pubitemid 43128279)
    • (2006) Arkivoc , vol.2006 , Issue.2 , pp. 143-149
    • Munasinghe, V.R.N.1    Corrie, J.E.T.2
  • 19
    • 37049075338 scopus 로고
    • Synthesis and characterisation of pure isomers of iodoacetamidotetramethylrhodamine
    • Corrie, J. E. T. and Craik, J. S. (1994) Synthesis and characterisation of pure isomers of iodoacetamidotetramethylrhodamine. J. Chem. Soc. Perkin Trans. I, 2967-2973
    • (1994) J. Chem. Soc. Perkin Trans. , vol.1 , pp. 2967-2973
    • Corrie, J.E.T.1    Craik, J.S.2
  • 20
    • 77949585672 scopus 로고    scopus 로고
    • Biochemical properties of the human guanylate binding protein 5 and a tumor-specific truncated splice variant
    • Wehner, M. and Herrmann, C. (2010) Biochemical properties of the human guanylate binding protein 5 and a tumor-specific truncated splice variant. FEBS J. 277, 1597-1605
    • (2010) FEBS J. , vol.277 , pp. 1597-1605
    • Wehner, M.1    Herrmann, C.2
  • 21
    • 0011756062 scopus 로고    scopus 로고
    • Version 5. Erithacus Software Ltd, Horley, U.K.
    • Leatherbarrow, R. J. (2001) Grafit Version 5. Erithacus Software Ltd, Horley, U.K.
    • (2001) Grafit
    • Leatherbarrow, R.J.1
  • 22
    • 33644835005 scopus 로고    scopus 로고
    • Structure of a transient intermediate for GTP hydrolysis by Ras
    • DOI 10.1016/j.str.2005.12.010, PII S0969212606000748
    • Ford, B., Hornak, V., Kleinman, H. and Nassar, N. (2006) Structure of a transient intermediate for GTP hydrolysis by ras. Structure 14, 427-436 (Pubitemid 43363476)
    • (2006) Structure , vol.14 , Issue.3 , pp. 427-436
    • Ford, B.1    Hornak, V.2    Kleinman, H.3    Nassar, N.4
  • 23
    • 38949129203 scopus 로고    scopus 로고
    • Molecular structure of the ParM polymer and the mechanism leading to its nucleotide-driven dynamic instability
    • DOI 10.1038/sj.emboj.7601978, PII 7601978
    • Popp, D., Narita, A., Oda, T., Fujisawa, T., Matsuo, H., Nitanai, Y., Iwasa, M., Maeda, K., Onishi, H. and Maeda, Y. (2008) Molecular structure of the ParM polymer and the mechanism leading to its nucleotide-driven dynamic instability. EMBO J. 27, 570-579 (Pubitemid 351225678)
    • (2008) EMBO Journal , vol.27 , Issue.3 , pp. 570-579
    • Popp, D.1    Narita, A.2    Oda, T.3    Fujisawa, T.4    Matsuo, H.5    Nitanai, Y.6    Iwasa, M.7    Maeda, K.8    Onishi, H.9    Maeda, Y.10
  • 24
    • 0345346100 scopus 로고
    • The preparation and enzymatic hydrolysis of reduced and S-carboxymethylated proteins
    • Crestfield, A. M., Moore, S. and Stein, W. H. (1963) The preparation and enzymatic hydrolysis of reduced and S-carboxymethylated proteins. J. Biol. Chem. 238, 622-627
    • (1963) J. Biol. Chem. , vol.238 , pp. 622-627
    • Crestfield, A.M.1    Moore, S.2    Stein, W.H.3
  • 25
    • 0006339343 scopus 로고
    • Chemical modification of proteins
    • Neurath, H., ed. Academic Press, New York
    • Glazer, A. N. (1976) Chemical modification of proteins. The Proteins, Vol. II (Neurath, H., ed.), pp. 1-103, Academic Press, New York
    • (1976) The Proteins , vol.2 , pp. 1-103
    • Glazer, A.N.1
  • 26
    • 77957008551 scopus 로고
    • Carboxymethylation
    • Gurd, F. R. N. (1967) Carboxymethylation. Methods Enzymol. 11, 532-541
    • (1967) Methods Enzymol. , vol.11 , pp. 532-541
    • Gurd, F.R.N.1
  • 27
    • 0033981862 scopus 로고    scopus 로고
    • Covalent modification as a strategy to block protein-protein interactions with small-molecule drugs
    • Way, J. C. (2000) Covalent modification as a strategy to block protein-protein interactions with small-molecule drugs. Curr. Opin. Chem. Biol. 4, 40-46
    • (2000) Curr. Opin. Chem. Biol. , vol.4 , pp. 40-46
    • Way, J.C.1
  • 29
    • 0019464274 scopus 로고
    • New fluorochromes for thiols: Maleimide and iodoacetamide derivatives of a 3-phenylcoumarin fluorophore
    • Sippel, T. O. (1981) New fluorochromes for thiols: maleimide and iodoacetamide derivatives of a 3-phenylcoumarin fluorophore. J. Histochem. Cytochem. 29, 314-316
    • (1981) J. Histochem. Cytochem. , vol.29 , pp. 314-316
    • Sippel, T.O.1
  • 30
    • 2942616852 scopus 로고    scopus 로고
    • GBP-5 splicing variants: New guanylate-binding proteins with tumor-associated expression and antigenicity
    • DOI 10.1111/j.0022-202X.2004.22613.x
    • Fellenberg, F., Hartmann, T. B., Dummer, R., Usener, D., Schadendorf, D. and Eichmuller, S. (2004) GBP-5 splicing variants: new guanylate-binding proteins with tumor-associated expression and antigenicity. J. Invest. Dermatol. 122, 1510-1517 (Pubitemid 38757235)
    • (2004) Journal of Investigative Dermatology , vol.122 , Issue.6 , pp. 1510-1517
    • Fellenberg, F.1    Hartmann, T.B.2    Dummer, R.3    Usener, D.4    Schadendorf, D.5    Eichmuller, S.6
  • 31
    • 0032493812 scopus 로고    scopus 로고
    • Increasing complexity of the Ras signaling pathway
    • DOI 10.1074/jbc.273.32.19925
    • Vojtek, A. B. and Der, C. J. (1998) Increasing complexity of the Ras signaling pathway. J. Biol. Chem. 273, 19925-19928 (Pubitemid 28377538)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.32 , pp. 19925-19928
    • Vojtek, A.B.1    Der, C.J.2
  • 32
    • 21844465952 scopus 로고    scopus 로고
    • Structure of the G60A mutant of Ras: Implications for the dominant negative effect
    • DOI 10.1074/jbc.M502240200
    • Ford, B., Skowronek, K., Boykevisch, S., Bar-Sagi, D. and Nassar, N. (2005) Structure of the G60A mutant of Ras: implications for the dominant negative effect. J. Biol. Chem. 280, 25697-25705 (Pubitemid 40962279)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.27 , pp. 25697-25705
    • Ford, B.1    Skowronek, K.2    Boykevisch, S.3    Bar-Sagi, D.4    Nassar, N.5
  • 34
    • 0344885558 scopus 로고    scopus 로고
    • Structural evidence for feedback activation by Ras.GTP of the Ras-specific nucleotide exchange factor SOS
    • DOI 10.1016/S0092-8674(03)00149-1
    • Margarit, S. M., Sondermann, H., Hall, B. E., Nagar, B., Hoelz, A., Pirruccello, M., Bar-Sagi, D. and Kuriyan, J. (2003) Structural evidence for feedback activation by Ras.GTP of the Ras-specific nucleotide exchange factor SOS. Cell 112, 685-695 (Pubitemid 36331780)
    • (2003) Cell , vol.112 , Issue.5 , pp. 685-695
    • Margarit, S.M.1    Sondermann, H.2    Hall, B.E.3    Nagar, B.4    Hoelz, A.5    Pirruccello, M.6    Bar-Sagi, D.7    Kuriyan, J.8
  • 35
    • 0025195630 scopus 로고
    • Hydrolysis of GTP by p21NRAS, the NRAS protooncogene product, is accompanied by a conformational change in the wild-type protein: Use of a single fluorescent probe at the catalytic site
    • Neal, S. E., Eccleston, J. F. and Webb, M. R. (1990) Hydrolysis of GTP by p21NRAS, the NRAS protooncogene product, is accompanied by a conformational change in the wild-type protein: use of a single fluorescent probe at the catalytic site. Proc. Natl. Acad. Sci. U.S.A. 87, 3562-3565
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 3562-3565
    • Neal, S.E.1    Eccleston, J.F.2    Webb, M.R.3
  • 36
    • 0032546533 scopus 로고    scopus 로고
    • Kinetic analysis by fluorescence of the interaction between Ras and the catalytic domain of the guanine nucleotide exchange factor Cdc25(Mm)
    • DOI 10.1021/bi972621j
    • Lenzen, C., Cool, R. H., Prinz, H., Kuhlmann, J. and Wittinghofer, A. (1998) Kinetic analysis by fluorescence of the interaction between Ras and the catalytic domain of the guanine nucleotide exchange factor Cdc25Mm. Biochemistry 37, 7420-7430 (Pubitemid 28235225)
    • (1998) Biochemistry , vol.37 , Issue.20 , pp. 7420-7430
    • Lenzen, C.1    Cool, R.H.2    Prinz, H.3    Kuhlmann, J.4    Wittinghofer, A.5
  • 37
    • 0035834388 scopus 로고    scopus 로고
    • The guanine nucleotide-binding switch in three dimensions
    • DOI 10.1126/science.1062023
    • Vetter, I. R. and Wittinghofer, A. (2001) The guanine nucleotide-binding switch in three dimensions. Science 294, 1299-1304 (Pubitemid 33063089)
    • (2001) Science , vol.294 , Issue.5545 , pp. 1299-1304
    • Vetter, I.R.1    Wittinghofer, A.2
  • 38
    • 0035942352 scopus 로고    scopus 로고
    • A fluorescent sensor of the phosphorylation state of nucleoside diphosphate kinase and its use to monitor nucleoside diphosphate concentrations in real time
    • DOI 10.1021/bi002484h
    • Brune, M., Corrie, J. E. and Webb, M. R. (2001) A fluorescent sensor of the phosphorylation state of nucleoside diphosphate kinase and its use to monitor nucleoside diphosphate concentrations in real time. Biochemistry 40, 5087-5094 (Pubitemid 32332556)
    • (2001) Biochemistry , vol.40 , Issue.16 , pp. 5087-5094
    • Brune, M.1    Corrie, J.E.T.2    Webb, M.R.3
  • 40
    • 0013946834 scopus 로고
    • A new micromethod for the colorimetric determination of inorganic phosphate
    • Itaya, K. and Ui, M. (1966) A new micromethod for the colorimetric determination of inorganic phosphate. Clin. Chim. Acta 14, 361-366
    • (1966) Clin. Chim. Acta , vol.14 , pp. 361-366
    • Itaya, K.1    Ui, M.2
  • 41
    • 30544443744 scopus 로고    scopus 로고
    • Rapid purification of native dynamin I and colorimetric GTPase assay
    • DOI 10.1016/S0076-6879(05)04049-8, PII S0076687905040498, 49, GTPases Regulating Membrane Dynamics
    • Quan, A. and Robinson, P. J. (2005) Rapid purification of native dynamin I and colorimetric GTPase assay. Methods Enzymol. 404, 556-569 (Pubitemid 43082015)
    • (2006) Methods in Enzymology , vol.404 , pp. 556-569
    • Quan, A.1    Robinson, P.J.2
  • 42
    • 0026684153 scopus 로고
    • A continuous spectrophotometric assay for inorganic phosphate and for measuring phosphate release kinetics in biological systems
    • Webb, M. R. (1992) A continuous spectrophotometric assay for inorganic phosphate and for measuring phosphate release kinetics in biological systems. Proc. Natl. Acad. Sci. U.S.A. 89, 4884-4887
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 4884-4887
    • Webb, M.R.1
  • 43
    • 0026670215 scopus 로고
    • Interaction of GTPase-activating protein with p21ras, measured using a continuous assay for inorganic phosphate release
    • Webb, M. R. and Hunter, J. L. (1992) Interaction of GTPase-activating protein with p21ras, measured using a continuous assay for inorganic phosphate release. Biochem. J. 287, 555-559
    • (1992) Biochem. J. , vol.287 , pp. 555-559
    • Webb, M.R.1    Hunter, J.L.2
  • 44
    • 0028789134 scopus 로고
    • Kinetics of inorganic phosphate release during the interaction of p21ras with the GTPase-activating proteins, p120-GAP and neurofibromin
    • Nixon, A. E., Brune, M., Lowe, P. N. and Webb, M. R. (1995) Kinetics of inorganic phosphate release during the interaction of p21ras with the GTPase-activating proteins, p120-GAP and neurofibromin. Biochemistry 34, 15592-15598
    • (1995) Biochemistry , vol.34 , pp. 15592-15598
    • Nixon, A.E.1    Brune, M.2    Lowe, P.N.3    Webb, M.R.4
  • 45
    • 0034691319 scopus 로고    scopus 로고
    • The mechanism of GTP hydrolysis by Dynamin II: A transient kinetic study
    • DOI 10.1021/bi000033r
    • Binns, D. D., Helms, M. K., Barylko, B., Davis, C. T., Jameson, D. M., Albanesi, J. P. and Eccleston, J. F. (2000) The mechanism of GTP hydrolysis by dynamin II: a transient kinetic study. Biochemistry 39, 7188-7196 (Pubitemid 30413108)
    • (2000) Biochemistry , vol.39 , Issue.24 , pp. 7188-7196
    • Binns, D.D.1    Helms, M.K.2    Barylko, B.3    Davis, C.T.4    Jameson, D.M.5    Albanesi, J.P.6    Eccleston, J.F.7
  • 46
    • 0023668228 scopus 로고
    • Interaction of a fluorescent analogue of GDP with elongation factor Tu: Steady-state and time-resolved fluorescence studies
    • Eccleston, J. F., Gratton, E. and Jameson, D. M. (1987) Interaction of a fluorescent analogue of GDP with elongation factor Tu: steady-state and time-resolved fluorescence studies. Biochemistry 26, 3902-3907
    • (1987) Biochemistry , vol.26 , pp. 3902-3907
    • Eccleston, J.F.1    Gratton, E.2    Jameson, D.M.3
  • 47
    • 0025337447 scopus 로고
    • Kinetics of interaction of nucleotides with nucleotide-free H-ras p21
    • DOI 10.1021/bi00477a025
    • John, J., Sohmen, R., Feuerstein, J., Linke, R., Wittinghofer, A. and Goody, R. S. (1990) Kinetics of interaction of nucleotides with nucleotide-free H-ras p21. Biochemistry 29, 6058-6065 (Pubitemid 20201412)
    • (1990) Biochemistry , vol.29 , Issue.25 , pp. 6058-6065
    • John, J.1    Sohmen, R.2    Feuerstein, J.3    Linke, R.4    Wittinghofer, A.5    Goody, R.S.6
  • 48
    • 30544454966 scopus 로고    scopus 로고
    • Nucleotide binding and self-stimulated GTPase activity of human guanylate-binding protein 1 (hGBP1)
    • Kunzelmann, S., Praefcke, G. J. and Herrmann, C. (2005) Nucleotide binding and self-stimulated GTPase activity of human guanylate-binding protein 1 (hGBP1). Methods Enzymol. 404, 512-527
    • (2005) Methods Enzymol. , vol.404 , pp. 512-527
    • Kunzelmann, S.1    Praefcke, G.J.2    Herrmann, C.3
  • 49
    • 0036928818 scopus 로고    scopus 로고
    • Fluorescently labelled guanine nucleotide binding proteins to analyse elementary steps of GAP-catalysed reactions
    • DOI 10.1016/S0022-2836(02)01136-1
    • Kraemer, A., Brinkmann, T., Plettner, I., Goody, R. and Wittinghofer, A. (2002) Fluorescently labelled guanine nucleotide binding proteins to analyse elementary steps of GAP-catalysed reactions. J. Mol. Biol. 324, 763-774 (Pubitemid 36044111)
    • (2002) Journal of Molecular Biology , vol.324 , Issue.4 , pp. 763-774
    • Kraemer, A.1    Brinkmann, T.2    Plettner, I.3    Goody, R.4    Wittinghofer, A.5
  • 50
    • 0033602921 scopus 로고    scopus 로고
    • The interaction between rac1 and its guanine nucleotide dissociation inhibitor (GDI), monitored by a single fluorescent coumarin attached to GDI
    • Newcombe, A. R., Stockley, R. W., Hunter, J. L. and Webb, M. R. (1999) The interaction between rac1 and its guanine nucleotide dissociation inhibitor (GDI), monitored by a single fluorescent coumarin attached to GDI. Biochemistry 38, 6879-6886
    • (1999) Biochemistry , vol.38 , pp. 6879-6886
    • Newcombe, A.R.1    Stockley, R.W.2    Hunter, J.L.3    Webb, M.R.4


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