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Volumn 76, Issue 6, 1999, Pages 3219-3226

Binding of calcium ions to bacteriorhodopsin

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACID; BACTERIORHODOPSIN; CALCIUM ION; CYSTEINE; EOSIN;

EID: 0242504873     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(99)77473-4     Document Type: Article
Times cited : (40)

References (55)
  • 1
    • 0024801589 scopus 로고
    • Factors affecting the absorption maxima of acidic forms of bacteriorhodopsin. A study with artificial pigments
    • Albeck, A., N. Friedman, M. Sheves, and M. Ottolenghi. 1989. Factors affecting the absorption maxima of acidic forms of bacteriorhodopsin. A study with artificial pigments. Biophys. J. 56:1259-1265.
    • (1989) Biophys. J. , vol.56 , pp. 1259-1265
    • Albeck, A.1    Friedman, N.2    Sheves, M.3    Ottolenghi, M.4
  • 2
    • 0028098029 scopus 로고
    • Surface charge of bacteriorhodopsin detected with covalently bound pH indicators at selected extracellular and cytoplasmic sites
    • Alexiev, U., T. Marti, M. P. Heyn, H. G. Khorana, and P. Scherrer. 1994. Surface charge of bacteriorhodopsin detected with covalently bound pH indicators at selected extracellular and cytoplasmic sites. Biochemistry. 33:298-306.
    • (1994) Biochemistry , vol.33 , pp. 298-306
    • Alexiev, U.1    Marti, T.2    Heyn, M.P.3    Khorana, H.G.4    Scherrer, P.5
  • 3
    • 0028887546 scopus 로고
    • Rapid long-range proton diffusion along the surface of the purple membrane and delayed proton transfer into the bulk
    • Alexiev, U., R. Mollaaghababa, P. Scherrer, H. G. Khorana, and M. P. Heyn. 1995. Rapid long-range proton diffusion along the surface of the purple membrane and delayed proton transfer into the bulk. Proc. Natl. Acad. Sci. USA. 92:372-376.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 372-376
    • Alexiev, U.1    Mollaaghababa, R.2    Scherrer, P.3    Khorana, H.G.4    Heyn, M.P.5
  • 4
    • 0022970570 scopus 로고
    • Characterization of metal ion-binding sites in bacteriorhodopsin
    • Ariki, M., and J. K. Lanyi. 1986. Characterization of metal ion-binding sites in bacteriorhodopsin. J. Biol. Chem. 261:8167-8174.
    • (1986) J. Biol. Chem. , vol.261 , pp. 8167-8174
    • Ariki, M.1    Lanyi, J.K.2
  • 5
    • 0023654484 scopus 로고
    • Metal ion binding sites of bacteriorhodopsin
    • Ariki, M., D. Magde, and J. K. Lanyi. 1987. Metal ion binding sites of bacteriorhodopsin. J. Biol. Chem. 262:4947-4951.
    • (1987) J. Biol. Chem. , vol.262 , pp. 4947-4951
    • Ariki, M.1    Magde, D.2    Lanyi, J.K.3
  • 6
    • 0030808219 scopus 로고    scopus 로고
    • Glutamate-194 to cysteine mutation inhibits fast light-induced proton release in bacteriorhodopsin
    • Balashov, S. P., E. S. Imasheva, T. G. Ebrey, N. Chen, D. R. Menick, and R. K. Crouch. 1997. Glutamate-194 to cysteine mutation inhibits fast light-induced proton release in bacteriorhodopsin. Biochemistry. 36: 8671-8676.
    • (1997) Biochemistry , vol.36 , pp. 8671-8676
    • Balashov, S.P.1    Imasheva, E.S.2    Ebrey, T.G.3    Chen, N.4    Menick, D.R.5    Crouch, R.K.6
  • 7
    • 0030069626 scopus 로고    scopus 로고
    • Titration of aspartate-85 in bacteriorhodopsin: What it says about chromophore isomerization and proton release
    • Balashov, S. P., E. S. Imasheva, R. Govindjee, and T. G. Ebrey. 1996. Titration of aspartate-85 in bacteriorhodopsin: what it says about chromophore isomerization and proton release. Biophys. J. 70:473-481.
    • (1996) Biophys. J. , vol.70 , pp. 473-481
    • Balashov, S.P.1    Imasheva, E.S.2    Govindjee, R.3    Ebrey, T.G.4
  • 8
    • 0030572372 scopus 로고    scopus 로고
    • Role of calcium in the proton pump of bacteriorhodopsin. Microwave evidence for a cation-gated mechanism
    • Birge, R. R., D. S. K. Govender, K. C. Izgi, and E. H. L Tan. 1996. Role of calcium in the proton pump of bacteriorhodopsin. Microwave evidence for a cation-gated mechanism. J. Phys. Chem. 100:9990-10004.
    • (1996) J. Phys. Chem. , vol.100 , pp. 9990-10004
    • Birge, R.R.1    Govender, D.S.K.2    Izgi, K.C.3    Tan, E.H.L.4
  • 9
    • 0033602998 scopus 로고    scopus 로고
    • Functional roles of aspartic acid residues at the cytoplasmic surface of bacteriorhodopsin
    • in press
    • Brown, L. S., R. Needleman, and J. K. Lanyi. 1999. Functional roles of aspartic acid residues at the cytoplasmic surface of bacteriorhodopsin. Biochemistry. (in press).
    • (1999) Biochemistry
    • Brown, L.S.1    Needleman, R.2    Lanyi, J.K.3
  • 10
    • 0028949144 scopus 로고
    • Relationship of proton release at the extracellular surface to deprotonation of the Schiff base in the bacteriorhodopsin photocycle
    • Cao, Y., L. S. Brown, J. Sasaki, A. Maeda, R. Needleman, and J. K. Lanyi. 1995. Relationship of proton release at the extracellular surface to deprotonation of the Schiff base in the bacteriorhodopsin photocycle. Biophys. J. 68:1518-1530.
    • (1995) Biophys. J. , vol.68 , pp. 1518-1530
    • Cao, Y.1    Brown, L.S.2    Sasaki, J.3    Maeda, A.4    Needleman, R.5    Lanyi, J.K.6
  • 12
    • 0001087887 scopus 로고
    • On the molecular mechanisms of the Schiff base deprotonation during the bacteriorhodopsin photocycle
    • Chronister, E. L., T. C. Corcoran, L. Song, and M. A. El-Sayed. 1986. On the molecular mechanisms of the Schiff base deprotonation during the bacteriorhodopsin photocycle. Proc. Natl. Acad. Sci. USA. 83: 8580-8584.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 8580-8584
    • Chronister, E.L.1    Corcoran, T.C.2    Song, L.3    El-Sayed, M.A.4
  • 13
    • 0023214570 scopus 로고
    • Evidence for the involvement of more than one metal cation in the Schiff base deprotonation process during the photocycle of bacteriorhodopsin
    • Corcoran, T. C., K. Z. Ismail, and M. A. El-Sayed. 1987. Evidence for the involvement of more than one metal cation in the Schiff base deprotonation process during the photocycle of bacteriorhodopsin. Proc. Natl. Acad. Sci. USA. 84:4094-4098.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 4094-4098
    • Corcoran, T.C.1    Ismail, K.Z.2    El-Sayed, M.A.3
  • 14
    • 0032562215 scopus 로고    scopus 로고
    • Existence of a proton transfer chain in bacteriorhodopsin: Participation of Glu-194 in the release of protons to the extracellular surface
    • Dioumaev, A. K., H. T. Richter, L. S. Brown, M. Tanio, S. Tuzi, H. Saitô, Y. Kimura, R. Needleman, and J. K. Lanyi. 1998. Existence of a proton transfer chain in bacteriorhodopsin: participation of Glu-194 in the release of protons to the extracellular surface. Biochemistry. 37: 2496-2506.
    • (1998) Biochemistry , vol.37 , pp. 2496-2506
    • Dioumaev, A.K.1    Richter, H.T.2    Brown, L.S.3    Tanio, M.4    Tuzi, S.5    Saitô, H.6    Kimura, Y.7    Needleman, R.8    Lanyi, J.K.9
  • 15
    • 0001564104 scopus 로고
    • Importance of bound divalent cations to the tyrosine deprotonation during the photocycle of bacteriorhodopsin
    • Dupuis, P., T. C. Corcoran, and M. A. El-Sayed. 1985. Importance of bound divalent cations to the tyrosine deprotonation during the photocycle of bacteriorhodopsin. Proc. Natl. Acad. Sci. USA. 82:3662-3664.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 3662-3664
    • Dupuis, P.1    Corcoran, T.C.2    El-Sayed, M.A.3
  • 16
    • 0002979180 scopus 로고
    • Light energy transduction in bacteriorhodopsin
    • M. Jackson, editor. CRC Press, Boca Raton, FL
    • Ebrey, T. G. 1993. Light energy transduction in bacteriorhodopsin. In Thermodynamics of Membranes, Receptors and Channels. M. Jackson, editor. CRC Press, Boca Raton, FL. 353-387.
    • (1993) Thermodynamics of Membranes, Receptors and Channels , pp. 353-387
    • Ebrey, T.G.1
  • 17
    • 0019197464 scopus 로고
    • Investigations into the effect of acid on the spectral and kinetic properties of purple membrane from Halobacterium halobium
    • Edgerton, M. E., T. A. Moore, and C. Greenwood. 1980. Investigations into the effect of acid on the spectral and kinetic properties of purple membrane from Halobacterium halobium. Biochem. J. 189:413-420.
    • (1980) Biochem. J. , vol.189 , pp. 413-420
    • Edgerton, M.E.1    Moore, T.A.2    Greenwood, C.3
  • 18
    • 0032578378 scopus 로고    scopus 로고
    • Lipid patches in membrane protein oligomers: Crystal structure of the bacteriorhodopsin-lipid complex
    • Essen, L. O., R. Siegert, W. D. Lehmann, and D. Oesterhelt. 1998. Lipid patches in membrane protein oligomers: crystal structure of the bacteriorhodopsin-lipid complex. Proc. Natl. Acad. Sci. USA. 95: 11673-11678.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11673-11678
    • Essen, L.O.1    Siegert, R.2    Lehmann, W.D.3    Oesterhelt, D.4
  • 19
    • 0018635144 scopus 로고
    • Chromophore equilibria in bacteriorhodopsin
    • Fischer, U., and D. Oesterhelt. 1979. Chromophore equilibria in bacteriorhodopsin. Biophys. J. 28:211-230.
    • (1979) Biophys. J. , vol.28 , pp. 211-230
    • Fischer, U.1    Oesterhelt, D.2
  • 20
    • 0030781314 scopus 로고    scopus 로고
    • Titration kinetics of Asp-85 in bacteriorhodopsin: Exclusion of the retinal pocket as the color-controlling cation binding site
    • Fu, X., S. Bressler, M. Ottolenghi, T. Eliash, N. Friedman, and M. Sheves. 1997. Titration kinetics of Asp-85 in bacteriorhodopsin: exclusion of the retinal pocket as the color-controlling cation binding site. FEBS Lett. 416:167-170.
    • (1997) FEBS Lett. , vol.416 , pp. 167-170
    • Fu, X.1    Bressler, S.2    Ottolenghi, M.3    Eliash, T.4    Friedman, N.5    Sheves, M.6
  • 21
    • 33748561199 scopus 로고    scopus 로고
    • Calcium and magnesium binding in native and structurally perturbed purple membrane
    • Griffiths, J. A., J. King, D. F. Yang, R. Browner, and M. A. El-Sayed. 1996. Calcium and magnesium binding in native and structurally perturbed purple membrane. J. Phys. Chem. 100:929-933.
    • (1996) J. Phys. Chem. , vol.100 , pp. 929-933
    • Griffiths, J.A.1    King, J.2    Yang, D.F.3    Browner, R.4    El-Sayed, M.A.5
  • 22
  • 23
    • 0028102402 scopus 로고
    • Proton migration along the membrane surface and retarded surface to bulk transfer
    • Heberle, J., J. Riesle, G. Thiedemann, D. Oesterhelt, and N. A. Dencher. 1994. Proton migration along the membrane surface and retarded surface to bulk transfer. Nature. 370:379-382.
    • (1994) Nature , vol.370 , pp. 379-382
    • Heberle, J.1    Riesle, J.2    Thiedemann, G.3    Oesterhelt, D.4    Dencher, N.A.5
  • 24
    • 0026007784 scopus 로고
    • Binding of a single divalent cation directly correlates with the blue-to-purple transition in bacteriorhodopsin
    • Jonas, R., and T. G. Ebrey. 1991. Binding of a single divalent cation directly correlates with the blue-to-purple transition in bacteriorhodopsin. Proc. Natl. Acad. Sci. USA. 88:149-153.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 149-153
    • Jonas, R.1    Ebrey, T.G.2
  • 25
    • 0025581345 scopus 로고
    • Purple membrane: Surface charge density and the multiple effect of pH and cations
    • Jonas, R., Y. Koutalos, and T. G. Ebrey. 1990. Purple membrane: surface charge density and the multiple effect of pH and cations. Photochem. Photobiol. 52:1163-1177.
    • (1990) Photochem. Photobiol. , vol.52 , pp. 1163-1177
    • Jonas, R.1    Koutalos, Y.2    Ebrey, T.G.3
  • 26
    • 21244499919 scopus 로고
    • Lipids of purple membrane from extreme halophiles and of methanogenic bacteria
    • Kates, M., S. C. Kushwaha, and G. D. Sprott. 1982. Lipids of purple membrane from extreme halophiles and of methanogenic bacteria. Methods Enzymol. 88:98-111.
    • (1982) Methods Enzymol. , vol.88 , pp. 98-111
    • Kates, M.1    Kushwaha, S.C.2    Sprott, G.D.3
  • 27
    • 0021524244 scopus 로고
    • Salt and pH-dependent changes of the purple membrane absorption spectrum
    • Kimura, Y., A. Ikegami, and W. Stoeckenius. 1984. Salt and pH-dependent changes of the purple membrane absorption spectrum. Photochem. Photobiol. 40:641-646.
    • (1984) Photochem. Photobiol. , vol.40 , pp. 641-646
    • Kimura, Y.1    Ikegami, A.2    Stoeckenius, W.3
  • 29
    • 0002515070 scopus 로고
    • Effect of pH on the photoreaction cycles of bacteriorhodopsin
    • Kobayashi, T., H. Ohtani, J.-I. Iwai, A. Ikegami, and H. Uchiki. 1983. Effect of pH on the photoreaction cycles of bacteriorhodopsin. FEBS Lett. 162:197-200.
    • (1983) FEBS Lett. , vol.162 , pp. 197-200
    • Kobayashi, T.1    Ohtani, H.2    Iwai, J.-I.3    Ikegami, A.4    Uchiki, H.5
  • 30
    • 0027769837 scopus 로고
    • Proton translocation mechanism and energetics in the light-driven pump bacteriorhodopsin
    • Lanyi, J. K. 1993. Proton translocation mechanism and energetics in the light-driven pump bacteriorhodopsin. Biochim. Biophys. Acta Bio-Energetics. 1183:241-261.
    • (1993) Biochim. Biophys. Acta Bio-Energetics , vol.1183 , pp. 241-261
    • Lanyi, J.K.1
  • 31
    • 0031282975 scopus 로고    scopus 로고
    • Mechanism of ion transport across membranes. Bacteriorhodopsin as a prototype for proton pumps
    • Lanyi, J. K. 1997. Mechanism of ion transport across membranes. Bacteriorhodopsin as a prototype for proton pumps. J. Biol. Chem. 272: 31209-31212.
    • (1997) J. Biol. Chem. , vol.272 , pp. 31209-31212
    • Lanyi, J.K.1
  • 32
    • 85005688720 scopus 로고
    • The photocycles of bacteriorhodopsin
    • Lanyi, J. K., and G. Váró. 1995. The photocycles of bacteriorhodopsin. Isr. J. Chem. 35:365-386.
    • (1995) Isr. J. Chem. , vol.35 , pp. 365-386
    • Lanyi, J.K.1    Váró, G.2
  • 33
    • 0032546920 scopus 로고    scopus 로고
    • Proton transfer pathways in bacteriorhodopsin at 2.3 Ångstrom resolution
    • Luecke, H., H. T. Richter, and J. K. Lanyi. 1998. Proton transfer pathways in bacteriorhodopsin at 2.3 Ångstrom resolution. Science. 280: 1934-1937.
    • (1998) Science , vol.280 , pp. 1934-1937
    • Luecke, H.1    Richter, H.T.2    Lanyi, J.K.3
  • 35
    • 0028798997 scopus 로고
    • Photovoltage kinetics of the acid-blue and acid-purple forms of bacteriorhodopsin: Evidence for no net charge transfer
    • Moltke, S., and M. P. Heyn. 1995. Photovoltage kinetics of the acid-blue and acid-purple forms of bacteriorhodopsin: evidence for no net charge transfer. Biophys. J. 69:2066-2073.
    • (1995) Biophys. J. , vol.69 , pp. 2066-2073
    • Moltke, S.1    Heyn, M.P.2
  • 36
    • 0018640375 scopus 로고
    • Effect of acid pH on the absorption spectra and photoreactions of bacteriorhodopsin
    • Mowery, P. C., R. H. Lozier, Q. Chae, Y. W. Tseng, M. Taylor, and W. Stoeckenius, 1979. Effect of acid pH on the absorption spectra and photoreactions of bacteriorhodopsin. Biochemistry. 18:4100-4107.
    • (1979) Biochemistry , vol.18 , pp. 4100-4107
    • Mowery, P.C.1    Lozier, R.H.2    Chae, Q.3    Tseng, Y.W.4    Taylor, M.5    Stoeckenius, W.6
  • 37
    • 0025323919 scopus 로고
    • Effect of a light-induced pH gradient on purple-to-blue and purple-to-red transitions of bacteriorhodopsin
    • Nasuda-Kouyama, A., K. Fukuda, T. Iio, and T. Kouyama. 1990. Effect of a light-induced pH gradient on purple-to-blue and purple-to-red transitions of bacteriorhodopsin. Biochemistry. 29:6778-6788.
    • (1990) Biochemistry , vol.29 , pp. 6778-6788
    • Nasuda-Kouyama, A.1    Fukuda, K.2    Iio, T.3    Kouyama, T.4
  • 38
    • 0016376428 scopus 로고
    • Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane
    • Oesterhelt, D., and W. Stoeckenius. 1974. Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane. Methods Enzymol. 31:667-678.
    • (1974) Methods Enzymol. , vol.31 , pp. 667-678
    • Oesterhelt, D.1    Stoeckenius, W.2
  • 39
    • 0021759973 scopus 로고
    • Induction of the blue form of bacteriorhodopsin by low concentrations of sodium dodecyl sulfate
    • Padros, E., M. Duñach, and M. Sabes. 1984. Induction of the blue form of bacteriorhodopsin by low concentrations of sodium dodecyl sulfate. Biochim. Biophys. Acta. 769:1-7.
    • (1984) Biochim. Biophys. Acta , vol.769 , pp. 1-7
    • Padros, E.1    Duñach, M.2    Sabes, M.3
  • 40
    • 0030864048 scopus 로고    scopus 로고
    • X-ray structure of bacteriorhodopsin at 2.5 Ångstroms from microcrystals grown in lipidic cubic phases
    • Pebay-Peyroula, E., G. Rummel, J. P. Rosenbusch, and E. M. Landau. 1997. X-ray structure of bacteriorhodopsin at 2.5 Ångstroms from microcrystals grown in lipidic cubic phases. Science. 277:1676-1681.
    • (1997) Science , vol.277 , pp. 1676-1681
    • Pebay-Peyroula, E.1    Rummel, G.2    Rosenbusch, J.P.3    Landau, E.M.4
  • 42
    • 0029665673 scopus 로고    scopus 로고
    • A linkage of the pKa's of Asp-85 and Glu-204 forms part of the reprotonation switch of bacteriorhodopsin
    • Richter, H. T., L. S. Brown, R. Needleman, and J. K. Lanyi. 1996. A linkage of the pKa's of Asp-85 and Glu-204 forms part of the reprotonation switch of bacteriorhodopsin. Biochemistry. 35:4054-4062.
    • (1996) Biochemistry , vol.35 , pp. 4054-4062
    • Richter, H.T.1    Brown, L.S.2    Needleman, R.3    Lanyi, J.K.4
  • 43
    • 0022021238 scopus 로고
    • Resonance Raman spectra of the acidified and deionized forms of bacteriorhodopsin
    • Smith, S. O., and R. A. Mathies. 1985. Resonance Raman spectra of the acidified and deionized forms of bacteriorhodopsin. Biophys. J. 47: 251-254.
    • (1985) Biophys. J. , vol.47 , pp. 251-254
    • Smith, S.O.1    Mathies, R.A.2
  • 44
    • 0025157075 scopus 로고
    • Protonation state of Asp (Glu)-85 regulates the purple-to-blue transition in bacteriorhodopsin mutants Arg-82 → Ala and Asp-85 → Glu: The blue form is inactive in proton translocation
    • Subramaniam, S., T. Marti, and H. G. Khorana. 1990. Protonation state of Asp (Glu)-85 regulates the purple-to-blue transition in bacteriorhodopsin mutants Arg-82 → Ala and Asp-85 → Glu: the blue form is inactive in proton translocation. Proc. Natl. Acad. Sci. USA. 87:1013-1017.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 1013-1017
    • Subramaniam, S.1    Marti, T.2    Khorana, H.G.3
  • 45
    • 0010172563 scopus 로고
    • Effect of lipid surface charges on the purple-to-blue transition of bacteriorhodopsin
    • Szundi, I., and W. Stoeckenius. 1987. Effect of lipid surface charges on the purple-to-blue transition of bacteriorhodopsin. Proc. Natl. Acad. Sci. USA. 84:3681-3684.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 3681-3684
    • Szundi, I.1    Stoeckenius, W.2
  • 46
    • 0024065110 scopus 로고
    • Purple-to-blue transition of bacteriorhodopsin in a neutral lipid environment
    • Szundi, I., and W. Stoeckenius. 1988. Purple-to-blue transition of bacteriorhodopsin in a neutral lipid environment. Biophys. J. 54:227-232.
    • (1988) Biophys. J. , vol.54 , pp. 227-232
    • Szundi, I.1    Stoeckenius, W.2
  • 47
    • 0024709605 scopus 로고
    • Surface pH controls purple-to-blue transition of bacteriorhodopsin. A theoretical model of purple membrane surface
    • Szundi, I., and W. Stoeckenius. 1989. Surface pH controls purple-to-blue transition of bacteriorhodopsin. A theoretical model of purple membrane surface. Biophys. J. 56:369-383.
    • (1989) Biophys. J. , vol.56 , pp. 369-383
    • Szundi, I.1    Stoeckenius, W.2
  • 49
    • 0018426023 scopus 로고
    • The low pH species of bacteriorhodopsin. Structure and proton pump activity
    • Tsuji, K., and K. Rosenheck. 1979. The low pH species of bacteriorhodopsin. Structure and proton pump activity. FEBS Lett. 98:368-372.
    • (1979) FEBS Lett. , vol.98 , pp. 368-372
    • Tsuji, K.1    Rosenheck, K.2
  • 51
    • 0024829218 scopus 로고
    • Photoreactions of bacteriorhodopsin at acid pH
    • Váró, G., and J. K. Lanyi. 1989. Photoreactions of bacteriorhodopsin at acid pH. Biophys. J. 56:1143-1151.
    • (1989) Biophys. J. , vol.56 , pp. 1143-1151
    • Váró, G.1    Lanyi, J.K.2
  • 52
    • 0028970553 scopus 로고
    • 2+ binding to deionized monomerized and to retinal removed bacteriorhodopsin
    • 2+ binding to deionized monomerized and to retinal removed bacteriorhodopsin. Biophys. J. 69:2056-2059.
    • (1995) Biophys. J. , vol.69 , pp. 2056-2059
    • Yang, D.F.1    El-Sayed, M.A.2


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