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Volumn 83, Issue 2, 2007, Pages 351-363

Comparison of stability predictions and simulated unfolding of rhodopsin structures

Author keywords

[No Author keywords available]

Indexed keywords

MAMMALIA;

EID: 34247211105     PISSN: 00318655     EISSN: None     Source Type: Journal    
DOI: 10.1562/2006-06-20-RA-942     Document Type: Conference Paper
Times cited : (19)

References (65)
  • 1
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson, C. M (2003) Protein folding and misfolding. Nature 426, 884-990.
    • (2003) Nature , vol.426 , pp. 884-990
    • Dobson, C.M.1
  • 3
    • 15944387765 scopus 로고    scopus 로고
    • Dual role of interactions between membranous and soluble portions of helical membrane receptors for folding and signaling
    • Klein-Seetharaman, J. (2005) Dual role of interactions between membranous and soluble portions of helical membrane receptors for folding and signaling. Trends Pharmacol. Sci. 26, 183-189.
    • (2005) Trends Pharmacol. Sci , vol.26 , pp. 183-189
    • Klein-Seetharaman, J.1
  • 4
    • 0029006086 scopus 로고
    • Retinitis pigmentosa and allied diseases. Implications of genetic heterogeneity
    • Dryja, T. P. and E. L. Berson (1995) Retinitis pigmentosa and allied diseases. Implications of genetic heterogeneity. Invest. Ophthalmol. Vis. Sci. 36, 1197-1200.
    • (1995) Invest. Ophthalmol. Vis. Sci , vol.36 , pp. 1197-1200
    • Dryja, T.P.1    Berson, E.L.2
  • 5
    • 0027537949 scopus 로고
    • Retinitis pigmentosa. The Friedenwald Lecture
    • Berson, E. L (1993) Retinitis pigmentosa. The Friedenwald Lecture. Invest. Ophthalmol. Vis. Sci. 34, 1659-1676.
    • (1993) Invest. Ophthalmol. Vis. Sci , vol.34 , pp. 1659-1676
    • Berson, E.L.1
  • 7
    • 84889439782 scopus 로고    scopus 로고
    • Microbial rhodopsins: Phylogenetic and functional diversity
    • Edited by W. R. Briggs and J .L. Spudich, Wiley-VCH, Weinheim, Germany
    • Spudich, J. L. and K-H. Jung (2005) Microbial rhodopsins: Phylogenetic and functional diversity. In Handbook of Photosensory Receptors (Edited by W. R. Briggs and J .L. Spudich). Wiley-VCH, Weinheim, Germany.
    • (2005) Handbook of Photosensory Receptors
    • Spudich, J.L.1    Jung, K.-H.2
  • 8
    • 0036532207 scopus 로고    scopus 로고
    • Structure of rhodopsin and the superfamily of seven-helical receptors: The same and not the same
    • Sakmar, T. P. (2002) Structure of rhodopsin and the superfamily of seven-helical receptors: The same and not the same. Curr. Opin. Cell Biol. 14, 189-195.
    • (2002) Curr. Opin. Cell Biol , vol.14 , pp. 189-195
    • Sakmar, T.P.1
  • 10
    • 0033515036 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: Further elucidation of the role of the intradiscal cysteines, Cys-110, -185, and -187, in rhodopsin folding and function
    • Hwa, J., P. J. Reeves, J. Klein-Seetharaman, F. Davidson and H. G. Khorana (1999) Structure and function in rhodopsin: Further elucidation of the role of the intradiscal cysteines, Cys-110, -185, and -187, in rhodopsin folding and function. Proc. Natl Acad. Sci. USA 96, 1932-1935.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 1932-1935
    • Hwa, J.1    Reeves, P.J.2    Klein-Seetharaman, J.3    Davidson, F.4    Khorana, H.G.5
  • 11
    • 0029944275 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: Correct folding and misfolding in point mutants at and in proximity to the site of the retinitis pigmentosa mutation Leu-125- > Arg in the transmembrane helix C
    • Garriga, P., X. Liu and H. G. Khorana (1996) Structure and function in rhodopsin: Correct folding and misfolding in point mutants at and in proximity to the site of the retinitis pigmentosa mutation Leu-125- > Arg in the transmembrane helix C. Proc. Natl Acad. Sci. USA 93, 4560-4564.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 4560-4564
    • Garriga, P.1    Liu, X.2    Khorana, H.G.3
  • 12
    • 0030931599 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: Packing of the helices in the transmembrane domain and folding to a tertiary structure in the intradiscal domain are coupled
    • Hwa, J., P. Garriga, X. Liu and H. G. Khorana (1997) Structure and function in rhodopsin: Packing of the helices in the transmembrane domain and folding to a tertiary structure in the intradiscal domain are coupled. Proc. Natl Acad. Sci. USA 94, 10571-10576.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 10571-10576
    • Hwa, J.1    Garriga, P.2    Liu, X.3    Khorana, H.G.4
  • 13
    • 0035942215 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: Mass spectrometric identification of the abnormal intradiscal disulfide bond in misfolded retinitis pigmentosa mutants
    • Hwa, J., J. Klein-Seetharaman and H. G. Khorana (2001) Structure and function in rhodopsin: Mass spectrometric identification of the abnormal intradiscal disulfide bond in misfolded retinitis pigmentosa mutants. Proc. Natl Acad. Sci. USA 98, 4872-4876.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 4872-4876
    • Hwa, J.1    Klein-Seetharaman, J.2    Khorana, H.G.3
  • 14
    • 0028351937 scopus 로고
    • Structure and function in rhodopsin: Replacement by alanine of cysteine residues 110 and 187, components of a conserved disulfide bond in rhodopsin, affects the light-activated metarhodopsin II state
    • Davidson, F. F., P. C. Loewen and H. G. Khorana (1994) Structure and function in rhodopsin: Replacement by alanine of cysteine residues 110 and 187, components of a conserved disulfide bond in rhodopsin, affects the light-activated metarhodopsin II state. Proc. Natl Acad. Sci. USA 91, 4029-4033.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 4029-4033
    • Davidson, F.F.1    Loewen, P.C.2    Khorana, H.G.3
  • 15
    • 0030904764 scopus 로고    scopus 로고
    • Intermediates in the assembly of bacteriorhodopsin investigated by time-resolved absorption spectroscopy
    • Booth, P. J. and A. Farooq (1997) Intermediates in the assembly of bacteriorhodopsin investigated by time-resolved absorption spectroscopy. Eur J. Biochem 246, 674-680.
    • (1997) Eur J. Biochem , vol.246 , pp. 674-680
    • Booth, P.J.1    Farooq, A.2
  • 16
    • 0019887931 scopus 로고
    • Refolding of an integral membrane protein: Denaturation, renaturation, and reconstitution of intact bacteriorhodopsin and two proteolytic fragments
    • Huang, K. S., H. Bayley, M. J. Liao, E. London and H. G. Khorana (1981) Refolding of an integral membrane protein: Denaturation, renaturation, and reconstitution of intact bacteriorhodopsin and two proteolytic fragments. J. Biol. Chem 256, 3802-3809.
    • (1981) J. Biol. Chem , vol.256 , pp. 3802-3809
    • Huang, K.S.1    Bayley, H.2    Liao, M.J.3    London, E.4    Khorana, H.G.5
  • 17
    • 0023583873 scopus 로고
    • Refolding of bacteriorhodopsin in lipid bilayers. A thermodynamically controlled two-stage process
    • Popot, J. L., S. E. Gerchman and D. M. Engelman (1987) Refolding of bacteriorhodopsin in lipid bilayers. A thermodynamically controlled two-stage process. J. Mol. Biol. 198, 655-676.
    • (1987) J. Mol. Biol , vol.198 , pp. 655-676
    • Popot, J.L.1    Gerchman, S.E.2    Engelman, D.M.3
  • 18
    • 0032502747 scopus 로고    scopus 로고
    • Refolding of bacteriorhodopsin from expressed polypeptide fragments
    • Marti, T. (1998) Refolding of bacteriorhodopsin from expressed polypeptide fragments. J. Biol. Chem. 273, 9312-9322.
    • (1998) J. Biol. Chem , vol.273 , pp. 9312-9322
    • Marti, T.1
  • 19
    • 0028931922 scopus 로고
    • In vivo assembly of rhodopsin from expressed polypeptide fragments
    • Ridge, K. D., S. S. Lee and L. L. Yao (1995) In vivo assembly of rhodopsin from expressed polypeptide fragments. Proc. Natl Acad. Sci. USA 92, 3204-3208.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 3204-3208
    • Ridge, K.D.1    Lee, S.S.2    Yao, L.L.3
  • 20
    • 0036888379 scopus 로고    scopus 로고
    • Identifying protein folding cores from the evolution of flexible regions during unfolding
    • Hespenheide, B. M., A. J. Rader, M. F. Thorpe and L. A. Kuhn (2002) Identifying protein folding cores from the evolution of flexible regions during unfolding. J. Mol. Graph. Model. 21, 195-207.
    • (2002) J. Mol. Graph. Model , vol.21 , pp. 195-207
    • Hespenheide, B.M.1    Rader, A.J.2    Thorpe, M.F.3    Kuhn, L.A.4
  • 23
    • 33751094833 scopus 로고    scopus 로고
    • Predisposition of the dark state of rhodopsin to functional changes in structure
    • Isin, B., A. J. Rader, H. K. Dhiman, J. Klein-Seetharaman and I. Bahar (2006) Predisposition of the dark state of rhodopsin to functional changes in structure. Proteins. 65, 970-983.
    • (2006) Proteins , vol.65 , pp. 970-983
    • Isin, B.1    Rader, A.J.2    Dhiman, H.K.3    Klein-Seetharaman, J.4    Bahar, I.5
  • 24
    • 0028922277 scopus 로고
    • Structure and function in rhodopsin. Separation and characterization of the correctly folded and misfolded opsins produced on expression of an opsin mutant gene containing only the native intradiscal cysteine codons
    • Ridge, K. D., Z. Lu, X. Liu and H. G. Khorana (1995) Structure and function in rhodopsin. Separation and characterization of the correctly folded and misfolded opsins produced on expression of an opsin mutant gene containing only the native intradiscal cysteine codons. Biochemistry 34, 3261-3267.
    • (1995) Biochemistry , vol.34 , pp. 3261-3267
    • Ridge, K.D.1    Lu, Z.2    Liu, X.3    Khorana, H.G.4
  • 25
    • 0028957661 scopus 로고
    • Structure and function in rhodopsin. Measurement of the rate of metarhodopsin II decay by fluorescence spectroscopy
    • Farrens, D. L. and H. G. Khorana (1995) Structure and function in rhodopsin. Measurement of the rate of metarhodopsin II decay by fluorescence spectroscopy. J. Biol. Chem. 270, 5073-5076.
    • (1995) J. Biol. Chem , vol.270 , pp. 5073-5076
    • Farrens, D.L.1    Khorana, H.G.2
  • 26
    • 4344581120 scopus 로고    scopus 로고
    • The retinal conformation and its environment in rhodopsin in light of a new 2.2 A crystal structure
    • Okada, T., M. Sugihara, A. N. Bondar, M. Elstner, P. Entel and V. Buss (2004) The retinal conformation and its environment in rhodopsin in light of a new 2.2 A crystal structure. J. Mol. Biol. 342, 571-583.
    • (2004) J. Mol. Biol , vol.342 , pp. 571-583
    • Okada, T.1    Sugihara, M.2    Bondar, A.N.3    Elstner, M.4    Entel, P.5    Buss, V.6
  • 27
    • 3843096037 scopus 로고    scopus 로고
    • Crystal structure of the M intermediate of bacteriorhodopsin: Allosteric structural changes mediated by sliding movement of a transmembrane helix
    • Takeda, K., Y. Matsui, N. Kamiya, S. Adachi, H. Okumura and T. Kouyama (2004) Crystal structure of the M intermediate of bacteriorhodopsin: Allosteric structural changes mediated by sliding movement of a transmembrane helix. J. Mol. Biol. 341, 1023-1037.
    • (2004) J. Mol. Biol , vol.341 , pp. 1023-1037
    • Takeda, K.1    Matsui, Y.2    Kamiya, N.3    Adachi, S.4    Okumura, H.5    Kouyama, T.6
  • 28
    • 23144461249 scopus 로고    scopus 로고
    • I-Mutant2.0: Predicting stability changes upon mutation from the protein sequence or structure
    • Capriotti, E., P. Fariselli and R. Casadio (2005) I-Mutant2.0: Predicting stability changes upon mutation from the protein sequence or structure. Nucleic Acids Res. 33, W306-W310.
    • (2005) Nucleic Acids Res , vol.33
    • Capriotti, E.1    Fariselli, P.2    Casadio, R.3
  • 29
    • 0036838311 scopus 로고    scopus 로고
    • Distance-scaled, finite ideal-gas reference state improves structure-derived potentials of mean force for structure selection and stability prediction
    • Zhou, H. and Y. Zhou (2002) Distance-scaled, finite ideal-gas reference state improves structure-derived potentials of mean force for structure selection and stability prediction. Protein Sci. 11, 2714-2726.
    • (2002) Protein Sci , vol.11 , pp. 2714-2726
    • Zhou, H.1    Zhou, Y.2
  • 30
    • 0036291145 scopus 로고    scopus 로고
    • Predicting changes in the stability of proteins and protein complexes: A study of more than 1000 mutations
    • Guerois, R., J. E. Nielsen and L. Serrano (2002) Predicting changes in the stability of proteins and protein complexes: A study of more than 1000 mutations. J. Mol. Biol. 320, 369-387.
    • (2002) J. Mol. Biol , vol.320 , pp. 369-387
    • Guerois, R.1    Nielsen, J.E.2    Serrano, L.3
  • 31
    • 0035427398 scopus 로고    scopus 로고
    • Protein flexibility predictions using graph theory
    • Jacobs, D. J., A. J. Rader, L. A. Kuhn and M. F. Thorpe (2001) Protein flexibility predictions using graph theory. Proteins 44, 150-165.
    • (2001) Proteins , vol.44 , pp. 150-165
    • Jacobs, D.J.1    Rader, A.J.2    Kuhn, L.A.3    Thorpe, M.F.4
  • 32
    • 0031718310 scopus 로고    scopus 로고
    • Homology modeling, model and software evaluation: Three related resources
    • Rodriguez, R., G. Chinea, N. Lopez, T. Pons and G. Vriend (1998) Homology modeling, model and software evaluation: Three related resources. Bioinformatics 14, 523-528.
    • (1998) Bioinformatics , vol.14 , pp. 523-528
    • Rodriguez, R.1    Chinea, G.2    Lopez, N.3    Pons, T.4    Vriend, G.5
  • 33
    • 0346492917 scopus 로고    scopus 로고
    • Folding core predictions from network models of proteins
    • Rader, A. J. and I. Bahar (2004) Folding core predictions from network models of proteins. Polymer 45, 659-668.
    • (2004) Polymer , vol.45 , pp. 659-668
    • Rader, A.J.1    Bahar, I.2
  • 35
    • 0029619259 scopus 로고
    • Knowledge-based protein secondary structure assignment
    • Frishman, D. and P. Argos (1995) Knowledge-based protein secondary structure assignment. Proteins 23, 566-579.
    • (1995) Proteins , vol.23 , pp. 566-579
    • Frishman, D.1    Argos, P.2
  • 36
    • 13444280419 scopus 로고    scopus 로고
    • PDB_TM: Selection and membrane localization of transmembrane proteins in the protein data bank
    • Tusnady, G. E., Z. Dosztanyi and I. Simon (2005) PDB_TM: Selection and membrane localization of transmembrane proteins in the protein data bank. Nucleic Acids Res. 33, D275-278.
    • (2005) Nucleic Acids Res , vol.33
    • Tusnady, G.E.1    Dosztanyi, Z.2    Simon, I.3
  • 37
    • 0037221599 scopus 로고    scopus 로고
    • Is there a unifying mechanism for protein folding?
    • Daggett, V. and A. R. Fersht (2003) Is there a unifying mechanism for protein folding? Trends Biochem. Sci. 28, 18-25.
    • (2003) Trends Biochem. Sci , vol.28 , pp. 18-25
    • Daggett, V.1    Fersht, A.R.2
  • 38
    • 0032584233 scopus 로고    scopus 로고
    • Structure-based prediction of the stability of transmembrane helix-helix interactions: The sequence dependence of glycophorin A dimerization
    • MacKenzie, K. R. and D. M. Engelman (1998) Structure-based prediction of the stability of transmembrane helix-helix interactions: The sequence dependence of glycophorin A dimerization. Proc. Natl Acad. Sci. USA 95, 3583-3590.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 3583-3590
    • MacKenzie, K.R.1    Engelman, D.M.2
  • 39
    • 17144406820 scopus 로고    scopus 로고
    • Prediction of the mutation-induced change in thermodynamic stabilities of membrane proteins from free energy simulations
    • Park, H. and S. Lee (2005) Prediction of the mutation-induced change in thermodynamic stabilities of membrane proteins from free energy simulations. Biophys. Chem. 114, 191-197.
    • (2005) Biophys. Chem , vol.114 , pp. 191-197
    • Park, H.1    Lee, S.2
  • 40
    • 0025306687 scopus 로고
    • Role of the intradiscal domain in rhodopsin assembly and function
    • Doi, T., R. S. Molday and H. G. Khorana (1990) Role of the intradiscal domain in rhodopsin assembly and function. Proc. Natl Acad. Sci. USA 87, 4991-4995.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 4991-4995
    • Doi, T.1    Molday, R.S.2    Khorana, H.G.3
  • 41
    • 0028318173 scopus 로고
    • The high affinity state of the beta 2-adrenergic receptor requires unique interaction between conserved and non-conserved extracellular loop cysteines
    • Noda, K., Y. Saad, R. M. Graham and S. S. Karnik (1994) The high affinity state of the beta 2-adrenergic receptor requires unique interaction between conserved and non-conserved extracellular loop cysteines. J. Biol. Chem. 269, 6743-6752.
    • (1994) J. Biol. Chem , vol.269 , pp. 6743-6752
    • Noda, K.1    Saad, Y.2    Graham, R.M.3    Karnik, S.S.4
  • 42
    • 0034051478 scopus 로고    scopus 로고
    • Folding and assembly of rhodopsin from expressed fragments
    • Ridge, K. D. and N. G. Abdulaev (2000) Folding and assembly of rhodopsin from expressed fragments. Methods Enzymol. 315, 59-70.
    • (2000) Methods Enzymol , vol.315 , pp. 59-70
    • Ridge, K.D.1    Abdulaev, N.G.2
  • 43
    • 29144532994 scopus 로고    scopus 로고
    • Characterizing molecular interactions in different bacteriorhodopsin assemblies by single-molecule force spectroscopy
    • Sapra, K. T., H. Besir, D. Oesterhelt and D. J. Muller (2006) Characterizing molecular interactions in different bacteriorhodopsin assemblies by single-molecule force spectroscopy. J. Mol. Biol. 355, 640-650.
    • (2006) J. Mol. Biol , vol.355 , pp. 640-650
    • Sapra, K.T.1    Besir, H.2    Oesterhelt, D.3    Muller, D.J.4
  • 46
    • 2942623955 scopus 로고    scopus 로고
    • Polytopic membrane protein folding and assembly in vitro and in vivo
    • Booth, P. J. and S. High (2004) Polytopic membrane protein folding and assembly in vitro and in vivo. Mol. Membr Biol. 21, 163-170.
    • (2004) Mol. Membr Biol , vol.21 , pp. 163-170
    • Booth, P.J.1    High, S.2
  • 47
    • 0035957523 scopus 로고    scopus 로고
    • Structure and function in bacteriorhodopsin: The effect of the interhelical loops on the protein folding kinetics
    • Allen, S. J., J. M. Kim, H. G. Khorana, H. Lu and P. J. Booth (2001) Structure and function in bacteriorhodopsin: The effect of the interhelical loops on the protein folding kinetics. J. Mol. Biol. 308, 423-435.
    • (2001) J. Mol. Biol , vol.308 , pp. 423-435
    • Allen, S.J.1    Kim, J.M.2    Khorana, H.G.3    Lu, H.4    Booth, P.J.5
  • 48
    • 0036932510 scopus 로고    scopus 로고
    • Stability of bacteriorhodopsin alpha-helices and loops analyzed by single-molecule force spectroscopy
    • Muller, D. J., M. Kessler, F. Oesterhelt, C. Moller, D. Oesterhelt and H. Gaub (2002) Stability of bacteriorhodopsin alpha-helices and loops analyzed by single-molecule force spectroscopy. Biophys. J. 83, 3578-3588.
    • (2002) Biophys. J , vol.83 , pp. 3578-3588
    • Muller, D.J.1    Kessler, M.2    Oesterhelt, F.3    Moller, C.4    Oesterhelt, D.5    Gaub, H.6
  • 50
    • 13844298943 scopus 로고    scopus 로고
    • Probing origins of molecular interactions stabilizing the membrane proteins halorhodopsin and bacteriorhodopsin
    • Cisneros, D. A., D. Oesterhelt and D. J. Muller (2005) Probing origins of molecular interactions stabilizing the membrane proteins halorhodopsin and bacteriorhodopsin. Structure 13, 235-242.
    • (2005) Structure , vol.13 , pp. 235-242
    • Cisneros, D.A.1    Oesterhelt, D.2    Muller, D.J.3
  • 51
    • 0032582541 scopus 로고    scopus 로고
    • Secondary structure of bacteriorhodopsin fragments. External sequence constraints specify the conformation of transmembrane helices
    • Luneberg, J., M. Widmann, M. Dathe and T. Marti (1998) Secondary structure of bacteriorhodopsin fragments. External sequence constraints specify the conformation of transmembrane helices. J. Biol. Chem. 273, 28822-28830.
    • (1998) J. Biol. Chem , vol.273 , pp. 28822-28830
    • Luneberg, J.1    Widmann, M.2    Dathe, M.3    Marti, T.4
  • 53
    • 4143101547 scopus 로고    scopus 로고
    • The machinery of membrane protein assembly
    • White, S. H. and G. V. Heijne (2004) The machinery of membrane protein assembly. Curr. Opin. Struct. Biol. 14, 397-404.
    • (2004) Curr. Opin. Struct. Biol , vol.14 , pp. 397-404
    • White, S.H.1    Heijne, G.V.2
  • 54
    • 0025249842 scopus 로고
    • Membrane protein folding and oligomerization: The two-stage model
    • Popot, J. L. and D. M. Engelman (1990) Membrane protein folding and oligomerization: The two-stage model. Biochemistry 29, 4031-4037.
    • (1990) Biochemistry , vol.29 , pp. 4031-4037
    • Popot, J.L.1    Engelman, D.M.2
  • 55
    • 0035367173 scopus 로고    scopus 로고
    • Helical membrane proteins: Diversity of functions in the context of simple architecture
    • Ubarretxena-Belandia, I. and D. M. Engelman (2001) Helical membrane proteins: Diversity of functions in the context of simple architecture. Curr. Opin. Struct. Biol. 11, 370-376.
    • (2001) Curr. Opin. Struct. Biol , vol.11 , pp. 370-376
    • Ubarretxena-Belandia, I.1    Engelman, D.M.2
  • 60
    • 0034717007 scopus 로고    scopus 로고
    • Structure of the light-driven chloride pump halorhodopsin at 1.8 A resolution
    • Kolbe, M., H. Besir, L. O. Essen and D. Oesterhelt (2000) Structure of the light-driven chloride pump halorhodopsin at 1.8 A resolution. Science 288, 1390-1396.
    • (2000) Science , vol.288 , pp. 1390-1396
    • Kolbe, M.1    Besir, H.2    Essen, L.O.3    Oesterhelt, D.4
  • 63
    • 0033824470 scopus 로고    scopus 로고
    • DaliLite workbench for protein structure comparison
    • Holm, L. and J. Park (2000) DaliLite workbench for protein structure comparison. Bioinformatics 16, 566-567.
    • (2000) Bioinformatics , vol.16 , pp. 566-567
    • Holm, L.1    Park, J.2


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