메뉴 건너뛰기




Volumn 51, Issue 6, 2010, Pages 1332-1343

New insights on the protein-ligand interaction differences between the two primary cellular retinol carriers

Author keywords

barrel fold; Cellular retinol binding proteins; Hydrogen deuterium exchange; Intracellular lipid binding proteins; Ligand affinity; Nuclear magnetic resonance; Spectroscopy structural stability

Indexed keywords

ALANINE; ARGININE; CELLULAR RETINOL BINDING PROTEIN; CELLULAR RETINOL BINDING PROTEIN 1; CELLULAR RETINOL BINDING PROTEIN 2; DEUTERIUM; HYDROGEN; ISOLEUCINE; LYSINE; PHENYLALANINE; RETINOL; THREONINE; UNCLASSIFIED DRUG; VALINE;

EID: 77952688100     PISSN: 00222275     EISSN: 15397262     Source Type: Journal    
DOI: 10.1194/jlr.M002006     Document Type: Article
Times cited : (13)

References (54)
  • 2
    • 33745387612 scopus 로고    scopus 로고
    • Overview of retinoid metabolism and function
    • Blomhoff, R., and H. K. Blomhoff. 2006. Overview of retinoid metabolism and function. J. Neurobiol. 66: 606-630.
    • (2006) J. Neurobiol. , vol.66 , pp. 606-630
    • Blomhoff, R.1    Blomhoff, H.K.2
  • 4
    • 0029846699 scopus 로고    scopus 로고
    • Structure/function of cytoplasmic vitamin A-binding proteins
    • Li, E., and A. W. Norris. 1996. Structure/function of cytoplasmic vitamin A-binding proteins. Annu. Rev. Nutr. 16: 205-234. (Pubitemid 26286853)
    • (1996) Annual Review of Nutrition , vol.16 , pp. 205-234
    • Li, E.1    Norris, A.W.2
  • 5
    • 0034660094 scopus 로고    scopus 로고
    • Retinoid-binding proteins: Mediators of retinoid action
    • DOI 10.1042/0264-6021:3480481
    • Noy, N. 2000. Retinoid-binding proteins: mediators of retinoid action. Biochem. J. 348: 481-495. (Pubitemid 30410236)
    • (2000) Biochemical Journal , vol.348 , Issue.3 , pp. 481-495
    • Noy, N.1
  • 6
    • 0025907475 scopus 로고
    • Fluorine nuclear magnetic resonance analysis of the ligand binding properties of two homologous rat cellular retinol-binding proteins expressed
    • Li, E., S. J. Qian, N. S. Winter, A. d'Avignon, M. S. Levin, and J. I. Gordon. 1991. Fluorine nuclear magnetic resonance analysis of the ligand binding properties of two homologous rat cellular retinol-binding proteins expressed in Escherichia coli. J. Biol. Chem. 266: 3622-3629.
    • (1991) Escherichia Coli. J. Biol. Chem. , vol.266 , pp. 3622-3629
    • Li, E.1    Qian, S.J.2    Winter, N.S.3    D'Avignon, A.4    Levin, M.S.5    Gordon, J.I.6
  • 7
    • 0015752625 scopus 로고
    • In vitro binding of retinol to rat-tissue components
    • Bashor, M. M., D. O. Toft, and F. Chytil. 1973. In vitro binding of retinol to rat-tissue components. Proc. Natl. Acad. Sci. USA. 70: 3483-3487.
    • (1973) Proc. Natl. Acad. Sci. USA , vol.70 , pp. 3483-3487
    • Bashor, M.M.1    Toft, D.O.2    Chytil, F.3
  • 8
    • 0017821248 scopus 로고
    • Cellular retinol-binding protein from rat liver. Purification and characterization
    • Ong, D. E., and F. Chytil. 1978. Cellular retinol-binding protein from rat liver. Purification and characterization. J. Biol. Chem. 253: 828-832. (Pubitemid 8271462)
    • (1978) Journal of Biological Chemistry , vol.253 , Issue.3 , pp. 828-832
    • Ong, D.E.1    Chytil, F.2
  • 9
    • 0032488909 scopus 로고    scopus 로고
    • The transfer of retinol from serum retinol-binding protein to cellular retinol-binding protein is mediated by a membrane receptor
    • DOI 10.1074/jbc.273.6.3336
    • Sundaram, M., A. Sivaprasadarao, M. M. DeSousa, and J. B. C. Findlay. 1998. The transfer of retinol from serum retinol-binding protein to cellular retinol-binding protein is mediated by a membrane receptor. J. Biol. Chem. 273: 3336-3342. (Pubitemid 28109748)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.6 , pp. 3336-3342
    • Sundaram, M.1    Sivaprasadarao, A.2    Desousa, M.M.3    Findlay, J.B.C.4
  • 10
    • 0023258566 scopus 로고
    • Vitamin a uptake from retinol-binding protein in a cell-free system from pigment epithelial cells of bovine retina. Retinol transfer from plasma retinol-binding protein to cytoplasmic retinol-binding protein with retinyl-ester formation as the intermediate step
    • Ottonello, S., S. Petrucco, and G. Maraini. 1987. Vitamin A uptake from retinol-binding protein in a cell-free system from pigment epithelial cells of bovine retina. Retinol transfer from plasma retinol-binding protein to cytoplasmic retinol-binding protein with retinyl-ester formation as the intermediate step. J. Biol. Chem. 262: 3975-3981. (Pubitemid 17102634)
    • (1987) Journal of Biological Chemistry , vol.262 , Issue.9 , pp. 3975-3981
    • Ottonello, S.1    Petrucco, S.2    Maraini, G.3
  • 11
    • 0026749335 scopus 로고
    • Differential interaction of lecithin-retinol acyltransferase with cellular retinol binding proteins
    • Herr, F. M., and D. E. Ong. 1992. Differential interaction of lecithin-retinol acyltransferase with cellular retinol binding proteins. Biochemistry. 31: 6748-6755.
    • (1992) Biochemistry , vol.31 , pp. 6748-6755
    • Herr, F.M.1    Ong, D.E.2
  • 13
    • 0025915907 scopus 로고
    • Holocellular retinol binding protein as a substrate for microsomal retinal synthesis
    • Posch, K. C., M. H. Boerman, R. D. Burns, and J. L. Napoli. 1991. Holocellular retinol binding protein as a substrate for microsomal retinal synthesis. Biochemistry. 30: 6224-6230.
    • (1991) Biochemistry , vol.30 , pp. 6224-6230
    • Posch, K.C.1    Boerman, M.H.2    Burns, R.D.3    Napoli, J.L.4
  • 14
    • 0033573832 scopus 로고    scopus 로고
    • Holo-cellular retinol-binding protein: Distinction of ligand-binding affinity from efficiency as substrate in retinal biosynthesis
    • Penzes, P., and J. L. Napoli. 1999. Holo-cellular retinol-binding protein: distinction of ligand-binding affinity from efficiency as substrate in retinal biosynthesis. Biochemistry. 38: 2088-2093. (Pubitemid 129506290)
    • (1999) Biochemistry , vol.38 , Issue.7 , pp. 2088-2093
    • Penzes, P.1    Napoli, J.L.2
  • 15
    • 0027537924 scopus 로고
    • Overview of retinoid metabolism
    • Ross, A. C. 1993. Overview of retinoid metabolism. J. Nutr. 123 (Suppl. 2): 346-350.
    • (1993) J. Nutr. , vol.123 , Issue.SUPPL. 2 , pp. 346-350
    • Ross, A.C.1
  • 16
    • 0032616999 scopus 로고    scopus 로고
    • Retinoic acid: Its biosynthesis and metabolism
    • Napoli, J. L. 1999. Retinoic acid: its biosynthesis and metabolism. Prog. Nucleic Acid Res. Mol. Biol. 63: 139-188.
    • (1999) Prog. Nucleic Acid Res. Mol. Biol. , vol.63 , pp. 139-188
    • Napoli, J.L.1
  • 17
    • 0021257996 scopus 로고
    • A novel retinol-binding protein from rat. Purification and partial characterization
    • Ong, D. E. 1984. A novel retinol-binding protein from rat. Purification and partial characterization. J. Biol. Chem. 259: 1476-1482. (Pubitemid 14104196)
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.3 , pp. 1476-1482
    • Ong, D.E.1
  • 19
    • 0038011971 scopus 로고    scopus 로고
    • Intracellular lipid binding proteins: Evolution, structure, and ligand binding
    • A. K. Duttaroy and F. Spener, editors. Wiley-VCH, Weinheim, Germany
    • Lücke, C., L. H. Gutiérrez-González, and J. A. Hamilton. 2003. Intracellular lipid binding proteins: evolution, structure, and ligand binding. In Cellular Proteins and Their Fatty Acids in Health and Disease. A. K. Duttaroy and F. Spener, editors. Wiley-VCH, Weinheim, Germany. 95-118.
    • (2003) Cellular Proteins and Their Fatty Acids in Health and Disease , pp. 95-118
    • Lücke, C.1    Gutiérrez-González, L.H.2    Hamilton, J.A.3
  • 20
    • 0039165184 scopus 로고    scopus 로고
    • A comparative study of the backbone dynamics of two closely related lipid binding proteins: Bovine heart fatty acid binding protein and porcine ileal lipid binding protein
    • Lücke, C., D. Fushman, C. Ludwig, J. A. Hamilton, J. C. Sacchettini, and H. Rüterjans. 1999. A comparative study of the backbone dyanamics of two closely related lipid binding proteins: bovine heart fatty acid binding protein and porcine ileal lipid binding protein. Mol. Cell. Biochem. 192: 109-121. (Pubitemid 29171460)
    • (1999) Molecular and Cellular Biochemistry , vol.192 , Issue.1-2 , pp. 109-121
    • Lucke, C.1    Fushman, D.2    Ludwig, C.3    Hamilton, J.A.4    Sacchettini, J.C.5    Ruterjans, H.6
  • 22
    • 0036812339 scopus 로고    scopus 로고
    • Evolution of the family of intracellular lipid binding proteins in vertebrates
    • DOI 10.1023/A:1020519011939
    • Schaap, F. G., G. J. van der Vusse, and J. F. Glatz. 2002. Evolution of the family of intracellular lipid binding proteins in vertebrates. Mol. Cell. Biochem. 239: 69-77. (Pubitemid 35385797)
    • (2002) Molecular and Cellular Biochemistry , vol.239 , Issue.1-2 , pp. 69-77
    • Schaap, F.G.1    Van Der Vusse, G.J.2    Glatz, J.F.C.3
  • 23
    • 0036784618 scopus 로고    scopus 로고
    • New insights into intracellular lipid binding proteins: The role of buried water
    • Lücke, C., S. Huang, M. Rademacher, and H. Rüterjans. 2002. New insights into intracellular lipid binding proteins: the role of buried water. Protein Sci. 11: 2382-2392.
    • (2002) Protein Sci. , vol.11 , pp. 2382-2392
    • Lücke, C.1    Huang, S.2    Rademacher, M.3    Rüterjans, H.4
  • 24
    • 0027310780 scopus 로고
    • Crystallographic studies on a family of cellular lipophilic transport proteins
    • Cowan, S. W., M. E. Newcomer, and T. A. Jones. 1993. Crystallographic studies on a family of cellular lipophilic transport proteins. J. Mol. Biol. 230: 1225-1246.
    • (1993) J. Mol. Biol. , vol.230 , pp. 1225-1246
    • Cowan, S.W.1    Newcomer, M.E.2    Jones, T.A.3
  • 28
    • 0033525633 scopus 로고    scopus 로고
    • The structure and dynamics of rat apo-cellular retinol-binding protein II in solution: Comparison with the X-ray structure
    • Lu, J., C-L. Lin, C. Tang, J. W. Ponder, J. L. F. Kao, D. P. Cistola, and E. Li. 1999. The structure and dynamics of rat apo-cellular retinol-binding protein II in solution: comparison with the X-ray structure. J. Mol. Biol. 286: 1179-1195.
    • (1999) J. Mol. Biol. , vol.286 , pp. 1179-1195
    • Lu, J.1    Lin, C.-L.2    Tang, C.3    Ponder, J.W.4    Kao, J.L.F.5    Cistola, D.P.6    Li, E.7
  • 29
    • 0027213028 scopus 로고
    • Crystal structures of holo and apo-cellular retinol-binding protein II
    • Winter, N. S., J. M. Bratt, and L. J. Banaszak. 1993. Crystal structures of holo and apo-cellular retinol-binding protein II. J. Mol. Biol. 230: 1247-1259.
    • (1993) J. Mol. Biol. , vol.230 , pp. 1247-1259
    • Winter, N.S.1    Bratt, J.M.2    Banaszak, L.J.3
  • 30
    • 0034647414 scopus 로고    scopus 로고
    • Binding of retinol induces changes in rat cellular retinol-binding protein II conformation and backbone dynamics
    • Lu, J., C-L. Lin, C. Tang, J. W. Ponder, J. L. F. Kao, D. P. Cistola, and E. Li. 2000. Binding of retinol induces changes in rat cellular retinol-binding protein II conformation and backbone dynamics. J. Mol. Biol. 300: 619-632.
    • (2000) J. Mol. Biol. , vol.300 , pp. 619-632
    • Lu, J.1    Lin, C.-L.2    Tang, C.3    Ponder, J.W.4    Kao, J.L.F.5    Cistola, D.P.6    Li, E.7
  • 31
    • 0025690173 scopus 로고
    • Structure-function analyses of mammalian cellular retinol-binding proteins by expression
    • Levin, M. S., E. Li, and J. I. Gordon. 1990. Structure-function analyses of mammalian cellular retinol-binding proteins by expression in Escherichia coli. Methods Enzymol. 189: 506-520.
    • (1990) Escherichia Coli. Methods Enzymol. , vol.189 , pp. 506-520
    • Levin, M.S.1    Li, E.2    Gordon, J.I.3
  • 32
    • 0031634651 scopus 로고    scopus 로고
    • Purification and fluorescent titration of cellular retinol-binding protein
    • Malpeli, G., C. Folli, D. Cavazzini, G. Sartori, and R. Berni. 1998. Purification and fluorescent titration of cellular retinol-binding protein. Methods Mol. Biol. 89: 111-122.
    • (1998) Methods Mol. Biol. , vol.89 , pp. 111-122
    • Malpeli, G.1    Folli, C.2    Cavazzini, D.3    Sartori, G.4    Berni, R.5
  • 34
    • 0035163373 scopus 로고    scopus 로고
    • Non-covalent binding of endogenous ligands to recombinant cellular retinol-binding proteins studied by mass spectrometric techniques
    • DOI 10.1002/rcm.497
    • Elviri, L., I. Zagnoni, M. Careri, D. Cavazzini, and G. L. Rossi. 2001. Non-covalent binding of endogenous ligands to recombinant cellular retinol-binding proteins studied by mass spectrometric techniques. Rapid Commun. Mass Spectrom. 15: 2186-2192. (Pubitemid 33077979)
    • (2001) Rapid Communications in Mass Spectrometry , vol.15 , Issue.22 , pp. 2186-2192
    • Elviri, L.1    Zagnoni, I.2    Careri, M.3    Cavazzini, D.4    Rossi, G.L.5
  • 36
    • 0030586026 scopus 로고    scopus 로고
    • Flexibility is a likely determinant of binding specificity in the case of ileal lipid binding protein
    • DOI 10.1016/S0969-2126(96)00086-X
    • Lücke, C., F. Zhang, H. Rüterjans, J. A. Hamilton, and J. C. Sacchettini. 1996. Flexibility is a likely determinant of binding specificity in the case of ileal lipid binding protein. Structure. 4: 785-800. (Pubitemid 26312363)
    • (1996) Structure , vol.4 , Issue.7 , pp. 785-800
    • Lucke, C.1    Zhang, F.2    Ruterjans, H.3    Hamilton, J.A.4    Sacchettini, J.C.5
  • 37
    • 0013571376 scopus 로고
    • NMR of amino acid residues and mononucleotides
    • John Wiley and Sons, New York
    • Wüthrich, K. ( 1986 ) NMR of amino acid residues and mononucleotides. In NMR of Proteins and Nucleic Acids. John Wiley and Sons, New York. 13-25.
    • (1986) NMR of Proteins and Nucleic Acids , pp. 13-25
    • Wüthrich, K.1
  • 38
    • 0026597879 scopus 로고
    • The chemical shift index: A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy
    • Wishart, D. S., B. D. Sykes, and F. M. Richards. 1992. The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry. 31: 1647-1651.
    • (1992) Biochemistry , vol.31 , pp. 1647-1651
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 39
    • 33745779277 scopus 로고    scopus 로고
    • Mass spectrometry techniques for detection of ligand-dependent changes in the conformational flexibility of cellular retinol-binding protein type I localized by hydrogen/deuterium exchange
    • DOI 10.1002/rcm.2547
    • Careri, M., L. Elviri, A. Mangia, I. Zagnoni, F. Torta, D. Cavazzini, and G. L. Rossi. 2006. Mass spectrometry techniques for detection of ligand-dependent changes in the conformational flexibility of cellular retinol-binding protein type I localized by hydrogen/deuterium exchange. Rapid Commun. Mass Spectrom. 20: 1973-1980. (Pubitemid 44024573)
    • (2006) Rapid Communications in Mass Spectrometry , vol.20 , Issue.13 , pp. 1973-1980
    • Careri, M.1    Elviri, L.2    Mangia, A.3    Zagnoni, I.4    Torta, F.5    Cavazzini, D.6    Rossi, G.L.7
  • 40
    • 0346159010 scopus 로고    scopus 로고
    • Acid-induced denaturation of cellular retinol-binding proteins types I and II studied by electrospray mass spectrometry
    • Careri, M., L. Elviri, I. Zagnoni, D. Cavazzini, and G. L. Rossi. 2003. Acid-induced denaturation of cellular retinol-binding proteins types I and II studied by electrospray mass spectrometry. Rapid Commun. Mass Spectrom. 17: 2773-2780. (Pubitemid 38029319)
    • (2003) Rapid Communications in Mass Spectrometry , vol.17 , Issue.24 , pp. 2773-2780
    • Careri, M.1    Elviri, L.2    Zagnoni, I.3    Cavazzini, D.4    Rossi, G.L.5
  • 42
    • 0034024888 scopus 로고    scopus 로고
    • A 'structural' water molecule in the family of fatty acid binding proteins
    • Likić, V. A., N. Juranić, S. Macura, and F. G. Prendergast. 2000. A "structural" water molecule in the family of fatty acid binding proteins. Protein Sci. 9: 497-504. (Pubitemid 30171640)
    • (2000) Protein Science , vol.9 , Issue.3 , pp. 497-504
    • Likic, V.A.1    Juranic, N.2    Macura, S.3    Prendergast, F.G.4
  • 43
    • 0034846083 scopus 로고    scopus 로고
    • Non-hydrogen bond interactions involving the methionine sulfur atom
    • Pal, D., and P. Chakrabarti. 2001. Non-hydrogen bond interactions involving the methionine sulfur atom. J. Biomol. Struct. Dyn. 19: 115-128. (Pubitemid 32844643)
    • (2001) Journal of Biomolecular Structure and Dynamics , vol.19 , Issue.1 , pp. 115-128
    • Pal, D.1    Chakrabarti, P.2
  • 45
    • 0042243493 scopus 로고    scopus 로고
    • Two homologous rat cellular retinol-binding proteins differ in local conformational flexibility
    • Lu, J., D. P. Cistola, and E. Li. 2003. Two homologous rat cellular retinol-binding proteins differ in local conformational flexibility. J. Mol. Biol. 330: 799-812.
    • (2003) J. Mol. Biol. , vol.330 , pp. 799-812
    • Lu, J.1    Cistola, D.P.2    Li, E.3
  • 46
    • 0033515649 scopus 로고    scopus 로고
    • Differential mechanisms of retinoid transfer from cellular retinol binding proteins types I and II to phospholipid membranes
    • Herr, F. M., E. Li, R. B. Weinberg, V. R. Cook, and J. Storch. 1999. Differential mechanisms of retinoid transfer from cellular retinol binding proteins types I and II to phospholipid membranes. J. Biol. Chem. 274: 9556-9563. (Pubitemid 129517931)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.14 , pp. 9556-9563
    • Herr, F.M.1    Li, E.2    Weinberg, R.B.3    Cook, V.R.4    Storch, J.5
  • 47
    • 0028307429 scopus 로고
    • Regulation of fluorescent fatty acid transfer from adipocyte and heart fatty acid binding proteins by acceptor membrane lipid composition and structure
    • Wootan, M. G., and J. Storch. 1994. Regulation of fluorescent fatty acid transfer from adipocyte and heart fatty acid binding proteins by acceptor membrane lipid composition and structure. J. Biol. Chem. 269: 10517-10523.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10517-10523
    • Wootan, M.G.1    Storch, J.2
  • 48
    • 0029993073 scopus 로고    scopus 로고
    • Fatty acid transfer from liver and intestinal fatty acid-binding proteins to membranes occurs by different mechanisms
    • Hsu, K-T., and J. Storch. 1996. Fatty acid transfer from liver and intestinal fatty acid-binding proteins to membranes occurs by different mechanisms. J. Biol. Chem. 271: 13317-13323.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13317-13323
    • Hsu, K.-T.1    Storch, J.2
  • 49
    • 0034917381 scopus 로고    scopus 로고
    • Collision-mediated transfer of long-chain fatty acids by neural tissue fatty acid-binding proteins (FABP): Studies with fluorescent analogs
    • Thumser, A. E. A., J. Tsai, and J. Storch. 2001. Collision-mediated transfer of long-chain fatty acids by neural tissue fatty acid-binding proteins (FABP): studies with fluorescent analogs. J. Mol. Neurosci. 16: 143-150.
    • (2001) J. Mol. Neurosci. , vol.16 , pp. 143-150
    • Thumser, A.E.A.1    Tsai, J.2    Storch, J.3
  • 50
    • 0034004499 scopus 로고    scopus 로고
    • Liver and intestinal fatty acid-binding proteins obtain fatty acids from phospholipid membranes by different mechanisms
    • Thumser, A. E. A., and J. Storch. 2000. Liver and intestinal fatty acid-binding proteins obtain fatty acids from phospholipid membranes by different mechanisms. J. Lipid Res. 41: 647-656.
    • (2000) J. Lipid Res. , vol.41 , pp. 647-656
    • Thumser, A.E.A.1    Storch, J.2
  • 52
    • 0027410255 scopus 로고
    • A comparative study of the conformational properties of Escherichia coli-derived rat intestinal and liver fatty acid binding proteins
    • DOI 10.1016/0167-4838(93)90293-Z
    • Muga, A., D. P. Cistola, and H. H. Mantsch. 1993. A comparative study of the conformational properties of Escherichia coli -derived rat intestinal and liver fatty acid binding proteins. Biochim. Biophys. Acta. 1162: 291-296. (Pubitemid 23094340)
    • (1993) Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology , vol.1162 , Issue.3 , pp. 291-296
    • Muga, A.1    Cistola, D.P.2    Mantsch, H.H.3
  • 53
    • 0027008445 scopus 로고
    • 1H-NMR assignment and determination of the secondary structure of bovine heart fatty-acid-binding protein
    • DOI 10.1111/j.1432-1033.1992.tb17494.x
    • Lücke, C., D. Lassen, H-J. Kreienkamp, F. Spener, and H. Rüterjans. 1992. Sequence-specific 1 H-NMR assignment and determination of the secondary structure of bovine heart fatty-acid-binding protein. Eur. J. Biochem. 210: 901-910. (Pubitemid 23015791)
    • (1992) European Journal of Biochemistry , vol.210 , Issue.3 , pp. 901-910
    • Lucke, C.1    Lassen, D.2    Kreienkamp, H.-J.3    Spener, F.4    Ruterjans, H.5
  • 54
    • 0026410969 scopus 로고
    • Relationship between nuclear magnetic resonance chemical shift and protein secondary structure
    • Wishart, D. S., B. D. Sykes, and F. M. Richards. 1991. Relationship between nuclear magnetic resonance chemical shift and protein secondary structure. J. Mol. Biol. 222: 311-333. (Pubitemid 121004009)
    • (1991) Journal of Molecular Biology , vol.222 , Issue.2 , pp. 311-333
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.