메뉴 건너뛰기




Volumn 79, Issue 5, 2011, Pages 1662-1671

Identification of functional motions in the adenylate kinase (ADK) protein family by computational hybrid approaches

Author keywords

Adenylate kinase; Correlated motion; Protein dynamics; Statistical coupling analysis

Indexed keywords

ADENYLATE KINASE;

EID: 79954627097     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22995     Document Type: Article
Times cited : (14)

References (69)
  • 1
    • 4344642067 scopus 로고    scopus 로고
    • Protein motions promote catalysis
    • Tousignant A, Pelletier JN. Protein motions promote catalysis. Chem Biol 2004; 11: 1037-1042.
    • (2004) Chem Biol , vol.11 , pp. 1037-1042
    • Tousignant, A.1    Pelletier, J.N.2
  • 3
    • 33644559358 scopus 로고    scopus 로고
    • Enzymes: An integrated view of structure, dynamics and function
    • Agarwal PK. Enzymes: An integrated view of structure, dynamics and function. Microb Cell Fact 2006; 5: 2.
    • (2006) Microb Cell Fact , vol.5 , pp. 2
    • Agarwal, P.K.1
  • 4
    • 12844268072 scopus 로고    scopus 로고
    • Statistical coevolution analysis and molecular dynamics: Identification of amino acid pairs essential for catalysis
    • Estabrook RA, Luo J, Purdy MM, Sharma V, Weakliem P, Bruice TC, Reich NO. Statistical coevolution analysis and molecular dynamics: Identification of amino acid pairs essential for catalysis. Proc Natl Acad Sci USA 2005; 102: 994-999.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 994-999
    • Estabrook, R.A.1    Luo, J.2    Purdy, M.M.3    Sharma, V.4    Weakliem, P.5    Bruice, T.C.6    Reich, N.O.7
  • 5
    • 35348942279 scopus 로고    scopus 로고
    • Allosteric communication in dihydrofolate reductase: Signaling network and pathways for closed to occluded transition and back
    • Chen J, Dima RI, Thirumalai D. Allosteric communication in dihydrofolate reductase: Signaling network and pathways for closed to occluded transition and back. J Mol Biol 2007; 374: 250-266.
    • (2007) J Mol Biol , vol.374 , pp. 250-266
    • Chen, J.1    Dima, R.I.2    Thirumalai, D.3
  • 6
    • 47649125643 scopus 로고    scopus 로고
    • Allosteric regulation and catalysis emerge via a common route
    • Goodey NM, Benkovic SJ. Allosteric regulation and catalysis emerge via a common route. Nat Chem Biol 2008; 4: 474-482.
    • (2008) Nat Chem Biol , vol.4 , pp. 474-482
    • Goodey, N.M.1    Benkovic, S.J.2
  • 7
    • 38349092279 scopus 로고    scopus 로고
    • Conformational transitions in adenylate kinase. Allosteric communication reduces misligation
    • Whitford PC, Gosavi S, Onuchic JN. Conformational transitions in adenylate kinase. Allosteric communication reduces misligation. J Biol Chem 2008; 283: 2042-2048.
    • (2008) J Biol Chem , vol.283 , pp. 2042-2048
    • Whitford, P.C.1    Gosavi, S.2    Onuchic, J.N.3
  • 9
    • 37249008315 scopus 로고    scopus 로고
    • What determines the speed limit on enzyme catalysis?
    • Frauenfelder H. What determines the speed limit on enzyme catalysis? Nat Chem Biol 2008; 4: 21-22.
    • (2008) Nat Chem Biol , vol.4 , pp. 21-22
    • Frauenfelder, H.1
  • 10
    • 55649083101 scopus 로고    scopus 로고
    • Coevolving residues of (beta/alpha)(8)-barrel proteins play roles in stabilizing active site architecture and coordinating protein dynamics
    • Shen H, Xu F, Hu H, Wang F, Wu Q, Huang Q, Wang H. Coevolving residues of (beta/alpha)(8)-barrel proteins play roles in stabilizing active site architecture and coordinating protein dynamics. J Struct Biol 2008; 164: 281-292.
    • (2008) J Struct Biol , vol.164 , pp. 281-292
    • Shen, H.1    Xu, F.2    Hu, H.3    Wang, F.4    Wu, Q.5    Huang, Q.6    Wang, H.7
  • 11
    • 51349086269 scopus 로고    scopus 로고
    • Identifying critical residues in protein folding: Insights from phi-value and P(fold) analysis
    • Faisca PF, Travasso RD, Ball RC, Shakhnovich EI. Identifying critical residues in protein folding: Insights from phi-value and P(fold) analysis. J Chem Phys 2008: 129; 095108.
    • (2008) J Chem Phys , vol.129 , pp. 095108
    • Faisca, P.F.1    Travasso, R.D.2    Ball, R.C.3    Shakhnovich, E.I.4
  • 12
    • 30744478915 scopus 로고    scopus 로고
    • Protein flexibility: Its role in structure and mechanism revealed by molecular simulations
    • Dodson G, Verma CS. Protein flexibility: Its role in structure and mechanism revealed by molecular simulations. Cell Mol Life Sci 2006; 63: 207-219.
    • (2006) Cell Mol Life Sci , vol.63 , pp. 207-219
    • Dodson, G.1    Verma, C.S.2
  • 13
    • 34548528158 scopus 로고    scopus 로고
    • Progress in computational protein design
    • Lippow SM, Tidor B. Progress in computational protein design. Curr Opin Biotechnol 2007; 18: 305-311.
    • (2007) Curr Opin Biotechnol , vol.18 , pp. 305-311
    • Lippow, S.M.1    Tidor, B.2
  • 14
    • 33746592898 scopus 로고    scopus 로고
    • Knowledge-based potentials in protein design
    • Poole AM, Ranganathan R. Knowledge-based potentials in protein design. Curr Opin Struct Biol 2006; 16: 508-513.
    • (2006) Curr Opin Struct Biol , vol.16 , pp. 508-513
    • Poole, A.M.1    Ranganathan, R.2
  • 16
    • 37249032102 scopus 로고    scopus 로고
    • Dynamic personalities of proteins
    • Henzler-Wildman K, Kern D. Dynamic personalities of proteins. Nature 2007; 450: 964-972.
    • (2007) Nature , vol.450 , pp. 964-972
    • Henzler-Wildman, K.1    Kern, D.2
  • 17
    • 18744371588 scopus 로고    scopus 로고
    • Molecular dynamics and protein function
    • Karplus M, Kuriyan J. Molecular dynamics and protein function. Proc Natl Acad Sci USA 2005; 102: 6679-6685.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 6679-6685
    • Karplus, M.1    Kuriyan, J.2
  • 20
    • 18444369978 scopus 로고    scopus 로고
    • The role of dynamically correlated conformational equilibria in the folding of macromolecular structures. A model for the design of folded dendrimers
    • Lockman JW, Paul NM, Parquette JR. The role of dynamically correlated conformational equilibria in the folding of macromolecular structures. A model for the design of folded dendrimers. Progr Polym Sci 30: 423-452, 2005.
    • (2005) Progr Polym Sci , vol.30 , pp. 423-452
    • Lockman, J.W.1    Paul, N.M.2    Parquette, J.R.3
  • 21
    • 12344256786 scopus 로고    scopus 로고
    • PCOAT: Positional correlation analysis using multiple methods
    • Qi Y, Grishin NV. PCOAT: Positional correlation analysis using multiple methods. Bioinformatics 2004; 20: 3697-3699.
    • (2004) Bioinformatics , vol.20 , pp. 3697-3699
    • Qi, Y.1    Grishin, N.V.2
  • 22
    • 0037219686 scopus 로고    scopus 로고
    • Evolutionarily conserved networks of residues mediate allosteric communication in proteins
    • Suel GM, Lockless SW, Wall MA, Ranganathan R. Evolutionarily conserved networks of residues mediate allosteric communication in proteins. Nat Struct Biol 2003; 10: 59-69.
    • (2003) Nat Struct Biol , vol.10 , pp. 59-69
    • Suel, G.M.1    Lockless, S.W.2    Wall, M.A.3    Ranganathan, R.4
  • 25
    • 58749094825 scopus 로고    scopus 로고
    • Small- and large-scale conformational changes of adenylate kinase: A molecular dynamics study of the subdomain motion and mechanics
    • Pontiggia F, Zen A, Micheletti C. Small- and large-scale conformational changes of adenylate kinase: A molecular dynamics study of the subdomain motion and mechanics. Biophys J 2008; 95: 5901-5912.
    • (2008) Biophys J , vol.95 , pp. 5901-5912
    • Pontiggia, F.1    Zen, A.2    Micheletti, C.3
  • 26
    • 36148979311 scopus 로고    scopus 로고
    • NMR identification of transient complexes critical to adenylate kinase catalysis
    • Aden J, Wolf-Watz M. NMR identification of transient complexes critical to adenylate kinase catalysis. J Am Chem Soc 2007; 129: 14003-14012.
    • (2007) J Am Chem Soc , vol.129 , pp. 14003-14012
    • Aden, J.1    Wolf-Watz, M.2
  • 28
    • 34347388470 scopus 로고    scopus 로고
    • UniRef: Comprehensive and non-redundant UniProt reference clusters
    • Suzek BE, Huang H, McGarvey P, Mazumder R, Wu CH. UniRef: Comprehensive and non-redundant UniProt reference clusters. Bioinformatics 2007; 23: 1282-1288.
    • (2007) Bioinformatics , vol.23 , pp. 1282-1288
    • Suzek, B.E.1    Huang, H.2    McGarvey, P.3    Mazumder, R.4    Wu, C.H.5
  • 30
    • 13244255415 scopus 로고    scopus 로고
    • MUSCLE. A multiple sequence alignment method with reduced time and space complexity
    • Edgar RC. MUSCLE. A multiple sequence alignment method with reduced time and space complexity. BMC Bioinformatics 2004; 5: 113.
    • (2004) BMC Bioinformatics , vol.5 , pp. 113
    • Edgar, R.C.1
  • 31
    • 0033536602 scopus 로고    scopus 로고
    • Evolutionarily conserved pathways of energetic connectivity in protein families
    • Lockless SW, Ranganathan R. Evolutionarily conserved pathways of energetic connectivity in protein families. Science 1999; 286: 295-299.
    • (1999) Science , vol.286 , pp. 295-299
    • Lockless, S.W.1    Ranganathan, R.2
  • 33
    • 33750407288 scopus 로고    scopus 로고
    • Anisotropic network model: Systematic evaluation and a new web interface
    • Eyal E, Yang LW, Bahar I. Anisotropic network model: Systematic evaluation and a new web interface. Bioinformatics 2006; 22: 2619-2627.
    • (2006) Bioinformatics , vol.22 , pp. 2619-2627
    • Eyal, E.1    Yang, L.W.2    Bahar, I.3
  • 34
    • 34848852941 scopus 로고    scopus 로고
    • Allosteric transitions in the chaperonin GroEL are captured by a dominant normal mode that is most robust to sequence variations
    • Zheng W, Brooks BR, Thirumalai D. Allosteric transitions in the chaperonin GroEL are captured by a dominant normal mode that is most robust to sequence variations. Biophys J 2007; 93: 2289-2299.
    • (2007) Biophys J , vol.93 , pp. 2289-2299
    • Zheng, W.1    Brooks, B.R.2    Thirumalai, D.3
  • 36
    • 33646742004 scopus 로고    scopus 로고
    • Low-frequency normal modes that describe allosteric transitions in biological nanomachines are robust to sequence variations
    • Zheng W, Brooks BR, Thirumalai D. Low-frequency normal modes that describe allosteric transitions in biological nanomachines are robust to sequence variations. Proc Natl Acad Sci USA 2006; 103: 7664-7669.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 7664-7669
    • Zheng, W.1    Brooks, B.R.2    Thirumalai, D.3
  • 37
    • 43049104657 scopus 로고    scopus 로고
    • Correspondences between low-energy modes in enzymes: Dynamics-based alignment of enzymatic functional families
    • Zen A, Carnevale V, Lesk AM, Micheletti C. Correspondences between low-energy modes in enzymes: Dynamics-based alignment of enzymatic functional families. Protein Sci 2008; 17: 918-929.
    • (2008) Protein Sci , vol.17 , pp. 918-929
    • Zen, A.1    Carnevale, V.2    Lesk, A.M.3    Micheletti, C.4
  • 38
    • 0037154793 scopus 로고    scopus 로고
    • Enzymology. A moving story
    • Falke JJ. Enzymology. A moving story. Science 2002; 295: 1480-1481.
    • (2002) Science , vol.295 , pp. 1480-1481
    • Falke, J.J.1
  • 39
    • 44949105262 scopus 로고    scopus 로고
    • Exploring allosteric coupling in the alpha-subunit of heterotrimeric G proteins using evolutionary and ensemble-based approaches
    • Sayar K, Ugur O, Liu T, Hilser VJ, Onaran O. Exploring allosteric coupling in the alpha-subunit of heterotrimeric G proteins using evolutionary and ensemble-based approaches. BMC Struct Biol 2008; 8: 23.
    • (2008) BMC Struct Biol , vol.8 , pp. 23
    • Sayar, K.1    Ugur, O.2    Liu, T.3    Hilser, V.J.4    Onaran, O.5
  • 40
    • 0028871926 scopus 로고
    • Dali: A network tool for protein structure comparison
    • Holm L, Sander C. Dali: A network tool for protein structure comparison. Trends Biochem Sci 1995; 20: 478-480.
    • (1995) Trends Biochem Sci , vol.20 , pp. 478-480
    • Holm, L.1    Sander, C.2
  • 42
    • 0037249966 scopus 로고    scopus 로고
    • Detection of hydrogen-bond signature patterns in protein families
    • Prasad T, Prathima MN, Chandra N. Detection of hydrogen-bond signature patterns in protein families. Bioinformatics 2003; 19: 167-168.
    • (2003) Bioinformatics , vol.19 , pp. 167-168
    • Prasad, T.1    Prathima, M.N.2    Chandra, N.3
  • 46
    • 0029644168 scopus 로고    scopus 로고
    • Adenylate kinase motions during catalysis: An energetic counterweight balancing substrate binding
    • Muller CW, Schlauderer GJ, Reinstein J, Schulz GE. Adenylate kinase motions during catalysis: An energetic counterweight balancing substrate binding. Structure 1996; 4: 147-156.
    • (1996) Structure , vol.4 , pp. 147-156
    • Muller, C.W.1    Schlauderer, G.J.2    Reinstein, J.3    Schulz, G.E.4
  • 47
    • 36849039429 scopus 로고    scopus 로고
    • A hierarchy of timescales in protein dynamics is linked to enzyme catalysis
    • Henzler-Wildman KA, Lei M, Thai V, Kerns SJ, Karplus M, Kern D. A hierarchy of timescales in protein dynamics is linked to enzyme catalysis. Nature 2007; 450: 913-916.
    • (2007) Nature , vol.450 , pp. 913-916
    • Henzler-Wildman, K.A.1    Lei, M.2    Thai, V.3    Kerns, S.J.4    Karplus, M.5    Kern, D.6
  • 49
    • 0031577566 scopus 로고    scopus 로고
    • Activation of adenylate kinase by denaturants is due to the increasing conformational flexibility at its active sites
    • Zhang HJ, Sheng XR, Pan XM, Zhou JM. Activation of adenylate kinase by denaturants is due to the increasing conformational flexibility at its active sites. Biochem Biophys Res Commun 1997; 238: 382-386.
    • (1997) Biochem Biophys Res Commun , vol.238 , pp. 382-386
    • Zhang, H.J.1    Sheng, X.R.2    Pan, X.M.3    Zhou, J.M.4
  • 50
    • 6344231648 scopus 로고    scopus 로고
    • Escherichia coli adenylate kinase dynamics: Comparison of elastic network model modes with mode-coupling (15)N-NMR relaxation data
    • Temiz NA, Meirovitch E, Bahar I. Escherichia coli adenylate kinase dynamics: Comparison of elastic network model modes with mode-coupling (15)N-NMR relaxation data. Proteins 2004; 57: 468-480.
    • (2004) Proteins , vol.57 , pp. 468-480
    • Temiz, N.A.1    Meirovitch, E.2    Bahar, I.3
  • 51
    • 0242268469 scopus 로고    scopus 로고
    • Nonlinear elasticity, proteinquakes, and the energy landscapes of functional transitions in proteins
    • Miyashita O, Onuchic JN, Wolynes PG. Nonlinear elasticity, proteinquakes, and the energy landscapes of functional transitions in proteins. Proc Natl Acad Sci USA 2003; 100: 12570-12575.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 12570-12575
    • Miyashita, O.1    Onuchic, J.N.2    Wolynes, P.G.3
  • 52
    • 70350131719 scopus 로고    scopus 로고
    • Rational modulation of conformational fluctuations in adenylate kinase reveals a local unfolding mechanism for allostery and functional adaptation in proteins
    • Schrank TP, Bolen DW, Hilser VJ. Rational modulation of conformational fluctuations in adenylate kinase reveals a local unfolding mechanism for allostery and functional adaptation in proteins. Proc Natl Acad Sci USA 2009; 106: 16984-16989.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 16984-16989
    • Schrank, T.P.1    Bolen, D.W.2    Hilser, V.J.3
  • 53
    • 0032563132 scopus 로고    scopus 로고
    • Genetically engineered zinc-chelating adenylate kinase from Escherichia coli with enhanced thermal stability
    • Perrier V, Burlacu-Miron S, Bourgeois S, Surewicz WK, Gilles AM. Genetically engineered zinc-chelating adenylate kinase from Escherichia coli with enhanced thermal stability. J Biol Chem 1998; 273: 19097-19101.
    • (1998) J Biol Chem , vol.273 , pp. 19097-19101
    • Perrier, V.1    Burlacu-Miron, S.2    Bourgeois, S.3    Surewicz, W.K.4    Gilles, A.M.5
  • 54
    • 0032563116 scopus 로고    scopus 로고
    • Structural and energetic factors of the increased thermal stability in a genetically engineered Escherichia coli adenylate kinase
    • Burlacu-Miron S, Perrier V, Gilles AM, Pistotnik E, Craescu CT. Structural and energetic factors of the increased thermal stability in a genetically engineered Escherichia coli adenylate kinase. J Biol Chem 1998; 273: 19102-19107.
    • (1998) J Biol Chem , vol.273 , pp. 19102-19107
    • Burlacu-Miron, S.1    Perrier, V.2    Gilles, A.M.3    Pistotnik, E.4    Craescu, C.T.5
  • 55
    • 4444371260 scopus 로고    scopus 로고
    • Anticorrelated motions as a driving force in enzyme catalysis: The dehydrogenase reaction
    • Luo J, Bruice TC. Anticorrelated motions as a driving force in enzyme catalysis: The dehydrogenase reaction. Proc Natl Acad Sci USA 2004; 101: 13152-13156.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 13152-13156
    • Luo, J.1    Bruice, T.C.2
  • 56
    • 53849096731 scopus 로고    scopus 로고
    • Testing geometrical discrimination within an enzyme active site: Constrained hydrogen bonding in the ketosteroid isomerase oxyanion hole
    • Sigala PA, Kraut DA, Caaveiro JM, Pybus B, Ruben EA, Ringe D, Petsko GA, Herschlag D. Testing geometrical discrimination within an enzyme active site: Constrained hydrogen bonding in the ketosteroid isomerase oxyanion hole. J Am Chem Soc 2008; 130: 13696-13708.
    • (2008) J Am Chem Soc , vol.130 , pp. 13696-13708
    • Sigala, P.A.1    Kraut, D.A.2    Caaveiro, J.M.3    Pybus, B.4    Ruben, E.A.5    Ringe, D.6    Petsko, G.A.7    Herschlag, D.8
  • 57
    • 33846847773 scopus 로고    scopus 로고
    • Conformational transitions of adenylate kinase: Switching by cracking
    • Whitford PC, Miyashita O, Levy Y, Onuchic JN. Conformational transitions of adenylate kinase: Switching by cracking. J Mol Biol 2007; 366: 1661-1671.
    • (2007) J Mol Biol , vol.366 , pp. 1661-1671
    • Whitford, P.C.1    Miyashita, O.2    Levy, Y.3    Onuchic, J.N.4
  • 59
    • 51749092455 scopus 로고    scopus 로고
    • Hydrogen bond networks determine emergent mechanical and thermodynamic properties across a protein family
    • Livesay DR, Huynh DH, Dallakyan S, Jacobs DJ. Hydrogen bond networks determine emergent mechanical and thermodynamic properties across a protein family. Chem Cent J 2008; 2: 17.
    • (2008) Chem Cent J , vol.2 , pp. 17
    • Livesay, D.R.1    Huynh, D.H.2    Dallakyan, S.3    Jacobs, D.J.4
  • 62
    • 0014753397 scopus 로고
    • Comparative allostery of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthetase as a molecular basis for classification
    • Jensen RA, Stenmark SL. Comparative allostery of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthetase as a molecular basis for classification. J Bacteriol 1970; 101: 763-769.
    • (1970) J Bacteriol , vol.101 , pp. 763-769
    • Jensen, R.A.1    Stenmark, S.L.2
  • 63
    • 0035336687 scopus 로고    scopus 로고
    • Cooperative hemoglobins: Conserved fold, diverse quaternary assemblies and allosteric mechanisms
    • Royer WEJr, Knapp JE, Strand K, Heaslet HA. Cooperative hemoglobins: Conserved fold, diverse quaternary assemblies and allosteric mechanisms. Trends Biochem Sci 2001; 26: 297-304.
    • (2001) Trends Biochem Sci , vol.26 , pp. 297-304
    • Royer Jr, W.E.1    Knapp, J.E.2    Strand, K.3    Heaslet, H.A.4
  • 64
    • 24644483073 scopus 로고    scopus 로고
    • Large amplitude conformational change in proteins explored with a plastic network model: Adenylate kinase
    • Maragakis P, Karplus M. Large amplitude conformational change in proteins explored with a plastic network model: Adenylate kinase. J Mol Biol 2005; 352: 807-822.
    • (2005) J Mol Biol , vol.352 , pp. 807-822
    • Maragakis, P.1    Karplus, M.2
  • 65
    • 0027528934 scopus 로고
    • Domain closure in adenylate kinase. Joints on either side of two helices close like neighboring fingers
    • Gerstein M, Schulz G, Chothia C. Domain closure in adenylate kinase. Joints on either side of two helices close like neighboring fingers. J Mol Biol 1993; 229: 494-501.
    • (1993) J Mol Biol , vol.229 , pp. 494-501
    • Gerstein, M.1    Schulz, G.2    Chothia, C.3
  • 66
    • 0028335096 scopus 로고
    • Structural mechanisms for domain movements in proteins
    • Gerstein M, Lesk AM, Chothia C. Structural mechanisms for domain movements in proteins. Biochemistry 1994; 33: 6739-6749.
    • (1994) Biochemistry , vol.33 , pp. 6739-6749
    • Gerstein, M.1    Lesk, A.M.2    Chothia, C.3
  • 67
    • 0030601771 scopus 로고    scopus 로고
    • Comment on a "fluctuation and cross correlation analysis of protein motions observed in nanosecond molecular dynamics simulations"
    • Karplus M, Ichiye T. Comment on a "fluctuation and cross correlation analysis of protein motions observed in nanosecond molecular dynamics simulations". J Mol Biol 1996; 263: 120-122.
    • (1996) J Mol Biol , vol.263 , pp. 120-122
    • Karplus, M.1    Ichiye, T.2
  • 68
    • 21244440196 scopus 로고    scopus 로고
    • Conservation of mus-ms enzyme motions in the apo- and substrate-mimicked state
    • Beach H, Cole R, Gill ML, Loria JP. Conservation of mus-ms enzyme motions in the apo- and substrate-mimicked state. J Am Chem Soc 2005; 127: 9167-9176.
    • (2005) J Am Chem Soc , vol.127 , pp. 9167-9176
    • Beach, H.1    Cole, R.2    Gill, M.L.3    Loria, J.P.4
  • 69
    • 64849101493 scopus 로고    scopus 로고
    • Protein dynamism and evolvability
    • Tokuriki N, Tawfik DS. Protein dynamism and evolvability. Science 2009; 324: 203-207.
    • (2009) Science , vol.324 , pp. 203-207
    • Tokuriki, N.1    Tawfik, D.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.