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Volumn 111, Issue 48, 2014, Pages 17170-17175

Global structural changes of an ion channel during its gating are followed by ion mobility mass spectrometry

Author keywords

Ion channel gating; Ion mobility mass spectrometry |; Membrane proteins |; MscL |; Structure function |

Indexed keywords

ESCHERICHIA COLI;

EID: 84914145406     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1413118111     Document Type: Article
Times cited : (57)

References (59)
  • 1
    • 0032545321 scopus 로고    scopus 로고
    • Structure of the MscL homolog from Mycobacterium tuberculosis: A gated mechanosensitive ion channel
    • Chang G, Spencer RH, Lee AT, Barclay MT, Rees DC (1998) Structure of the MscL homolog from Mycobacterium tuberculosis: A gated mechanosensitive ion channel. Science 282(5397):2220-2226.
    • (1998) Science , vol.282 , Issue.5397 , pp. 2220-2226
    • Chang, G.1    Spencer, R.H.2    Lee, A.T.3    Barclay, M.T.4    Rees, D.C.5
  • 2
    • 0030901623 scopus 로고    scopus 로고
    • Mechanosensitive channels of Escherichia coli: The MscL gene, protein, and activities
    • Sukharev SI, Blount P, Martinac B, Kung C (1997) Mechanosensitive channels of Escherichia coli: The MscL gene, protein, and activities. Annu Rev Physiol 59:633-657.
    • (1997) Annu Rev Physiol , vol.59 , pp. 633-657
    • Sukharev, S.I.1    Blount, P.2    Martinac, B.3    Kung, C.4
  • 3
    • 0032844441 scopus 로고    scopus 로고
    • Bacterial mechanosensitive channels: Integrating physiology, structure and function
    • Blount P, Moe PC (1999) Bacterial mechanosensitive channels: integrating physiology, structure and function. Trends Microbiol 7(10):420-424.
    • (1999) Trends Microbiol , vol.7 , Issue.10 , pp. 420-424
    • Blount, P.1    Moe, P.C.2
  • 4
    • 0032826458 scopus 로고    scopus 로고
    • Hydrophilicity of a single residue within MscL correlates with increased channel mechanosensitivity
    • Yoshimura K, Batiza A, Schroeder M, Blount P, Kung C (1999) Hydrophilicity of a single residue within MscL correlates with increased channel mechanosensitivity. Biophys J 77(4):1960-1972.
    • (1999) Biophys J , vol.77 , Issue.4 , pp. 1960-1972
    • Yoshimura, K.1    Batiza, A.2    Schroeder, M.3    Blount, P.4    Kung, C.5
  • 5
    • 0034910316 scopus 로고    scopus 로고
    • Structural models of the MscL gating mechanism
    • Sukharev S, Durell SR, Guy HR (2001) Structural models of the MscL gating mechanism. Biophys J 81(2):917-936.
    • (2001) Biophys J , vol.81 , Issue.2 , pp. 917-936
    • Sukharev, S.1    Durell, S.R.2    Guy, H.R.3
  • 6
    • 0037194760 scopus 로고    scopus 로고
    • Open channel structure of MscL and the gating mechanism of mechanosensitive channels
    • Perozo E, Cortes DM, Sompornpisut P, Kloda A, Martinac B (2002) Open channel structure of MscL and the gating mechanism of mechanosensitive channels. Nature 418(6901):942-948.
    • (2002) Nature , vol.418 , Issue.6901 , pp. 942-948
    • Perozo, E.1    Cortes, D.M.2    Sompornpisut, P.3    Kloda, A.4    Martinac, B.5
  • 7
    • 0036725152 scopus 로고    scopus 로고
    • Physical principles underlying the transduction of bilayer deformation forces during mechanosensitive channel gating
    • Perozo E, Kloda A, Cortes DM, Martinac B (2002) Physical principles underlying the transduction of bilayer deformation forces during mechanosensitive channel gating. Nat Struct Biol 9(9):696-703.
    • (2002) Nat Struct Biol , vol.9 , Issue.9 , pp. 696-703
    • Perozo, E.1    Kloda, A.2    Cortes, D.M.3    Martinac, B.4
  • 8
    • 69949160755 scopus 로고    scopus 로고
    • Structure of a tetrameric MscL in an expanded intermediate state
    • Liu Z, Gandhi CS, Rees DC (2009) Structure of a tetrameric MscL in an expanded intermediate state. Nature 461(7260):120-124.
    • (2009) Nature , vol.461 , Issue.7260 , pp. 120-124
    • Liu, Z.1    Gandhi, C.S.2    Rees, D.C.3
  • 9
    • 77957833040 scopus 로고    scopus 로고
    • An improved open-channel structure of MscL determined from FRET confocal microscopy and simulation
    • Corry B, et al. (2010) An improved open-channel structure of MscL determined from FRET confocal microscopy and simulation. J Gen Physiol 136(4):483-494.
    • (2010) J Gen Physiol , vol.136 , Issue.4 , pp. 483-494
    • Corry, B.1
  • 10
    • 0035825634 scopus 로고    scopus 로고
    • The gating mechanism of the large mechanosensitive channel MscL
    • Sukharev S, Betanzos M, Chiang CS, Guy HR (2001) The gating mechanism of the large mechanosensitive channel MscL. Nature 409(6821):720-724.
    • (2001) Nature , vol.409 , Issue.6821 , pp. 720-724
    • Sukharev, S.1    Betanzos, M.2    Chiang, C.S.3    Guy, H.R.4
  • 11
    • 0036728233 scopus 로고    scopus 로고
    • A large iris-like expansion of a mechanosensitive channel protein induced by membrane tension
    • Betanzos M, Chiang C-S, Guy HR, Sukharev S (2002) A large iris-like expansion of a mechanosensitive channel protein induced by membrane tension. Nat Struct Biol 9(9):704-710.
    • (2002) Nat Struct Biol , vol.9 , Issue.9 , pp. 704-710
    • Betanzos, M.1    Chiang, C.-S.2    Guy, H.R.3    Sukharev, S.4
  • 12
    • 28444478453 scopus 로고    scopus 로고
    • Conformational changes involved in MscL channel gating measured using FRET spectroscopy
    • Corry B, Rigby P, Liu Z-W, Martinac B (2005) Conformational changes involved in MscL channel gating measured using FRET spectroscopy. Biophys J 89(6):L49-L51.
    • (2005) Biophys J , vol.89 , Issue.6 , pp. L49-L51
    • Corry, B.1    Rigby, P.2    Liu, Z.-W.3    Martinac, B.4
  • 13
    • 0141754098 scopus 로고    scopus 로고
    • Gating of MscL studied by steered molecular dynamics
    • Gullingsrud J, Schulten K (2003) Gating of MscL studied by steered molecular dynamics. Biophys J 85(4):2087-2099.
    • (2003) Biophys J , vol.85 , Issue.4 , pp. 2087-2099
    • Gullingsrud, J.1    Schulten, K.2
  • 16
    • 84864674576 scopus 로고    scopus 로고
    • Hydrophobic gating of mechanosensitive channel of large conductance evidenced by single-subunit resolution
    • Birkner JP, Poolman B, Koçer A (2012) Hydrophobic gating of mechanosensitive channel of large conductance evidenced by single-subunit resolution. Proc Natl Acad Sci USA 109(32):12944-12949.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.32 , pp. 12944-12949
    • Birkner, J.P.1    Poolman, B.2    Koçer, A.3
  • 17
    • 0030621966 scopus 로고    scopus 로고
    • Studying noncovalent protein complexes by electrospray ionization mass spectrometry
    • Loo JA (1997) Studying noncovalent protein complexes by electrospray ionization mass spectrometry. Mass Spectrom Rev 16(1):1-23.
    • (1997) Mass Spectrom Rev , vol.16 , Issue.1 , pp. 1-23
    • Loo, J.A.1
  • 18
    • 0037086063 scopus 로고    scopus 로고
    • A tandem mass spectrometer for improved transmission and analysis of large macromolecular assemblies
    • Sobott F, Hernández H, McCammon MG, Tito MA, Robinson CV (2002) A tandem mass spectrometer for improved transmission and analysis of large macromolecular assemblies. Anal Chem 74(6):1402-1407.
    • (2002) Anal Chem , vol.74 , Issue.6 , pp. 1402-1407
    • Sobott, F.1    Hernández, H.2    McCammon, M.G.3    Tito, M.A.4    Robinson, C.V.5
  • 19
    • 4444243006 scopus 로고    scopus 로고
    • Investigation of intact protein complexes by mass spectrometry
    • Heck AJR, Van Den Heuvel RHH (2004) Investigation of intact protein complexes by mass spectrometry. Mass Spectrom Rev 23(5):368-389.
    • (2004) Mass Spectrom Rev , vol.23 , Issue.5 , pp. 368-389
    • Heck, A.J.R.1    Van Den Heuvel, R.H.H.2
  • 21
    • 34347228701 scopus 로고    scopus 로고
    • Determining the stoichiometry and interactions of macromolecular assemblies from mass spectrometry
    • Hernández H, Robinson CV (2007) Determining the stoichiometry and interactions of macromolecular assemblies from mass spectrometry. Nat Protoc 2(3):715-726.
    • (2007) Nat Protoc , vol.2 , Issue.3 , pp. 715-726
    • Hernández, H.1    Robinson, C.V.2
  • 22
    • 28844474910 scopus 로고    scopus 로고
    • Evidence for macromolecular protein rings in the absence of bulk water
    • Ruotolo BT, et al. (2005) Evidence for macromolecular protein rings in the absence of bulk water. Science 310(5754):1658-1661.
    • (2005) Science , vol.310 , Issue.5754 , pp. 1658-1661
    • Ruotolo, B.T.1
  • 24
  • 25
    • 84878106641 scopus 로고    scopus 로고
    • Native ion mobility-mass spectrometry and related methods in structural biology
    • Konijnenberg A, Butterer A, Sobott F (2013) Native ion mobility-mass spectrometry and related methods in structural biology. Biochim Biophys Acta 1834(6):1239-1256.
    • (2013) Biochim Biophys Acta , vol.1834 , Issue.6 , pp. 1239-1256
    • Konijnenberg, A.1    Butterer, A.2    Sobott, F.3
  • 26
    • 47249106965 scopus 로고    scopus 로고
    • Micelles protect membrane complexes from solution to vacuum
    • Barrera NP, Di Bartolo N, Booth PJ, Robinson CV (2008) Micelles protect membrane complexes from solution to vacuum. Science 321(5886):243-246.
    • (2008) Science , vol.321 , Issue.5886 , pp. 243-246
    • Barrera, N.P.1    Di Bartolo, N.2    Booth, P.J.3    Robinson, C.V.4
  • 27
    • 80054844184 scopus 로고    scopus 로고
    • Mass spectrometry of intact V-type ATPases reveals bound lipids and the effects of nucleotide binding
    • Zhou M, et al. (2011) Mass spectrometry of intact V-type ATPases reveals bound lipids and the effects of nucleotide binding. Science 334(6054):380-385.
    • (2011) Science , vol.334 , Issue.6054 , pp. 380-385
    • Zhou, M.1
  • 29
    • 84876726004 scopus 로고    scopus 로고
    • Detergent release prolongs the lifetime of native-like membrane protein conformations in the gas-phase
    • Borysik AJ, Hewitt DJ, Robinson CV (2013) Detergent release prolongs the lifetime of native-like membrane protein conformations in the gas-phase. J Am Chem Soc 135(16):6078-6083.
    • (2013) J Am Chem Soc , vol.135 , Issue.16 , pp. 6078-6083
    • Borysik, A.J.1    Hewitt, D.J.2    Robinson, C.V.3
  • 30
    • 79959456892 scopus 로고    scopus 로고
    • Advances in the mass spectrometry of membrane proteins: From individual proteins to intact complexes
    • Barrera NP, Robinson CV (2011) Advances in the mass spectrometry of membrane proteins: From individual proteins to intact complexes. Annu Rev Biochem 80: 247-271.
    • (2011) Annu Rev Biochem , vol.80 , pp. 247-271
    • Barrera, N.P.1    Robinson, C.V.2
  • 31
    • 0026088998 scopus 로고
    • The influence of heptane-1,2,3-triol on the size and shape of LDAO micelles. Implications for the crystallisation of membrane proteins
    • Timmins PA, Hauk J, Wacker T, WelteW(1991) The influence of heptane-1,2,3-triol on the size and shape of LDAO micelles. Implications for the crystallisation of membrane proteins. FEBS Lett 280(1):115-120.
    • (1991) FEBS Lett , vol.280 , Issue.1 , pp. 115-120
    • Timmins, P.A.1    Hauk, J.2    Wacker, T.3    Welte, W.4
  • 32
    • 78650476908 scopus 로고    scopus 로고
    • S. Aureus MscL is a pentamer in vivo but of variable stoichiometries in vitro: Implications for detergentsolubilized membrane proteins
    • Dorwart MR, Wray R, Brautigam CA, Jiang Y, Blount P (2010) S. aureus MscL is a pentamer in vivo but of variable stoichiometries in vitro: Implications for detergentsolubilized membrane proteins. PLoS Biol 8(12):e1000555.
    • (2010) PLoS Biol , vol.8 , Issue.12 , pp. e1000555
    • Dorwart, M.R.1    Wray, R.2    Brautigam, C.A.3    Jiang, Y.4    Blount, P.5
  • 33
    • 84901936908 scopus 로고    scopus 로고
    • Membrane proteins bind lipids selectively to modulate their structure and function
    • Laganowsky A, et al. (2014) Membrane proteins bind lipids selectively to modulate their structure and function. Nature 510(7503):172-175.
    • (2014) Nature , vol.510 , Issue.7503 , pp. 172-175
    • Laganowsky, A.1
  • 34
    • 0030866749 scopus 로고    scopus 로고
    • Estimation of the pore size of the large-conductance mechanosensitive ion channel of Escherichia coli
    • Cruickshank CC, Minchin RF, Le Dain AC, Martinac B (1997) Estimation of the pore size of the large-conductance mechanosensitive ion channel of Escherichia coli. Biophys J 73(4):1925-1931.
    • (1997) Biophys J , vol.73 , Issue.4 , pp. 1925-1931
    • Cruickshank, C.C.1    Minchin, R.F.2    Le Dain, A.C.3    Martinac, B.4
  • 35
    • 84898741942 scopus 로고    scopus 로고
    • Single molecule FRET reveals pore size and opening mechanism of a mechano-sensitive ion channel
    • Wang Y, et al. (2014) Single molecule FRET reveals pore size and opening mechanism of a mechano-sensitive ion channel. eLife 3:e01834.
    • (2014) ELife , vol.3 , pp. e01834
    • Wang, Y.1
  • 36
    • 0035035068 scopus 로고    scopus 로고
    • Chemically charging the pore constriction opens the mechanosensitive channel MscL
    • Yoshimura K, Batiza A, Kung C (2001) Chemically charging the pore constriction opens the mechanosensitive channel MscL. Biophys J 80(5):2198-2206.
    • (2001) Biophys J , vol.80 , Issue.5 , pp. 2198-2206
    • Yoshimura, K.1    Batiza, A.2    Kung, C.3
  • 37
    • 23044503853 scopus 로고    scopus 로고
    • A light-actuated nanovalve derived from a channel protein
    • Koçer A, Walko M, Meijberg W, Feringa BL (2005) A light-actuated nanovalve derived from a channel protein. Science 309(5735):755-758.
    • (2005) Science , vol.309 , Issue.5735 , pp. 755-758
    • Koçer, A.1    Walko, M.2    Meijberg, W.3    Feringa, B.L.4
  • 38
    • 33746216389 scopus 로고    scopus 로고
    • Rationally designed chemical modulators convert a bacterial channel protein into a pH-sensory valve
    • Koçer A, et al. (2006) Rationally designed chemical modulators convert a bacterial channel protein into a pH-sensory valve. Angew Chem Int Ed Engl 45(19):3126-3130.
    • (2006) Angew Chem Int Ed Engl , vol.45 , Issue.19 , pp. 3126-3130
    • Koçer, A.1
  • 39
    • 84874603235 scopus 로고    scopus 로고
    • On the role of individual subunits in MscL gating: "All for one, one for all?
    • Mika JT, Birkner JP, Poolman B, Koçer A (2013) On the role of individual subunits in MscL gating: "All for one, one for all?". FASEB J 27(3):882-892.
    • (2013) FASEB J , vol.27 , Issue.3 , pp. 882-892
    • Mika, J.T.1    Birkner, J.P.2    Poolman, B.3    Koçer, A.4
  • 40
    • 34047126893 scopus 로고    scopus 로고
    • Structures of the prokaryotic mechanosensitive channels MscL and MscS
    • Steinbacher S, Bass R, Strop P, Rees DC (2007) Structures of the prokaryotic mechanosensitive channels MscL and MscS. Curr Top Membr 58:1-24.
    • (2007) Curr Top Membr , vol.58 , pp. 1-24
    • Steinbacher, S.1    Bass, R.2    Strop, P.3    Rees, D.C.4
  • 41
    • 3042829627 scopus 로고    scopus 로고
    • An in vivo assay identifies changes in residue accessibility on mechanosensitive channel gating
    • Bartlett JL, Levin G, Blount P (2004) An in vivo assay identifies changes in residue accessibility on mechanosensitive channel gating. Proc Natl Acad Sci USA 101(27): 10161-10165.
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.27 , pp. 10161-10165
    • Bartlett, J.L.1    Levin, G.2    Blount, P.3
  • 42
    • 33751217731 scopus 로고    scopus 로고
    • Mechanosensitive channel gating transitions resolved by functional changes upon pore modification
    • Bartlett JL, Li Y, Blount P (2006) Mechanosensitive channel gating transitions resolved by functional changes upon pore modification. Biophys J 91(10):3684-3691.
    • (2006) Biophys J , vol.91 , Issue.10 , pp. 3684-3691
    • Bartlett, J.L.1    Li, Y.2    Blount, P.3
  • 43
    • 41649103734 scopus 로고    scopus 로고
    • Gating-associated conformational changes in the mechanosensitive channel MscL
    • Yoshimura K, Usukura J, Sokabe M (2008) Gating-associated conformational changes in the mechanosensitive channel MscL. Proc Natl Acad Sci USA 105(10):4033-4038.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.10 , pp. 4033-4038
    • Yoshimura, K.1    Usukura, J.2    Sokabe, M.3
  • 44
    • 0033812585 scopus 로고    scopus 로고
    • Identifying conformational changes with site-directed spin labeling
    • Hubbell WL, Cafiso DS, Altenbach C (2000) Identifying conformational changes with site-directed spin labeling. Nat Struct Biol 7(9):735-739.
    • (2000) Nat Struct Biol , vol.7 , Issue.9 , pp. 735-739
    • Hubbell, W.L.1    Cafiso, D.S.2    Altenbach, C.3
  • 45
    • 1642485164 scopus 로고    scopus 로고
    • Coarse grained model for semiquantitative lipid simulations
    • Marrink SJ, de Vries AH, Mark AE (2004) Coarse grained model for semiquantitative lipid simulations. J Phys Chem B 108:750-760.
    • (2004) J Phys Chem B , vol.108 , pp. 750-760
    • Marrink, S.J.1    De Vries, A.H.2    Mark, A.E.3
  • 47
    • 49449113010 scopus 로고    scopus 로고
    • The MARTINI coarse-grained force field: Extension to proteins
    • Monticelli L, et al. (2008) The MARTINI coarse-grained force field: Extension to proteins. J Chem Theory Comput 4:819-834.
    • (2008) J Chem Theory Comput , vol.4 , pp. 819-834
    • Monticelli, L.1
  • 48
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • Hess B, Kutzner C, van der Spoel D, Lindahl E (2008) GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation. J Chem Theory Comput 4(3):435-447.
    • (2008) J Chem Theory Comput , vol.4 , Issue.3 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 50
    • 84894191338 scopus 로고    scopus 로고
    • Going backward: A flexible geometric approach to reverse transformation from coarse grained to atomistic models
    • Wassenaar TA, Pluhackova K, Böckmann RA, Marrink SJ, Tieleman DP (2014) Going backward: A flexible geometric approach to reverse transformation from coarse grained to atomistic models. J Chem Theory Comput 10(2):676-690.
    • (2014) J Chem Theory Comput , vol.10 , Issue.2 , pp. 676-690
    • Wassenaar, T.A.1    Pluhackova, K.2    Böckmann, R.A.3    Marrink, S.J.4    Tieleman, D.P.5
  • 51
    • 79959713919 scopus 로고    scopus 로고
    • Definition and testing of the GROMOS force-field versions 54A7 and 54B7
    • Schmid N, et al. (2011) Definition and testing of the GROMOS force-field versions 54A7 and 54B7. Eur Biophys J 40(7):843-856.
    • (2011) Eur Biophys J , vol.40 , Issue.7 , pp. 843-856
    • Schmid, N.1
  • 52
  • 53
    • 33748887803 scopus 로고    scopus 로고
    • Structural information from ion mobility measurements: Effects of the long-range potential
    • Mesleh MF, Hunter JM, Shvartsburg AA, Schatz GC, Jarrold MF (1996) Structural information from ion mobility measurements: Effects of the long-range potential. J Phys Chem 100(40):16082-16086.
    • (1996) J Phys Chem , vol.100 , Issue.40 , pp. 16082-16086
    • Mesleh, M.F.1    Hunter, J.M.2    Shvartsburg, A.A.3    Schatz, G.C.4    Jarrold, M.F.5
  • 54
    • 0030580028 scopus 로고    scopus 로고
    • An exact hard-spheres scattering model for the mobilities of polyatomic ions
    • Shvartsburg AA, Jarrold MF (1996) An exact hard-spheres scattering model for the mobilities of polyatomic ions. Chem Phys Lett 261(1-2):86-91.
    • (1996) Chem Phys Lett , vol.261 , Issue.1-2 , pp. 86-91
    • Shvartsburg, A.A.1    Jarrold, M.F.2
  • 55
    • 84863416219 scopus 로고    scopus 로고
    • Charge-state dependent compaction and dissociation of protein complexes: Insights from ion mobility and molecular dynamics
    • Hall Z, Politis A, Bush MF, Smith LJ, Robinson CV (2012) Charge-state dependent compaction and dissociation of protein complexes: Insights from ion mobility and molecular dynamics. J Am Chem Soc 134(7):3429-3438.
    • (2012) J Am Chem Soc , vol.134 , Issue.7 , pp. 3429-3438
    • Hall, Z.1    Politis, A.2    Bush, M.F.3    Smith, L.J.4    Robinson, C.V.5
  • 56
    • 0029878720 scopus 로고    scopus 로고
    • VMD: Visual molecular dynamics
    • 27-28
    • Humphrey W, Dalke A, Schulten K (1996) VMD: Visual molecular dynamics. J Mol Graph 14(1):33-38, 27-28.
    • (1996) J Mol Graph , vol.14 , Issue.1 , pp. 33-38
    • Humphrey, W.1    Dalke, A.2    Schulten, K.3
  • 57
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields
    • Frank J, et al. (1996) SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields. J Struct Biol 116(1):190-199.
    • (1996) J Struct Biol , vol.116 , Issue.1 , pp. 190-199
    • Frank, J.1
  • 58
    • 0025286635 scopus 로고
    • Classification of macromolecular assemblies studied as 'single particles'
    • Frank J (1990) Classification of macromolecular assemblies studied as 'single particles'. Q Rev Biophys 23(3):281-329.
    • (1990) Q Rev Biophys , vol.23 , Issue.3 , pp. 281-329
    • Frank, J.1
  • 59
    • 34250757116 scopus 로고    scopus 로고
    • Synthesis and utilization of reversible and irreversible light-activated nanovalves derived from the channel protein MscL
    • Koçer A, Walko M, Feringa BL (2007) Synthesis and utilization of reversible and irreversible light-activated nanovalves derived from the channel protein MscL. Nat Protoc 2(6):1426-1437.
    • (2007) Nat Protoc , vol.2 , Issue.6 , pp. 1426-1437
    • Koçer, A.1    Walko, M.2    Feringa, B.L.3


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