메뉴 건너뛰기




Volumn 110, Issue 46, 2013, Pages 18484-18489

Structures of intermediate transport states of ZneA, a Zn(II)/proton antiporter

Author keywords

[No Author keywords available]

Indexed keywords

ANTIPORTER; HEAVY METAL; PROTON; ZINC;

EID: 84887446447     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1318705110     Document Type: Article
Times cited : (34)

References (51)
  • 1
    • 0028365952 scopus 로고
    • Two novel families of bacterial membrane proteins concerned with nodulation, cell division and transport
    • DOI 10.1111/j.1365-2958.1994.tb00362.x
    • Saier MH, Jr., Tam R, Reizer A, Reizer J (1994) Two novel families of bacterial membrane proteins concerned with nodulation, cell division and transport. Mol Microbiol 11(5):841-847. (Pubitemid 24199651)
    • (1994) Molecular Microbiology , vol.11 , Issue.5 , pp. 841-847
    • Saier Jr., M.H.1    Tam, R.2    Reizer, A.3    Reizer, J.4
  • 2
    • 0033170990 scopus 로고    scopus 로고
    • The RND permease superfamily: An ancient, ubiquitous and diverse family that includes human disease and development proteins
    • Tseng TT, et al. (1999) The RND permease superfamily: An ancient, ubiquitous and diverse family that includes human disease and development proteins. J Mol Microbiol Biotechnol 1(1):107-125.
    • (1999) J Mol Microbiol Biotechnol , vol.1 , Issue.1 , pp. 107-125
    • Tseng, T.T.1
  • 3
    • 0035782865 scopus 로고    scopus 로고
    • Phylogeny of multidrug transporters
    • Saier MH, Jr., Paulsen IT (2001) Phylogeny of multidrug transporters. Semin Cell Dev Biol 12(3):205-213.
    • (2001) Semin Cell Dev Biol , vol.12 , Issue.3 , pp. 205-213
    • Saier Jr., M.H.1    Paulsen, I.T.2
  • 4
    • 0036286250 scopus 로고    scopus 로고
    • Genetic locus encoding functions involved in biosynthesis and outer membrane localization of xanthomonadin in Xanthomonas oryzae pv. oryzae
    • DOI 10.1128/JB.184.13.3539-3548.2002
    • Goel AK, Rajagopal L, Nagesh N, Sonti RV (2002) Genetic locus encoding functions involved in biosynthesis and outer membrane localization of xanthomonadin in Xanthomonas oryzae pv. oryzae. J Bacteriol 184(13):3539-3548. (Pubitemid 34625662)
    • (2002) Journal of Bacteriology , vol.184 , Issue.13 , pp. 3539-3548
    • Goel, A.K.1    Rajagopal, L.2    Nagesh, N.3    Sonti, R.V.4
  • 5
    • 0037020216 scopus 로고    scopus 로고
    • Hedgehog-mediated patterning of the mammalian embryo requires transporter-like function of dispatched
    • Ma Y, et al. (2002) Hedgehog-mediated patterning of the mammalian embryo requires transporter-like function of dispatched. Cell 111(1):63-75.
    • (2002) Cell , vol.111 , Issue.1 , pp. 63-75
    • Ma, Y.1
  • 6
    • 0029845913 scopus 로고    scopus 로고
    • Multidrug efflux pumps of gram-negative bacteria
    • Nikaido H (1996) Multidrug efflux pumps of gram-negative bacteria. J Bacteriol 178(20):5853-5859.
    • (1996) J Bacteriol , vol.178 , Issue.20 , pp. 5853-5859
    • Nikaido, H.1
  • 7
    • 0031278034 scopus 로고    scopus 로고
    • A family of Gram-negative bacterial outer membrane factors that function in the export of proteins, carbohydrates, drugs and heavy metals from Gram-negative bacteria
    • DOI 10.1016/S0378-1097(97)00379-0, PII S0378109797003790
    • Paulsen IT, Park JH, Choi PS, Saier MH, Jr. (1997) A family of gram-negative bacterial outer membrane factors that function in the export of proteins, carbohydrates, drugs and heavy metals from gram-negative bacteria. FEMS Microbiol Lett 156(1):1-8. (Pubitemid 28091826)
    • (1997) FEMS Microbiology Letters , vol.156 , Issue.1 , pp. 1-8
    • Paulsen, I.T.1    Park, J.H.2    Choi, P.S.3    Saier Jr., M.H.4
  • 8
    • 0028318241 scopus 로고
    • A family of extracytoplasmic proteins that allow transport of large molecules across the outer membranes of gram-negative bacteria
    • Dinh T, Paulsen IT, Saier MH, Jr. (1994) A family of extracytoplasmic proteins that allow transport of large molecules across the outer membranes of gram-negative bacteria. J Bacteriol 176(13):3825-3831. (Pubitemid 24191264)
    • (1994) Journal of Bacteriology , vol.176 , Issue.13 , pp. 3825-3831
    • Dinh, T.1    Paulsen, I.T.2    Saier Jr., M.H.3
  • 9
    • 64649096369 scopus 로고    scopus 로고
    • Mechanisms of RND multidrug efflux pumps
    • Nikaido H, Takatsuka Y (2009) Mechanisms of RND multidrug efflux pumps. Biochim Biophys Acta 1794(5):769-781.
    • (2009) Biochim Biophys Acta , vol.1794 , Issue.5 , pp. 769-781
    • Nikaido, H.1    Takatsuka, Y.2
  • 10
    • 64649100965 scopus 로고    scopus 로고
    • Drug transport mechanism of the AcrB efflux pump
    • Pos KM (2009) Drug transport mechanism of the AcrB efflux pump. Biochim Biophys Acta 1794(5):782-793.
    • (2009) Biochim Biophys Acta , vol.1794 , Issue.5 , pp. 782-793
    • Pos, K.M.1
  • 11
    • 0037057652 scopus 로고    scopus 로고
    • Crystal structure of bacterial multidrug efflux transporter AcrB
    • Murakami S, Nakashima R, Yamashita E, Yamaguchi A (2002) Crystal structure of bacterial multidrug efflux transporter AcrB. Nature 419(6907):587-593.
    • (2002) Nature , vol.419 , Issue.6907 , pp. 587-593
    • Murakami, S.1    Nakashima, R.2    Yamashita, E.3    Yamaguchi, A.4
  • 12
    • 33748670458 scopus 로고    scopus 로고
    • Crystal structures of a multidrug transporter reveal a functionally rotating mechanism
    • DOI 10.1038/nature05076, PII NATURE05076
    • Murakami S, Nakashima R, Yamashita E, Matsumoto T, Yamaguchi A (2006) Crystal structures of a multidrug transporter reveal a functionally rotating mechanism. Nature 443(7108):173-179. (Pubitemid 44387601)
    • (2006) Nature , vol.443 , Issue.7108 , pp. 173-179
    • Murakami, S.1    Nakashima, R.2    Yamashita, E.3    Matsumoto, T.4    Yamaguchi, A.5
  • 13
    • 84859567740 scopus 로고    scopus 로고
    • Transport of drugs by the multidrug transporter AcrB involves an access and a deep binding pocket that are separated by a switch-loop
    • Eicher T, et al. (2012) Transport of drugs by the multidrug transporter AcrB involves an access and a deep binding pocket that are separated by a switch-loop. Proc Natl Acad Sci USA 109(15):5687-5692.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.15 , pp. 5687-5692
    • Eicher, T.1
  • 14
    • 33748310520 scopus 로고    scopus 로고
    • Structural asymmetry of AcrB trimer suggests a peristaltic pump mechanism
    • DOI 10.1126/science.1131542
    • Seeger MA, et al. (2006) Structural asymmetry of AcrB trimer suggests a peristaltic pump mechanism. Science 313(5791):1295-1298. (Pubitemid 44330954)
    • (2006) Science , vol.313 , Issue.5791 , pp. 1295-1298
    • Seeger, M.A.1    Schiefner, A.2    Eicher, T.3    Verrey, F.4    Diederichs, K.5    Pos, K.M.6
  • 15
    • 84355166442 scopus 로고    scopus 로고
    • Structures of the multidrug exporter AcrB reveal a proximal multisite drug-binding pocket
    • Nakashima R, Sakurai K, Yamasaki S, Nishino K, Yamaguchi A (2011) Structures of the multidrug exporter AcrB reveal a proximal multisite drug-binding pocket. Nature 480(7378):565-569.
    • (2011) Nature , vol.480 , Issue.7378 , pp. 565-569
    • Nakashima, R.1    Sakurai, K.2    Yamasaki, S.3    Nishino, K.4    Yamaguchi, A.5
  • 16
    • 65449155090 scopus 로고    scopus 로고
    • Crystal structure of the multidrug exporter MexB from Pseudomonas aeruginosa
    • Sennhauser G, Bukowska MA, Briand C, Grütter MG (2009) Crystal structure of the multidrug exporter MexB from Pseudomonas aeruginosa. J Mol Biol 389(1):134-145.
    • (2009) J Mol Biol , vol.389 , Issue.1 , pp. 134-145
    • Sennhauser, G.1    Bukowska, M.A.2    Briand, C.3    Grütter, M.G.4
  • 17
    • 79958281760 scopus 로고    scopus 로고
    • Structure and function of a membrane component SecDF that enhances protein export
    • Tsukazaki T, et al. (2011) Structure and function of a membrane component SecDF that enhances protein export. Nature 474(7350):235-238.
    • (2011) Nature , vol.474 , Issue.7350 , pp. 235-238
    • Tsukazaki, T.1
  • 18
    • 77957141422 scopus 로고    scopus 로고
    • Crystal structures of the CusA efflux pump suggest methionine-mediated metal transport
    • Long F, et al. (2010) Crystal structures of the CusA efflux pump suggest methionine-mediated metal transport. Nature 467(7314):484-488.
    • (2010) Nature , vol.467 , Issue.7314 , pp. 484-488
    • Long, F.1
  • 19
    • 79952145187 scopus 로고    scopus 로고
    • Crystal structure of the CusBA heavy-metal efflux complex of Escherichia coli
    • Su C-C, et al. (2011) Crystal structure of the CusBA heavy-metal efflux complex of Escherichia coli. Nature 470(7335):558-562.
    • (2011) Nature , vol.470 , Issue.7335 , pp. 558-562
    • Su, C.-C.1
  • 20
    • 84865088476 scopus 로고    scopus 로고
    • Charged amino acids (R83, E567, D617, E625, R669, and K678) of CusA are required for metal ion transport in the Cus efflux system
    • Su C-C, et al. (2012) Charged amino acids (R83, E567, D617, E625, R669, and K678) of CusA are required for metal ion transport in the Cus efflux system. J Mol Biol 422(3): 429-441.
    • (2012) J Mol Biol , vol.422 , Issue.3 , pp. 429-441
    • Su, C.-C.1
  • 21
    • 63049131979 scopus 로고    scopus 로고
    • Covalently linked trimer of the AcrB multidrug efflux pump provides support for the functional rotating mechanism
    • Takatsuka Y, Nikaido H (2009) Covalently linked trimer of the AcrB multidrug efflux pump provides support for the functional rotating mechanism. J Bacteriol 191(6): 1729-1737.
    • (2009) J Bacteriol , vol.191 , Issue.6 , pp. 1729-1737
    • Takatsuka, Y.1    Nikaido, H.2
  • 23
    • 36749045119 scopus 로고    scopus 로고
    • Site-directed disulfide cross-linking shows that cleft flexibility in the periplasmic domain is needed for the multidrug efflux pump AcrB of Escherichia coli
    • DOI 10.1128/JB.01127-07
    • Takatsuka Y, Nikaido H (2007) Site-directed disulfide cross-linking shows that cleft flexibility in the periplasmic domain is needed for the multidrug efflux pump AcrB of Escherichia coli. J Bacteriol 189(23):8677-8684. (Pubitemid 350210038)
    • (2007) Journal of Bacteriology , vol.189 , Issue.23 , pp. 8677-8684
    • Takatsuka, Y.1    Nikaido, H.2
  • 24
    • 0017852917 scopus 로고
    • Extrachromosomal inheritance controlling resistance to cadmium, cobalt, copper and zinc ions: Evidence from curing in a pseudomonas
    • Mergeay M, Houba C, Gerits J (1978) Extrachromosomal inheritance controlling resistance to cadmium, cobalt, copper and zinc ions: Evidence from curing in a Pseudomonas [proceedings]. Arch Int Physiol Biochim 86(2):440-442. (Pubitemid 8391179)
    • (1978) Archives Internationales de Physiologie et de Biochimie , vol.86 , Issue.2 , pp. 440-442
    • Mergeay, M.1    Houba, C.2    Gerits, J.3
  • 25
    • 0021925630 scopus 로고
    • Alcaligenes eutrophus CH34 is a facultative chemolithotroph with plasmid-bound resistance to heavy metals
    • Mergeay M, et al. (1985) Alcaligenes eutrophus CH34 is a facultative chemolithotroph with plasmid-bound resistance to heavy metals. J Bacteriol 162(1):328-334. (Pubitemid 15095872)
    • (1985) Journal of Bacteriology , vol.162 , Issue.1 , pp. 328-334
    • Mergeay, M.1    Nies, D.2    Schlegel, H.G.3
  • 27
    • 77956398098 scopus 로고    scopus 로고
    • The complete genome sequence of Cupriavidus metallidurans strain CH34, a master survivalist in harsh and anthropogenic environments
    • Janssen PJ, et al. (2010) The complete genome sequence of Cupriavidus metallidurans strain CH34, a master survivalist in harsh and anthropogenic environments. PLoS ONE 5(5):e10433.
    • (2010) PLoS ONE , vol.5 , Issue.5
    • Janssen, P.J.1
  • 28
    • 0031035708 scopus 로고    scopus 로고
    • Two-component regulatory system involved in transcriptional control of heavy-metal homoeostasis in Alcaligenes eutrophus
    • van der Lelie D, et al. (1997) Two-component regulatory system involved in transcriptional control of heavy-metal homoeostasis in Alcaligenes eutrophus. Mol Microbiol 23(3):493-503.
    • (1997) Mol Microbiol , vol.23 , Issue.3 , pp. 493-503
    • Van Der Lelie, D.1
  • 29
    • 0033543578 scopus 로고    scopus 로고
    • Energetics and topology of CzcA, a cation/proton antiporter of the resistance-nodulation-cell division protein family
    • Goldberg M, Pribyl T, Juhnke S, Nies DH (1999) Energetics and topology of CzcA, a cation/proton antiporter of the resistance-nodulation-cell division protein family. J Biol Chem 274(37):26065-26070.
    • (1999) J Biol Chem , vol.274 , Issue.37 , pp. 26065-26070
    • Goldberg, M.1    Pribyl, T.2    Juhnke, S.3    Nies, D.H.4
  • 31
    • 0342751307 scopus 로고    scopus 로고
    • Regulation of the cnr cobalt and nickel resistance determinant from Ralstonia sp. strain CH34
    • DOI 10.1128/JB.182.5.1390-1398.2000
    • Grass G, Grosse C, Nies DH (2000) Regulation of the cnr cobalt and nickel resistance determinant from Ralstonia sp. strain CH34. J Bacteriol 182(5):1390-1398. (Pubitemid 30104419)
    • (2000) Journal of Bacteriology , vol.182 , Issue.5 , pp. 1390-1398
    • Grass, G.1    Grosse, C.2    Nies, D.H.3
  • 32
    • 0033950956 scopus 로고    scopus 로고
    • Regulation of the cnr cobalt and nickel resistance determinant of Ralstonia eutropha (Alcaligenes eutrophus) CH34
    • DOI 10.1128/JB.182.5.1399-1409.2000
    • Tibazarwa C, Wuertz S, Mergeay M, Wyns L, van Der Lelie D (2000) Regulation of the cnr cobalt and nickel resistance determinant of Ralstonia eutropha (Alcaligenes eutrophus) CH34. J Bacteriol 182(5):1399-1409. (Pubitemid 30104420)
    • (2000) Journal of Bacteriology , vol.182 , Issue.5 , pp. 1399-1409
    • Tibazarwa, C.1    Wuertz, S.2    Mergeay, M.3    Wyns, L.4    Van Der, L.D.5
  • 33
    • 24744452563 scopus 로고    scopus 로고
    • Control of expression of a periplasmic nickel efflux pump by periplasmic nickel concentrations
    • DOI 10.1007/s10534-005-3718-6
    • Grass G, Fricke B, Nies DH (2005) Control of expression of a periplasmic nickel efflux pump by periplasmic nickel concentrations. Biometals 18(4):437-448. (Pubitemid 41298027)
    • (2005) BioMetals , vol.18 , Issue.4 , pp. 437-448
    • Grass, G.1    Fricke, B.2    Nies, D.H.3
  • 35
    • 77954656149 scopus 로고    scopus 로고
    • Metal-induced conformational changes in ZneB suggest an active role of membrane fusion proteins in efflux resistance systems
    • De Angelis F, et al. (2010) Metal-induced conformational changes in ZneB suggest an active role of membrane fusion proteins in efflux resistance systems. Proc Natl Acad Sci USA 107(24):11038-11043.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.24 , pp. 11038-11043
    • De Angelis, F.1
  • 36
    • 56549089911 scopus 로고    scopus 로고
    • The interaction of biological and noxious transition metals with the zinc probes FluoZin-3 and Newport Green
    • Zhao J, Bertoglio BA, Devinney MJ, Jr., Dineley KE, Kay AR (2009) The interaction of biological and noxious transition metals with the zinc probes FluoZin-3 and Newport Green. Anal Biochem 384(1):34-41.
    • (2009) Anal Biochem , vol.384 , Issue.1 , pp. 34-41
    • Zhao, J.1    Bertoglio, B.A.2    Devinney Jr., M.J.3    Dineley, K.E.4    Kay, A.R.5
  • 37
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissinel E, Henrick K (2004) Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr D Biol Crystallogr 60(pt 12 pt 1):2256-2268.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , Issue.PART 12 PART 1 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 38
    • 0042430540 scopus 로고    scopus 로고
    • Multidrug-exporting secondary transporters
    • DOI 10.1016/S0959-440X(03)00109-X
    • Murakami S, Yamaguchi A (2003) Multidrug-exporting secondary transporters. Curr Opin Struct Biol 13(4):443-452. (Pubitemid 37011449)
    • (2003) Current Opinion in Structural Biology , vol.13 , Issue.4 , pp. 443-452
    • Murakami, S.1    Yamaguchi, A.2
  • 39
    • 33749630424 scopus 로고    scopus 로고
    • Threonine-978 in the transmembrane segment of the multidrug efflux pump AcrB of Escherichia coli is crucial for drug transport as a probable component of the proton relay network
    • DOI 10.1128/JB.00683-06
    • Takatsuka Y, Nikaido H (2006) Threonine-978 in the transmembrane segment of the multidrug efflux pump AcrB of Escherichia coli is crucial for drug transport as a probable component of the proton relay network. J Bacteriol 188(20):7284-7289. (Pubitemid 44547633)
    • (2006) Journal of Bacteriology , vol.188 , Issue.20 , pp. 7284-7289
    • Takatsuka, Y.1    Nikaido, H.2
  • 40
    • 67649583295 scopus 로고    scopus 로고
    • Crucial role of Asp408 in the proton translocation pathway of multidrug transporter AcrB: Evidence from site-directed mutagenesis and carbodiimide labeling
    • Seeger MA, von Ballmoos C, Verrey F, Pos KM (2009) Crucial role of Asp408 in the proton translocation pathway of multidrug transporter AcrB: Evidence from site-directed mutagenesis and carbodiimide labeling. Biochemistry 48(25):5801-5812.
    • (2009) Biochemistry , vol.48 , Issue.25 , pp. 5801-5812
    • Seeger, M.A.1    Von Ballmoos, C.2    Verrey, F.3    Pos, K.M.4
  • 42
    • 34748870747 scopus 로고    scopus 로고
    • Analysis of the structural consensus of the zinc coordination centers of metalloprotein structures
    • DOI 10.1016/j.bbapap.2007.07.010, PII S1570963907001628
    • Patel K, Kumar A, Durani S (2007) Analysis of the structural consensus of the zinc coordination centers of metalloprotein structures. Biochim Biophys Acta 1774(10): 1247-1253. (Pubitemid 47484291)
    • (2007) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1774 , Issue.10 , pp. 1247-1253
    • Patel, K.1    Kumar, A.2    Durani, S.3
  • 43
    • 84874431455 scopus 로고    scopus 로고
    • Multidrug binding properties of the AcrB efflux pump characterized by molecular dynamics simulations
    • Vargiu AV, Nikaido H (2012) Multidrug binding properties of the AcrB efflux pump characterized by molecular dynamics simulations. Proc Natl Acad Sci USA 109(50): 20637-20642.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.50 , pp. 20637-20642
    • Vargiu, A.V.1    Nikaido, H.2
  • 44
    • 0037565061 scopus 로고    scopus 로고
    • Efflux-mediated heavy metal resistance in prokaryotes
    • Nies DH (2003) Efflux-mediated heavy metal resistance in prokaryotes. FEMS Microbiol Rev 27(2-3):313-339.
    • (2003) FEMS Microbiol Rev , vol.27 , Issue.2-3 , pp. 313-339
    • Nies, D.H.1
  • 45
    • 79956087446 scopus 로고    scopus 로고
    • Switch or funnel: How RND-type transport systems control periplasmic metal homeostasis
    • Kim E-H, Nies DH, McEvoy MM, Rensing C (2011) Switch or funnel: How RND-type transport systems control periplasmic metal homeostasis. J Bacteriol 193(10):2381-2387.
    • (2011) J Bacteriol , vol.193 , Issue.10 , pp. 2381-2387
    • Kim, E.-H.1    Nies, D.H.2    McEvoy, M.M.3    Rensing, C.4
  • 46
    • 70349558132 scopus 로고    scopus 로고
    • Crystal structure of the membrane fusion protein CusB from Escherichia coli
    • Su C-C, et al. (2009) Crystal structure of the membrane fusion protein CusB from Escherichia coli. J Mol Biol 393(2):342-355.
    • (2009) J Mol Biol , vol.393 , Issue.2 , pp. 342-355
    • Su, C.-C.1
  • 47
    • 33644833626 scopus 로고    scopus 로고
    • Conformational flexibility in the multidrug efflux system protein AcrA
    • DOI 10.1016/j.str.2005.11.015, PII S0969212606000633
    • Mikolosko J, Bobyk K, Zgurskaya HI, Ghosh P (2006) Conformational flexibility in the multidrug effl ux system protein AcrA. Structure 14(3):577-587. (Pubitemid 43363490)
    • (2006) Structure , vol.14 , Issue.3 , pp. 577-587
    • Mikolosko, J.1    Bobyk, K.2    Zgurskaya, H.I.3    Ghosh, P.4
  • 48
    • 0022574419 scopus 로고
    • Cation/proton antiport systems in Escherichia coli. Solubilization and reconstitution of deltapH-driven sodium/proton and calcium/proton antiporters
    • Nakamura T, Hsu C, Rosen BP (1986) Cation/proton antiport systems in Escherichia coli. Solubilization and reconstitution of delta pH-driven sodium/proton and calcium/proton antiporters. J Biol Chem 261(2):678-683. (Pubitemid 16161724)
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.2 , pp. 678-683
    • Nakamura, T.1    Hsu, C.2    Rosen, B.P.3
  • 50
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macro-molecular structure solution
    • Adams PD, et al. (2010) PHENIX: A comprehensive Python-based system for macro-molecular structure solution. Acta Crystallogr D Biol Crystallogr 66(pt 2):213-221.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , Issue.PART 2 , pp. 213-221
    • Adams, P.D.1
  • 51
    • 84868156224 scopus 로고    scopus 로고
    • CAVER 3.0: A tool for the analysis of transport pathways in dynamic protein structures
    • Chovancova E, et al. (2012) CAVER 3.0: A tool for the analysis of transport pathways in dynamic protein structures. PLOS Comput Biol 8(10):e1002708.
    • (2012) PLOS Comput Biol , vol.8 , Issue.10
    • Chovancova, E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.