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Volumn 466, Issue 12, 2014, Pages 2191-2204

ClC-1 and ClC-2 form hetero-dimeric channels with novel protopore functions

Author keywords

Channel gating; CLC chloride channel; Single channel recording

Indexed keywords

CHLORIDE CHANNEL; CLC 1 CHLORIDE CHANNEL; CLC 2 CHLORIDE CHANNEL; HETERODIMER; HYBRID PROTEIN; MONOMER; UNCLASSIFIED DRUG; CLC-1 CHANNEL; CLC-2 CHLORIDE CHANNELS; PROTEIN BINDING;

EID: 84912011877     PISSN: 00316768     EISSN: 14322013     Source Type: Journal    
DOI: 10.1007/s00424-014-1490-6     Document Type: Article
Times cited : (20)

References (43)
  • 1
    • 0035426049 scopus 로고    scopus 로고
    • Drastic reduction of the slow gate of human muscle chloride channel (ClC-1) by mutation C277S
    • COI: 1:CAS:528:DC%2BD3MXlvF2nsr0%3D, PID: 11483705
    • Accardi A, Ferrera L, Pusch M (2001) Drastic reduction of the slow gate of human muscle chloride channel (ClC-1) by mutation C277S. J Physiol 534:745–752. doi:10.1111/j.1469-7793.2001.00745.x
    • (2001) J Physiol , vol.534 , pp. 745-752
    • Accardi, A.1    Ferrera, L.2    Pusch, M.3
  • 2
    • 0033811517 scopus 로고    scopus 로고
    • Fast and slow gating relaxations in the muscle chloride channel ClC-1
    • Accardi A, Pusch M (2000) Fast and slow gating relaxations in the muscle chloride channel ClC-1. J Gen Physiol 116:433–444. doi:10.1085/jgp.116.3.433
    • (2000) J Gen Physiol , vol.116 , pp. 433-444
    • Accardi, A.1    Pusch, M.2
  • 3
    • 0034960407 scopus 로고    scopus 로고
    • Fast and slow gating of ClC-1: differential effects of 2-(4-chlorophenoxy) propionic acid and dominant negative mutations
    • Aromataris EC, Rychkov GY, Bennetts B et al (2001) Fast and slow gating of ClC-1: differential effects of 2-(4-chlorophenoxy) propionic acid and dominant negative mutations. Mol Pharmacol 60:200–208. doi:10.1124/mol.60.1.200
    • (2001) Mol Pharmacol , vol.60 , pp. 200-208
    • Aromataris, E.C.1    Rychkov, G.Y.2    Bennetts, B.3
  • 4
    • 84885168677 scopus 로고    scopus 로고
    • Molecular determinants of common gating of a ClC chloride channel
    • PID: 24064982
    • Bennetts B, Parker MW (2013) Molecular determinants of common gating of a ClC chloride channel. Nat Commun 4:2507. doi:10.1038/ncomms3507
    • (2013) Nat Commun , vol.4 , pp. 2507
    • Bennetts, B.1    Parker, M.W.2
  • 5
    • 0015170319 scopus 로고
    • Chloride conductance in normal and myotonic muscle fibres and the action of monocarboxylic aromatic acids
    • COI: 1:CAS:528:DyaE38XlslCisw%3D%3D, PID: 5316641
    • Bryant SH, Morales-Aguilera A (1971) Chloride conductance in normal and myotonic muscle fibres and the action of monocarboxylic aromatic acids. J Physiol 219:367–383
    • (1971) J Physiol , vol.219 , pp. 367-383
    • Bryant, S.H.1    Morales-Aguilera, A.2
  • 6
    • 0034940574 scopus 로고    scopus 로고
    • + of the muscle-type ClC chloride channels
    • + of the muscle-type ClC chloride channels. J Gen Physiol 118:23–32. doi:10.1085/jgp.118.1.23
    • (2001) J Gen Physiol , vol.118 , pp. 23-32
    • Chen, M.-F.1    Chen, T.-Y.2
  • 7
    • 84876251947 scopus 로고    scopus 로고
    • Novel brain expression of CIC-1 chloride channels and enrichment of CLCN1 variants in epilepsy
    • Chen TT, Klassen TL, Goldman AM et al (2013) Novel brain expression of CIC-1 chloride channels and enrichment of CLCN1 variants in epilepsy. Neurology 80:1078–1085. doi:10.1212/WNL.0b013e31828868e7
    • (2013) Neurology , vol.80 , pp. 1078-1085
    • Chen, T.T.1    Klassen, T.L.2    Goldman, A.M.3
  • 8
    • 1142310688 scopus 로고    scopus 로고
    • Conduction mechanisms of chloride ions in CLC-type channels
    • Corry B, O’Mara M, Chung S-H (2004) Conduction mechanisms of chloride ions in CLC-type channels. Biophys J 86:846–860. doi:10.1016/S0006-3495(04)74160-0
    • (2004) Biophys J , vol.86 , pp. 846-860
    • Corry, B.1    O’Mara, M.2    Chung, S.-H.3
  • 9
    • 28244475369 scopus 로고    scopus 로고
    • Quantitative analysis of the voltage-dependent gating of mouse parotid ClC-2 chloride channel
    • PID: 16286506
    • De Santiago JA, Nehrke K, Arreola J (2005) Quantitative analysis of the voltage-dependent gating of mouse parotid ClC-2 chloride channel. J Gen Physiol 126:591–603. doi:10.1085/jgp.200509310
    • (2005) J Gen Physiol , vol.126 , pp. 591-603
    • De Santiago, J.A.1    Nehrke, K.2    Arreola, J.3
  • 10
    • 0037122805 scopus 로고    scopus 로고
    • X-ray structure of a CLC chloride channel at 3.0 A reveals the molecular basis of anion selectivity
    • Dutzler R, Campbell EB, Cadene M et al (2002) X-ray structure of a CLC chloride channel at 3.0 A reveals the molecular basis of anion selectivity. Nature 415:287–294. doi:10.1038/415287a
    • (2002) Nature , vol.415 , pp. 287-294
    • Dutzler, R.1    Campbell, E.B.2    Cadene, M.3
  • 11
    • 0037418859 scopus 로고    scopus 로고
    • Gating the selectivity filter in ClC chloride channels
    • COI: 1:CAS:528:DC%2BD3sXis1Cgt74%3D, PID: 12649487
    • Dutzler R, Campbell EB, MacKinnon R (2003) Gating the selectivity filter in ClC chloride channels. Science 300:108–112. doi:10.1126/science.1082708
    • (2003) Science , vol.300 , pp. 108-112
    • Dutzler, R.1    Campbell, E.B.2    MacKinnon, R.3
  • 12
    • 34748882655 scopus 로고    scopus 로고
    • The mechanism of fast-gate opening in ClC-0
    • COI: 1:CAS:528:DC%2BD2sXht1WmsrvF, PID: 17846164
    • Engh AM, Faraldo-Gómez JD, Maduke M (2007) The mechanism of fast-gate opening in ClC-0. J Gen Physiol 130:335–349. doi:10.1085/jgp.200709759
    • (2007) J Gen Physiol , vol.130 , pp. 335-349
    • Engh, A.M.1    Faraldo-Gómez, J.D.2    Maduke, M.3
  • 13
    • 0345146920 scopus 로고    scopus 로고
    • Conservation of chloride channel structure revealed by an inhibitor binding site in ClC-1
    • PID: 12691663
    • Estévez R, Schroeder BC, Accardi A et al (2003) Conservation of chloride channel structure revealed by an inhibitor binding site in ClC-1. Neuron 38:47–59. doi:10.1016/S0896-6273(03)00168-5
    • (2003) Neuron , vol.38 , pp. 47-59
    • Estévez, R.1    Schroeder, B.C.2    Accardi, A.3
  • 14
    • 0035910572 scopus 로고    scopus 로고
    • Residues lining the inner pore vestibule of human muscle chloride channels
    • COI: 1:CAS:528:DC%2BD3MXotVCjtw%3D%3D, PID: 11035024
    • Fahlke C, Desai RR, Gillani N, George AL (2001) Residues lining the inner pore vestibule of human muscle chloride channels. J Biol Chem 276:1759–1765. doi:10.1074/jbc.M007649200
    • (2001) J Biol Chem , vol.276 , pp. 1759-1765
    • Fahlke, C.1    Desai, R.R.2    Gillani, N.3    George, A.L.4
  • 15
    • 0031022816 scopus 로고    scopus 로고
    • Subunit stoichiometry of human muscle chloride channels
    • COI: 1:CAS:528:DyaK2sXnsFSjuw%3D%3D, PID: 8997668
    • Fahlke C, Knittle T, Gurnett CA et al (1997) Subunit stoichiometry of human muscle chloride channels. J Gen Physiol 109:93–104. doi:10.1085/jgp.109.1.93
    • (1997) J Gen Physiol , vol.109 , pp. 93-104
    • Fahlke, C.1    Knittle, T.2    Gurnett, C.A.3
  • 16
    • 0029738742 scopus 로고    scopus 로고
    • Mechanism of voltage-dependent gating in skeletal muscle chloride channels
    • COI: 1:CAS:528:DyaK28XkslOqtbw%3D, PID: 8842208
    • Fahlke C, Rosenbohm A, Mitrovic N et al (1996) Mechanism of voltage-dependent gating in skeletal muscle chloride channels. Biophys J 71:695–706. doi:10.1016/S0006-3495(96)79269-X
    • (1996) Biophys J , vol.71 , pp. 695-706
    • Fahlke, C.1    Rosenbohm, A.2    Mitrovic, N.3
  • 17
    • 0028950604 scopus 로고
    • Chloride currents across the membrane of mammalian skeletal muscle fibres
    • COI: 1:CAS:528:DyaK2MXlt1Grt7c%3D, PID: 7602531
    • Fahlke C, Rüdel R (1995) Chloride currents across the membrane of mammalian skeletal muscle fibres. J Physiol 484:355–368
    • (1995) J Physiol , vol.484 , pp. 355-368
    • Fahlke, C.1    Rüdel, R.2
  • 18
    • 0029162517 scopus 로고
    • An aspartic acid residue important for voltage-dependent gating of human muscle chloride channels
    • COI: 1:CAS:528:DyaK2MXnvVWltrc%3D, PID: 7646898
    • Fahlke C, Rüdel R, Mitrovic N et al (1995) An aspartic acid residue important for voltage-dependent gating of human muscle chloride channels. Neuron 15:463–472. doi:10.1016/0896-6273(95)90050-0
    • (1995) Neuron , vol.15 , pp. 463-472
    • Fahlke, C.1    Rüdel, R.2    Mitrovic, N.3
  • 19
    • 77955625453 scopus 로고    scopus 로고
    • Barttin activates ClC-K channel function by modulating gating
    • PID: 20538786
    • Fischer M, Janssen AGH, Fahlke C (2010) Barttin activates ClC-K channel function by modulating gating. J Am Soc Nephrol. doi:10.1681/ASN.2009121274
    • (2010) J Am Soc Nephrol
    • Fischer, M.1    Janssen, A.G.H.2    Fahlke, C.3
  • 20
    • 56649100778 scopus 로고    scopus 로고
    • Gating of human ClC-2 chloride channels and regulation by carboxy-terminal domains
    • COI: 1:CAS:528:DC%2BD1cXhsVKitbfO, PID: 18801843
    • Garcia-Olivares J, Alekov A, Boroumand MR et al (2008) Gating of human ClC-2 chloride channels and regulation by carboxy-terminal domains. J Physiol 586:5325–5336. doi:10.1113/jphysiol.2008.158097
    • (2008) J Physiol , vol.586 , pp. 5325-5336
    • Garcia-Olivares, J.1    Alekov, A.2    Boroumand, M.R.3
  • 21
    • 4544326747 scopus 로고    scopus 로고
    • A trimeric quaternary structure is conserved in bacterial and human glutamate transporters
    • COI: 1:CAS:528:DC%2BD2cXnsVKktrY%3D, PID: 15265858
    • Gendreau S, Voswinkel S, Torres-Salazar D et al (2004) A trimeric quaternary structure is conserved in bacterial and human glutamate transporters. J Biol Chem 279:39505–39512. doi:10.1074/jbc.M408038200
    • (2004) J Biol Chem , vol.279 , pp. 39505-39512
    • Gendreau, S.1    Voswinkel, S.2    Torres-Salazar, D.3
  • 22
    • 1842424664 scopus 로고    scopus 로고
    • The role of the carboxyl terminus in ClC chloride channel function
    • COI: 1:CAS:528:DC%2BD2cXitl2nsro%3D, PID: 14718533
    • Hebeisen S, Biela A, Giese B et al (2004) The role of the carboxyl terminus in ClC chloride channel function. J Biol Chem 279:13140–13147. doi:10.1074/jbc.M312649200
    • (2004) J Biol Chem , vol.279 , pp. 13140-13147
    • Hebeisen, S.1    Biela, A.2    Giese, B.3
  • 23
    • 24144461620 scopus 로고    scopus 로고
    • Carboxy-terminal truncations modify the outer pore vestibule of muscle chloride channels
    • COI: 1:CAS:528:DC%2BD2MXpvF2ktbg%3D, PID: 15980168
    • Hebeisen S, Fahlke C (2005) Carboxy-terminal truncations modify the outer pore vestibule of muscle chloride channels. Biophys J 89:1710–1720. doi:10.1529/biophysj.104.056093
    • (2005) Biophys J , vol.89 , pp. 1710-1720
    • Hebeisen, S.1    Fahlke, C.2
  • 24
    • 0037379688 scopus 로고    scopus 로고
    • Anion permeation in human ClC-4 channels
    • COI: 1:CAS:528:DC%2BD3sXivVent7c%3D, PID: 12668439
    • Hebeisen S, Heidtmann H, Cosmelli D et al (2003) Anion permeation in human ClC-4 channels. Biophys J 84:2306–2318. doi:10.1016/S0006-3495(03)75036-X
    • (2003) Biophys J , vol.84 , pp. 2306-2318
    • Hebeisen, S.1    Heidtmann, H.2    Cosmelli, D.3
  • 25
    • 58149494673 scopus 로고    scopus 로고
    • Disease-causing dysfunctions of barttin in Bartter syndrome type IV
    • COI: 1:CAS:528:DC%2BD1MXhvV2lurY%3D, PID: 18776122
    • Janssen AGH, Scholl U, Domeyer C et al (2009) Disease-causing dysfunctions of barttin in Bartter syndrome type IV. J Am Soc Nephrol 20:145–153. doi:10.1681/ASN.2008010102
    • (2009) J Am Soc Nephrol , vol.20 , pp. 145-153
    • Janssen, A.G.H.1    Scholl, U.2    Domeyer, C.3
  • 26
    • 0033781187 scopus 로고    scopus 로고
    • Cysteine modification of a putative pore residue in ClC-0 implication for the pore stoichiometry of Clc chloride channels
    • Lin C-W, Chen T-Y (2000) Cysteine modification of a putative pore residue in ClC-0 implication for the pore stoichiometry of Clc chloride channels. J Gen Physiol 116:535–546. doi:10.1085/jgp.116.4.535
    • (2000) J Gen Physiol , vol.116 , pp. 535-546
    • Lin, C.-W.1    Chen, T.-Y.2
  • 27
    • 0033000370 scopus 로고    scopus 로고
    • Elimination of the slow gating of Clc-0 chloride channel by a point mutation
    • COI: 1:CAS:528:DyaK1MXkslOns7k%3D, PID: 10398688
    • Lin Y-W, Lin C-W, Chen T-Y (1999) Elimination of the slow gating of Clc-0 chloride channel by a point mutation. J Gen Physiol 114:1–12. doi:10.1085/jgp.114.1.1
    • (1999) J Gen Physiol , vol.114 , pp. 1-12
    • Lin, Y.-W.1    Lin, C.-W.2    Chen, T.-Y.3
  • 28
    • 0029843417 scopus 로고    scopus 로고
    • Heteromultimeric CLC chloride channels with novel properties
    • COI: 1:CAS:528:DyaK28XmvFSntr4%3D, PID: 8917596
    • Lorenz C, Pusch M, Jentsch TJ (1996) Heteromultimeric CLC chloride channels with novel properties. Proc Natl Acad Sci U S A 93:13362–13366
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 13362-13366
    • Lorenz, C.1    Pusch, M.2    Jentsch, T.J.3
  • 29
    • 0030840713 scopus 로고    scopus 로고
    • Independent gating of single pores in ClC-0 chloride channels
    • Ludewig U, Pusch M, Jentsch TJ (1997) Independent gating of single pores in ClC-0 chloride channels. Biophys J 73:789–797. doi:10.1016/S0006-3495(97)78111-6
    • (1997) Biophys J , vol.73 , pp. 789-797
    • Ludewig, U.1    Pusch, M.2    Jentsch, T.J.3
  • 30
    • 0020440405 scopus 로고
    • Open-state substructure of single chloride channels from Torpedo electroplax
    • COI: 1:CAS:528:DyaL3sXivFynsA%3D%3D, PID: 6130538
    • Miller C (1982) Open-state substructure of single chloride channels from Torpedo electroplax. Philos Trans R Soc Lond B Biol Sci 299:401–411
    • (1982) Philos Trans R Soc Lond B Biol Sci , vol.299 , pp. 401-411
    • Miller, C.1
  • 31
    • 0028040145 scopus 로고
    • Low single channel conductance of the major skeletal muscle chloride channel, ClC-1
    • COI: 1:CAS:528:DyaK2cXkslKgsL8%3D, PID: 8130334
    • Pusch M, Steinmeyer K, Jentsch TJ (1994) Low single channel conductance of the major skeletal muscle chloride channel, ClC-1. Biophys J 66:149–152. doi:10.1016/S0006-3495(94)80753-2
    • (1994) Biophys J , vol.66 , pp. 149-152
    • Pusch, M.1    Steinmeyer, K.2    Jentsch, T.J.3
  • 32
    • 78650171241 scopus 로고    scopus 로고
    • Design, function and structure of a monomeric ClC transporter
    • COI: 1:CAS:528:DC%2BC3cXhtlOhtLvO, PID: 21048711
    • Robertson JL, Kolmakova-Partensky L, Miller C (2010) Design, function and structure of a monomeric ClC transporter. Nature 468:844–847. doi:10.1038/nature09556
    • (2010) Nature , vol.468 , pp. 844-847
    • Robertson, J.L.1    Kolmakova-Partensky, L.2    Miller, C.3
  • 33
    • 0029961958 scopus 로고    scopus 로고
    • Concentration and pH dependence of skeletal muscle chloride channel ClC-1
    • COI: 1:CAS:528:DyaK2sXisFCq, PID: 8961185
    • Rychkov GY, Pusch M, Astill DS et al (1996) Concentration and pH dependence of skeletal muscle chloride channel ClC-1. J Physiol 497(Pt 2):423–435
    • (1996) J Physiol , vol.497 , pp. 423-435
    • Rychkov, G.Y.1    Pusch, M.2    Astill, D.S.3
  • 34
    • 0031750188 scopus 로고    scopus 로고
    • Permeation and block of the skeletal muscle chloride channel, ClC-1, by foreign anions
    • COI: 1:CAS:528:DyaK1cXjtFWgsbg%3D, PID: 9565403
    • Rychkov GY, Pusch M, Roberts ML et al (1998) Permeation and block of the skeletal muscle chloride channel, ClC-1, by foreign anions. J Gen Physiol 111:653–665. doi:10.1085/jgp.111.5.653
    • (1998) J Gen Physiol , vol.111 , pp. 653-665
    • Rychkov, G.Y.1    Pusch, M.2    Roberts, M.L.3
  • 35
    • 84865589565 scopus 로고    scopus 로고
    • Sequential interaction of chloride and proton ions with the fast gate steer the voltage-dependent gating in ClC-2 chloride channels
    • PID: 22753549
    • Sánchez-Rodríguez JE, Santiago-Castillo JAD, Contreras-Vite JA et al (2012) Sequential interaction of chloride and proton ions with the fast gate steer the voltage-dependent gating in ClC-2 chloride channels. J Physiol 590:4239–4253. doi:10.1113/jphysiol.2012.232660
    • (2012) J Physiol , vol.590 , pp. 4239-4253
    • Sánchez-Rodríguez, J.E.1    Santiago-Castillo, J.A.D.2    Contreras-Vite, J.A.3
  • 36
    • 0032921415 scopus 로고    scopus 로고
    • The muscle chloride channel ClC-1 has a double-barreled appearance that is differentially affected in dominant and recessive myotonia
    • COI: 1:CAS:528:DyaK1MXhvVShsrs%3D, PID: 10051520
    • Saviane C, Conti F, Pusch M (1999) The muscle chloride channel ClC-1 has a double-barreled appearance that is differentially affected in dominant and recessive myotonia. J Gen Physiol 113:457–468. doi:10.1085/jgp.113.3.457
    • (1999) J Gen Physiol , vol.113 , pp. 457-468
    • Saviane, C.1    Conti, F.2    Pusch, M.3
  • 37
    • 33746628034 scopus 로고    scopus 로고
    • Barttin modulates trafficking and function of ClC-K channels
    • COI: 1:CAS:528:DC%2BD28XnvVarsL8%3D, PID: 16849430
    • Scholl U, Hebeisen S, Janssen AGH et al (2006) Barttin modulates trafficking and function of ClC-K channels. Proc Natl Acad Sci U S A 103:11411–11416. doi:10.1073/pnas.0601631103
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 11411-11416
    • Scholl, U.1    Hebeisen, S.2    Janssen, A.G.H.3
  • 38
    • 84884909638 scopus 로고    scopus 로고
    • Regulation of ClC-2 gating by intracellular ATP
    • Stölting G, Teodorescu G, Begemann B et al (2013) Regulation of ClC-2 gating by intracellular ATP. Pflugers Arch-Eur J Physiol 465:1423–1437. doi:10.1007/s00424-013-1286-0
    • (2013) Pflugers Arch-Eur J Physiol , vol.465 , pp. 1423-1437
    • Stölting, G.1    Teodorescu, G.2    Begemann, B.3
  • 39
    • 0026522116 scopus 로고
    • A chloride channel widely expressed in epithelial and non-epithelial cells
    • COI: 1:CAS:528:DyaK38Xks1Cqsbw%3D, PID: 1311421
    • Thiemann A, Gründer S, Pusch M, Jentsch TJ (1992) A chloride channel widely expressed in epithelial and non-epithelial cells. Nature 356:57–60. doi:10.1038/356057a0
    • (1992) Nature , vol.356 , pp. 57-60
    • Thiemann, A.1    Gründer, S.2    Pusch, M.3    Jentsch, T.J.4
  • 40
    • 0036759083 scopus 로고    scopus 로고
    • The myotonia congenita mutation A331T confers a novel hyperpolarization-activated gate to the muscle chloride channel ClC-1
    • COI: 1:CAS:528:DC%2BD38XmvFCmsbo%3D, PID: 12196568
    • Warnstedt M, Sun C, Poser B et al (2002) The myotonia congenita mutation A331T confers a novel hyperpolarization-activated gate to the muscle chloride channel ClC-1. J Neurosci 22:7462–7470
    • (2002) J Neurosci , vol.22 , pp. 7462-7470
    • Warnstedt, M.1    Sun, C.2    Poser, B.3
  • 41
    • 84864302396 scopus 로고    scopus 로고
    • Disease-causing mutations C277R and C277Y modify gating of human ClC-1 chloride channels in myotonia congenita
    • PID: 22641783
    • Weinberger S, Wojciechowski D, Sternberg D et al (2012) Disease-causing mutations C277R and C277Y modify gating of human ClC-1 chloride channels in myotonia congenita. J Physiol. doi:10.1113/jphysiol.2012.232785
    • (2012) J Physiol
    • Weinberger, S.1    Wojciechowski, D.2    Sternberg, D.3
  • 42
    • 0035951822 scopus 로고    scopus 로고
    • Pores formed by single subunits in mixed dimers of different CLC chloride channels
    • COI: 1:CAS:528:DC%2BD3MXhtVCqu7Y%3D, PID: 11035003
    • Weinreich F, Jentsch TJ (2001) Pores formed by single subunits in mixed dimers of different CLC chloride channels. J Biol Chem 276:2347–2353. doi:10.1074/jbc.M005733200
    • (2001) J Biol Chem , vol.276 , pp. 2347-2353
    • Weinreich, F.1    Jentsch, T.J.2
  • 43
    • 1642524953 scopus 로고    scopus 로고
    • The voltage-dependent ClC-2 chloride channel has a dual gating mechanism
    • PID: 14724195
    • Zúñiga L, Niemeyer MI, Varela D et al (2004) The voltage-dependent ClC-2 chloride channel has a dual gating mechanism. J Physiol 555:671–682. doi:10.1113/jphysiol.2003.060046
    • (2004) J Physiol , vol.555 , pp. 671-682
    • Zúñiga, L.1    Niemeyer, M.I.2    Varela, D.3


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