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Volumn 88, Issue 12, 2014, Pages 6586-6598

A complex comprising phosphatidylinositol 4-kinase IIIβ, ACBD3, and Aichi virus proteins enhances phosphatidylinositol 4-phosphate synthesis and is critical for formation of the viral replication complex

Author keywords

[No Author keywords available]

Indexed keywords

2B PROTEIN; 2BC PROTEIN; 2C PROTEIN; 3A PROTEIN; 3AB PROTEIN; ACYL COENZYME A BINDING DOMAIN CONTAINING 3 PROTEIN; DIAZEPAM BINDING INHIBITOR; PHOSPHATIDYLINOSITOL 4 KINASE IIIBETA; PHOSPHATIDYLINOSITOL 4 PHOSPHATE; PHOSPHATIDYLINOSITOL KINASE; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 84901344291     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00208-14     Document Type: Article
Times cited : (48)

References (48)
  • 1
    • 0029814801 scopus 로고    scopus 로고
    • Membrane permeabilization by poliovirus proteins 2B and 2BC
    • Aldabe R, Barco A, Carrasco L. 1996. Membrane permeabilization by poliovirus proteins 2B and 2BC. J. Biol. Chem. 271:23134-23137. http://dx.doi.org/10.1074/jbc.271.38.23134.
    • (1996) J. Biol. Chem. , vol.271 , pp. 23134-23137
    • Aldabe, R.1    Barco, A.2    Carrasco, L.3
  • 2
    • 0028037893 scopus 로고
    • Membrane rearrangement and vesicle induction by recombinant poliovirus 2C and 2BC in human cells
    • Cho MW, Teterina N, Egger D, Bienz K, Ehrenfeld E. 1994. Membrane rearrangement and vesicle induction by recombinant poliovirus 2C and 2BC in human cells. Virology 202:129-145. http://dx.doi.org/10.1006/viro.1994.1329.
    • (1994) Virology , vol.202 , pp. 129-145
    • Cho, M.W.1    Teterina, N.2    Egger, D.3    Bienz, K.4    Ehrenfeld, E.5
  • 3
    • 0033919961 scopus 로고    scopus 로고
    • Formation of the poliovirus replication complex requires coupled viral translation, vesicle production, and viral RNA synthesis
    • Egger D, Teterina N, Ehrenfeld E, Bienz K. 2000. Formation of the poliovirus replication complex requires coupled viral translation, vesicle production, and viral RNA synthesis. J. Virol. 74:6570-6580. http://dx.doi.org/10.1128/JVI.74.14.6570-6580.2000.
    • (2000) J. Virol. , vol.74 , pp. 6570-6580
    • Egger, D.1    Teterina, N.2    Ehrenfeld, E.3    Bienz, K.4
  • 4
    • 14744300849 scopus 로고    scopus 로고
    • Foot-and-mouth disease virus replication sites form next to the nucleus and close to the Golgi apparatus, but exclude marker proteins associated with host membrane compartments
    • Knox C, Moffat K, Ali S, Ryan M, Wileman T. 2005. Foot-and-mouth disease virus replication sites form next to the nucleus and close to the Golgi apparatus, but exclude marker proteins associated with host membrane compartments. J. Gen. Virol. 86:687-696. http://dx.doi.org/10.1099/vir.0.80208-0.
    • (2005) J. Gen. Virol. , vol.86 , pp. 687-696
    • Knox, C.1    Moffat, K.2    Ali, S.3    Ryan, M.4    Wileman, T.5
  • 5
    • 33847652985 scopus 로고    scopus 로고
    • Intracellular localization and effects of individually expressed human parechovirus 1 nonstructural proteins
    • Krogerus C, Samuilova O, Pöyry T, Jokitalo E, Hyypiä T. 2007. Intracellular localization and effects of individually expressed human parechovirus 1 nonstructural proteins. J. Gen. Virol. 88:831-841. http://dx.doi.org/10.1099/vir.0.82201-0.
    • (2007) J. Gen. Virol. , vol.88 , pp. 831-841
    • Krogerus, C.1    Samuilova, O.2    Pöyry, T.3    Jokitalo, E.4    Hyypiä, T.5
  • 6
    • 15244349265 scopus 로고    scopus 로고
    • Effects of foot-and-mouth disease virus nonstructural proteins on the structure and function of the early secretory pathway: 2BC but not 3A blocks endoplasmic reticulum-to-Golgi transport
    • Moffat K, Howell G, Knox C, Belsham GJ, Monaghan P, Ryan MD, Wileman T. 2005. Effects of foot-and-mouth disease virus nonstructural proteins on the structure and function of the early secretory pathway: 2BC but not 3A blocks endoplasmic reticulum-to-Golgi transport. J. Virol. 79:4382-4395. http://dx.doi.org/10.1128/JVI.79.7.4382-4395.2005.
    • (2005) J. Virol. , vol.79 , pp. 4382-4395
    • Moffat, K.1    Howell, G.2    Knox, C.3    Belsham, G.J.4    Monaghan, P.5    Ryan, M.D.6    Wileman, T.7
  • 7
    • 0033798416 scopus 로고    scopus 로고
    • Remodeling the endoplasmic reticulum by poliovirus infection and by individual viral proteins: an autophagy-like origin for virus-induced vesicles
    • Suhy DA, Giddings TH, Kirkegaard K. 2000. Remodeling the endoplasmic reticulum by poliovirus infection and by individual viral proteins: an autophagy-like origin for virus-induced vesicles. J. Virol. 74:8953-8965. http://dx.doi.org/10.1128/JVI.74.19.8953-8965.2000.
    • (2000) J. Virol. , vol.74 , pp. 8953-8965
    • Suhy, D.A.1    Giddings, T.H.2    Kirkegaard, K.3
  • 8
    • 0030807887 scopus 로고    scopus 로고
    • Poliovirus 2C protein determinants of membrane binding and rearrangements in mammalian cells
    • Teterina NL, Gorbalenya AE, Egger D, Bienz K, Ehrenfeld E. 1997. Poliovirus 2C protein determinants of membrane binding and rearrangements in mammalian cells. J. Virol. 71:8962-8972.
    • (1997) J. Virol. , vol.71 , pp. 8962-8972
    • Teterina, N.L.1    Gorbalenya, A.E.2    Egger, D.3    Bienz, K.4    Ehrenfeld, E.5
  • 9
    • 0029998594 scopus 로고    scopus 로고
    • Determinants of membrane association for poliovirus protein 3AB
    • Towner JS, Ho TV, Semler BL. 1996. Determinants of membrane association for poliovirus protein 3AB. J. Biol. Chem. 271:26810-26818. http://dx.doi.org/10.1074/jbc.271.43.26810.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26810-26818
    • Towner, J.S.1    Ho, T.V.2    Semler, B.L.3
  • 10
    • 42349086670 scopus 로고    scopus 로고
    • Modification of intracellular membrane structures for virus replication
    • Miller S, Krijnse-Locker J. 2008. Modification of intracellular membrane structures for virus replication. Nat. Rev. Microbiol. 6:363-374. http://dx.doi.org/10.1038/nrmicro1890.
    • (2008) Nat. Rev. Microbiol. , vol.6 , pp. 363-374
    • Miller, S.1    Krijnse-locker, J.2
  • 11
    • 33745933535 scopus 로고    scopus 로고
    • Phosphatidylinositol 4-kinases: old enzymes with emerging functions
    • Balla A, Balla T. 2006. Phosphatidylinositol 4-kinases: old enzymes with emerging functions. Trends Cell Biol. 16:351-361. http://dx.doi.org/10.1016/j.tcb.2006.05.003.
    • (2006) Trends Cell Biol. , vol.16 , pp. 351-361
    • Balla, A.1    Balla, T.2
  • 12
    • 47649123929 scopus 로고    scopus 로고
    • The multiple roles of PtdIns(4)P-not just the precursor of PtdIns(4,5)P2
    • D'Angelo G, Vicinanza M, Di Campli A, De Matteis MA. 2008. The multiple roles of PtdIns(4)P-not just the precursor of PtdIns(4,5)P2. J. Cell Sci. 121:1955-1963. http://dx.doi.org/10.1242/jcs.023630.
    • (2008) J. Cell Sci. , vol.121 , pp. 1955-1963
    • D'angelo, G.1    Vicinanza, M.2    Di Campli, A.3    De Matteis, M.A.4
  • 13
    • 79151470948 scopus 로고    scopus 로고
    • Coordination of Golgi functions by phosphatidylinositol 4-kinases
    • Graham TR, Burd CG. 2011. Coordination of Golgi functions by phosphatidylinositol 4-kinases. Trends Cell Biol. 21:113-121. http://dx.doi.org/10.1016/j.tcb.2010.10.002.
    • (2011) Trends Cell Biol. , vol.21 , pp. 113-121
    • Graham, T.R.1    Burd, C.G.2
  • 15
    • 80052284074 scopus 로고    scopus 로고
    • Hepatitis C virus stimulates the phosphatidylinositol 4-kinase IIIα-dependent phosphatidylinositol 4-phosphate production that is essential for its replication
    • Berger KL, Kelly SM, Jordan TX, Tartell MA, Randall G. 2011. Hepatitis C virus stimulates the phosphatidylinositol 4-kinase IIIα-dependent phosphatidylinositol 4-phosphate production that is essential for its replication. J. Virol. 85:8870-8883. http://dx.doi.org/10.1128/JVI.00059-11.
    • (2011) J. Virol. , vol.85 , pp. 8870-8883
    • Berger, K.L.1    Kelly, S.M.2    Jordan, T.X.3    Tartell, M.A.4    Randall, G.5
  • 16
    • 79953221885 scopus 로고    scopus 로고
    • Hepatitis C virus NS5A protein interacts with phosphatidylinositol 4-kinase type IIIα and regulates viral propagation
    • Lim YS, Hwang SB. 2011. Hepatitis C virus NS5A protein interacts with phosphatidylinositol 4-kinase type IIIα and regulates viral propagation. J. Biol. Chem. 286:11290-11298. http://dx.doi.org/10.1074/jbc. M110.194472.
    • (2011) J. Biol. Chem. , vol.286 , pp. 11290-11298
    • Lim, Y.S.1    Hwang, S.B.2
  • 18
    • 80053962863 scopus 로고    scopus 로고
    • The role of the phosphatidylinositol 4-kinase PI4KA in hepatitis C virus-induced host membrane rearrangement
    • Tai AW, Salloum S. 2011. The role of the phosphatidylinositol 4-kinase PI4KA in hepatitis C virus-induced host membrane rearrangement. PLoS One 6:e26300. http://dx.doi.org/10.1371/journal.pone.0026300.
    • (2011) PLoS One , vol.6
    • Tai, A.W.1    Salloum, S.2
  • 20
    • 79551707738 scopus 로고    scopus 로고
    • Phosphatidylinositol 4-kinase III beta is a target of enviroxime-like compounds for antipoliovirus activity
    • Arita M, Kojima H, Nagano T, Okabe T, Wakita T, Shimizu H. 2011. Phosphatidylinositol 4-kinase III beta is a target of enviroxime-like compounds for antipoliovirus activity. J. Virol. 85:2364-2372. http://dx.doi.org/10.1128/JVI.02249-10.
    • (2011) J. Virol. , vol.85 , pp. 2364-2372
    • Arita, M.1    Kojima, H.2    Nagano, T.3    Okabe, T.4    Wakita, T.5    Shimizu, H.6
  • 22
    • 0025996328 scopus 로고
    • Isolation of cytopathic small round viruses with BS-C-1 cells from patients with gastroenteritis
    • Yamashita T, Kobayashi S, Sakae K, Nakata S, Chiba S, Ishihara Y, Isomura S. 1991. Isolation of cytopathic small round viruses with BS-C-1 cells from patients with gastroenteritis. J. Infect. Dis. 164:954-957. http://dx.doi.org/10.1093/infdis/164.5.954.
    • (1991) J. Infect. Dis. , vol.164 , pp. 954-957
    • Yamashita, T.1    Kobayashi, S.2    Sakae, K.3    Nakata, S.4    Chiba, S.5    Ishihara, Y.6    Isomura, S.7
  • 24
    • 44449104906 scopus 로고    scopus 로고
    • Seroprevalence distribution of Aichi virus among a French population in 2006-2007
    • Goyer M, Aho LS, Bour JB, Ambert-Balay K, Pothier P. 2008. Seroprevalence distribution of Aichi virus among a French population in 2006-2007. Arch. Virol. 153:1171-1174. http://dx.doi.org/10.1007/s00705-008-0091-0.
    • (2008) Arch. Virol. , vol.153 , pp. 1171-1174
    • Goyer, M.1    Aho, L.S.2    Bour, J.B.3    Ambert-Balay, K.4    Pothier, P.5
  • 25
    • 33744461028 scopus 로고    scopus 로고
    • Molecular characterization of the first Aichi viruses isolated in Europe and in South America
    • Oh DY, Silva PA, Hauroeder B, Diedrich S, Cardoso DDP, Schreier E. 2006. Molecular characterization of the first Aichi viruses isolated in Europe and in South America. Arch. Virol. 151:1199-1206. http://dx.doi.org/10.1007/s00705-005-0706-7.
    • (2006) Arch. Virol. , vol.151 , pp. 1199-1206
    • Oh, D.Y.1    Silva, P.A.2    Hauroeder, B.3    Diedrich, S.4    Cardoso, D.D.P.5    Schreier, E.6
  • 26
    • 34547622267 scopus 로고    scopus 로고
    • Isolation and molecular characterization of Aichi viruses from fecal specimens collected in Japan, Bangladesh, Thailand, and Vietnam
    • Pham NTK, Khamrin P, Nguyen TA, Kanti DS, Phan TG, Okitsu S, Ushijima H. 2007. Isolation and molecular characterization of Aichi viruses from fecal specimens collected in Japan, Bangladesh, Thailand, and Vietnam. J. Clin. Microbiol. 45:2287-2288. http://dx.doi.org/10.1128/JCM.00525-07.
    • (2007) J. Clin. Microbiol. , vol.45 , pp. 2287-2288
    • Pham, N.T.K.1    Khamrin, P.2    Nguyen, T.A.3    Kanti, D.S.4    Phan, T.G.5    Okitsu, S.6    Ushijima, H.7
  • 27
    • 70449730467 scopus 로고    scopus 로고
    • Detection of Aichi virus shedding in a child with enteric and extraintestinal symptoms in Hungary
    • Reuter G, Boldizsår Å, Papp G, Pankovics P. 2009. Detection of Aichi virus shedding in a child with enteric and extraintestinal symptoms in Hungary. Arch. Virol. 154:1529-1532. http://dx.doi.org/10.1007/s00705-009-0473-y.
    • (2009) Arch. Virol. , vol.154 , pp. 1529-1532
    • Reuter, G.1    Boldizsår, Å.2    Papp, G.3    Pankovics, P.4
  • 29
    • 0029014856 scopus 로고
    • Isolation of cytopathic small round virus (Aichi virus) from Pakistani children and Japanese travelers from Southeast Asia
    • Yamashita T, Sakae K, Kobayashi S, Ishihara Y, Miyake T, Mubina A, Isomura S. 1995. Isolation of cytopathic small round virus (Aichi virus) from Pakistani children and Japanese travelers from Southeast Asia. Microbiol. Immunol. 39:433-435. http://dx.doi.org/10.1111/j.1348-0421.1995.tb02225.x.
    • (1995) Microbiol. Immunol. , vol.39 , pp. 433-435
    • Yamashita, T.1    Sakae, K.2    Kobayashi, S.3    Ishihara, Y.4    Miyake, T.5    Mubina, A.6    Isomura, S.7
  • 30
    • 0033876196 scopus 로고    scopus 로고
    • Application of a reverse transcription-PCR for identification and differentiation of Aichi virus, a new member of the Picornavirus family associated with gastroenteritis in humans
    • Yamashita T, Sugiyama M, Tsuzuki H, Sakae K, Suzuki Y, Miyazaki Y. 2000. Application of a reverse transcription-PCR for identification and differentiation of Aichi virus, a new member of the Picornavirus family associated with gastroenteritis in humans. J. Clin. Microbiol. 38:2955-2961.
    • (2000) J. Clin. Microbiol. , vol.38 , pp. 2955-2961
    • Yamashita, T.1    Sugiyama, M.2    Tsuzuki, H.3    Sakae, K.4    Suzuki, Y.5    Miyazaki, Y.6
  • 31
    • 70349976322 scopus 로고    scopus 로고
    • Aichi virus strains in children with gastroenteritis, China
    • Yang S, Zhang W, Shen Q, Yang Z, Zhu J, Cui L, Hua X. 2009. Aichi virus strains in children with gastroenteritis, China. Emerg. Infect. Dis. 15:1703-1705. http://dx.doi.org/10.3201/eid1510.090522.
    • (2009) Emerg. Infect. Dis. , vol.15 , pp. 1703-1705
    • Yang, S.1    Zhang, W.2    Shen, Q.3    Yang, Z.4    Zhu, J.5    Cui, L.6    Hua, X.7
  • 32
    • 84856501318 scopus 로고    scopus 로고
    • ACBD3-mediated recruitment of PI4KB to picornavirus RNA replication sites
    • Sasaki J, Ishikawa K, Arita M, Taniguchi K. 2012. ACBD3-mediated recruitment of PI4KB to picornavirus RNA replication sites. EMBO J. 31:754-766. http://dx.doi.org/10.1038/emboj.2011.429.
    • (2012) EMBO J. , vol.31 , pp. 754-766
    • Sasaki, J.1    Ishikawa, K.2    Arita, M.3    Taniguchi, K.4
  • 33
    • 84859594211 scopus 로고    scopus 로고
    • The 3A protein from multiple picornaviruses utilizes the Golgi adaptor protein ACBD3 to recruit PI4KIIIβ
    • Greninger AL, Knudsen GM, Betegon M, Burlingame AL, DeRisi JL. 2012. The 3A protein from multiple picornaviruses utilizes the Golgi adaptor protein ACBD3 to recruit PI4KIIIβ. J. Virol. 86:3605-3616. http://dx.doi.org/10.1128/JVI.06778-11.
    • (2012) J. Virol. , vol.86 , pp. 3605-3616
    • Greninger, A.L.1    Knudsen, G.M.2    Betegon, M.3    Burlingame, A.L.4    DeRisi, J.L.5
  • 34
    • 0042389497 scopus 로고    scopus 로고
    • Functional analysis of the stem-loop structures at the 5= end of the Aichi virus genome
    • Nagashima S, Sasaki J, Taniguchi K. 2003. Functional analysis of the stem-loop structures at the 5= end of the Aichi virus genome. Virology 313:56-65. http://dx.doi.org/10.1016/S0042-6822(03)00346-5.
    • (2003) Virology , vol.313 , pp. 56-65
    • Nagashima, S.1    Sasaki, J.2    Taniguchi, K.3
  • 35
    • 18744405099 scopus 로고    scopus 로고
    • The 5=-terminal region of the Aichi virus genome encodes cis-acting replication elements required for positive-and negative-strand RNA synthesis
    • Nagashima S, Sasaki J, Taniguchi K. 2005. The 5=-terminal region of the Aichi virus genome encodes cis-acting replication elements required for positive-and negative-strand RNA synthesis. J. Virol. 79:6918-6931. http://dx.doi.org/10.1128/JVI.79.11.6918-6931.2005.
    • (2005) J. Virol. , vol.79 , pp. 6918-6931
    • Nagashima, S.1    Sasaki, J.2    Taniguchi, K.3
  • 36
    • 45749103715 scopus 로고    scopus 로고
    • Interaction between polypeptide 3ABC and the 5=-terminal structural elements of the genome of Aichi virus: implication for negative-strand RNA synthesis
    • Nagashima S, Sasaki J, Taniguchi K. 2008. Interaction between polypeptide 3ABC and the 5=-terminal structural elements of the genome of Aichi virus: implication for negative-strand RNA synthesis. J. Virol. 82:6161-6171. http://dx.doi.org/10.1128/JVI.02151-07.
    • (2008) J. Virol. , vol.82 , pp. 6161-6171
    • Nagashima, S.1    Sasaki, J.2    Taniguchi, K.3
  • 37
    • 0034875872 scopus 로고    scopus 로고
    • Construction of an infectious cDNA clone of Aichi virus (a new member of the family Picornaviridae) and mutational analysis of a stem-loop structure at the 5= end of the genome
    • Sasaki J, Kusuhara Y, Maeno Y, Kobayashi N, Yamashita T, Sakae K, Takeda N, Taniguchi K. 2001. Construction of an infectious cDNA clone of Aichi virus (a new member of the family Picornaviridae) and mutational analysis of a stem-loop structure at the 5= end of the genome. J. Virol. 75:8021-8030. http://dx.doi.org/10.1128/JVI.75.17.8021-8030.2001.
    • (2001) J. Virol. , vol.75 , pp. 8021-8030
    • Sasaki, J.1    Kusuhara, Y.2    Maeno, Y.3    Kobayashi, N.4    Yamashita, T.5    Sakae, K.6    Takeda, N.7    Taniguchi, K.8
  • 38
    • 80054009114 scopus 로고    scopus 로고
    • A homogeneous and nonisotopic assay for phosphatidylinositol 4-kinases
    • Tai AW, Bojjireddy N, Balla T. 2011. A homogeneous and nonisotopic assay for phosphatidylinositol 4-kinases. Anal. Biochem. 417:97-102. http://dx.doi.org/10.1016/j.ab.2011.05.046.
    • (2011) Anal. Biochem. , vol.417 , pp. 97-102
    • Tai, A.W.1    Bojjireddy, N.2    Balla, T.3
  • 39
    • 28444476999 scopus 로고    scopus 로고
    • Membrane curvature and mechanisms of dynamic cell membrane remodeling
    • McMahon HT, Gallop JL. 2005. Membrane curvature and mechanisms of dynamic cell membrane remodeling. Nature 438:590-596. http://dx.doi.org/10.1038/nature04396.
    • (2005) Nature , vol.438 , pp. 590-596
    • McMahon, H.T.1    Gallop, J.L.2
  • 44
    • 23944443368 scopus 로고    scopus 로고
    • FAPP2 is involved in the transport of apical cargo in polarized MDCK cells
    • Vieira OV, Verkade P, Manninen A, Simons K. 2005. FAPP2 is involved in the transport of apical cargo in polarized MDCK cells. J. Cell Biol. 170:521-526. http://dx.doi.org/10.1083/jcb.200503078.
    • (2005) J. Cell Biol. , vol.170 , pp. 521-526
    • Vieira, O.V.1    Verkade, P.2    Manninen, A.3    Simons, K.4
  • 46
    • 79956320991 scopus 로고    scopus 로고
    • Molecular basis of phosphatidylinositol 4-phosphate and ARF1 GTPase recognition by the FAPP1 pleckstrin homology (PH) domain
    • He J, Scott JL, Heroux A, Roy S, Lenoir M, Overduin M, Stahelin RV, Kutateladze TG. 2011. Molecular basis of phosphatidylinositol 4-phosphate and ARF1 GTPase recognition by the FAPP1 pleckstrin homology (PH) domain. J. Biol. Chem. 286:18650-18657. http://dx.doi.org/10.1074/jbc. M111.233015.
    • (2011) J. Biol. Chem. , vol.286 , pp. 18650-18657
    • He, J.1    Scott, J.L.2    Heroux, A.3    Roy, S.4    Lenoir, M.5    Overduin, M.6    Stahelin, R.V.7    Kutateladze, T.G.8
  • 47
    • 80455132064 scopus 로고    scopus 로고
    • The transformation of enterovirus replication structures: a three-dimensional study of single-and doublemembrane compartments
    • Limpens RW, van der Schaar HM, Kumar D, Koster AJ, Snijder EJ, van Kuppeveld FJ, Bárcena M. 2011. The transformation of enterovirus replication structures: a three-dimensional study of single-and doublemembrane compartments. mBio 2:e00166-11. http://dx.doi.org/10.1128/mBio.00166-11.
    • (2011) mBio , vol.2
    • Limpens, R.W.1    van der Schaar, H.M.2    Kumar, D.3    Koster, A.J.4    Snijder, E.J.5    van Kuppeveld, F.J.6    Bárcena, M.7
  • 48
    • 84875776334 scopus 로고    scopus 로고
    • Oxysterol-binding protein family I is the target of minor enviroximelike compounds
    • Arita M, Kojima H, Nagano T, Okabe T, Wakita T, Shimizu H. 2013. Oxysterol-binding protein family I is the target of minor enviroximelike compounds. J. Virol. 87:4252-4260. http://dx.doi.org/10.1128/JVI.03546-12.
    • (2013) J. Virol. , vol.87 , pp. 4252-4260
    • Arita, M.1    Kojima, H.2    Nagano, T.3    Okabe, T.4    Wakita, T.5    Shimizu, H.6


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