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Volumn 173, Issue 5, 2006, Pages 795-807

Mapping of tetraspanin-enriched microdomains that can function as gateways for HIV-1

Author keywords

[No Author keywords available]

Indexed keywords

CD63 ANTIGEN; CD81 ANTIGEN; CD82 ANTIGEN; CD9 ANTIGEN; GAG PROTEIN; GLYCOPROTEIN; INTEGRIN; LIPID; PROTEIN; TETRASPANIN; VIRUS PROTEIN; FIBRINOGEN RECEPTOR; LEUKOCYTE ANTIGEN; LYSOSOMAL PROTEIN GP53; MEMBRANE PROTEIN; VIRUS ENVELOPE PROTEIN;

EID: 33747394451     PISSN: 00219525     EISSN: 00219525     Source Type: Journal    
DOI: 10.1083/jcb.200508165     Document Type: Article
Times cited : (202)

References (58)
  • 1
    • 0025744022 scopus 로고
    • CD63/Pltgp40: A platelet activation antigen identical to the stage-specific, melanoma-associated antigen ME491
    • Azorsa, D.O., J.A. Hyman, and J.E. Hildreth. 1991. CD63/Pltgp40: a platelet activation antigen identical to the stage-specific, melanoma-associated antigen ME491. Blood. 78:280-284.
    • (1991) Blood , vol.78 , pp. 280-284
    • Azorsa, D.O.1    Hyman, J.A.2    Hildreth, J.E.3
  • 2
    • 0035207920 scopus 로고    scopus 로고
    • Complexes of tetraspanins with integrins: More than meets the eye
    • Berditchevski, F. 2001. Complexes of tetraspanins with integrins: more than meets the eye. J. Cell Sci. 114:4143-4151.
    • (2001) J. Cell Sci , vol.114 , pp. 4143-4151
    • Berditchevski, F.1
  • 3
    • 0033606802 scopus 로고    scopus 로고
    • Characterization of integrin-tetraspanin adhesion complexes: Role of tetraspanins in integrin signaling
    • Berditchevski, F., and E. Odintsova. 1999. Characterization of integrin-tetraspanin adhesion complexes: role of tetraspanins in integrin signaling. J. Cell Biol. 146:477-492.
    • (1999) J. Cell Biol , vol.146 , pp. 477-492
    • Berditchevski, F.1    Odintsova, E.2
  • 4
    • 0031018172 scopus 로고    scopus 로고
    • A novel link between integrins, transmembrane-4 superfamily proteins (CD63 and CD81), and phosphatidylinositol 4-kinase
    • Berditchevski, F., K.F. Tolias, K. Wong, C.L. Carpenter, and M.E. Hemler. 1997. A novel link between integrins, transmembrane-4 superfamily proteins (CD63 and CD81), and phosphatidylinositol 4-kinase. J. Biol. Chem. 272:2595-2598.
    • (1997) J. Biol. Chem , vol.272 , pp. 2595-2598
    • Berditchevski, F.1    Tolias, K.F.2    Wong, K.3    Carpenter, C.L.4    Hemler, M.E.5
  • 5
    • 0038618759 scopus 로고    scopus 로고
    • Targeting of the human immunodeficiency virus type 1 envelope to the trans-Golgi network through binding to TIP47 is required for Env incorporation into virions and infectivity
    • Blot, G., K. Janvier, S. Le Panse, R. Benarous, and C. Berlioz-Torrent. 2003. Targeting of the human immunodeficiency virus type 1 envelope to the trans-Golgi network through binding to TIP47 is required for Env incorporation into virions and infectivity. J. Virol. 77:6931-6945.
    • (2003) J. Virol , vol.77 , pp. 6931-6945
    • Blot, G.1    Janvier, K.2    Le Panse, S.3    Benarous, R.4    Berlioz-Torrent, C.5
  • 7
    • 0037154214 scopus 로고    scopus 로고
    • Overexpression of the N-terminal domain of TSG101 inhibits HIV-1 budding by blocking late domain function
    • Demirov, D.G., A. Ono, J.M. Orenstein, and E.O. Freed. 2002. Overexpression of the N-terminal domain of TSG101 inhibits HIV-1 budding by blocking late domain function. Proc. Natl. Acad. Sci. USA. 99:955-960.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 955-960
    • Demirov, D.G.1    Ono, A.2    Orenstein, J.M.3    Freed, E.O.4
  • 8
    • 0037302342 scopus 로고    scopus 로고
    • Independent segregation of human immunodeficiency virus type 1 Gag protein complexes and lipid rafts
    • Ding, L., A. Derdowski, J.J. Wang, and P. Spearman. 2003. Independent segregation of human immunodeficiency virus type 1 Gag protein complexes and lipid rafts. J. Virol. 77:1916-1926.
    • (2003) J. Virol , vol.77 , pp. 1916-1926
    • Ding, L.1    Derdowski, A.2    Wang, J.J.3    Spearman, P.4
  • 9
    • 0037959071 scopus 로고    scopus 로고
    • The state of lipid rafts: From model membranes to cells
    • Edidin, M. 2003. The state of lipid rafts: from model membranes to cells. Annu. Rev. Biophys. Biomol. Struct. 32:257-283.
    • (2003) Annu. Rev. Biophys. Biomol. Struct , vol.32 , pp. 257-283
    • Edidin, M.1
  • 10
    • 0032493658 scopus 로고    scopus 로고
    • Selective enrichment of tetraspan proteins on the internal vesicles of multivesicular endosomes and on exosomes secreted by human B-lymphocytes
    • Escola, J.M., M.J. Kleijmeer, W. Stoorvogel, J.M. Griffith, O. Yoshie, and H.J. Geuze. 1998. Selective enrichment of tetraspan proteins on the internal vesicles of multivesicular endosomes and on exosomes secreted by human B-lymphocytes. J. Biol. Chem. 273:20121-20127.
    • (1998) J. Biol. Chem , vol.273 , pp. 20121-20127
    • Escola, J.M.1    Kleijmeer, M.J.2    Stoorvogel, W.3    Griffith, J.M.4    Yoshie, O.5    Geuze, H.J.6
  • 11
    • 0037947831 scopus 로고    scopus 로고
    • Unbiased quantitative proteomics of lipid rafts reveals high specificity for signaling factors
    • Foster, L.J., C.L. De Hoog, and M. Mann. 2003. Unbiased quantitative proteomics of lipid rafts reveals high specificity for signaling factors. Proc. Natl. Acad. Sci. USA. 100:5813-5818.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 5813-5818
    • Foster, L.J.1    De Hoog, C.L.2    Mann, M.3
  • 13
    • 0035167651 scopus 로고    scopus 로고
    • The human cytomegalovirus US28 protein is located in endocytic vesicles and undergoes constitutive endocytosis and recycling
    • Fraile-Ramos, A., T.N. Kledal, A. Pelchen-Matthews, K. Bowers, T.W. Schwartz, and M. Marsh. 2001. The human cytomegalovirus US28 protein is located in endocytic vesicles and undergoes constitutive endocytosis and recycling. Mol. Biol. Cell. 12:1737-1749.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1737-1749
    • Fraile-Ramos, A.1    Kledal, T.N.2    Pelchen-Matthews, A.3    Bowers, K.4    Schwartz, T.W.5    Marsh, M.6
  • 16
    • 0042839654 scopus 로고    scopus 로고
    • 4D imaging to assay complex dynamics in live specimens
    • Gerlich, D., and J. Ellenberg. 2003. 4D imaging to assay complex dynamics in live specimens. Nat. Cell Biol. 5(Suppl.):S14-S19.
    • (2003) Nat. Cell Biol , vol.5 , Issue.SUPPL.
    • Gerlich, D.1    Ellenberg, J.2
  • 17
    • 0031592609 scopus 로고    scopus 로고
    • Cell membrane vesicles are a major contaminant of gradient-enriched human immunodeficiency virus type-1 preparations
    • Gluschankof, P., I. Mondor, H.R. Gelderblom, and Q.J. Sattentau. 1997. Cell membrane vesicles are a major contaminant of gradient-enriched human immunodeficiency virus type-1 preparations. Virology. 230:125-133.
    • (1997) Virology , vol.230 , pp. 125-133
    • Gluschankof, P.1    Mondor, I.2    Gelderblom, H.R.3    Sattentau, Q.J.4
  • 18
    • 0035490884 scopus 로고    scopus 로고
    • The endocytic pathway: A mosaic of domains
    • Gruenberg, J. 2001. The endocytic pathway: a mosaic of domains. Nat. Rev. Mol. Cell Biol. 2:721-730.
    • (2001) Nat. Rev. Mol. Cell Biol , vol.2 , pp. 721-730
    • Gruenberg, J.1
  • 19
    • 0344708475 scopus 로고    scopus 로고
    • Tetraspanin proteins mediate cellular penetration, invasion, and fusion events and define a novel type of membrane microdomain
    • Hemler, M.E. 2003. Tetraspanin proteins mediate cellular penetration, invasion, and fusion events and define a novel type of membrane microdomain. Annu. Rev. Cell Dev. Biol. 19:397-422.
    • (2003) Annu. Rev. Cell Dev. Biol , vol.19 , pp. 397-422
    • Hemler, M.E.1
  • 20
    • 28444441957 scopus 로고    scopus 로고
    • Tetraspanin functions and associated microdomains
    • Hemler, M.E. 2005. Tetraspanin functions and associated microdomains. Nat. Rev. Mol. Cell Biol. 6:801-811.
    • (2005) Nat. Rev. Mol. Cell Biol , vol.6 , pp. 801-811
    • Hemler, M.E.1
  • 21
    • 0033856584 scopus 로고    scopus 로고
    • Localization of human immunodeficiency virus type 1 Gag and Env at the plasma membrane by confocal imaging
    • Hermida-Matsumoto, L., and M.D. Resh. 2000. Localization of human immunodeficiency virus type 1 Gag and Env at the plasma membrane by confocal imaging. J. Virol. 74:8670-8679.
    • (2000) J. Virol , vol.74 , pp. 8670-8679
    • Hermida-Matsumoto, L.1    Resh, M.D.2
  • 22
    • 22344442585 scopus 로고    scopus 로고
    • Quantitative electron microscopy and fluorescence spectroscopy of the membrane distribution of influenza hemagglutinin
    • Hess, S.T., M. Kumar, A. Verma, J. Farrington, A. Kenworthy, and J. Zimmerberg. 2005. Quantitative electron microscopy and fluorescence spectroscopy of the membrane distribution of influenza hemagglutinin. J. Cell Biol. 169:965-976.
    • (2005) J. Cell Biol , vol.169 , pp. 965-976
    • Hess, S.T.1    Kumar, M.2    Verma, A.3    Farrington, J.4    Kenworthy, A.5    Zimmerberg, J.6
  • 23
    • 8844224911 scopus 로고    scopus 로고
    • Differential use of two AP-3-mediated pathways by lysosomal membrane proteins
    • Ihrke, G., A. Kyttala, M.R. Russell, B.A. Rous, and J.P. Luzio. 2004. Differential use of two AP-3-mediated pathways by lysosomal membrane proteins. Traffic. 5:946-962.
    • (2004) Traffic , vol.5 , pp. 946-962
    • Ihrke, G.1    Kyttala, A.2    Russell, M.R.3    Rous, B.A.4    Luzio, J.P.5
  • 24
    • 19344375822 scopus 로고    scopus 로고
    • Synaptotagmin VII restricts fusion pore expansion during lysosomal exocytosis
    • Jaiswal, J.K., S. Chakrabarti, N.W. Andrews, and S.M. Simon. 2004. Synaptotagmin VII restricts fusion pore expansion during lysosomal exocytosis. PLoS Biol. 2:E233.
    • (2004) PLoS Biol , vol.2
    • Jaiswal, J.K.1    Chakrabarti, S.2    Andrews, N.W.3    Simon, S.M.4
  • 25
    • 24344449035 scopus 로고    scopus 로고
    • Role of the endocytic machinery in the sorting of lysosome-associated membrane proteins
    • Janvier, K., and J.S. Bonifacino. 2005. Role of the endocytic machinery in the sorting of lysosome-associated membrane proteins. Mol. Biol. Cell. 16:4231-4242.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 4231-4242
    • Janvier, K.1    Bonifacino, J.S.2
  • 26
    • 1642540589 scopus 로고    scopus 로고
    • HIV-1 cell to cell transfer across an Env-induced, actin-dependent synapse
    • Jolly, C., K. Kashefi, M. Hollinshead, and Q.J. Sattentau. 2004. HIV-1 cell to cell transfer across an Env-induced, actin-dependent synapse. J. Exp. Med. 199:283-293.
    • (2004) J. Exp. Med , vol.199 , pp. 283-293
    • Jolly, C.1    Kashefi, K.2    Hollinshead, M.3    Sattentau, Q.J.4
  • 28
    • 13444259476 scopus 로고    scopus 로고
    • The tetraspanin web modulates immune-signalling complexes
    • Levy, S., and T. Shoham. 2005. The tetraspanin web modulates immune-signalling complexes. Nat. Rev. Immunol. 5:136-148.
    • (2005) Nat. Rev. Immunol , vol.5 , pp. 136-148
    • Levy, S.1    Shoham, T.2
  • 29
    • 0034864631 scopus 로고    scopus 로고
    • Multimerization of human immunodeficiency virus type 1 Gag promotes its localization to barges, raft-like membrane microdomains
    • Lindwasser, O.W., and M.D. Resh. 2001. Multimerization of human immunodeficiency virus type 1 Gag promotes its localization to barges, raft-like membrane microdomains. J. Virol. 75:7913-7924.
    • (2001) J. Virol , vol.75 , pp. 7913-7924
    • Lindwasser, O.W.1    Resh, M.D.2
  • 30
    • 2442662800 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Gag contains a dileucine-like motif that regulates association with multivesicular bodies
    • Lindwasser, O.W., and M.D. Resh. 2004. Human immunodeficiency virus type 1 Gag contains a dileucine-like motif that regulates association with multivesicular bodies. J. Virol. 78:6013-6023.
    • (2004) J. Virol , vol.78 , pp. 6013-6023
    • Lindwasser, O.W.1    Resh, M.D.2
  • 31
    • 0029762913 scopus 로고    scopus 로고
    • Improving structural integrity of cryosections for immunogold labeling
    • Liou, W., H.J. Geuze, and J.W. Slot. 1996. Improving structural integrity of cryosections for immunogold labeling. Histochem. Cell Biol. 106:41-58.
    • (1996) Histochem. Cell Biol , vol.106 , pp. 41-58
    • Liou, W.1    Geuze, H.J.2    Slot, J.W.3
  • 32
    • 0035658023 scopus 로고    scopus 로고
    • HIV-1 and Ebola virus encode small peptide motifs that recruit Tsg101 to sites of particle assembly to facilitate egress
    • Martin-Serrano, J., T. Zang, and P.D. Bieniasz. 2001. HIV-1 and Ebola virus encode small peptide motifs that recruit Tsg101 to sites of particle assembly to facilitate egress. Nat. Med. 7:1313-1319.
    • (2001) Nat. Med , vol.7 , pp. 1313-1319
    • Martin-Serrano, J.1    Zang, T.2    Bieniasz, P.D.3
  • 33
    • 0037383128 scopus 로고    scopus 로고
    • Role of ESCRT-I in retroviral budding
    • Martin-Serrano, J., T. Zang, and P.D. Bieniasz. 2003. Role of ESCRT-I in retroviral budding. J. Virol. 77:4794-4804.
    • (2003) J. Virol , vol.77 , pp. 4794-4804
    • Martin-Serrano, J.1    Zang, T.2    Bieniasz, P.D.3
  • 38
    • 0034015604 scopus 로고    scopus 로고
    • Evidence for budding of human immunodeficiency virus type 1 selectively from glycolipid-enriched membrane lipid rafts
    • Nguyen, D.H., and J.E. Hildreth. 2000. Evidence for budding of human immunodeficiency virus type 1 selectively from glycolipid-enriched membrane lipid rafts. J. Virol. 74:3264-3272.
    • (2000) J. Virol , vol.74 , pp. 3264-3272
    • Nguyen, D.H.1    Hildreth, J.E.2
  • 39
    • 0346937486 scopus 로고    scopus 로고
    • HIV-1 Egress is gated through late endosomal membranes
    • Nydegger, S., M. Foti, A. Derdowski, P. Spearman, and M. Thali. 2003. HIV-1 Egress is gated through late endosomal membranes. Traffic. 4:902-910.
    • (2003) Traffic , vol.4 , pp. 902-910
    • Nydegger, S.1    Foti, M.2    Derdowski, A.3    Spearman, P.4    Thali, M.5
  • 40
    • 0035923525 scopus 로고    scopus 로고
    • Plasma membrane rafts play a critical role in HIV-1 assembly and release
    • Ono, A., and E.O. Freed. 2001. Plasma membrane rafts play a critical role in HIV-1 assembly and release. Proc. Natl. Acad. Sci. USA. 98:13925-13930.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 13925-13930
    • Ono, A.1    Freed, E.O.2
  • 41
    • 0027332763 scopus 로고
    • Association of host cell surface adhesion receptors and other membrane proteins with HIV and SIV
    • Orentas, R.J., and J.E. Hildreth. 1993. Association of host cell surface adhesion receptors and other membrane proteins with HIV and SIV. AIDS Res. Hum. Retroviruses. 9:1157-1165.
    • (1993) AIDS Res. Hum. Retroviruses , vol.9 , pp. 1157-1165
    • Orentas, R.J.1    Hildreth, J.E.2
  • 42
    • 0036845721 scopus 로고    scopus 로고
    • Potential roles of cellular proteins in HIV-1
    • Ott, D.E. 2002. Potential roles of cellular proteins in HIV-1. Rev. Med. Virol. 12:359-374.
    • (2002) Rev. Med. Virol , vol.12 , pp. 359-374
    • Ott, D.E.1
  • 43
    • 0041488655 scopus 로고    scopus 로고
    • Infectious HIV-1 assembles in late endosomes in primary macrophages
    • Pelchen-Matthews, A., B. Kramer, and M. Marsh. 2003. Infectious HIV-1 assembles in late endosomes in primary macrophages. J. Cell Biol. 162:443-455.
    • (2003) J. Cell Biol , vol.162 , pp. 443-455
    • Pelchen-Matthews, A.1    Kramer, B.2    Marsh, M.3
  • 44
    • 0028233744 scopus 로고
    • The role of cell-to-cell transmission in HIV infection
    • Phillips, D.M. 1994. The role of cell-to-cell transmission in HIV infection. AIDS. 8:719-731.
    • (1994) AIDS , vol.8 , pp. 719-731
    • Phillips, D.M.1
  • 46
    • 0020569368 scopus 로고
    • Assembly of enveloped viruses in Madin-Darby canine kidney cells: Polarized budding from single attached cells and from clusters of cells in suspension
    • Rodriguez-Boulan, E., K.T. Paskiet, and D.D. Sabatini. 1983. Assembly of enveloped viruses in Madin-Darby canine kidney cells: polarized budding from single attached cells and from clusters of cells in suspension. J. Cell Biol. 96:866-874.
    • (1983) J. Cell Biol , vol.96 , pp. 866-874
    • Rodriguez-Boulan, E.1    Paskiet, K.T.2    Sabatini, D.D.3
  • 48
    • 0034610368 scopus 로고    scopus 로고
    • Palmitoylation of the HIV-1 envelope glycoprotein is critical for viral infectivity
    • Rousso, I., M.B. Mixon, B.K. Chen, and P.S. Kim. 2000. Palmitoylation of the HIV-1 envelope glycoprotein is critical for viral infectivity. Proc. Natl. Acad. Sci. USA. 97:13523-13525.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13523-13525
    • Rousso, I.1    Mixon, M.B.2    Chen, B.K.3    Kim, P.S.4
  • 49
    • 10244261559 scopus 로고    scopus 로고
    • CD9, CD63, CD81, and CD82 are components of a surface tetraspan network connected to HLA-DR and VLA integrins
    • Rubinstein, E., F. Le Naour, C. Lagaudriere-Gesbert, M. Billard, H. Conjeaud, and C. Boucheix. 1996. CD9, CD63, CD81, and CD82 are components of a surface tetraspan network connected to HLA-DR and VLA integrins. Eur. J. Immunol. 26:2657-2665.
    • (1996) Eur. J. Immunol , vol.26 , pp. 2657-2665
    • Rubinstein, E.1    Le Naour, F.2    Lagaudriere-Gesbert, C.3    Billard, M.4    Conjeaud, H.5    Boucheix, C.6
  • 50
    • 15344350796 scopus 로고    scopus 로고
    • Dynamic fluorescent imaging of human immunodeficiency virus type 1 Gag in live cells by biarsenical labeling
    • Rudner, L., S. Nydegger, L.V. Coren, K. Nagashima, M. Thali, and D.E. Ott. 2005. Dynamic fluorescent imaging of human immunodeficiency virus type 1 Gag in live cells by biarsenical labeling. J. Virol. 79:4055-4065.
    • (2005) J. Virol , vol.79 , pp. 4055-4065
    • Rudner, L.1    Nydegger, S.2    Coren, L.V.3    Nagashima, K.4    Thali, M.5    Ott, D.E.6
  • 51
    • 0025799606 scopus 로고
    • Simultaneous visualization of LDL receptor distribution and clathrin lattices on membranes torn from the upper surface of cultured cells
    • Sanan, D.A., and R.G. Anderson. 1991. Simultaneous visualization of LDL receptor distribution and clathrin lattices on membranes torn from the upper surface of cultured cells. J. Histochem. Cytochem. 39:1017-1024.
    • (1991) J. Histochem. Cytochem , vol.39 , pp. 1017-1024
    • Sanan, D.A.1    Anderson, R.G.2
  • 52
    • 0033523774 scopus 로고    scopus 로고
    • Regulated secretion from hemopoietic cells
    • Stinchcombe, J.C., and G.M. Griffiths. 1999. Regulated secretion from hemopoietic cells. J. Cell Biol. 147:1-6.
    • (1999) J. Cell Biol , vol.147 , pp. 1-6
    • Stinchcombe, J.C.1    Griffiths, G.M.2
  • 54
    • 0347482478 scopus 로고    scopus 로고
    • Influenza virus hemagglutinin concentrates in lipid raft microdomains for efficient viral fusion
    • Takeda, M., G.P. Leser, C.J. Russell, and R.A. Lamb. 2003. Influenza virus hemagglutinin concentrates in lipid raft microdomains for efficient viral fusion. Proc. Natl. Acad. Sci. USA. 100:14610-14617.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 14610-14617
    • Takeda, M.1    Leser, G.P.2    Russell, C.J.3    Lamb, R.A.4
  • 55
    • 0242302578 scopus 로고    scopus 로고
    • Tetraspanins: Molecular organisers of the leukocyte surface
    • Tarrant, J.M., L. Robb, A.B. van Spriel, and M.D. Wright. 2003. Tetraspanins: molecular organisers of the leukocyte surface. Trends Immunol. 24:610-617.
    • (2003) Trends Immunol , vol.24 , pp. 610-617
    • Tarrant, J.M.1    Robb, L.2    van Spriel, A.B.3    Wright, M.D.4
  • 57
    • 0036863574 scopus 로고    scopus 로고
    • Clustering of MHC- peptide complexes prior to their engagement in the immunological synapse: Lipid raft and tetraspan microdomains
    • Vogt, A.B., S. Spindeldreher, and H. Kropshofer. 2002. Clustering of MHC- peptide complexes prior to their engagement in the immunological synapse: lipid raft and tetraspan microdomains. Immunol. Rev. 189:136-151.
    • (2002) Immunol. Rev , vol.189 , pp. 136-151
    • Vogt, A.B.1    Spindeldreher, S.2    Kropshofer, H.3
  • 58
    • 11244304502 scopus 로고    scopus 로고
    • Palmitoylation supports assembly and function of integrin-tetraspanin complexes
    • Yang, X., O.V. Kovalenko, W. Tang, C. Claas, C.S. Stipp, and M.E. Hemler. 2004. Palmitoylation supports assembly and function of integrin-tetraspanin complexes. J. Cell Biol. 167:1231-1240.
    • (2004) J. Cell Biol , vol.167 , pp. 1231-1240
    • Yang, X.1    Kovalenko, O.V.2    Tang, W.3    Claas, C.4    Stipp, C.S.5    Hemler, M.E.6


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