메뉴 건너뛰기




Volumn 19, Issue , 2003, Pages 397-422

Tetraspanin Proteins Mediate Cellular Penetration, Invasion, and Fusion Events and Define a Novel Type of Membrane Microdomain

Author keywords

CD151; CD81; CD9; EWI 2; EWI F; Exosomes; Fertilization; Integrins; Lipid raft; Palmitoylation; Peripherin; Uroplakin

Indexed keywords

CD9 ANTIGEN; CELL SURFACE RECEPTOR; GROWTH FACTOR; INTEGRIN; LIPID; TETRASPANIN;

EID: 0344708475     PISSN: 10810706     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.cellbio.19.111301.153609     Document Type: Conference Paper
Times cited : (711)

References (149)
  • 2
    • 15844412034 scopus 로고    scopus 로고
    • Disruption of the Cr2 locus results in a reduction in B-1a cells and in an impaired B cell response to T-dependent antigen
    • Ahearn JM, Fischer MB, Croix D, Goerg S, Ma M, et al. 1996. Disruption of the Cr2 locus results in a reduction in B-1a cells and in an impaired B cell response to T-dependent antigen. Immunity 4:251-62
    • (1996) Immunity , vol.4 , pp. 251-262
    • Ahearn, J.M.1    Fischer, M.B.2    Croix, D.3    Goerg, S.4    Ma, M.5
  • 3
    • 0028057606 scopus 로고
    • Association of four antigens of the tetraspan family (CD37,CD53, TAPA-1 and R2/C33) with MHC class II glycoproteins
    • Angelisova P, Hilgert I, Horejsi V. 1994. Association of four antigens of the tetraspan family (CD37,CD53, TAPA-1 and R2/C33) with MHC class II glycoproteins. Immunogenetics 39:249-56
    • (1994) Immunogenetics , vol.39 , pp. 249-256
    • Angelisova, P.1    Hilgert, I.2    Horejsi, V.3
  • 4
    • 0037097563 scopus 로고    scopus 로고
    • C-kit associated with the transmembrane 4 superfamily proteins constitutes a functionally distinct subunit in human hematopoietic progenitors
    • Anzai N, Lee Y, Youn BS, Fukuda S, Kim YJ, et al. 2002. C-kit associated with the transmembrane 4 superfamily proteins constitutes a functionally distinct subunit in human hematopoietic progenitors. Blood 99:4413-21
    • (2002) Blood , vol.99 , pp. 4413-4421
    • Anzai, N.1    Lee, Y.2    Youn, B.S.3    Fukuda, S.4    Kim, Y.J.5
  • 5
    • 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. 114:4143-51
    • (2001) J. Cell Sci. , vol.114 , pp. 4143-4151
    • Berditchevski, F.1
  • 7
    • 0033606802 scopus 로고    scopus 로고
    • Characterization of integrin-tetraspanin adhesion complexes: Role of tetraspanins in integrin signaling
    • Berditchevski F, Odintsova E. 1999. Characterization of integrin-tetraspanin adhesion complexes: role of tetraspanins in integrin signaling. J. Cell Biol. 146:477-92
    • (1999) J. Cell Biol. , vol.146 , pp. 477-492
    • Berditchevski, F.1    Odintsova, E.2
  • 8
    • 0037020085 scopus 로고    scopus 로고
    • Expression of the palmitoylation-deficient CD151 weakens the association of alpha3beta1 integrin with the tetraspanin-enriched microdomains and affects integrin-dependent signalling
    • Berditchevski F, Odintsova E, Sawada S, Gilbert E. 2002. Expression of the palmitoylation-deficient CD151 weakens the association of alpha3beta1 integrin with the tetraspanin-enriched microdomains and affects integrin-dependent signalling. J. Biol. Chem. 277:36991-7000
    • (2002) J. Biol. Chem. , vol.277 , pp. 36991-37000
    • Berditchevski, F.1    Odintsova, E.2    Sawada, S.3    Gilbert, E.4
  • 9
    • 0035162539 scopus 로고    scopus 로고
    • KAI1, a prostate metastasis suppressor: Prediction of solvated structure and interactions with binding partners; integrins, cadherins, and cell-surface receptor proteins
    • Bienstock RJ, Barrett JC. 2001. KAI1, a prostate metastasis suppressor: prediction of solvated structure and interactions with binding partners; integrins, cadherins, and cell-surface receptor proteins. Mol. Carcinog. 32:139-53
    • (2001) Mol. Carcinog. , vol.32 , pp. 139-153
    • Bienstock, R.J.1    Barrett, J.C.2
  • 10
    • 0032733143 scopus 로고    scopus 로고
    • A novel rat tetraspan protein in cells of the oligodendrocyte lineage
    • Birling MC, Tait S, Hardy RJ, Brophy PJ. 1999. A novel rat tetraspan protein in cells of the oligodendrocyte lineage. J. Neurochem. 73:2600-8
    • (1999) J. Neurochem. , vol.73 , pp. 2600-2608
    • Birling, M.C.1    Tait, S.2    Hardy, R.J.3    Brophy, P.J.4
  • 14
    • 0032421354 scopus 로고    scopus 로고
    • Functions of lipid rafts in biological membranes
    • Brown DA, London E. 1998. Functions of lipid rafts in biological membranes. Annu. Rev. Cell Dev. Biol. 14:111-36
    • (1998) Annu. Rev. Cell Dev. Biol. , vol.14 , pp. 111-136
    • Brown, D.A.1    London, E.2
  • 15
    • 0035872923 scopus 로고    scopus 로고
    • Quality control of transmembrane domain assembly in the tetraspanin CD82
    • Cannon KS, Cresswell P. 2001. Quality control of transmembrane domain assembly in the tetraspanin CD82. EMBO J. 20:2443-53
    • (2001) EMBO J. , vol.20 , pp. 2443-2453
    • Cannon, K.S.1    Cresswell, P.2
  • 16
    • 0029067385 scopus 로고
    • Association of the transmembrane 4 superfamily molecule CD53 with a tyrosine phosphatase activity
    • Carmo AM, Wright MD. 1995. Association of the transmembrane 4 superfamily molecule CD53 with a tyrosine phosphatase activity. Eur. J. Immunol. 25:2090-95
    • (1995) Eur. J. Immunol. , vol.25 , pp. 2090-2095
    • Carmo, A.M.1    Wright, M.D.2
  • 17
    • 0034629169 scopus 로고    scopus 로고
    • Cell surface monkey CD9 antigen is a coreceptor that increases diphtheria toxin sensitivity and diphtheria toxin receptor affinity
    • Cha JH, Brooke JS, Ivey KN, Eidels L. 2000. Cell surface monkey CD9 antigen is a coreceptor that increases diphtheria toxin sensitivity and diphtheria toxin receptor affinity. J. Biol. Chem. 275:6901-7
    • (2000) J. Biol. Chem. , vol.275 , pp. 6901-6907
    • Cha, J.H.1    Brooke, J.S.2    Ivey, K.N.3    Eidels, L.4
  • 18
    • 0035958026 scopus 로고    scopus 로고
    • The major CD9 and CD81 molecular partner. Identification and characterization of the complexes
    • Charrin S, Le Naour F, Oualid M, Billard M, Faure G, et al. 2001. The major CD9 and CD81 molecular partner. Identification and characterization of the complexes. J. Biol. Chem. 276:14329-37
    • (2001) J. Biol. Chem. , vol.276 , pp. 14329-14337
    • Charrin, S.1    Le Naour, F.2    Oualid, M.3    Billard, M.4    Faure, G.5
  • 19
    • 0037051906 scopus 로고    scopus 로고
    • Differential stability of tetraspanin/tetraspanin interactions: Role of palmitoylation
    • Charrin S, Manie S, Oualid M, Billard M, Boucheix C, Rubinstein E. 2002. Differential stability of tetraspanin/tetraspanin interactions: role of palmitoylation. FEBS Lett. 516:139-44
    • (2002) FEBS Lett. , vol.516 , pp. 139-144
    • Charrin, S.1    Manie, S.2    Oualid, M.3    Billard, M.4    Boucheix, C.5    Rubinstein, E.6
  • 20
    • 0035896648 scopus 로고    scopus 로고
    • Evaluation of prototype TM4SF protein complexes and their relation to lipid rafts
    • Claas C, Stipp CS, Hemler ME. 2001. Evaluation of prototype TM4SF protein complexes and their relation to lipid rafts. J. Biol. Chem. 276:7974-84
    • (2001) J. Biol. Chem. , vol.276 , pp. 7974-7984
    • Claas, C.1    Stipp, C.S.2    Hemler, M.E.3
  • 21
    • 0035500912 scopus 로고    scopus 로고
    • Pgrl is a major CD81-associated protein on lymphocytes and distinguishes a new family of cell surface proteins
    • Clark KL, Zeng Z, Langford AL, Bowen SM, Todd SC. 2001. Pgrl is a major CD81-associated protein on lymphocytes and distinguishes a new family of cell surface proteins. J. Immunol. 167:5115-21
    • (2001) J. Immunol. , vol.167 , pp. 5115-5121
    • Clark, K.L.1    Zeng, Z.2    Langford, A.L.3    Bowen, S.M.4    Todd, S.C.5
  • 22
    • 0034106721 scopus 로고    scopus 로고
    • Rom-1 is required for rod photoreceptor viability and the regulation of disk morphogenesis
    • Clarke G, Goldberg AF, Vidgen D, Collins L, Ploder L, et al. 2000. Rom-1 is required for rod photoreceptor viability and the regulation of disk morphogenesis. Nat. Genet. 25:67-73
    • (2000) Nat. Genet. , vol.25 , pp. 67-73
    • Clarke, G.1    Goldberg, A.F.2    Vidgen, D.3    Collins, L.4    Ploder, L.5
  • 23
    • 0035811017 scopus 로고    scopus 로고
    • PLS1, a gene encoding a tetraspanin-like protein, is required for penetration of rice leaf by the fungal pathogen Magnaporthe grisea
    • Clergeot PH, Gourgues M, Cots J, Laurans F, Latorse MP, et al. 2001. PLS1, a gene encoding a tetraspanin-like protein, is required for penetration of rice leaf by the fungal pathogen Magnaporthe grisea. Proc. Natl. Acad. Sci. USA 98:6963-68
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 6963-6968
    • Clergeot, P.H.1    Gourgues, M.2    Cots, J.3    Laurans, F.4    Latorse, M.P.5
  • 24
    • 0026078839 scopus 로고
    • Photoreceptor peripherin is the normal product of the gene responsible for retinal degeneration in the rds mouse
    • Cornell G, Bascom R, Molday L, Reid D, McInnes RR, Molday RS. 1991. Photoreceptor peripherin is the normal product of the gene responsible for retinal degeneration in the rds mouse. Proc. Natl. Acad. Sci. USA 88: 723-26
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 723-726
    • Cornell, G.1    Bascom, R.2    Molday, L.3    Reid, D.4    McInnes, R.R.5    Molday, R.S.6
  • 26
    • 0035283345 scopus 로고    scopus 로고
    • CD81 and microglial activation in vitro: Proliferation, phagocytosis and nitric oxide production
    • Dijkstra S, Geisert EE Jr, Dijkstra CD, Bar PR, Joosten EA. 2001. CD81 and microglial activation in vitro: proliferation, phagocytosis and nitric oxide production. J. Neuroimmunol. 114:151-59
    • (2001) J. Neuroimmunol. , vol.114 , pp. 151-159
    • Dijkstra, S.1    Geisert Jr., E.E.2    Dijkstra, C.D.3    Bar, P.R.4    Joosten, E.A.5
  • 27
    • 0030931136 scopus 로고    scopus 로고
    • Dominant and digenic mutations in the peripherin/RDS and ROM1 genes in retinitis pigmentosa
    • Dryja TP, Hahn LB, Kajiwara K, Berson EL. 1997. Dominant and digenic mutations in the peripherin/RDS and ROM1 genes in retinitis pigmentosa. Invest. Ophthalmol. Vis. Sci. 38:1972-82
    • (1997) Invest. Ophthalmol. Vis. Sci. , vol.38 , pp. 1972-1982
    • Dryja, T.P.1    Hahn, L.B.2    Kajiwara, K.3    Berson, E.L.4
  • 28
    • 0032497835 scopus 로고    scopus 로고
    • Signalling functions of protein palmitoylation
    • Dunphy JT, Linder ME. 1998. Signalling functions of protein palmitoylation. Biochim. Biophys. Acta 1436:245-61
    • (1998) Biochim. Biophys. Acta , vol.1436 , pp. 245-261
    • Dunphy, J.T.1    Linder, M.E.2
  • 29
    • 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 JM, Kleijmeer MJ, Stoorvogel W, Griffith JM, Yoshie O, Geuze HJ. 1998. Selective enrichment of tetraspan proteins on the internal vesicles of multivesicular endosomes and on exosomes secreted by human B-lymphocytes. J. Biol. Chem. 273:20121-27
    • (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
  • 30
    • 0034914182 scopus 로고    scopus 로고
    • Fertilin beta and other ADAMs as integrin ligands: Insights into cell adhesion and fertilization
    • Evans JP. 2001. Fertilin beta and other ADAMs as integrin ligands: insights into cell adhesion and fertilization. BioEssays 23:628-39
    • (2001) BioEssays , vol.23 , pp. 628-639
    • Evans, J.P.1
  • 31
    • 0028958669 scopus 로고
    • The CD19/CR2/ TAPA-1 complex of B lymphocytes: Linking natural and acquired immunity
    • Fearon DT, Carter RH. 1995. The CD19/CR2/ TAPA-1 complex of B lymphocytes: linking natural and acquired immunity. Annu. Rev. Immunol. 13:127-49
    • (1995) Annu. Rev. Immunol. , vol.13 , pp. 127-149
    • Fearon, D.T.1    Carter, R.H.2
  • 32
    • 0034773236 scopus 로고    scopus 로고
    • In search of hepatitis C virus receptor(s)
    • Flint M, Quinn ER, Levy S. 2001. In search of hepatitis C virus receptor(s). Clin. Liver Dis. 5:873-93
    • (2001) Clin. Liver Dis. , vol.5 , pp. 873-893
    • Flint, M.1    Quinn, E.R.2    Levy, S.3
  • 33
    • 0037108924 scopus 로고    scopus 로고
    • Genomewide analysis of the Drosophila tetraspanins reveals a subset with similar function in the formation of the embryonic synapse
    • Fradkin LG, Kamphorst JT, DiAntonio A, Goodman CS, Noordermeer JN. 2002. Genomewide analysis of the Drosophila tetraspanins reveals a subset with similar function in the formation of the embryonic synapse. Proc. Natl. Acad. Sci. USA 99: 13663-68
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 13663-13668
    • Fradkin, L.G.1    Kamphorst, J.T.2    DiAntonio, A.3    Goodman, C.S.4    Noordermeer, J.N.5
  • 35
    • 0026537225 scopus 로고
    • Identification of membrane antigen C33 recognized by monoclonal antibodies inhibitory to human T-cell leukemia virus type 1 (HTLV-1)-induced syncytium formation: Altered glycosylation of C33 antigen in HTLV-1-positive T cells
    • Fukudome K, Furuse M, Imai T, Nishimura M, Takagi S, et al. 1992. Identification of membrane antigen C33 recognized by monoclonal antibodies inhibitory to human T-cell leukemia virus type 1 (HTLV-1)-induced syncytium formation: altered glycosylation of C33 antigen in HTLV-1-positive T cells. J. Virol. 66:1394-401
    • (1992) J. Virol. , vol.66 , pp. 1394-1401
    • Fukudome, K.1    Furuse, M.2    Imai, T.3    Nishimura, M.4    Takagi, S.5
  • 36
    • 0034923747 scopus 로고    scopus 로고
    • Pattern of expression of the tetraspanin Tspan-5 during brain development in the mouse
    • Garcia-Frigola C, Burgaya F, de Lecea L, Soriano E. 2001. Pattern of expression of the tetraspanin Tspan-5 during brain development in the mouse. Mech. Dev. 106:207-12
    • (2001) Mech. Dev. , vol.106 , pp. 207-212
    • Garcia-Frigola, C.1    Burgaya, F.2    De Lecea, L.3    Soriano, E.4
  • 37
    • 0035171135 scopus 로고    scopus 로고
    • Differential tissue expression of epitopes of the tetraspanin CD151 recognised by monoclonal antibodies
    • Geary SM, Cambareri AC, Sincock PM, Fitter S, Ashman LK. 2001. Differential tissue expression of epitopes of the tetraspanin CD151 recognised by monoclonal antibodies. Tissue Antigens 58:141-53
    • (2001) Tissue Antigens , vol.58 , pp. 141-153
    • Geary, S.M.1    Cambareri, A.C.2    Sincock, P.M.3    Fitter, S.4    Ashman, L.K.5
  • 39
    • 9444259757 scopus 로고    scopus 로고
    • Astrocyte growth, reactivity, and the target of the antiproliferative antibody, TAPA
    • Geisert EE Jr, Yang L, Irwin MH. 1996. Astrocyte growth, reactivity, and the target of the antiproliferative antibody, TAPA. J. Neurosci. 16:5478-87
    • (1996) J. Neurosci. , vol.16 , pp. 5478-5487
    • Geisert Jr., E.E.1    Yang, L.2    Irwin, M.H.3
  • 40
    • 18644384019 scopus 로고    scopus 로고
    • TM4SF2 gene involvement reconsidered in an XLMR family after neuropsychological assessment
    • Gomot M, Ronce N, Dessay S, Zemni R, Ayrault AD, et al. 2002. TM4SF2 gene involvement reconsidered in an XLMR family after neuropsychological assessment. Am. J. Med. Genet. 112:400-4
    • (2002) Am. J. Med. Genet. , vol.112 , pp. 400-404
    • Gomot, M.1    Ronce, N.2    Dessay, S.3    Zemni, R.4    Ayrault, A.D.5
  • 42
    • 0035969998 scopus 로고    scopus 로고
    • Polar side chains drive the association of model transmembrane peptides
    • Gratkowski H, Lear JD, DeGrado WF. 2001. Polar side chains drive the association of model transmembrane peptides. Proc. Natl. Acad. Sci. USA 98:880-85
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 880-885
    • Gratkowski, H.1    Lear, J.D.2    DeGrado, W.F.3
  • 43
    • 0347297508 scopus 로고    scopus 로고
    • A functionally relevant conformational epitope on the CD9 tetraspanin depends on the association with activated beta1 integrin
    • Gutierrez-Lopez MD, Ovalle S, Yánez-Mó M, Sanchez-Sanchez N, Rubinstein E, et al. 2003. A functionally relevant conformational epitope on the CD9 tetraspanin depends on the association with activated beta1 integrin. J. Biol. Chem. 278:208-18
    • (2003) J. Biol. Chem. , vol.278 , pp. 208-218
    • Gutierrez-Lopez, M.D.1    Ovalle, S.2    Yánez-Mó, M.3    Sanchez-Sanchez, N.4    Rubinstein, E.5
  • 45
    • 0031720629 scopus 로고    scopus 로고
    • Integrin-associated proteins
    • Hemler ME. 1998. Integrin-associated proteins. Curr. Opin. Cell Biol. 10:578-85
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 578-585
    • Hemler, M.E.1
  • 46
    • 0035945363 scopus 로고    scopus 로고
    • Specific tetraspanin functions
    • Hemler ME. 2001. Specific tetraspanin functions. J. Cell Biol. 155:1103-7
    • (2001) J. Cell Biol. , vol.155 , pp. 1103-1107
    • Hemler, M.E.1
  • 47
    • 0025298280 scopus 로고
    • Purification and partial characterization of CD9 antigen of human platelets
    • Higashihara M, Takahata K, Yatomi Y, Nakahara K, Kurokawa K. 1990. Purification and partial characterization of CD9 antigen of human platelets. FEBS Lett. 264:270-74
    • (1990) FEBS Lett. , vol.264 , pp. 270-274
    • Higashihara, M.1    Takahata, K.2    Yatomi, Y.3    Nakahara, K.4    Kurokawa, K.5
  • 48
    • 0028963636 scopus 로고
    • The membrane protein CD9/DRAP27 potentiates the juxtacrine growth factor activity of the membrane-anchored heparin-binding EGF-like growth factor
    • Higashiyama S, Iwamoto R, Goishi K, Raab G, Taniguchi N, et al. 1995. The membrane protein CD9/DRAP27 potentiates the juxtacrine growth factor activity of the membrane-anchored heparin-binding EGF-like growth factor. J. Cell Biol. 128:929-38
    • (1995) J. Cell Biol. , vol.128 , pp. 929-938
    • Higashiyama, S.1    Iwamoto, R.2    Goishi, K.3    Raab, G.4    Taniguchi, N.5
  • 49
    • 18844463856 scopus 로고    scopus 로고
    • Identification of amino acid residues in CD81 critical for interaction with hepatitis C virus envelope glycoprotein E2
    • Higginbottom A, Quinn ER, Kuo CC, Flint M, Wilson LH, et al. 2000. Identification of amino acid residues in CD81 critical for interaction with hepatitis C virus envelope glycoprotein E2. J. Virol. 74:3642-49
    • (2000) J. Virol. , vol.74 , pp. 3642-3649
    • Higginbottom, A.1    Quinn, E.R.2    Kuo, C.C.3    Flint, M.4    Wilson, L.H.5
  • 51
    • 0032720373 scopus 로고    scopus 로고
    • Molecular cloning of a cDNA encoding mouse A15, a member of the transmembrane 4 superfamily, and its preferential expression in brain neurons
    • Hosokawa Y, Ueyama E, Morikawa Y, Maeda Y, Seto M, Senba E. 1999. Molecular cloning of a cDNA encoding mouse A15, a member of the transmembrane 4 superfamily, and its preferential expression in brain neurons. Neurosci. Res. 35:281-90
    • (1999) Neurosci. Res. , vol.35 , pp. 281-290
    • Hosokawa, Y.1    Ueyama, E.2    Morikawa, Y.3    Maeda, Y.4    Seto, M.5    Senba, E.6
  • 52
    • 0023898289 scopus 로고
    • Molecular cloning and characterization of an antigen associated with early stages of melanoma tumor progression
    • Hotta H, Ross AH, Huebner K, Isobe M, Wendeborn S, et al. 1988. Molecular cloning and characterization of an antigen associated with early stages of melanoma tumor progression. Cancer Res. 48:2955-62
    • (1988) Cancer Res. , vol.48 , pp. 2955-2962
    • Hotta, H.1    Ross, A.H.2    Huebner, K.3    Isobe, M.4    Wendeborn, S.5
  • 53
    • 0034722328 scopus 로고    scopus 로고
    • Ablation of uroplakin III gene results in small urothelial plaques, urothelial leakage, and vesicoureteral reflux
    • Hu P, Deng FM, Liang FX, Hu CM, Auerbach AB, et al. 2000. Ablation of uroplakin III gene results in small urothelial plaques, urothelial leakage, and vesicoureteral reflux. J. Cell Biol. 151:961-72
    • (2000) J. Cell Biol. , vol.151 , pp. 961-972
    • Hu, P.1    Deng, F.M.2    Liang, F.X.3    Hu, C.M.4    Auerbach, A.B.5
  • 54
    • 0030974057 scopus 로고    scopus 로고
    • Possible role of coexpression of CD9 with membrane-anchored heparin-binding EGF-like growth factor and amphiregulin in cultured human keratinocyte growth
    • Inui S, Higashiyama S, Hashimoto K, Higashiyama M, Yoshikawa K, Taniguchi N. 1997. Possible role of coexpression of CD9 with membrane-anchored heparin-binding EGF-like growth factor and amphiregulin in cultured human keratinocyte growth. J. Cell Physiol. 171:291-98
    • (1997) J. Cell Physiol. , vol.171 , pp. 291-298
    • Inui, S.1    Higashiyama, S.2    Hashimoto, K.3    Higashiyama, M.4    Yoshikawa, K.5    Taniguchi, N.6
  • 55
    • 0028284810 scopus 로고
    • Heparin-binding EGF-like growth factor, which acts as a diphtheria toxin receptor, forms a complex with membrane protein DRAP27/CD9, which upregulates functional receptors and diphtheria toxin sensitivity
    • Iwamoto R, Higashiyama S, Mitamura T, Taniguchi N, Klagsbrun M, Mekada E. 1994. Heparin-binding EGF-like growth factor, which acts as a diphtheria toxin receptor, forms a complex with membrane protein DRAP27/CD9, which upregulates functional receptors and diphtheria toxin sensitivity. EMBO J. 13:2322-30
    • (1994) EMBO J. , vol.13 , pp. 2322-2330
    • Iwamoto, R.1    Higashiyama, S.2    Mitamura, T.3    Taniguchi, N.4    Klagsbrun, M.5    Mekada, E.6
  • 56
    • 0033556282 scopus 로고    scopus 로고
    • Three-dimensional analysis of the 16-nm urothelial plaque particle: Luminal surface exposure, preferential head-to-head interaction, and hinge formation
    • Kachar B, Liang F, Lins U, Ding M, Wu XR, et al. 1999. Three-dimensional analysis of the 16-nm urothelial plaque particle: luminal surface exposure, preferential head-to-head interaction, and hinge formation. J. Mol. Biol. 285:595-608
    • (1999) J. Mol. Biol. , vol.285 , pp. 595-608
    • Kachar, B.1    Liang, F.2    Lins, U.3    Ding, M.4    Wu, X.R.5
  • 57
    • 0036302083 scopus 로고    scopus 로고
    • Infertility of CD9-deficient mouse eggs is reversed by mouse CD9, human CD9, or mouse CD81; Polyadenylated mRNA injection developed for molecular analysis of sperm-egg fusion
    • Kaji K, Oda S, Miyazaki S, Kudo A. 2002. Infertility of CD9-deficient mouse eggs is reversed by mouse CD9, human CD9, or mouse CD81; Polyadenylated mRNA injection developed for molecular analysis of sperm-egg fusion. Dev. Biol. 247:327-34
    • (2002) Dev. Biol. , vol.247 , pp. 327-334
    • Kaji, K.1    Oda, S.2    Miyazaki, S.3    Kudo, A.4
  • 58
    • 0034091646 scopus 로고    scopus 로고
    • The gamete fusion process is defective in eggs of Cd9-deficient mice
    • Kaji K, Oda S, Shikano T, Ohnuki T, Uematsu Y, et al. 2000. The gamete fusion process is defective in eggs of Cd9-deficient mice. Nat. Genet. 24:279-82
    • (2000) Nat. Genet. , vol.24 , pp. 279-282
    • Kaji, K.1    Oda, S.2    Shikano, T.3    Ohnuki, T.4    Uematsu, Y.5
  • 59
    • 0028245437 scopus 로고
    • Digenic retinitis pigmentosa due to mutations at the unlinked peripherin/RDS and ROM1 loci
    • Kajiwara K, Berson EL, Dryja TP. 1994. Digenic retinitis pigmentosa due to mutations at the unlinked peripherin/RDS and ROM1 loci. Science 264:1604-8
    • (1994) Science , vol.264 , pp. 1604-1608
    • Kajiwara, K.1    Berson, E.L.2    Dryja, T.P.3
  • 60
    • 0036735322 scopus 로고    scopus 로고
    • CD9 expression in solid non-neuroepithelial tumors and infiltrative astrocytic tumors
    • Kawashima M, Doh-ura K, Mekada E, Fukui M, Iwaki T. 2002. CD9 expression in solid non-neuroepithelial tumors and infiltrative astrocytic tumors. J. Histochem. Cytochem. 50:1195-203
    • (2002) J. Histochem. Cytochem. , vol.50 , pp. 1195-1203
    • Kawashima, M.1    Doh-ura, K.2    Mekada, E.3    Fukui, M.4    Iwaki, T.5
  • 61
    • 0037144837 scopus 로고    scopus 로고
    • An extracellular site on tetraspanin CD151 determines α3 and α6 integrin-dependent cellular morphology
    • Kazarov AR, Yang X, Stipp CS, Sehgal B, Hemler ME. 2002. An extracellular site on tetraspanin CD151 determines α3 and α6 integrin-dependent cellular morphology. J. Cell Biol. 158:1299-309
    • (2002) J. Cell Biol. , vol.158 , pp. 1299-1309
    • Kazarov, A.R.1    Yang, X.2    Stipp, C.S.3    Sehgal, B.4    Hemler, M.E.5
  • 63
    • 0035862964 scopus 로고    scopus 로고
    • CD81 extracellular domain 3D structure: Insight into the tetraspanin superfamily structural motifs
    • Kitadokoro K, Bordo D, Galli G, Petracca R, Falugi F, et al. 2001. CD81 extracellular domain 3D structure: insight into the tetraspanin superfamily structural motifs. EMBO J. 20:12-18
    • (2001) EMBO J. , vol.20 , pp. 12-18
    • Kitadokoro, K.1    Bordo, D.2    Galli, G.3    Petracca, R.4    Falugi, F.5
  • 64
    • 0036755086 scopus 로고    scopus 로고
    • Subunit association and conformational flexibility in the head sub-domain of human CD81 large extracellular loop
    • Kitadokoro K, Ponassi M, Galli G, Petracca R, Falugi F, et al. 2002. Subunit association and conformational flexibility in the head sub-domain of human CD81 large extracellular loop. Biol. Chem. 383:1447-52
    • (2002) Biol. Chem. , vol.383 , pp. 1447-1452
    • Kitadokoro, K.1    Ponassi, M.2    Galli, G.3    Petracca, R.4    Falugi, F.5
  • 65
    • 0033910657 scopus 로고    scopus 로고
    • Targeted inactivation of the tetraspanin CD37 impairs T-cell-dependent B-cell response under sub-optimal costimulatory conditions
    • Knobeloch KP, Wright MD, Ochsenbein AF, Liesenfeld O, Lohler J, et al. 2000. Targeted inactivation of the tetraspanin CD37 impairs T-cell-dependent B-cell response under sub-optimal costimulatory conditions. Mol. Cell. Biol. 20:5363-69
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 5363-5369
    • Knobeloch, K.P.1    Wright, M.D.2    Ochsenbein, A.F.3    Liesenfeld, O.4    Lohler, J.5
  • 67
    • 0029988151 scopus 로고    scopus 로고
    • A neural tetraspanin, encoded by late bloomer, that facilitates synapse formation
    • Kopczynski CC, Davis GW, Goodman CS. 1996. A neural tetraspanin, encoded by late bloomer, that facilitates synapse formation. Science 271:1867-70
    • (1996) Science , vol.271 , pp. 1867-1870
    • Kopczynski, C.C.1    Davis, G.W.2    Goodman, C.S.3
  • 68
    • 0036144745 scopus 로고    scopus 로고
    • Tetraspan microdomains distinct from lipid rafts enrich select peptide-MHC class II complexes
    • Kropshofer H, Spindeldreher S, Rohn TA, Platania N, Grygar C, et al. 2002. Tetraspan microdomains distinct from lipid rafts enrich select peptide-MHC class II complexes. Nat. Immunol. 3:61-68
    • (2002) Nat. Immunol. , vol.3 , pp. 61-68
    • Kropshofer, H.1    Spindeldreher, S.2    Rohn, T.A.3    Platania, N.4    Grygar, C.5
  • 69
    • 0031045464 scopus 로고    scopus 로고
    • Genomic structure and promoter analysis of the gene encoding MM3, a member of transmembrane 4 superfamily
    • Kurihara T, Kataoka K, Hong D, Shioda S, Sugano S, et al. 1997. Genomic structure and promoter analysis of the gene encoding MM3, a member of transmembrane 4 superfamily. Gene 185:277-83
    • (1997) Gene , vol.185 , pp. 277-283
    • Kurihara, T.1    Kataoka, K.2    Hong, D.3    Shioda, S.4    Sugano, S.5
  • 70
    • 0036169066 scopus 로고    scopus 로고
    • Molecular assembly of CD46 with CD9, alpha3-beta1 integrin and protein tyrosine phosphatase SHP-1 in human macrophages through differentiation by GM-CSF
    • Kurita-Taniguchi M, Hazeki K, Murabayashi N, Fukui A, Tsuji S, et al. 2002. Molecular assembly of CD46 with CD9, alpha3-beta1 integrin and protein tyrosine phosphatase SHP-1 in human macrophages through differentiation by GM-CSF. Mol. Immunol. 38:689-700
    • (2002) Mol. Immunol. , vol.38 , pp. 689-700
    • Kurita-Taniguchi, M.1    Hazeki, K.2    Murabayashi, N.3    Fukui, A.4    Tsuji, S.5
  • 71
    • 0031573837 scopus 로고    scopus 로고
    • Functional analysis of four tetraspans, CD9, CD53, CD81, and CD82, suggests a common role in costimulation, cell adhesion, and migration: Only CD9 upregulates HB-EGF activity
    • Lagaudriere-Gesbert C, Le Naour F, Lebel-Binay S, Billard M, Lemichez E, et al. 1997. Functional analysis of four tetraspans, CD9, CD53, CD81, and CD82, suggests a common role in costimulation, cell adhesion, and migration: only CD9 upregulates HB-EGF activity. Cell. Immunol. 182:105-12
    • (1997) Cell. Immunol. , vol.182 , pp. 105-112
    • Lagaudriere-Gesbert, C.1    Le Naour, F.2    Lebel-Binay, S.3    Billard, M.4    Lemichez, E.5
  • 75
    • 0031895778 scopus 로고    scopus 로고
    • CD81 (TAPA-1): A molecule involved in signal transduction and cell adhesion in the immune system
    • Levy S, Todd SC, Maecker HT. 1998. CD81 (TAPA-1): a molecule involved in signal transduction and cell adhesion in the immune system. Annu. Rev. Immunol. 16:89-109
    • (1998) Annu. Rev. Immunol. , vol.16 , pp. 89-109
    • Levy, S.1    Todd, S.C.2    Maecker, H.T.3
  • 76
    • 0035310999 scopus 로고    scopus 로고
    • Organization of uroplakin subunits: Transmembrane topology, pair formation and plaque composition
    • Liang FX, Riedel I, Deng FM, Zhou G, Xu C, et al. 2001. Organization of uroplakin subunits: transmembrane topology, pair formation and plaque composition. Biochem. J. 355:13-18
    • (2001) Biochem. J. , vol.355 , pp. 13-18
    • Liang, F.X.1    Riedel, I.2    Deng, F.M.3    Zhou, G.4    Xu, C.5
  • 77
    • 0034052943 scopus 로고    scopus 로고
    • Disulfide-mediated oligomerization of peripherin/Rds and Rom-1 in photoreceptor disk membranes. Implications for photoreceptor outer segment morphogenesis and degeneration
    • Loewen CJ, Molday RS. 2000. Disulfide-mediated oligomerization of peripherin/Rds and Rom-1 in photoreceptor disk membranes. Implications for photoreceptor outer segment morphogenesis and degeneration. J. Biol. Chem. 275:5370-78
    • (2000) J. Biol. Chem. , vol.275 , pp. 5370-5378
    • Loewen, C.J.1    Molday, R.S.2
  • 78
    • 0037031839 scopus 로고    scopus 로고
    • Chinese hamster ovary cell motility to fibronectin is modulated by the second extracellular loop of CD9. Identification of a putative fibronectin binding site
    • Longhurst CM, Jacobs JD, White MM, Crossno JT Jr, Fitzgerald DA, et al. 2002. Chinese hamster ovary cell motility to fibronectin is modulated by the second extracellular loop of CD9. Identification of a putative fibronectin binding site. J. Biol. Chem. 277:32445-52
    • (2002) J. Biol. Chem. , vol.277 , pp. 32445-32452
    • Longhurst, C.M.1    Jacobs, J.D.2    White, M.M.3    Crossno Jr., J.T.4    Fitzgerald, D.A.5
  • 79
    • 0030948267 scopus 로고    scopus 로고
    • Normal lymphocyte development but delayed humoral immune response in CD81-null mice
    • Maecker HT, Levy S. 1997. Normal lymphocyte development but delayed humoral immune response in CD81-null mice. J. Exp. Med. 185:1505-10
    • (1997) J. Exp. Med. , vol.185 , pp. 1505-1510
    • Maecker, H.T.1    Levy, S.2
  • 80
    • 0030947554 scopus 로고    scopus 로고
    • The tetraspanin superfamily: Molecular facilitators
    • Maecker HT, Todd SC, Levy S. 1997. The tetraspanin superfamily: molecular facilitators. FASEB J. 11:428-42
    • (1997) FASEB J. , vol.11 , pp. 428-442
    • Maecker, H.T.1    Todd, S.C.2    Levy, S.3
  • 81
    • 0036682475 scopus 로고    scopus 로고
    • Stomatin is a major lipid-raft component of platelet alpha granules
    • Mairhofer M, Steiner M, Mosgoeller W, Prohaska R, Salzer U. 2002. Stomatin is a major lipid-raft component of platelet alpha granules. Blood 100:897-904
    • (2002) Blood , vol.100 , pp. 897-904
    • Mairhofer, M.1    Steiner, M.2    Mosgoeller, W.3    Prohaska, R.4    Salzer, U.5
  • 82
    • 0035869540 scopus 로고    scopus 로고
    • CD36 associates with CD9 and integrins on human blood platelets
    • Miao WM, Vasile E, Lane WS, Lawler J. 2001. CD36 associates with CD9 and integrins on human blood platelets. Blood 97:1689-96
    • (2001) Blood , vol.97 , pp. 1689-1696
    • Miao, W.M.1    Vasile, E.2    Lane, W.S.3    Lawler, J.4
  • 83
    • 0034640885 scopus 로고    scopus 로고
    • Normal fertilization occurs with eggs lacking the integrin alpha6beta1 and is CD9-dependent
    • Miller BJ, Georges-Labouesse E, Primakoff P, Myles DG. 2000. Normal fertilization occurs with eggs lacking the integrin alpha6beta1 and is CD9-dependent. J. Cell Biol. 149:1289-96
    • (2000) J. Cell Biol. , vol.149 , pp. 1289-1296
    • Miller, B.J.1    Georges-Labouesse, E.2    Primakoff, P.3    Myles, D.G.4
  • 84
    • 0036290481 scopus 로고    scopus 로고
    • Localization of uroplakin Ia, the urothelial receptor for bacterial adhesin FimH, on the six inner domains of the 16-nm urothelial plaque particle
    • Min G, Stolz M, Zhou G, Liang F, Sebbel P, et al. 2002. Localization of uroplakin Ia, the urothelial receptor for bacterial adhesin FimH, on the six inner domains of the 16-nm urothelial plaque particle. J. Mol. Biol. 317: 697-706
    • (2002) J. Mol. Biol. , vol.317 , pp. 697-706
    • Min, G.1    Stolz, M.2    Zhou, G.3    Liang, F.4    Sebbel, P.5
  • 85
    • 0037114132 scopus 로고    scopus 로고
    • Cutting edge: Dynamic redistribution of tetraspanin CD81 at the central zone of the immune synapse in both T lymphocytes and APC
    • Mittelbrunn M, Yánez-Mó M, Sancho D, Ursa A, Sanchez-Madrid F. 2002. Cutting edge: Dynamic redistribution of tetraspanin CD81 at the central zone of the immune synapse in both T lymphocytes and APC. J. Immunol. 169:6691-95
    • (2002) J. Immunol. , vol.169 , pp. 6691-6695
    • Mittelbrunn, M.1    Yánez-Mó, M.2    Sancho, D.3    Ursa, A.4    Sanchez-Madrid, F.5
  • 86
    • 0033958932 scopus 로고    scopus 로고
    • Requirement of CD9 on the egg plasma membrane for fertilization
    • Miyado K, Yamada G, Yamada S, Hasuwa H, Nakamura Y, et al. 2000. Requirement of CD9 on the egg plasma membrane for fertilization. Science 287:321-24
    • (2000) Science , vol.287 , pp. 321-324
    • Miyado, K.1    Yamada, G.2    Yamada, S.3    Hasuwa, H.4    Nakamura, Y.5
  • 87
    • 0343052739 scopus 로고    scopus 로고
    • Normal development but differentially altered proliferative responses of lymphocytes in mice lacking CD81
    • Miyazaki T, Muller U, Campbell KS. 1997. Normal development but differentially altered proliferative responses of lymphocytes in mice lacking CD81. EMBO J. 16:4217-25
    • (1997) EMBO J. , vol.16 , pp. 4217-4225
    • Miyazaki, T.1    Muller, U.2    Campbell, K.S.3
  • 88
    • 0031049748 scopus 로고    scopus 로고
    • Why did the sperm cross the cumulus? To get to the oocyte. Functions of the sperm surface proteins PH-20 and fertilin in arriving at, and fusing with, the egg
    • Myles DG, Primakoff P. 1997. Why did the sperm cross the cumulus? To get to the oocyte. Functions of the sperm surface proteins PH-20 and fertilin in arriving at, and fusing with, the egg. Biol. Reprod. 56:320-27
    • (1997) Biol. Reprod. , vol.56 , pp. 320-327
    • Myles, D.G.1    Primakoff, P.2
  • 89
    • 0034674432 scopus 로고    scopus 로고
    • Importance of the major extracellular domain of CD9 and the epidermal growth factor (EGF)-like domain of heparin-binding EGF-like growth factor for up-regulation of binding and activity
    • Nakamura K, Mitamura T, Takahashi T, Kobayashi T, Mekada E. 2000. Importance of the major extracellular domain of CD9 and the epidermal growth factor (EGF)-like domain of heparin-binding EGF-like growth factor for up-regulation of binding and activity. J. Biol. Chem. 275:18284-90
    • (2000) J. Biol. Chem. , vol.275 , pp. 18284-18290
    • Nakamura, K.1    Mitamura, T.2    Takahashi, T.3    Kobayashi, T.4    Mekada, E.5
  • 91
    • 0034710619 scopus 로고    scopus 로고
    • Attenuation of EGF receptor signaling by a metastasis suppressor, the tetraspanin CD82/KAI-1
    • Odintsova E, Sugiura T, Berditchevski F. 2000. Attenuation of EGF receptor signaling by a metastasis suppressor, the tetraspanin CD82/KAI-1. Curr. Biol. 10:1009-12
    • (2000) Curr. Biol. , vol.10 , pp. 1009-1012
    • Odintsova, E.1    Sugiura, T.2    Berditchevski, F.3
  • 92
    • 0035967503 scopus 로고    scopus 로고
    • GM3 ganglioside inhibits CD9-facilitated haptotactic cell motility: Coexpression of GM3 and CD9 is essential in the downregulation of tumor cell motility and malignancy
    • Ono M, Handa K, Sonnino S, Withers DA, Nagai H, Hakomori S. 2001. GM3 ganglioside inhibits CD9-facilitated haptotactic cell motility: coexpression of GM3 and CD9 is essential in the downregulation of tumor cell motility and malignancy. Biochemistry 40:6414-21
    • (2001) Biochemistry , vol.40 , pp. 6414-6421
    • Ono, M.1    Handa, K.2    Sonnino, S.3    Withers, D.A.4    Nagai, H.5    Hakomori, S.6
  • 93
    • 0035940960 scopus 로고    scopus 로고
    • Structure of the major membrane protein complex from urinary bladder epithelial cells by cryo-electron crystallography
    • Oostergetel GT, Keegstra W, Brisson A. 2001. Structure of the major membrane protein complex from urinary bladder epithelial cells by cryo-electron crystallography. J. Mol. Biol. 314:245-52
    • (2001) J. Mol. Biol. , vol.314 , pp. 245-252
    • Oostergetel, G.T.1    Keegstra, W.2    Brisson, A.3
  • 94
    • 0025284826 scopus 로고
    • TAPA-1, the target of an antiproliferative antibody, defines a new family of transmembrane proteins
    • Oren R, Takahashi S, Doss C, Levy R, Levy S. 1990. TAPA-1, the target of an antiproliferative antibody, defines a new family of transmembrane proteins. Mol. Cell. Biol. 10: 4007-15
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 4007-4015
    • Oren, R.1    Takahashi, S.2    Doss, C.3    Levy, R.4    Levy, S.5
  • 95
    • 0034772748 scopus 로고    scopus 로고
    • Phosphoinositides as key regulators of synaptic function
    • Osborne SL, Meunier FA, Schiavo G. 2001. Phosphoinositides as key regulators of synaptic function. Neuron 32:9-12
    • (2001) Neuron , vol.32 , pp. 9-12
    • Osborne, S.L.1    Meunier, F.A.2    Schiavo, G.3
  • 96
    • 0032748306 scopus 로고    scopus 로고
    • Tetraspanins expressed in the embryonic chick nervous system
    • Perron JC, Bixby JL. 1999. Tetraspanins expressed in the embryonic chick nervous system. FEBS Lett. 461:86-90
    • (1999) FEBS Lett. , vol.461 , pp. 86-90
    • Perron, J.C.1    Bixby, J.L.2
  • 98
    • 0032875098 scopus 로고    scopus 로고
    • Fatty acylation of proteins: New insights into membrane targeting of myristoylated and palmitoylated proteins
    • Resh MD. 1999. Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins. Biochim. Biophys. Acta 1451:1-16
    • (1999) Biochim. Biophys. Acta , vol.1451 , pp. 1-16
    • Resh, M.D.1
  • 99
    • 0029064680 scopus 로고
    • Impairment of T-cell-dependent B-cell responses and B-1 cell development in CD19-deficient mice
    • Rickert RC, Rajewsky K, Roes J. 1995. Impairment of T-cell-dependent B-cell responses and B-1 cell development in CD19-deficient mice. Nature 376:352-55
    • (1995) Nature , vol.376 , pp. 352-355
    • Rickert, R.C.1    Rajewsky, K.2    Roes, J.3
  • 100
    • 0035846450 scopus 로고    scopus 로고
    • Molecular characterisation of mouse and human TSSC6: Evidence that TSSC6 is a genuine member of the tetraspanin superfamily and is expressed specifically in haematopoietic organs
    • Robb L, Tarrant J, Groom J, Ibrahim M, Li R, et al. 2001. Molecular characterisation of mouse and human TSSC6: evidence that TSSC6 is a genuine member of the tetraspanin superfamily and is expressed specifically in haematopoietic organs. Biochim. Biophys. Acta 1522(1):31-41
    • (2001) Biochim. Biophys. Acta , vol.1522 , Issue.1 , pp. 31-41
    • Robb, L.1    Tarrant, J.2    Groom, J.3    Ibrahim, M.4    Li, R.5
  • 101
    • 0029558617 scopus 로고
    • The CD19 signal transduction molecule is a response regulator of B-lymphocyte differentiation
    • Sato S, Steeber DA, Tedder TF. 1995. The CD19 signal transduction molecule is a response regulator of B-lymphocyte differentiation. Proc. Natl. Acad. Sci. USA 92:11558-62
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 11558-11562
    • Sato, S.1    Steeber, D.A.2    Tedder, T.F.3
  • 102
    • 0030021514 scopus 로고    scopus 로고
    • CD9 of mouse brain is implicated in neurite outgrowth and cell migration in vitro and is associated with the α6/β1 integrin and the neural adhesion molecule L1
    • Schmidt C, Künemund V, Wintergerst ES, Schmitz B, Schachner M. 1996. CD9 of mouse brain is implicated in neurite outgrowth and cell migration in vitro and is associated with the α6/β1 integrin and the neural adhesion molecule L1. J. Neurosci. Res. 43:12-31
    • (1996) J. Neurosci. Res. , vol.43 , pp. 12-31
    • Schmidt, C.1    Künemund, V.2    Wintergerst, E.S.3    Schmitz, B.4    Schachner, M.5
  • 103
    • 0035955657 scopus 로고    scopus 로고
    • Structure of the tetraspanin main extracellular domain. A partially conserved fold with a structurally variable domain insertion
    • Seigneuret M, Delaguillaumie A, Lagaudriere-Gesbert C, Conjeaud H. 2001. Structure of the tetraspanin main extracellular domain. A partially conserved fold with a structurally variable domain insertion. J. Biol. Chem. 276:40055-64
    • (2001) J. Biol. Chem. , vol.276 , pp. 40055-40064
    • Seigneuret, M.1    Delaguillaumie, A.2    Lagaudriere-Gesbert, C.3    Conjeaud, H.4
  • 104
    • 0033563224 scopus 로고    scopus 로고
    • Selective tetraspan-integrin complexes (CD81/alpha4beta1, CD151/ alpha3beta1, CD151/alpha6beta1) under conditions disrupting tetraspan interactions
    • Serru V, Le Naour F, Billard M, Azorsa DO, Lanza F, et al. 1999. Selective tetraspan-integrin complexes (CD81/alpha4beta1, CD151/ alpha3beta1, CD151/alpha6beta1) under conditions disrupting tetraspan interactions. Biochem. J. 340(Pt. 1): 103-11
    • (1999) Biochem. J. , vol.340 , Issue.1 PART , pp. 103-111
    • Serru, V.1    Le Naour, F.2    Billard, M.3    Azorsa, D.O.4    Lanza, F.5
  • 105
    • 0034614938 scopus 로고    scopus 로고
    • The tetraspanin CD9 associates with transmembrane TGF-alpha and regulates TGF-alpha-induced EGF receptor activation and cell proliferation
    • Shi W, Fan H, Shum L, Derynck R. 2000. The tetraspanin CD9 associates with transmembrane TGF-alpha and regulates TGF-alpha-induced EGF receptor activation and cell proliferation. J. Cell Biol. 148:591-602
    • (2000) J. Cell Biol. , vol.148 , pp. 591-602
    • Shi, W.1    Fan, H.2    Shum, L.3    Derynck, R.4
  • 106
    • 0037234454 scopus 로고    scopus 로고
    • Hepatocyte CD81 is required for Plasmodium falciparum and Plasmodium yoelii sporozoite infectivity
    • Silvie O, Rubinstein E, Franetich JF, Prenant M, Belnoue E, et al. 2003. Hepatocyte CD81 is required for Plasmodium falciparum and Plasmodium yoelii sporozoite infectivity. Nat. Med. 9:93-96
    • (2003) Nat. Med. , vol.9 , pp. 93-96
    • Silvie, O.1    Rubinstein, E.2    Franetich, J.F.3    Prenant, M.4    Belnoue, E.5
  • 107
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K, Ikonen E. 1997. Functional rafts in cell membranes. Nature 387:569-72
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 108
    • 0032948124 scopus 로고    scopus 로고
    • PETA-3/CD151, a member of the transmembrane 4 superfamily, is localised to the plasma membrane and endocytic system of endothelial cells, associates with multiple integrins and modulates cell function
    • Sincock PM, Fitter S, Parton RG, Berndt MC, Gamble JR, Ashman LK. 1999. PETA-3/CD151, a member of the transmembrane 4 superfamily, is localised to the plasma membrane and endocytic system of endothelial cells, associates with multiple integrins and modulates cell function. J. Cell Sci. 112:833-44
    • (1999) J. Cell Sci. , vol.112 , pp. 833-844
    • Sincock, P.M.1    Fitter, S.2    Parton, R.G.3    Berndt, M.C.4    Gamble, J.R.5    Ashman, L.K.6
  • 109
    • 0030975429 scopus 로고    scopus 로고
    • Localization of the transmembrane 4 superfamily (TM4SF) member PETA-3 (CD151) in normal human tissues - Comparison with CD9, CD63, and α5β1 integrin
    • Sincock PM, Mayrohofer G, Ashman LK. 1997. Localization of the transmembrane 4 superfamily (TM4SF) member PETA-3 (CD151) in normal human tissues - comparison with CD9, CD63, and α5β1 integrin. J. Histochem. Cytochem. 45:515-25
    • (1997) J. Histochem. Cytochem. , vol.45 , pp. 515-525
    • Sincock, P.M.1    Mayrohofer, G.2    Ashman, L.K.3
  • 110
    • 0030587912 scopus 로고    scopus 로고
    • CD63 associates with tyrosine kinase activity and CD11/CD18, and transmits an activation signal in neutrophils
    • Skubitz KM, Campbell KD, Iida J, Skubitz APN. 1996. CD63 associates with tyrosine kinase activity and CD11/CD18, and transmits an activation signal in neutrophils. J. Immunol. 157:3617-26
    • (1996) J. Immunol. , vol.157 , pp. 3617-3626
    • Skubitz, K.M.1    Campbell, K.D.2    Iida, J.3    Skubitz, A.P.N.4
  • 111
    • 0037331586 scopus 로고    scopus 로고
    • T cell costimulation by hepatitis C virus envelope protein E2 binding to CD81 is mediated by Lck
    • Soldaini E, Wack A, D'Oro U, Nuti S, Ulivieri C, et al. 2003. T cell costimulation by hepatitis C virus envelope protein E2 binding to CD81 is mediated by Lck. Eur. J. Immunol. 33:455-64
    • (2003) Eur. J. Immunol. , vol.33 , pp. 455-464
    • Soldaini, E.1    Wack, A.2    D'Oro, U.3    Nuti, S.4    Ulivieri, C.5
  • 112
    • 0034658462 scopus 로고    scopus 로고
    • The tetraspan molecule CD151, a novel constituent of hemidesmosomes, associates with the integrin alpha6beta4 and may regulate the spatial organization of hemidesmosomes
    • Sterk LM, Geuijen CA, Oomen LC, Calafat J, Janssen H, Sonnenberg A. 2000. The tetraspan molecule CD151, a novel constituent of hemidesmosomes, associates with the integrin alpha6beta4 and may regulate the spatial organization of hemidesmosomes. J. Cell Biol. 149:969-82
    • (2000) J. Cell Biol. , vol.149 , pp. 969-982
    • Sterk, L.M.1    Geuijen, C.A.2    Oomen, L.C.3    Calafat, J.4    Janssen, H.5    Sonnenberg, A.6
  • 113
    • 0037087710 scopus 로고    scopus 로고
    • Association of the tetraspanin CD151 with the laminin-binding integrins alpha3beta1, alpha6beta1, alpha6beta4 and alpha7beta1 in cells in culture and in vivo
    • Sterk LM, Geuijen CA, van den Berg JG, Claessen N, Weening JJ, Sonnenberg A. 2002. Association of the tetraspanin CD151 with the laminin-binding integrins alpha3beta1, alpha6beta1, alpha6beta4 and alpha7beta1 in cells in culture and in vivo. J. Cell Sci. 115:1161-73
    • (2002) J. Cell Sci. , vol.115 , pp. 1161-1173
    • Sterk, L.M.1    Geuijen, C.A.2    Van Den Berg, J.G.3    Claessen, N.4    Weening, J.J.5    Sonnenberg, A.6
  • 114
    • 0034049945 scopus 로고    scopus 로고
    • Transmembrane-4-superfamily proteins CD151 and CD81 associate with α3β1 integrin, and selectively contribute to α3β1- dependent neunte outgrowth
    • Stipp CS, Hemler ME. 2000. Transmembrane-4-superfamily proteins CD151 and CD81 associate with α3β1 integrin, and selectively contribute to α3β1-dependent neunte outgrowth. J. Cell Sci. 113:1871-82
    • (2000) J. Cell Sci. , vol.113 , pp. 1871-1882
    • Stipp, C.S.1    Hemler, M.E.2
  • 115
    • 0035798537 scopus 로고    scopus 로고
    • EWI-2 is a major CD9 and CD81 partner, and member of a novel Ig protein subfamily
    • Stipp CS, Kolesnikova TV, Hemler ME. 2001a. EWI-2 is a major CD9 and CD81 partner, and member of a novel Ig protein subfamily. J. Biol. Chem. 276:40545-54
    • (2001) J. Biol. Chem. , vol.276 , pp. 40545-40554
    • Stipp, C.S.1    Kolesnikova, T.V.2    Hemler, M.E.3
  • 117
    • 0035895876 scopus 로고    scopus 로고
    • FPRP: A major, highly stoichiometric, highly specific CD81 and CD9-associated protein
    • Stipp CS, Orlicky D, Hemler ME. 2001b. FPRP: A major, highly stoichiometric, highly specific CD81 and CD9-associated protein. J. Biol. Chem. 276:4853-62
    • (2001) J. Biol. Chem. , vol.276 , pp. 4853-4862
    • Stipp, C.S.1    Orlicky, D.2    Hemler, M.E.3
  • 118
    • 0032490543 scopus 로고    scopus 로고
    • Expression of rat target of the antiproliferative antibody (TAPA) in the developing brain
    • Sullivan CD, Geisert EE Jr. 1998. Expression of rat target of the antiproliferative antibody (TAPA) in the developing brain. J. Comp. Neurol. 396:366-80
    • (1998) J. Comp. Neurol. , vol.396 , pp. 366-380
    • Sullivan, C.D.1    Geisert Jr., E.E.2
  • 119
    • 0033598128 scopus 로고    scopus 로고
    • Role of transmembrane-4 superfamily (TM4SF) proteins CD9 and CD81 in muscle cell fusion and myotube maintenance
    • Tachibana I, Hemler ME. 1999. Role of transmembrane-4 superfamily (TM4SF) proteins CD9 and CD81 in muscle cell fusion and myotube maintenance. J. Cell Biol. 146:893-904
    • (1999) J. Cell Biol. , vol.146 , pp. 893-904
    • Tachibana, I.1    Hemler, M.E.2
  • 120
    • 0029067101 scopus 로고
    • Identification of a highly specific surface marker of T-cell acute lymphoblastic leukemia and neuroblastoma as a new member of the transmembrane 4 superfamily
    • Takagi S, Fujikawa K, Imai T, Fukuhara N, Fukudome K, et al. 1995. Identification of a highly specific surface marker of T-cell acute lymphoblastic leukemia and neuroblastoma as a new member of the transmembrane 4 superfamily. Int. J. Cancer 61:706-15
    • (1995) Int. J. Cancer , vol.61 , pp. 706-715
    • Takagi, S.1    Fujikawa, K.2    Imai, T.3    Fukuhara, N.4    Fukudome, K.5
  • 121
    • 0032896681 scopus 로고    scopus 로고
    • CD9 molecule expressed on stromal cells is involved in osteoclastogenesis
    • Tanio Y, Yamazaki H, Kunisada T, Miyake K, Hayashi SI. 1999. CD9 molecule expressed on stromal cells is involved in osteoclastogenesis. Exp. Hematol. 27:853-59
    • (1999) Exp. Hematol. , vol.27 , pp. 853-859
    • Tanio, Y.1    Yamazaki, H.2    Kunisada, T.3    Miyake, K.4    Hayashi, S.I.5
  • 122
    • 0036291471 scopus 로고    scopus 로고
    • The absence of Tssc6, a member of the tetraspanin superfamily, does not affect lymphoid development but enhances in vitro T-cell proliferative responses
    • Tarrant JM, Groom J, Metcalf D, Li R, Borobokas B, et al. 2002. The absence of Tssc6, a member of the tetraspanin superfamily, does not affect lymphoid development but enhances in vitro T-cell proliferative responses. Mol. Cell Biol. 22(14):5006-18
    • (2002) Mol. Cell Biol. , vol.22 , Issue.14 , pp. 5006-5018
    • Tarrant, J.M.1    Groom, J.2    Metcalf, D.3    Li, R.4    Borobokas, B.5
  • 123
    • 0035897413 scopus 로고    scopus 로고
    • OSP/claudin-11 forms a complex with a novel member of the tetraspanin super family and beta1 integrin and regulates proliferation and migration of oligodendrocytes
    • Tiwari-Woodruff SK, Buznikov AG, Vu TQ, Micevych PE, Chen K, et al. 2001. OSP/claudin-11 forms a complex with a novel member of the tetraspanin super family and beta1 integrin and regulates proliferation and migration of oligodendrocytes. J. Cell Biol. 153:295-305
    • (2001) J. Cell Biol. , vol.153 , pp. 295-305
    • Tiwari-Woodruff, S.K.1    Buznikov, A.G.2    Vu, T.Q.3    Micevych, P.E.4    Chen, K.5
  • 125
    • 0027446527 scopus 로고
    • Epitope mapping of anti-rat CD53 monoclonal antibodies: Implications for the membrane orientation of the transmembrane 4 superfamily
    • Tomlinson MG, Williams AF, Wright MD. 1993. Epitope mapping of anti-rat CD53 monoclonal antibodies: implications for the membrane orientation of the transmembrane 4 superfamily. Eur. J. Immunol. 23:136-40
    • (1993) Eur. J. Immunol. , vol.23 , pp. 136-140
    • Tomlinson, M.G.1    Williams, A.F.2    Wright, M.D.3
  • 126
    • 0030886882 scopus 로고    scopus 로고
    • Impaired CD19 expression and signaling, enhanced antibody response to type II T independent antigen and reduction of B-1 cells in CD81-deficient mice
    • Tsitsikov EN, Gutierrez-Ramos JC, Geha RS. 1997. Impaired CD19 expression and signaling, enhanced antibody response to type II T independent antigen and reduction of B-1 cells in CD81-deficient mice. Proc. Natl. Acad. Sci. USA 94:10844-49
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10844-10849
    • Tsitsikov, E.N.1    Gutierrez-Ramos, J.C.2    Geha, R.S.3
  • 127
    • 0036863574 scopus 로고    scopus 로고
    • Clustering of MHC-peptide complexes prior to their engagement in the immunological synapse: Lipid raft and tetraspan microdomains
    • Vogt AB, Spindeldreher S, Kropshofer H. 2002. Clustering of MHC-peptide complexes prior to their engagement in the immunological synapse: lipid raft and tetraspan microdomains. Immunol. Rev. 189:136-51
    • (2002) Immunol. Rev. , vol.189 , pp. 136-151
    • Vogt, A.B.1    Spindeldreher, S.2    Kropshofer, H.3
  • 128
    • 0037148519 scopus 로고    scopus 로고
    • Murine CD9 is the receptor for pregnancy-specific glycoprotein 17
    • Waterhouse R, Ha C, Dveksler GS. 2002. Murine CD9 is the receptor for pregnancy-specific glycoprotein 17. J. Exp. Med. 195: 277-82
    • (2002) J. Exp. Med. , vol.195 , pp. 277-282
    • Waterhouse, R.1    Ha, C.2    Dveksler, G.S.3
  • 129
    • 0031051160 scopus 로고    scopus 로고
    • Inhibition of feline immunodeficiency virus infection by CD9 antibody operates after virus entry and is independent of virus tropism
    • Willett B, Hosie M, Shaw A, Neil J. 1997. Inhibition of feline immunodeficiency virus infection by CD9 antibody operates after virus entry and is independent of virus tropism. J. Gen. Virol. 78:611-18
    • (1997) J. Gen. Virol. , vol.78 , pp. 611-618
    • Willett, B.1    Hosie, M.2    Shaw, A.3    Neil, J.4
  • 130
    • 20244373139 scopus 로고    scopus 로고
    • Tumor-derived exosomes are a source of shared tumor rejection antigens for CTL cross-priming
    • Wolfers J, Lozier A, Raposo G, Regnault A, Thery C, et al. 2001. Tumor-derived exosomes are a source of shared tumor rejection antigens for CTL cross-priming. Nat. Med. 7:297-303
    • (2001) Nat. Med. , vol.7 , pp. 297-303
    • Wolfers, J.1    Lozier, A.2    Raposo, G.3    Regnault, A.4    Thery, C.5
  • 131
    • 0030589505 scopus 로고    scopus 로고
    • ADAMs in fertilization and development
    • Wolfsberg TG, White JM. 1996. ADAMs in fertilization and development. Dev. Biol. 180: 389-401
    • (1996) Dev. Biol. , vol.180 , pp. 389-401
    • Wolfsberg, T.G.1    White, J.M.2
  • 132
    • 0035816640 scopus 로고    scopus 로고
    • Analysis of fertilin alpha (ADAM1)-mediated sperm-egg cell adhesion during fertilization and identification of an adhesion-mediating sequence in the disintegrin-like domain
    • Wong GE, Zhu X, Prater CE, Oh E, Evans JP. 2001. Analysis of fertilin alpha (ADAM1)-mediated sperm-egg cell adhesion during fertilization and identification of an adhesion-mediating sequence in the disintegrin-like domain. J. Biol. Chem. 276:24937-45
    • (2001) J. Biol. Chem. , vol.276 , pp. 24937-24945
    • Wong, G.E.1    Zhu, X.2    Prater, C.E.3    Oh, E.4    Evans, J.P.5
  • 133
    • 0025193411 scopus 로고
    • r 23,000 integral membrane protein of Schistosoma mansoni worms that closely resembles a human tumor-associated antigen
    • r 23,000 integral membrane protein of Schistosoma mansoni worms that closely resembles a human tumor-associated antigen. J. Immunol. 144:3195-200
    • (1990) J. Immunol. , vol.144 , pp. 3195-3200
    • Wright, M.D.1    Henkle, K.J.2    Mitchell, G.F.3
  • 134
    • 0034607831 scopus 로고    scopus 로고
    • Peripherin/rds influences membrane vesicle morphology. Implications for retinopathies
    • Wrigley JD, Ahmed T, Nevett CL, Findlay JB. 2000. Peripherin/rds influences membrane vesicle morphology. Implications for retinopathies. J. Biol. Chem. 275:13191-94
    • (2000) J. Biol. Chem. , vol.275 , pp. 13191-13194
    • Wrigley, J.D.1    Ahmed, T.2    Nevett, C.L.3    Findlay, J.B.4
  • 135
    • 0029618912 scopus 로고
    • Selective interactions of UPIa and UPIb, two members of the transmembrane 4 superfamily, with distinct single transmembrane-domained proteins in differentiated urothelial cells
    • Wu X-R, Medina JJ, Sun T-T. 1995. Selective interactions of UPIa and UPIb, two members of the transmembrane 4 superfamily, with distinct single transmembrane-domained proteins in differentiated urothelial cells. J. Biol. Chem. 270:29752-59
    • (1995) J. Biol. Chem. , vol.270 , pp. 29752-29759
    • Wu, X.-R.1    Medina, J.J.2    Sun, T.-T.3
  • 136
    • 0037157854 scopus 로고    scopus 로고
    • The metalloprotease kuzbanian (ADAM10) mediates the transactivation of EGF receptor by G protein-coupled receptors
    • Yan Y, Shirakabe K, Werb Z. 2002. The metalloprotease kuzbanian (ADAM10) mediates the transactivation of EGF receptor by G protein-coupled receptors. J. Cell Biol. 158:221-26
    • (2002) J. Cell Biol. , vol.158 , pp. 221-226
    • Yan, Y.1    Shirakabe, K.2    Werb, Z.3
  • 137
    • 0032482216 scopus 로고    scopus 로고
    • Regulation of endothelial cell motility by complexes of tetraspan molecules CD81/TAPA-1 and CD151/PETA-3 with α3β1 integrin localized at endothelial lateral junctions
    • Yánez-Mó M, Alfranca A, Cabañas C, Marazuela M, Tejedor R, et al. 1998. Regulation of endothelial cell motility by complexes of tetraspan molecules CD81/TAPA-1 and CD151/PETA-3 with α3β1 integrin localized at endothelial lateral junctions. J. Cell Biol. 141:791-804
    • (1998) J. Cell Biol. , vol.141 , pp. 791-804
    • Yánez-Mó, M.1    Alfranca, A.2    Cabañas, C.3    Marazuela, M.4    Tejedor, R.5
  • 139
    • 0345150637 scopus 로고    scopus 로고
    • Palmitoylation of tetraspanin proteins: Modulation of CD151 lateral interactions, subcellular distribution, and integrin-dependent cell morphology
    • Yang X, Claas C, Kraeft S-K, Chen LB, Wang Z, et al. 2002. Palmitoylation of tetraspanin proteins: modulation of CD151 lateral interactions, subcellular distribution, and integrin-dependent cell morphology. Mol. Biol. Cell 50:1-2
    • (2002) Mol. Biol. Cell , vol.50 , pp. 1-2
    • Yang, X.1    Claas, C.2    Kraeft, S.-K.3    Chen, L.B.4    Wang, Z.5
  • 140
    • 0034141469 scopus 로고    scopus 로고
    • Non-CD28 co-stimulatory molecules present in T cell rafts induce T cell costimulation by enhancing the association of TCR with rafts
    • Yashiro-Ohtani Y, Zhou XY, Toyo-Oka K, Tai XG, Park CS, et al. 2000. Non-CD28 co-stimulatory molecules present in T cell rafts induce T cell costimulation by enhancing the association of TCR with rafts. J. Immunol. 164:1251-59
    • (2000) J. Immunol. , vol.164 , pp. 1251-1259
    • Yashiro-Ohtani, Y.1    Zhou, X.Y.2    Toyo-Oka, K.3    Tai, X.G.4    Park, C.S.5
  • 141
    • 0031660652 scopus 로고    scopus 로고
    • Highly stoichiometric, stable and specific association of integrin α3β1 with CD151 provides a major link to phosphatidylinositol 4-kinase and may regulate cell migration
    • Yauch RL, Berditchevski F, Harler MB, Reichner J, Hemler ME. 1998. Highly stoichiometric, stable and specific association of integrin α3β1 with CD151 provides a major link to phosphatidylinositol 4-kinase and may regulate cell migration. Mol. Biol. Cell 9:2751-65
    • (1998) Mol. Biol. Cell , vol.9 , pp. 2751-2765
    • Yauch, R.L.1    Berditchevski, F.2    Harler, M.B.3    Reichner, J.4    Hemler, M.E.5
  • 142
    • 0034331438 scopus 로고    scopus 로고
    • Specific interactions among transmembrane 4 superfamily (TM4SF) proteins and phosphatidylinositol 4-kinase
    • Yauch RL, Hemler ME. 2000. Specific interactions among transmembrane 4 superfamily (TM4SF) proteins and phosphatidylinositol 4-kinase. Biochem. J. 351:629-37
    • (2000) Biochem. J. , vol.351 , pp. 629-637
    • Yauch, R.L.1    Hemler, M.E.2
  • 143
    • 0034737471 scopus 로고    scopus 로고
    • Direct extracellular contact between integrin α3β1 and TM4SF protein CD151
    • Yauch RL, Kazarov AR, Desai B, Lee RT, Hemler ME. 2000. Direct extracellular contact between integrin α3β1 and TM4SF protein CD151. J. Biol. Chem. 275:9230-38
    • (2000) J. Biol. Chem. , vol.275 , pp. 9230-9238
    • Yauch, R.L.1    Kazarov, A.R.2    Desai, B.3    Lee, R.T.4    Hemler, M.E.5
  • 144
    • 0033968407 scopus 로고    scopus 로고
    • A new gene involved in X-linked mental retardation identified by analysis of an X;2 balanced translocation
    • Zemni R, Bienvenu T, Vinet MC, Sefiani A, Carrie A, et al. 2000. A new gene involved in X-linked mental retardation identified by analysis of an X;2 balanced translocation. Nat. Genet. 24:167-70
    • (2000) Nat. Genet. , vol.24 , pp. 167-170
    • Zemni, R.1    Bienvenu, T.2    Vinet, M.C.3    Sefiani, A.4    Carrie, A.5
  • 145
    • 0035816663 scopus 로고    scopus 로고
    • TM4SF proteins associate with activated PKC and Link PKC to specific beta1 integrins
    • Zhang XA, Bontrager AL, Hemler ME. 2001. TM4SF proteins associate with activated PKC and Link PKC to specific beta1 integrins. J. Biol. Chem. 276:25005-13
    • (2001) J. Biol. Chem. , vol.276 , pp. 25005-25013
    • Zhang, X.A.1    Bontrager, A.L.2    Hemler, M.E.3
  • 148
    • 0036333987 scopus 로고    scopus 로고
    • Residues SFQ (173-175) in the large extracellular loop of CD9 are required for gamete fusion
    • Zhu GZ, Miller BJ, Boucheix C, Rubinstein E, Liu CC, et al. 2002. Residues SFQ (173-175) in the large extracellular loop of CD9 are required for gamete fusion. Development 129(8):1995-2002
    • (2002) Development , vol.129 , Issue.8 , pp. 1995-2002
    • Zhu, G.Z.1    Miller, B.J.2    Boucheix, C.3    Rubinstein, E.4    Liu, C.C.5
  • 149
    • 0036197618 scopus 로고    scopus 로고
    • Analysis of the roles of RGD-binding integrins, alpha(4)/alpha(9) integrins, alpha(6) integrins, and CD9 in the interaction of the fertilin beta (ADAM2) disintegrin domain with the mouse egg membrane
    • Zhu X, Evans JP. 2002. Analysis of the roles of RGD-binding integrins, alpha(4)/alpha(9) integrins, alpha(6) integrins, and CD9 in the interaction of the fertilin beta (ADAM2) disintegrin domain with the mouse egg membrane. Biol. Reprod. 66:1193-202
    • (2002) Biol. Reprod. , vol.66 , pp. 1193-1202
    • Zhu, X.1    Evans, J.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.