메뉴 건너뛰기




Volumn 236, Issue 1-2, 2005, Pages 179-187

Evaluation of specificity and effects of monoclonal antibodies submitted to the Eighth Human Leucocyte Differentiation Antigen Workshop on rotavirus-cell attachment and entry

Author keywords

Adhesion molecules; Integrins; Monoclonal antibodies; Rotavirus infection; Rotavirus cell attachment

Indexed keywords

ANTIGEN; BETA1 INTEGRIN; BETA2 INTEGRIN; CD82 ANTIGEN; DIFFERENTIATION ANTIGEN; MONOCLONAL ANTIBODY; PROTEIN ANTIBODY; VERY LATE ACTIVATION ANTIGEN 4;

EID: 28844491720     PISSN: 00088749     EISSN: 10902163     Source Type: Journal    
DOI: 10.1016/j.cellimm.2005.08.025     Document Type: Conference Paper
Times cited : (4)

References (55)
  • 1
    • 4544264420 scopus 로고    scopus 로고
    • Pathogenesis of intestinal and systemic rotavirus infection
    • R.F. Ramig Pathogenesis of intestinal and systemic rotavirus infection J. Virol. 78 2004 10213 10220
    • (2004) J. Virol. , vol.78 , pp. 10213-10220
    • Ramig, R.F.1
  • 2
    • 0033954018 scopus 로고    scopus 로고
    • Rotavirus infection induces an increase in intracellular calcium concentration in human intestinal epithelial cells: Role in microvillar actin alteration
    • J.P. Brunet, J. Cotte-Laffitte, C. Linxe, A.M. Quero, M. Geniteau-Legendre, and A. Servin Rotavirus infection induces an increase in intracellular calcium concentration in human intestinal epithelial cells: role in microvillar actin alteration J. Virol. 74 2000 2323 2332
    • (2000) J. Virol. , vol.74 , pp. 2323-2332
    • Brunet, J.P.1    Cotte-Laffitte, J.2    Linxe, C.3    Quero, A.M.4    Geniteau-Legendre, M.5    Servin, A.6
  • 3
    • 0025991526 scopus 로고
    • Comparative growth of different rotavirus strains in differentiated cells (MA104, HepG2, and CaCo-2)
    • N. Kitamoto, R.F. Ramig, D.O. Matson, and M.K. Estes Comparative growth of different rotavirus strains in differentiated cells (MA104, HepG2, and CaCo-2) Virology 184 1991 729 737
    • (1991) Virology , vol.184 , pp. 729-737
    • Kitamoto, N.1    Ramig, R.F.2    Matson, D.O.3    Estes, M.K.4
  • 4
    • 0029070241 scopus 로고
    • Identification of group a rotavirus genes associated with virulence of a porcine rotavirus and host range restriction of a human rotavirus in the gnotobiotic piglet model
    • Y. Hoshino, L.J. Saif, S.Y. Kang, M.M. Sereno, W.K. Chen, and A.Z. Kapikian Identification of group A rotavirus genes associated with virulence of a porcine rotavirus and host range restriction of a human rotavirus in the gnotobiotic piglet model Virology 209 1995 274 280
    • (1995) Virology , vol.209 , pp. 274-280
    • Hoshino, Y.1    Saif, L.J.2    Kang, S.Y.3    Sereno, M.M.4    Chen, W.K.5    Kapikian, A.Z.6
  • 5
    • 0022624974 scopus 로고
    • Molecular basis of rotavirus virulence: Role of gene segment 4
    • P.A. Offit, G. Blavat, H.B. Greenberg, and H.F. Clark Molecular basis of rotavirus virulence: role of gene segment 4 J. Virol. 57 1986 46 49
    • (1986) J. Virol. , vol.57 , pp. 46-49
    • Offit, P.A.1    Blavat, G.2    Greenberg, H.B.3    Clark, H.F.4
  • 6
    • 0025914887 scopus 로고
    • Identification and partial characterization of a rhesus rotavirus binding glycoprotein on murine enterocytes
    • D.M. Bass, E.R. Mackow, and H.B. Greenberg Identification and partial characterization of a rhesus rotavirus binding glycoprotein on murine enterocytes Virology 183 1991 602 610
    • (1991) Virology , vol.183 , pp. 602-610
    • Bass, D.M.1    MacKow, E.R.2    Greenberg, H.B.3
  • 7
    • 0028102107 scopus 로고
    • Characterization of virus-like particles produced by the expression of rotavirus capsid proteins in insect cells
    • S.E. Crawford, M. Labbe, J. Cohen, M.H. Burroughs, Y.J. Zhou, and M.K. Estes Characterization of virus-like particles produced by the expression of rotavirus capsid proteins in insect cells J. Virol. 68 1994 5945 5952
    • (1994) J. Virol. , vol.68 , pp. 5945-5952
    • Crawford, S.E.1    Labbe, M.2    Cohen, J.3    Burroughs, M.H.4    Zhou, Y.J.5    Estes, M.K.6
  • 8
    • 0031691267 scopus 로고    scopus 로고
    • Attachment and growth of human rotaviruses RV-3 and S12/85 in Caco-2 cells depend on VP4
    • C.D. Kirkwood, R.F. Bishop, and B.S. Coulson Attachment and growth of human rotaviruses RV-3 and S12/85 in Caco-2 cells depend on VP4 J. Virol. 72 1998 9348 9352
    • (1998) J. Virol. , vol.72 , pp. 9348-9352
    • Kirkwood, C.D.1    Bishop, R.F.2    Coulson, B.S.3
  • 9
    • 0029655241 scopus 로고    scopus 로고
    • Genetic mapping indicates that VP4 is the rotavirus cell attachment protein in vitro and in vivo
    • J.E. Ludert, N. Feng, J.H. Yu, R.L. Broome, Y. Hoshino, and H.B. Greenberg Genetic mapping indicates that VP4 is the rotavirus cell attachment protein in vitro and in vivo J. Virol. 70 1996 487 493
    • (1996) J. Virol. , vol.70 , pp. 487-493
    • Ludert, J.E.1    Feng, N.2    Yu, J.H.3    Broome, R.L.4    Hoshino, Y.5    Greenberg, H.B.6
  • 11
    • 0029793570 scopus 로고    scopus 로고
    • Trypsin activation pathway of rotavirus infectivity
    • C.F. Arias, P. Romero, V. Alvarez, and S. Lopez Trypsin activation pathway of rotavirus infectivity J. Virol. 70 1996 5832 5839
    • (1996) J. Virol. , vol.70 , pp. 5832-5839
    • Arias, C.F.1    Romero, P.2    Alvarez, V.3    Lopez, S.4
  • 12
    • 0019441945 scopus 로고
    • Trypsin enhancement of rotavirus infectivity: Mechanism of enhancement
    • S.M. Clark, J.R. Roth, M.L. Clark, B.B. Barnett, and R.S. Spendlove Trypsin enhancement of rotavirus infectivity: mechanism of enhancement J. Virol. 39 1981 816 822
    • (1981) J. Virol. , vol.39 , pp. 816-822
    • Clark, S.M.1    Roth, J.R.2    Clark, M.L.3    Barnett, B.B.4    Spendlove, R.S.5
  • 13
    • 0019378955 scopus 로고
    • Structural polypeptides of simian rotavirus SA11 and the effect of trypsin
    • R.T. Espejo, S. Lopez, and C. Arias Structural polypeptides of simian rotavirus SA11 and the effect of trypsin J. Virol. 37 1981 156 160
    • (1981) J. Virol. , vol.37 , pp. 156-160
    • Espejo, R.T.1    Lopez, S.2    Arias, C.3
  • 14
    • 0019440664 scopus 로고
    • Proteolytic enhancement of rotavirus infectivity: Molecular mechanisms
    • M.K. Estes, D.Y. Graham, and B.B. Mason Proteolytic enhancement of rotavirus infectivity: molecular mechanisms J. Virol. 39 1981 879 888
    • (1981) J. Virol. , vol.39 , pp. 879-888
    • Estes, M.K.1    Graham, D.Y.2    Mason, B.B.3
  • 15
    • 0018911088 scopus 로고
    • Attachment of SA-11 rotavirus to erythrocyte receptors
    • J.W. Bastardo, and I.H. Holmes Attachment of SA-11 rotavirus to erythrocyte receptors Infect. Immun. 29 1980 1134 1140
    • (1980) Infect. Immun. , vol.29 , pp. 1134-1140
    • Bastardo, J.W.1    Holmes, I.H.2
  • 16
    • 0035128179 scopus 로고    scopus 로고
    • Glycosphingolipid binding specificities of rotavirus: Identification of a sialic acid-binding epitope
    • C. Delorme, H. Brussow, J. Sidoti, N. Roche, K.A. Karlsson, J.R. Neeser, and S. Teneberg Glycosphingolipid binding specificities of rotavirus: identification of a sialic acid-binding epitope J. Virol. 75 2001 2276 2287
    • (2001) J. Virol. , vol.75 , pp. 2276-2287
    • Delorme, C.1    Brussow, H.2    Sidoti, J.3    Roche, N.4    Karlsson, K.A.5    Neeser, J.R.6    Teneberg, S.7
  • 17
    • 0024426261 scopus 로고
    • Comparison of human, simian, and bovine rotaviruses for requirement of sialic acid in hemagglutination and cell adsorption
    • K. Fukudome, O. Yoshie, and T. Konno Comparison of human, simian, and bovine rotaviruses for requirement of sialic acid in hemagglutination and cell adsorption Virology 172 1989 196 205
    • (1989) Virology , vol.172 , pp. 196-205
    • Fukudome, K.1    Yoshie, O.2    Konno, T.3
  • 19
    • 0034665251 scopus 로고    scopus 로고
    • Rotavirus infection of MA104 cells is inhibited by Ricinus lectin and separately expressed single binding domains
    • C.L. Jolly, B.M. Beisner, and I.H. Holmes Rotavirus infection of MA104 cells is inhibited by Ricinus lectin and separately expressed single binding domains Virology 275 2000 89 97
    • (2000) Virology , vol.275 , pp. 89-97
    • Jolly, C.L.1    Beisner, B.M.2    Holmes, I.H.3
  • 22
    • 0027494242 scopus 로고
    • Rotaviruses preferentially bind O-linked sialylglycoconjugates and sialomucins
    • R.E. Willoughby Rotaviruses preferentially bind O-linked sialylglycoconjugates and sialomucins Glycobiology 3 1993 437 445
    • (1993) Glycobiology , vol.3 , pp. 437-445
    • Willoughby, R.E.1
  • 23
    • 0024503201 scopus 로고
    • The rhesus rotavirus outer capsid protein VP4 functions as a hemagglutinin and is antigenically conserved when expressed by a baculovirus recombinant
    • E.R. Mackow, J.W. Barnett, H. Chan, and H.B. Greenberg The rhesus rotavirus outer capsid protein VP4 functions as a hemagglutinin and is antigenically conserved when expressed by a baculovirus recombinant J. Virol. 63 1989 1661 1668
    • (1989) J. Virol. , vol.63 , pp. 1661-1668
    • MacKow, E.R.1    Barnett, J.W.2    Chan, H.3    Greenberg, H.B.4
  • 24
    • 0030998380 scopus 로고    scopus 로고
    • Rotavirus contains integrin ligand sequences and a disintegrin-like domain that are implicated in virus entry into cells
    • B.S. Coulson, S.L. Londrigan, and D.J. Lee Rotavirus contains integrin ligand sequences and a disintegrin-like domain that are implicated in virus entry into cells Proc. Natl. Acad. Sci. USA 94 1997 5389 5394
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 5389-5394
    • Coulson, B.S.1    Londrigan, S.L.2    Lee, D.J.3
  • 26
    • 0033622332 scopus 로고    scopus 로고
    • Integrins alpha2beta1 and alpha4beta1 can mediate SA11 rotavirus attachment and entry into cells
    • M.J. Hewish, Y. Takada, and B.S. Coulson Integrins alpha2beta1 and alpha4beta1 can mediate SA11 rotavirus attachment and entry into cells J. Virol. 74 2000 228 236
    • (2000) J. Virol. , vol.74 , pp. 228-236
    • Hewish, M.J.1    Takada, Y.2    Coulson, B.S.3
  • 27
    • 0033830310 scopus 로고    scopus 로고
    • Growth of rotaviruses in continuous human and monkey cell lines that vary in their expression of integrins
    • S.L. Londrigan, M.J. Hewish, M.J. Thomson, G.M. Sanders, H. Mustafa, and B.S. Coulson Growth of rotaviruses in continuous human and monkey cell lines that vary in their expression of integrins J. Gen. Virol. 81 2000 2203 2213
    • (2000) J. Gen. Virol. , vol.81 , pp. 2203-2213
    • Londrigan, S.L.1    Hewish, M.J.2    Thomson, M.J.3    Sanders, G.M.4    Mustafa, H.5    Coulson, B.S.6
  • 28
    • 0034610177 scopus 로고    scopus 로고
    • Integrin alpha2beta1 mediates the cell attachment of the rotavirus neuraminidase-resistant variant nar3
    • S. Zarate, R. Espinosa, P. Romero, C.A. Guerrero, C.F. Arias, and S. Lopez Integrin alpha2beta1 mediates the cell attachment of the rotavirus neuraminidase-resistant variant nar3 Virology 278 2000 50 54
    • (2000) Virology , vol.278 , pp. 50-54
    • Zarate, S.1    Espinosa, R.2    Romero, P.3    Guerrero, C.A.4    Arias, C.F.5    Lopez, S.6
  • 29
    • 0141458927 scopus 로고    scopus 로고
    • Integrin-using rotaviruses bind alpha2beta1 integrin alpha2 I domain via VP4 DGE sequence and recognize alphaXbeta2 and alphaVbeta3 by using VP7 during cell entry
    • K.L. Graham, P. Halasz, Y. Tan, M.J. Hewish, Y. Takada, E.R. Mackow, M.K. Robinson, and B.S. Coulson Integrin-using rotaviruses bind alpha2beta1 integrin alpha2 I domain via VP4 DGE sequence and recognize alphaXbeta2 and alphaVbeta3 by using VP7 during cell entry J. Virol. 77 2003 9969 9978
    • (2003) J. Virol. , vol.77 , pp. 9969-9978
    • Graham, K.L.1    Halasz, P.2    Tan, Y.3    Hewish, M.J.4    Takada, Y.5    MacKow, E.R.6    Robinson, M.K.7    Coulson, B.S.8
  • 30
    • 0041387421 scopus 로고    scopus 로고
    • Monkey rotavirus binding to alpha2beta1 integrin requires the alpha2 I domain and is facilitated by the homologous beta1 subunit
    • S.L. Londrigan, K.L. Graham, Y. Takada, P. Halasz, and B.S. Coulson Monkey rotavirus binding to alpha2beta1 integrin requires the alpha2 I domain and is facilitated by the homologous beta1 subunit J. Virol. 77 2003 9486 9501
    • (2003) J. Virol. , vol.77 , pp. 9486-9501
    • Londrigan, S.L.1    Graham, K.L.2    Takada, Y.3    Halasz, P.4    Coulson, B.S.5
  • 31
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signaling in cell adhesion
    • R.O. Hynes Integrins: versatility, modulation, and signaling in cell adhesion Cell 69 1992 11 25
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 32
    • 0035047433 scopus 로고    scopus 로고
    • Role of the cytoplasmic domain of the beta-subunit of integrin alpha(v)beta6 in infection by foot-and-mouth disease virus
    • L.C. Miller, W. Blakemore, D. Sheppard, A. Atakilit, A.M. King, and T. Jackson Role of the cytoplasmic domain of the beta-subunit of integrin alpha(v)beta6 in infection by foot-and-mouth disease virus J. Virol. 75 2001 4158 4164
    • (2001) J. Virol. , vol.75 , pp. 4158-4164
    • Miller, L.C.1    Blakemore, W.2    Sheppard, D.3    Atakilit, A.4    King, A.M.5    Jackson, T.6
  • 34
    • 0030614485 scopus 로고    scopus 로고
    • Identification of the alpha6 integrin as a candidate receptor for papillomaviruses
    • M. Evander, I.H. Frazer, E. Payne, Y.M. Qi, K. Hengst, and N.A. McMillan Identification of the alpha6 integrin as a candidate receptor for papillomaviruses J. Virol. 71 1997 2449 2456
    • (1997) J. Virol. , vol.71 , pp. 2449-2456
    • Evander, M.1    Frazer, I.H.2    Payne, E.3    Qi, Y.M.4    Hengst, K.5    McMillan, N.A.6
  • 35
    • 6344277169 scopus 로고    scopus 로고
    • Effects on rotavirus cell binding and infection of monomeric and polymeric peptides containing alpha2beta1 and alphaxbeta2 integrin ligand sequences
    • K.L. Graham, W. Zeng, Y. Takada, D.C. Jackson, and B.S. Coulson Effects on rotavirus cell binding and infection of monomeric and polymeric peptides containing alpha2beta1 and alphaxbeta2 integrin ligand sequences J. Virol. 78 2004 11786 11797
    • (2004) J. Virol. , vol.78 , pp. 11786-11797
    • Graham, K.L.1    Zeng, W.2    Takada, Y.3    Jackson, D.C.4    Coulson, B.S.5
  • 36
    • 0033558218 scopus 로고    scopus 로고
    • Transmembrane 4 superfamily protein CD151 (PETA-3) associates with beta 1 and alpha IIb beta 3 integrins in haemopoietic cell lines and modulates cell-cell adhesion
    • S. Fitter, P.M. Sincock, C.N. Jolliffe, and L.K. Ashman Transmembrane 4 superfamily protein CD151 (PETA-3) associates with beta 1 and alpha IIb beta 3 integrins in haemopoietic cell lines and modulates cell-cell adhesion Biochem. J. 338 Pt. 1 1999 61 70
    • (1999) Biochem. J. , vol.338 , Issue.1 PART , pp. 61-70
    • Fitter, S.1    Sincock, P.M.2    Jolliffe, C.N.3    Ashman, L.K.4
  • 37
    • 0030239653 scopus 로고    scopus 로고
    • Transmembrane-4 superfamily proteins CD81 (TAPA-1), CD82, CD63, and CD53 specifically associated with integrin alpha 4 beta 1 (CD49d/CD29)
    • B.A. Mannion, F. Berditchevski, S.K. Kraeft, L.B. Chen, and M.E. Hemler Transmembrane-4 superfamily proteins CD81 (TAPA-1), CD82, CD63, and CD53 specifically associated with integrin alpha 4 beta 1 (CD49d/CD29) J. Immunol. 157 1996 2039 2047
    • (1996) J. Immunol. , vol.157 , pp. 2039-2047
    • Mannion, B.A.1    Berditchevski, F.2    Kraeft, S.K.3    Chen, L.B.4    Hemler, M.E.5
  • 38
    • 0031660652 scopus 로고    scopus 로고
    • Highly stoichiometric, stable, and specific association of integrin alpha3beta1 with CD151 provides a major link to phosphatidylinositol 4-kinase, and may regulate cell migration
    • R.L. Yauch, F. Berditchevski, M.B. Harler, J. Reichner, and M.E. Hemler Highly stoichiometric, stable, and specific association of integrin alpha3beta1 with CD151 provides a major link to phosphatidylinositol 4-kinase, and may regulate cell migration Mol. Biol. Cell 9 1998 2751 2765
    • (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
  • 39
    • 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
    • L.M. Sterk, C.A. Geuijen, J.G. van den Berg, N. Claessen, J.J. Weening, and A. Sonnenberg 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 2002 1161 1173
    • (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
  • 41
    • 12344335722 scopus 로고    scopus 로고
    • Tetraspanin-Fc receptor interactions
    • G.W. Moseley Tetraspanin-Fc receptor interactions Platelets 16 2005 3 12
    • (2005) Platelets , vol.16 , pp. 3-12
    • Moseley, G.W.1
  • 42
    • 0141644213 scopus 로고    scopus 로고
    • The JAM family of junctional adhesion molecules
    • G. Bazzoni The JAM family of junctional adhesion molecules Curr. Opin. Cell Biol. 15 2003 525 530
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 525-530
    • Bazzoni, G.1
  • 44
    • 0036008013 scopus 로고    scopus 로고
    • JAM-1 is a ligand of the beta (2) integrin LFA-1 involved in transendothelial migration of leukocytes
    • G. Ostermann, K.S. Weber, A. Zernecke, A. Schroder, and C. Weber JAM-1 is a ligand of the beta (2) integrin LFA-1 involved in transendothelial migration of leukocytes Nat. Immunol. 3 2002 151 158
    • (2002) Nat. Immunol. , vol.3 , pp. 151-158
    • Ostermann, G.1    Weber, K.S.2    Zernecke, A.3    Schroder, A.4    Weber, C.5
  • 45
    • 0141679018 scopus 로고    scopus 로고
    • Signaling through JAM-1 and alphavbeta3 is required for the angiogenic action of bFGF: Dissociation of the JAM-1 and alphavbeta3 complex
    • M.U. Naik, S.A. Mousa, C.A. Parkos, and U.P. Naik Signaling through JAM-1 and alphavbeta3 is required for the angiogenic action of bFGF: dissociation of the JAM-1 and alphavbeta3 complex Blood 102 2003 2108 2114
    • (2003) Blood , vol.102 , pp. 2108-2114
    • Naik, M.U.1    Mousa, S.A.2    Parkos, C.A.3    Naik, U.P.4
  • 46
    • 0040888844 scopus 로고    scopus 로고
    • Functional interactions of the immunoglobulin superfamily member F11 are differentially regulated by the extracellular matrix proteins tenascin-R and tenascin-C
    • U. Zacharias, U. Norenberg, and F.G. Rathjen Functional interactions of the immunoglobulin superfamily member F11 are differentially regulated by the extracellular matrix proteins tenascin-R and tenascin-C J. Biol. Chem. 274 1999 24357 24365
    • (1999) J. Biol. Chem. , vol.274 , pp. 24357-24365
    • Zacharias, U.1    Norenberg, U.2    Rathjen, F.G.3
  • 47
    • 0032008545 scopus 로고    scopus 로고
    • Functional cooperation of beta1-integrins and members of the Ig superfamily in neurite outgrowth induction
    • U. Treubert, and T. Brummendorf Functional cooperation of beta1-integrins and members of the Ig superfamily in neurite outgrowth induction J. Neurosci. 18 1998 1795 1805
    • (1998) J. Neurosci. , vol.18 , pp. 1795-1805
    • Treubert, U.1    Brummendorf, T.2
  • 49
    • 0027514525 scopus 로고
    • Typing of human rotavirus VP4 by an enzyme immunoassay using monoclonal antibodies
    • B.S. Coulson Typing of human rotavirus VP4 by an enzyme immunoassay using monoclonal antibodies J. Clin. Microbiol. 31 1993 1 8
    • (1993) J. Clin. Microbiol. , vol.31 , pp. 1-8
    • Coulson, B.S.1
  • 50
    • 0024309360 scopus 로고
    • Neutralizing monoclonal antibodies against three serotypes of porcine rotavirus
    • H.S. Nagesha, L.E. Brown, and I.H. Holmes Neutralizing monoclonal antibodies against three serotypes of porcine rotavirus J. Virol. 63 1989 3545 3549
    • (1989) J. Virol. , vol.63 , pp. 3545-3549
    • Nagesha, H.S.1    Brown, L.E.2    Holmes, I.H.3
  • 51
    • 0022051276 scopus 로고
    • Neutralizing monoclonal antibodies to human rotavirus and indications of antigenic drift among strains from neonates
    • B.S. Coulson, K.J. Fowler, R.F. Bishop, and R.G. Cotton Neutralizing monoclonal antibodies to human rotavirus and indications of antigenic drift among strains from neonates J. Virol. 54 1985 14 20
    • (1985) J. Virol. , vol.54 , pp. 14-20
    • Coulson, B.S.1    Fowler, K.J.2    Bishop, R.F.3    Cotton, R.G.4
  • 52
    • 0022449164 scopus 로고
    • Derivation of neutralizing monoclonal antibodies to human rotaviruses and evidence that an immunodominant neutralization site is shared between serotypes 1 and 3
    • B.S. Coulson, J.M. Tursi, W.J. McAdam, and R.F. Bishop Derivation of neutralizing monoclonal antibodies to human rotaviruses and evidence that an immunodominant neutralization site is shared between serotypes 1 and 3 Virology 154 1986 302 312
    • (1986) Virology , vol.154 , pp. 302-312
    • Coulson, B.S.1    Tursi, J.M.2    McAdam, W.J.3    Bishop, R.F.4
  • 53
    • 0023096371 scopus 로고
    • Simple and specific enzyme immunoassay using monoclonal antibodies for serotyping human rotaviruses
    • B.S. Coulson, L.E. Unicomb, G.A. Pitson, and R.F. Bishop Simple and specific enzyme immunoassay using monoclonal antibodies for serotyping human rotaviruses J. Clin. Microbiol. 25 1987 509 515
    • (1987) J. Clin. Microbiol. , vol.25 , pp. 509-515
    • Coulson, B.S.1    Unicomb, L.E.2    Pitson, G.A.3    Bishop, R.F.4
  • 54
    • 0034705379 scopus 로고    scopus 로고
    • Vascular endothelial junction-associated molecule, a novel member of the immunoglobulin superfamily, is localized to intercellular boundaries of endothelial cells
    • D. Palmeri, A. van Zante, C.C. Huang, S. Hemmerich, and S.D. Rosen Vascular endothelial junction-associated molecule, a novel member of the immunoglobulin superfamily, is localized to intercellular boundaries of endothelial cells J. Biol. Chem. 275 2000 19139 19145
    • (2000) J. Biol. Chem. , vol.275 , pp. 19139-19145
    • Palmeri, D.1    Van Zante, A.2    Huang, C.C.3    Hemmerich, S.4    Rosen, S.D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.