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Volumn 72, Issue 11, 1998, Pages 8669-8675

Interactions of soluble recombinant integrin αvβ5 with human adenoviruses

Author keywords

[No Author keywords available]

Indexed keywords

ARGINYLGLYCYLASPARTIC ACID; INTEGRIN; MATRIX PROTEIN; RECEPTOR PROTEIN; SYNTHETIC PEPTIDE; VITRONECTIN;

EID: 0031691062     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.72.11.8669-8675.1998     Document Type: Article
Times cited : (68)

References (37)
  • 1
    • 0031984752 scopus 로고    scopus 로고
    • Pervasive conformational fluctuations on microsecond time scales in a fibronectin type III domain
    • Akke, M., J. Liu, J. Cavanagh, H. P. Erickson, and A. G. Palmer III. 1998. Pervasive conformational fluctuations on microsecond time scales in a fibronectin type III domain. Nat. Struct. Biol. 5:55-59.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 55-59
    • Akke, M.1    Liu, J.2    Cavanagh, J.3    Erickson, H.P.4    Palmer III, A.G.5
  • 2
    • 0028145867 scopus 로고
    • Vitronectin receptor antibodies inhibit infection of HeLa and A549 cells by adenovirus type 12 but not by adenovirus type 2
    • Bai, M., L. Campisi, and P. Freimuth. 1994. Vitronectin receptor antibodies inhibit infection of HeLa and A549 cells by adenovirus type 12 but not by adenovirus type 2. J. Virol. 68:5925-5932.
    • (1994) J. Virol. , vol.68 , pp. 5925-5932
    • Bai, M.1    Campisi, L.2    Freimuth, P.3
  • 3
    • 0027221062 scopus 로고
    • Mutations that alter an Arg-Gly-Asp (RGD) sequence in the adenovirus type 2 penton base protein abolish its cell-rounding activity and delay virus reproduction in flat cells
    • Bai, M., B. Harfe, and P. Freimuth. 1993. Mutations that alter an Arg-Gly-Asp (RGD) sequence in the adenovirus type 2 penton base protein abolish its cell-rounding activity and delay virus reproduction in flat cells. J. Virol. 67:5198-5205.
    • (1993) J. Virol. , vol.67 , pp. 5198-5205
    • Bai, M.1    Harfe, B.2    Freimuth, P.3
  • 5
    • 0026580865 scopus 로고
    • Identification of the integrin VLA-2 as a receptor for echovirus I
    • Bergelson, J. M., M. P. Shepley, B. M. C. Chan, M. E. Hemler, and R. W. Finberg. 1992. Identification of the integrin VLA-2 as a receptor for echovirus I. Science 255:1718-1720.
    • (1992) Science , vol.255 , pp. 1718-1720
    • Bergelson, J.M.1    Shepley, M.P.2    Chan, B.M.C.3    Hemler, M.E.4    Finberg, R.W.5
  • 6
    • 3543098119 scopus 로고    scopus 로고
    • Submitted for publication
    • Chiu, C., et al. Submitted for publication.
    • Chiu, C.1
  • 9
    • 0017336387 scopus 로고
    • Synthesis and processing of the precursor to the major core protein of adenovirus type 2
    • Everitt, E., S. A. Meador, and A. S. Levine. 1977. Synthesis and processing of the precursor to the major core protein of adenovirus type 2. J. Virol. 21: 199-214.
    • (1977) J. Virol. , vol.21 , pp. 199-214
    • Everitt, E.1    Meador, S.A.2    Levine, A.S.3
  • 11
    • 0030695436 scopus 로고    scopus 로고
    • Phagocytosis of rod outer segments by retinal pigment epithelial cells requires αvβ5 integrin for binding but not for internalization
    • Finnemann, S. C., V. L. Bonilha, A. D. Marmorstein, and E. Rodriguez-Boulan. 1997. Phagocytosis of rod outer segments by retinal pigment epithelial cells requires αvβ5 integrin for binding but not for internalization. Proc. Natl. Acad. Sci. USA 94:12932-12937.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12932-12937
    • Finnemann, S.C.1    Bonilha, V.L.2    Marmorstein, A.D.3    Rodriguez-Boulan, E.4
  • 12
    • 0029794845 scopus 로고    scopus 로고
    • Gradient of RGD-dependent entry of adenoviral vector in nasal and intrapulmonary epithelia: Implications for gene therapy of cystic fibrosis
    • Goldman, M., Q. Su, and J. M. Wilson. 1996. Gradient of RGD-dependent entry of adenoviral vector in nasal and intrapulmonary epithelia: implications for gene therapy of cystic fibrosis. Gene Ther. 3:811-818.
    • (1996) Gene Ther. , vol.3 , pp. 811-818
    • Goldman, M.1    Su, Q.2    Wilson, J.M.3
  • 13
    • 0028981979 scopus 로고
    • Expression of αvβ5 integrin is necessary for efficient adenovirus-mediated gene transfer in the human airway
    • Goldman, M. J., and J. M. Wilson. 1995. Expression of αvβ5 integrin is necessary for efficient adenovirus-mediated gene transfer in the human airway. J. Virol. 69:5951-5958.
    • (1995) J. Virol. , vol.69 , pp. 5951-5958
    • Goldman, M.J.1    Wilson, J.M.2
  • 14
    • 0026771406 scopus 로고
    • Adenoviruses in the immunocompromised host
    • Hierholzer, J. C. 1992. Adenoviruses in the immunocompromised host. Clin. Microbiol. Rev. 5:262-274.
    • (1992) Clin. Microbiol. Rev. , vol.5 , pp. 262-274
    • Hierholzer, J.C.1
  • 15
    • 0029939555 scopus 로고    scopus 로고
    • Adenovirus interaction with distinct integrins mediates separate events in cell entry and gene delivery to hematopoietic cells
    • Huang, S., T. Kamata, Y. Takada, Z. M. Ruggeri, and G. R. Nemerow. 1996. Adenovirus interaction with distinct integrins mediates separate events in cell entry and gene delivery to hematopoietic cells. J. Virol. 70:4502-4508.
    • (1996) J. Virol. , vol.70 , pp. 4502-4508
    • Huang, S.1    Kamata, T.2    Takada, Y.3    Ruggeri, Z.M.4    Nemerow, G.R.5
  • 16
    • 0030759829 scopus 로고    scopus 로고
    • Growth arrest of Epstein-Barr virus immortalized B lymphocytes by adenovirus-delivered ribozymes
    • Huang, S., D. G. Stupack, P. Mathias, Y. Wang, and G. Nemerow. 1997. Growth arrest of Epstein-Barr virus immortalized B lymphocytes by adenovirus-delivered ribozymes. Proc. Natl. Acad. Sci. USA 94:8156-8161.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 8156-8161
    • Huang, S.1    Stupack, D.G.2    Mathias, P.3    Wang, Y.4    Nemerow, G.5
  • 17
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signaling in cell adhesion
    • Hynes, R. O. 1992. Integrins: versatility, modulation, and signaling in cell adhesion. Cell 69:11-25.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 18
    • 0028912193 scopus 로고
    • The mechanism of phagocytic uptake promoted by invasin-integrin interaction
    • Isberg, R. R., and G. Tran Van Nhieu. 1995. The mechanism of phagocytic uptake promoted by invasin-integrin interaction. Trends Cell Biol. 120:120-124.
    • (1995) Trends Cell Biol. , vol.120 , pp. 120-124
    • Isberg, R.R.1    Tran Van Nhieu, G.2
  • 19
    • 0028001464 scopus 로고
    • Bordeltella pertussis filamentous hemagglutinin interacts with a leukocyte signal transduction complex and stimulates bacterial adherence to monocyte CR3 (CD11b/CD18)
    • Ishibashi, Y., S. Claus, and D. A. Relman. 1994. Bordeltella pertussis filamentous hemagglutinin interacts with a leukocyte signal transduction complex and stimulates bacterial adherence to monocyte CR3 (CD11b/CD18). J. Exp. Med. 180:1225-1233.
    • (1994) J. Exp. Med. , vol.180 , pp. 1225-1233
    • Ishibashi, Y.1    Claus, S.2    Relman, D.A.3
  • 21
    • 0028303125 scopus 로고
    • The structural bases of integrin-ligand interactions
    • Kühn, K., and J. Eble. 1994. The structural bases of integrin-ligand interactions. Trends Cell Biol. 4:256-261.
    • (1994) Trends Cell Biol. , vol.4 , pp. 256-261
    • Kühn, K.1    Eble, J.2
  • 22
    • 0027972994 scopus 로고
    • Integrin-mediated cell adhesion: The extracellular face
    • Loftus, J. W., J. C. Smith, and M. H. Ginsberg. 1994. Integrin-mediated cell adhesion: the extracellular face. J. Biol. Chem. 269:25235-25238.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25235-25238
    • Loftus, J.W.1    Smith, J.C.2    Ginsberg, M.H.3
  • 23
    • 0028201747 scopus 로고
    • RGD sequence of foot-and-mouth disease virus is essential for infecting cells via the natural receptor but can be bypassed by an antibody-dependent enhancement pathway
    • Mason, P. W., E. Rieder, and B. Baxt. 1994. RGD sequence of foot-and-mouth disease virus is essential for infecting cells via the natural receptor but can be bypassed by an antibody-dependent enhancement pathway. Proc. Natl. Acad. Sci. USA 91:1932-1936.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 1932-1936
    • Mason, P.W.1    Rieder, E.2    Baxt, B.3
  • 24
    • 0028086074 scopus 로고
    • Multiple adenovirus serotypes use αv integrins for infection
    • Mathias, P., T. J. Wickham, M. Moore, and G. Nemerow. 1994. Multiple adenovirus serotypes use αv integrins for infection. J. Virol. 68:6811-6814.
    • (1994) J. Virol. , vol.68 , pp. 6811-6814
    • Mathias, P.1    Wickham, T.J.2    Moore, M.3    Nemerow, G.4
  • 25
    • 0029807068 scopus 로고    scopus 로고
    • Molecular requirements for assembly and function of a minimized human integrin
    • McKay, B. S., D. S. Annis, S. Honda, D. Christie, and T. J. Kunicki. 1996. Molecular requirements for assembly and function of a minimized human integrin. J. Biol. Chem. 271:30544-30547.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30544-30547
    • McKay, B.S.1    Annis, D.S.2    Honda, S.3    Christie, D.4    Kunicki, T.J.5
  • 26
    • 0027601438 scopus 로고
    • Distribution of integrin cell adhesion receptors on normal bronchial epithelial cells and lung cancer cells in vitro and in vivo
    • Mette, S. A., J. Pilewski, C. A. Buck, and S. M. Albelda. 1993. Distribution of integrin cell adhesion receptors on normal bronchial epithelial cells and lung cancer cells in vitro and in vivo. Am. J. Respir. Cell Mol. Biol. 8:562-572.
    • (1993) Am. J. Respir. Cell Mol. Biol. , vol.8 , pp. 562-572
    • Mette, S.A.1    Pilewski, J.2    Buck, C.A.3    Albelda, S.M.4
  • 27
    • 0025248597 scopus 로고
    • Cloning, primary structure ana properties of a novel human integrin β subunit
    • Ramaswamy, H., and M. E. Hemler. 1990. Cloning, primary structure ana properties of a novel human integrin β subunit. EMBO J. 9:1561-1568.
    • (1990) EMBO J. , vol.9 , pp. 1561-1568
    • Ramaswamy, H.1    Hemler, M.E.2
  • 28
    • 0026018224 scopus 로고
    • RGD-dependent entry of coxsackievirus A9 into host cells and its bypass after cleavage of VP1 protein by intestinal proteases
    • Roivaninen, M., T. Hypiä, L. Pirainen, N. Kalkkinen, G. Stanway, and T. Hovi. 1991. RGD-dependent entry of coxsackievirus A9 into host cells and its bypass after cleavage of VP1 protein by intestinal proteases. J. Virol. 65: 4735-4740.
    • (1991) J. Virol. , vol.65 , pp. 4735-4740
    • Roivaninen, M.1    Hypiä, T.2    Pirainen, L.3    Kalkkinen, N.4    Stanway, G.5    Hovi, T.6
  • 29
    • 0023637601 scopus 로고
    • New perspectives in cell adhesion: RGD and integrins
    • Ruoslahti, E., and M. D. Pierschbacher. 1987. New perspectives in cell adhesion: RGD and integrins. Science 238:491-497.
    • (1987) Science , vol.238 , pp. 491-497
    • Ruoslahti, E.1    Pierschbacher, M.D.2
  • 30
    • 0025164935 scopus 로고
    • Vitronectin receptor-mediated phagocytosis of cells undergoing apoptosis
    • Savill, J., I. Dransfield, N. Hogg, and C. Haslett. 1990. Vitronectin receptor-mediated phagocytosis of cells undergoing apoptosis. Nature 343:170-173.
    • (1990) Nature , vol.343 , pp. 170-173
    • Savill, J.1    Dransfield, I.2    Hogg, N.3    Haslett, C.4
  • 31
    • 0025340173 scopus 로고
    • Purification and functional characterization of integrin αvβ5: An adhesion receptor for vitronectin
    • Smith, J. W., D. J. Vestal, S. V. Irwin, T. A. Burke, and D. A. Cheresh. 1990 Purification and functional characterization of integrin αvβ5: an adhesion receptor for vitronectin. J. Biol. Chem. 265:11008-11013.
    • (1990) J. Biol. Chem. , vol.265 , pp. 11008-11013
    • Smith, J.W.1    Vestal, D.J.2    Irwin, S.V.3    Burke, T.A.4    Cheresh, D.A.5
  • 32
    • 0031003549 scopus 로고    scopus 로고
    • Localization of an integrin binding motif (RGD) on adenovirus type 2 particles by cryo-electron microscopy
    • Stewart, P. L., C. Chiu, S. Huang, T. Muir, Y. Zhao, B. Chait, P. Mathias, and G. Nemerow. 1997. Localization of an integrin binding motif (RGD) on adenovirus type 2 particles by cryo-electron microscopy. EMBO J. 16:1189-1198.
    • (1997) EMBO J. , vol.16 , pp. 1189-1198
    • Stewart, P.L.1    Chiu, C.2    Huang, S.3    Muir, T.4    Zhao, Y.5    Chait, B.6    Mathias, P.7    Nemerow, G.8
  • 33
    • 2042439878 scopus 로고
    • cDNA and amino acid sequences of the cell adhesion protein receptor recognizing vitronectin reveal a transmembrane domain and homologies with other adhesion protein receptors
    • Suzuki, S., W. S. Argraves, R. Pytela, H. Arai, T. Krusius, M. D. Pierschbacher, and E. Ruoslahti. 1986. cDNA and amino acid sequences of the cell adhesion protein receptor recognizing vitronectin reveal a transmembrane domain and homologies with other adhesion protein receptors. Proc. Natl. Acad. Sci. USA 83:8614-8618.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 8614-8618
    • Suzuki, S.1    Argraves, W.S.2    Pytela, R.3    Arai, H.4    Krusius, T.5    Pierschbacher, M.D.6    Ruoslahti, E.7
  • 34
    • 0030915715 scopus 로고    scopus 로고
    • HCAR and MAR: The human and mouse cellular receptors for subgroup C adenoviruses and group B coxsackieviruses
    • Tomko, R. P., R. Xu, and L. Philipson. 1997. HCAR and MAR: the human and mouse cellular receptors for subgroup C adenoviruses and group B coxsackieviruses. Proc. Natl. Acad. Sci. USA 94:3352-3356.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3352-3356
    • Tomko, R.P.1    Xu, R.2    Philipson, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.