메뉴 건너뛰기




Volumn 16, Issue 4, 1997, Pages 143-151

Structural basis of integrin-mediated signal transduction

Author keywords

Integrin; Ligand binding; Signal transduction

Indexed keywords

CATION; EPITOPE; INTEGRIN; LIGAND; PROTEIN SUBUNIT;

EID: 0031259184     PISSN: 0945053X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0945-053X(97)90002-0     Document Type: Short Survey
Times cited : (35)

References (61)
  • 2
    • 0028858576 scopus 로고
    • Monoclonal antibody 9EG7 defines a novel β1 integrin epitope induced by soluble ligand and manganese, but inhibited by calcium
    • Bazzoni G., Shih D.T., Buck C.A., Hemler M.E. Monoclonal antibody 9EG7 defines a novel β1 integrin epitope induced by soluble ligand and manganese, but inhibited by calcium. J. Biol. Chem. 270:1995;25570-25577.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25570-25577
    • Bazzoni, G.1    Shih, D.T.2    Buck, C.A.3    Hemler, M.E.4
  • 4
    • 0026594737 scopus 로고
    • Binding of glycoprotein IIIa-derived peptide 217-231 to fibrinogen and von Willebrand factors and its inhibition by platelet glycoprotein IIb/IIIa complex
    • Cook J., Trybulec M., Lasz E., Khan S., Niewiarowski S. Binding of glycoprotein IIIa-derived peptide 217-231 to fibrinogen and von Willebrand factors and its inhibition by platelet glycoprotein IIb/IIIa complex. Biochim. Biophys. A. 1119:1992;312-321.
    • (1992) Biochim. Biophys. A. , vol.1119 , pp. 312-321
    • Cook, J.1    Trybulec, M.2    Lasz, E.3    Khan, S.4    Niewiarowski, S.5
  • 5
    • 0024280898 scopus 로고
    • Localization of an Arg-Gly-Asp recognition site within an integrin adhesion receptor
    • D'Souza S., Ginsberg M.H., Burke T.A., Lam S.C.-T., Plow E.F. Localization of an Arg-Gly-Asp recognition site within an integrin adhesion receptor. Science. 242:1988;91-93.
    • (1988) Science , vol.242 , pp. 91-93
    • D'Souza, S.1    Ginsberg, M.H.2    Burke, T.A.3    Lam, S.C.-T.4    Plow, E.F.5
  • 6
    • 0025216612 scopus 로고
    • The ligand binding site of the platelet integrin receptor GPIIb-IIIa is proximal to the second calcium binding domain of its α subunit
    • D'Souza S., Ginsberg M.H., Burke T.A., Plow E.F. The ligand binding site of the platelet integrin receptor GPIIb-IIIa is proximal to the second calcium binding domain of its α subunit. J. Biol. Chem. 265:1990;3440-3446.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3440-3446
    • D'Souza, S.1    Ginsberg, M.H.2    Burke, T.A.3    Plow, E.F.4
  • 7
    • 0026035464 scopus 로고
    • A discrete sequence in a platelet integrin is involved in ligand recognition
    • D'Souza S., Ginsberg M.H., Matsueda G.R., Plow E.F. A discrete sequence in a platelet integrin is involved in ligand recognition. Nature. 350:1991;66.
    • (1991) Nature , vol.350 , pp. 66
    • D'Souza, S.1    Ginsberg, M.H.2    Matsueda, G.R.3    Plow, E.F.4
  • 8
    • 0028077510 scopus 로고
    • Ligand and cation binding are dual functions of a discrete segment of the integrin β3 subunit: Cation displacement from this site is implicated in ligand binding
    • D'Souza S.E., Haas T.A., Piotrowicz R.S., Byers-Ward V., McGrath E., et al. Ligand and cation binding are dual functions of a discrete segment of the integrin β3 subunit: cation displacement from this site is implicated in ligand binding. Cell. 79:1994;659-667.
    • (1994) Cell , vol.79 , pp. 659-667
    • D'Souza, S.E.1    Haas, T.A.2    Piotrowicz, R.S.3    Byers-Ward, V.4    McGrath, E.5
  • 9
    • 0027530684 scopus 로고
    • The I-domain is a major recognition site on the leukocyte integrin Mac-1 (CD11b/CD18) for four distinct adhesion ligands
    • Diamond M.S., Garcia-Aguilar J., Bickford J.K., Corbi A.L., Springer T.A. The I-domain is a major recognition site on the leukocyte integrin Mac-1 (CD11b/CD18) for four distinct adhesion ligands. J. Cell Biol. 120:1993;1031-1043.
    • (1993) J. Cell Biol. , vol.120 , pp. 1031-1043
    • Diamond, M.S.1    Garcia-Aguilar, J.2    Bickford, J.K.3    Corbi, A.L.4    Springer, T.A.5
  • 10
    • 16944367173 scopus 로고    scopus 로고
    • Contribution of the I and EF hand domains to the divalent cation-dependent collagen binding activity of the α2β1 integrin
    • Dickenson S.K., Walsh J.J., Santoro S.A. Contribution of the I and EF hand domains to the divalent cation-dependent collagen binding activity of the α2β1 integrin. J. Biol. Chem. 272:1997;7661-7668.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7661-7668
    • Dickenson, S.K.1    Walsh, J.J.2    Santoro, S.A.3
  • 11
    • 0027525561 scopus 로고
    • Long range propagation of conformational changes in integrin αIIbβ3
    • Du X., Gu M., Weisel J., Nagaswami C., Bennett J., et al. Long range propagation of conformational changes in integrin αIIbβ3. J. Biol. Chem. 268:1993;23087-23092.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23087-23092
    • Du, X.1    Gu, M.2    Weisel, J.3    Nagaswami, C.4    Bennett, J.5
  • 12
    • 0029796131 scopus 로고    scopus 로고
    • Identifying the putative metal ion-dependent adhesion site in the β2 (CD18) subunit required for aLb2 and aMb2 ligand interactions
    • Goodman T., Bajt M. Identifying the putative metal ion-dependent adhesion site in the β2 (CD18) subunit required for aLb2 and aMb2 ligand interactions. J. Biol. Chem. 271:1996;23729-23736.
    • (1996) J. Biol. Chem. , vol.271 , pp. 23729-23736
    • Goodman, T.1    Bajt, M.2
  • 13
    • 0025218924 scopus 로고
    • VLA proteins in the integrin family:structures, functions, and their role on leukocytes
    • Hemler M.E. VLA proteins in the integrin family:structures, functions, and their role on leukocytes. Ann. Rev. Immunol. 8:1990;365-400.
    • (1990) Ann. Rev. Immunol. , vol.8 , pp. 365-400
    • Hemler, M.E.1
  • 14
    • 0029039630 scopus 로고
    • Topography of ligand-induced binding sites, including a novel cation-sensitive epitope (AP5) at the amino terminus, of the human integrin β3 subunit
    • Honda S., Tomiyama Y., Pelletier A., Annis D., Honda Y., et al. Topography of ligand-induced binding sites, including a novel cation-sensitive epitope (AP5) at the amino terminus, of the human integrin β3 subunit. J. Biol. Chem. 270:1995;11947-11954.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11947-11954
    • Honda, S.1    Tomiyama, Y.2    Pelletier, A.3    Annis, D.4    Honda, Y.5
  • 15
    • 0029351899 scopus 로고
    • A point mutation in the integrin beta 6 subunit abolishes both αvβ6 binding to fibronectin and receptor localization to focal contacts
    • Huang X., Chen A., Agrez M., Sheppard D. A point mutation in the integrin beta 6 subunit abolishes both αvβ6 binding to fibronectin and receptor localization to focal contacts. Am. J. Resp. Cell Mol. Biol. 13:1995;245-251.
    • (1995) Am. J. Resp. Cell Mol. Biol. , vol.13 , pp. 245-251
    • Huang, X.1    Chen, A.2    Agrez, M.3    Sheppard, D.4
  • 17
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation and signaling in cell adhesion
    • Hynes R.O. Integrins: versatility, modulation and signaling in cell adhesion. Cell. 69:1992;11-25.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 18
    • 0028805249 scopus 로고
    • Critical amino acid residues for ligand binding are clustered in a predicted β-turn of the third amino-terminal repeat in the integrin α4 and α5 subunits
    • Irie A., Kamata T., Puzon-McLaughlin W., Takada Y. Critical amino acid residues for ligand binding are clustered in a predicted β-turn of the third amino-terminal repeat in the integrin α4 and α5 subunits. EMBO J. 14:1995;5542-5549.
    • (1995) EMBO J. , vol.14 , pp. 5542-5549
    • Irie, A.1    Kamata, T.2    Puzon-McLaughlin, W.3    Takada, Y.4
  • 19
    • 0030788570 scopus 로고    scopus 로고
    • Multiple loop structures critical for ligand binding of the integrin α4 subunit in the upper face of the β-propeller model
    • Irie A., Kamata T., Takada Y. Multiple loop structures critical for ligand binding of the integrin α4 subunit in the upper face of the β-propeller model. Proc. Natl. Acad. Sci. U.S.A. 94:1997;7198-7203.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 7198-7203
    • Irie, A.1    Kamata, T.2    Takada, Y.3
  • 20
    • 0029780525 scopus 로고    scopus 로고
    • Critical residues of the αIIb subunit of integrin αIIβ3 (GPIIb-IIIa) for binding to fibrinogen and ligand-mimetic antibodies (PAC-1, OP-G2 and LJ-CP3)
    • Kamata T., Irie A., Takada Y. Critical residues of the αIIb subunit of integrin αIIβ3 (GPIIb-IIIa) for binding to fibrinogen and ligand-mimetic antibodies (PAC-1, OP-G2 and LJ-CP3). J. Biol. Chem. 271:1996;18610-18615.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18610-18615
    • Kamata, T.1    Irie, A.2    Takada, Y.3
  • 21
    • 0028225987 scopus 로고
    • Identification of putative ligand binding sites within I-domain of integrin α2β1 (VLA-2, CD49b/CD29)
    • Kamata T., Puzon W., Takada Y. Identification of putative ligand binding sites within I-domain of integrin α2β1 (VLA-2, CD49b/CD29). J. Biol. Chem. 269:1994;9659-9663.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9659-9663
    • Kamata, T.1    Puzon, W.2    Takada, Y.3
  • 22
    • 0028900673 scopus 로고
    • Identification of putative ligand binding sites of the integrin α4β1 (VLA-4, CD49d/CD29)
    • Kamata T., Puzon W., Takada Y. Identification of putative ligand binding sites of the integrin α4β1 (VLA-4, CD49d/CD29). Biochem. J. 305:1995;945-951.
    • (1995) Biochem. J. , vol.305 , pp. 945-951
    • Kamata, T.1    Puzon, W.2    Takada, Y.3
  • 23
    • 0028075817 scopus 로고
    • Direct binding of collagen to the I-domain of integrin α2β1 (VLA-2, CD49b/CD29) in a divalent cation-independent manner
    • Kamata T., Takada Y. Direct binding of collagen to the I-domain of integrin α2β1 (VLA-2, CD49b/CD29) in a divalent cation-independent manner. J. Biol. Chem. 269:1994;26006-26010.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26006-26010
    • Kamata, T.1    Takada, Y.2
  • 24
    • 0029015716 scopus 로고
    • Critical Thr and Asp residues within the I-domains of β2 integrins for interactions with ICAM-1 and C3bi
    • Kamata T., Wright R., Takada Y. Critical Thr and Asp residues within the I-domains of β2 integrins for interactions with ICAM-1 and C3bi. J. Biol. Chem. 270:1995;12531-12535.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12531-12535
    • Kamata, T.1    Wright, R.2    Takada, Y.3
  • 25
    • 0027933588 scopus 로고
    • The role of the I-domain in ligand binding of the human integrin α1β1
    • Kern A., Briesewitz R., Bank I., Marcantonio E. The role of the I-domain in ligand binding of the human integrin α1β1. J. Biol. Chem. 269:1994;22811-22816.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22811-22816
    • Kern, A.1    Briesewitz, R.2    Bank, I.3    Marcantonio, E.4
  • 26
    • 0027502939 scopus 로고
    • A novel LFA-1 activation epitope maps to the I-domain
    • Landis R., Bennett R., Hogg N. A novel LFA-1 activation epitope maps to the I-domain. J. Cell Biol. 120:1993;1519-1527.
    • (1993) J. Cell Biol. , vol.120 , pp. 1519-1527
    • Landis, R.1    Bennett, R.2    Hogg, N.3
  • 27
    • 0027337581 scopus 로고
    • Beta 3 integrin derived peptide 217-230 inhibits fibrinogen binding and platelet aggregation: Significance of RGD sequences and fibrinogen A alpha-chain
    • Lasz E., McLane M., Trybulec M., Kowalska M., Khan S., et al. Beta 3 integrin derived peptide 217-230 inhibits fibrinogen binding and platelet aggregation: significance of RGD sequences and fibrinogen A alpha-chain. Biochem. Biophys. Res. Commun. 190:1993;118-124.
    • (1993) Biochem. Biophys. Res. Commun. , vol.190 , pp. 118-124
    • Lasz, E.1    McLane, M.2    Trybulec, M.3    Kowalska, M.4    Khan, S.5
  • 28
    • 0028986196 scopus 로고
    • Crystal structure of the A domain from the a subunit of integrin CR3 (CD11b/CD18)
    • Lee J.-O., Rieu P., Arnaout M.A., Liddington R. Crystal structure of the A domain from the a subunit of integrin CR3 (CD11b/CD18). Cell. 80:1995;631-638.
    • (1995) Cell , vol.80 , pp. 631-638
    • Lee, J.-O.1    Rieu, P.2    Arnaout, M.A.3    Liddington, R.4
  • 30
    • 0027972994 scopus 로고
    • Integrin-mediated cell adhesion: The extracellular face
    • Loftus J.C., Smith J.W., Ginsberg M.H. Integrin-mediated cell adhesion: the extracellular face. J. Biol. Chem. 269:1994;25235-25238.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25235-25238
    • Loftus, J.C.1    Smith, J.W.2    Ginsberg, M.H.3
  • 31
    • 15844363687 scopus 로고    scopus 로고
    • Activated conformations of VLA integrins detected by a group of antibodies specific for a novel regulatory region (355-425) of the common β1 chain
    • Luque A., Gomez-Gutierrez M., Puzon W., Takada Y., Sanchez-Madrid F., Cabanas C. Activated conformations of VLA integrins detected by a group of antibodies specific for a novel regulatory region (355-425) of the common β1 chain. J. Biol. Chem. 271:1996;11067-11075.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11067-11075
    • Luque, A.1    Gomez-Gutierrez, M.2    Puzon, W.3    Takada, Y.4    Sanchez-Madrid, F.5    Cabanas, C.6
  • 32
    • 0027483226 scopus 로고
    • A novel divalent cation-binding site in the A domain of the β2 integrin CR3 (CD11b/CD18) is essential for ligand binding
    • Michishita M., Videm V., Arnaout M.A. A novel divalent cation-binding site in the A domain of the β2 integrin CR3 (CD11b/CD18) is essential for ligand binding. Cell. 72:1993;857-867.
    • (1993) Cell , vol.72 , pp. 857-867
    • Michishita, M.1    Videm, V.2    Arnaout, M.A.3
  • 33
    • 0028954797 scopus 로고
    • Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function
    • Miyamoto S., Akiyama S.K., Yamada K.M. Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function. Science. 267:1995;883-885.
    • (1995) Science , vol.267 , pp. 883-885
    • Miyamoto, S.1    Akiyama, S.K.2    Yamada, K.M.3
  • 34
    • 0028801218 scopus 로고
    • Integrin function: Molecular hierarchies of cytoskeletal and signaling molecules
    • Miyamoto S., Teramoto H., Coso O.A., Gutkind J.S., Burbelo P.D., et al. Integrin function: Molecular hierarchies of cytoskeletal and signaling molecules. J. Cell Biol. 131:1995;791-805.
    • (1995) J. Cell Biol. , vol.131 , pp. 791-805
    • Miyamoto, S.1    Teramoto, H.2    Coso, O.A.3    Gutkind, J.S.4    Burbelo, P.D.5
  • 35
    • 0029664954 scopus 로고    scopus 로고
    • The inhibitory anti-β1 integrin monoclonal antibody 13 recognizes an epitope that is attenuated by ligand occupancy: Evidence for allosteric inhibition of integrin function
    • Mould A., Akiyama S., Humphries M. The inhibitory anti-β1 integrin monoclonal antibody 13 recognizes an epitope that is attenuated by ligand occupancy: evidence for allosteric inhibition of integrin function. J. Biol. Chem. 271:1996;20365-20374.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20365-20374
    • Mould, A.1    Akiyama, S.2    Humphries, M.3
  • 36
    • 0030798854 scopus 로고    scopus 로고
    • Defining the topology of integrin α5β1-fibronectin interactions using inhibitory anti-α5 and anti-β1 monoclonal antibodies: Evidence that the synergy sequence of fibronectin is recognized by the N-terminal repeats of the α5 subunit
    • Mould A.P., Askari J.A., Aota S.I., Yamada K.M., Irie A., Takada Y., Mardon H.J., Humphries M.J. Defining the topology of integrin α5β1-fibronectin interactions using inhibitory anti-α5 and anti-β1 monoclonal antibodies: Evidence that the synergy sequence of fibronectin is recognized by the N-terminal repeats of the α5 subunit. J. Biol. Chem. 272:1997;17283-17292.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17283-17292
    • Mould, A.P.1    Askari, J.A.2    Aota, S.I.3    Yamada, K.M.4    Irie, A.5    Takada, Y.6    Mardon, H.J.7    Humphries, M.J.8
  • 37
    • 0028020563 scopus 로고
    • Functional interaction between the integrin antagonist neutrophil inhibitory factor and the I-domain of CD11b/CD18
    • Muchowski P.J., Zhang L., Chang E.R., Soule H.R., Plow E.F., Moyle M. Functional interaction between the integrin antagonist neutrophil inhibitory factor and the I-domain of CD11b/CD18. J. Biol. Chem. 269:1994;26419-26423.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26419-26423
    • Muchowski, P.J.1    Zhang, L.2    Chang, E.R.3    Soule, H.R.4    Plow, E.F.5    Moyle, M.6
  • 38
    • 0029120428 scopus 로고
    • A peptide isolated from phage display libraries is a structural and functional mimic of an RGD-binding site on integrins
    • Pasqualini R., Koivunen E., Ruoslahti E. A peptide isolated from phage display libraries is a structural and functional mimic of an RGD-binding site on integrins. J. Cell Biol. 130:1995;1189-1196.
    • (1995) J. Cell Biol. , vol.130 , pp. 1189-1196
    • Pasqualini, R.1    Koivunen, E.2    Ruoslahti, E.3
  • 39
    • 0029786408 scopus 로고    scopus 로고
    • Critical residues for ligand binding in the integrin b1 subunit
    • Puzon-McLaughlin W., Takada Y. Critical residues for ligand binding in the integrin b1 subunit. J. Biol. Chem. 271:1996;20438-20443.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20438-20443
    • Puzon-McLaughlin, W.1    Takada, Y.2
  • 40
    • 0029953173 scopus 로고    scopus 로고
    • Regulation of conformation and ligand binding function of integrin α5β1 by the β1 cytoplasmic domain
    • Puzon-McLaughlin W., Yednock T., Takada Y. Regulation of conformation and ligand binding function of integrin α5β1 by the β1 cytoplasmic domain. J. Biol. Chem. 271:1996;16580-16585.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16580-16585
    • Puzon-McLaughlin, W.1    Yednock, T.2    Takada, Y.3
  • 41
    • 0028822128 scopus 로고
    • Crystal structure of the I-domain of the CD11a/CD18 (LFA-1, αLβ2) integrin
    • Qu A., Leahy D.J. Crystal structure of the I-domain of the CD11a/CD18 (LFA-1, αLβ2) integrin. Proc. Natl. Acad. Sci. USA. 92:1995;10277-10281.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10277-10281
    • Qu, A.1    Leahy, D.J.2
  • 42
    • 0028180681 scopus 로고
    • I-domain of β2 integrin lymphocyte function associated antigen-1 contains a binding site for ligand intercellular adhesion molecule-1
    • Randi A.M., Hogg N. I-domain of β2 integrin lymphocyte function associated antigen-1 contains a binding site for ligand intercellular adhesion molecule-1. J. Biol. Chem. 269:1994;12395-12398.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12395-12398
    • Randi, A.M.1    Hogg, N.2
  • 43
    • 0028557171 scopus 로고
    • The A-domain of β2 integrin CR3(CD11b/CD18) is a receptor for the hookworm-derived neutrophil adhesion inhibitor NIF
    • Rieu P., Ueda T., Haruta I., Sharma C.P., Arnaout M.A. The A-domain of β2 integrin CR3(CD11b/CD18) is a receptor for the hookworm-derived neutrophil adhesion inhibitor NIF. J. Cell Biol. 127:1994;2081-2091.
    • (1994) J. Cell Biol. , vol.127 , pp. 2081-2091
    • Rieu, P.1    Ueda, T.2    Haruta, I.3    Sharma, C.P.4    Arnaout, M.A.5
  • 45
    • 0029060141 scopus 로고
    • Molecular mapping of functional antibody binding sites of α4 integrin
    • Schiffer S., Hemler M., Lobb R., Tizard R., Osborn L. Molecular mapping of functional antibody binding sites of α4 integrin. J. Biol. Chem. 270:1995;14270-14273.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14270-14273
    • Schiffer, S.1    Hemler, M.2    Lobb, R.3    Tizard, R.4    Osborn, L.5
  • 46
    • 0025062198 scopus 로고
    • Integrin (αVβ3) ligand interaction: Identification of a divalent cation-dependent heterodimeric RGD binding site on the vitronectin receptor
    • Smith J.W., Cheresh D.A. Integrin (αVβ3) ligand interaction: Identification of a divalent cation-dependent heterodimeric RGD binding site on the vitronectin receptor. J. Biol. Chem. 265:1990;2168-2172.
    • (1990) J. Biol. Chem. , vol.265 , pp. 2168-2172
    • Smith, J.W.1    Cheresh, D.A.2
  • 47
    • 0027982876 scopus 로고
    • Traffic signals for lymphocyte recirculation and leukocyte emigration: The multistep paradigm
    • Springer T.A. Traffic signals for lymphocyte recirculation and leukocyte emigration: the multistep paradigm. Cell. 76:1994;301-314.
    • (1994) Cell , vol.76 , pp. 301-314
    • Springer, T.A.1
  • 48
    • 0031013031 scopus 로고    scopus 로고
    • Folding of the N-terminal, ligand binding region of integrin α subunits into a β-propeller domain
    • Springer T. Folding of the N-terminal, ligand binding region of integrin α subunits into a β-propeller domain. Proc. Natl. Acad. Sci. USA. 94:1997;65-72.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 65-72
    • Springer, T.1
  • 49
    • 0027534578 scopus 로고
    • Peptides derived from a sequence within beta 3 integrin bind to platelet alpha IIb beta 3 (GPIIb-IIIa) and inhibit ligand binding
    • Steiner B., Trzeciak A., Pfenninger G., Kouns W. Peptides derived from a sequence within beta 3 integrin bind to platelet alpha IIb beta 3 (GPIIb-IIIa) and inhibit ligand binding. J. Biol. Chem. 268:1993;6870-6873.
    • (1993) J. Biol. Chem. , vol.268 , pp. 6870-6873
    • Steiner, B.1    Trzeciak, A.2    Pfenninger, G.3    Kouns, W.4
  • 50
    • 0027248518 scopus 로고
    • Identification of a regulatory region of integrin β1 subunit using activating and inhibiting antibodies
    • Takada Y., Puzon W. Identification of a regulatory region of integrin β1 subunit using activating and inhibiting antibodies. J. Biol. Chem. 268:1993;17597-17601.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17597-17601
    • Takada, Y.1    Puzon, W.2
  • 51
    • 0026460174 scopus 로고
    • A point mutation of integrin β1 subunit blocks binding of α5β1 to fibronectin and invasin but not recruitment to adhesion plaques
    • Takada Y., Ylänne J., Mandelman D., Puzon W., Ginsberg M. A point mutation of integrin β1 subunit blocks binding of α5β1 to fibronectin and invasin but not recruitment to adhesion plaques. J. Cell Biol. 119:1992;913-921.
    • (1992) J. Cell Biol. , vol.119 , pp. 913-921
    • Takada, Y.1    Ylänne, J.2    Mandelman, D.3    Puzon, W.4    Ginsberg, M.5
  • 52
    • 0030913268 scopus 로고    scopus 로고
    • Structural interlock between ligand-binding site and stalk-like region of β1 integrin revealed by a monoclonal antibody recognizing conformation-dependent epitope
    • Takagi J., Isobe T., Takada Y., Saito Y. Structural interlock between ligand-binding site and stalk-like region of β1 integrin revealed by a monoclonal antibody recognizing conformation-dependent epitope. J. Biochem. 121:1997;914-921.
    • (1997) J. Biochem. , vol.121 , pp. 914-921
    • Takagi, J.1    Isobe, T.2    Takada, Y.3    Saito, Y.4
  • 53
    • 0030856555 scopus 로고    scopus 로고
    • Changing ligand specificities of αvβ1 and αvβ3 integrins by swapping a short diverse sequence of β subunit
    • Takagi J., Kamata T., Meredith J., Puzon-McLaughlin W., Takda Y. Changing ligand specificities of αvβ1 and αvβ3 integrins by swapping a short diverse sequence of β subunit. J. Biol. Chem. 272:1997;19794-19800.
    • (1997) J. Biol. Chem. , vol.272 , pp. 19794-19800
    • Takagi, J.1    Kamata, T.2    Meredith, J.3    Puzon-McLaughlin, W.4    Takda, Y.5
  • 54
    • 0029786892 scopus 로고    scopus 로고
    • Ligand binding to integrin αIIbβ3 is dependent on a MIDAS like domain in the β3 subunit
    • Tozer E., Liddington R., Sutcliffe M., Smeeton A., Loftus J. Ligand binding to integrin αIIbβ3 is dependent on a MIDAS like domain in the β3 subunit. J. Biol. Chem. 271:1996;21978-21984.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21978-21984
    • Tozer, E.1    Liddington, R.2    Sutcliffe, M.3    Smeeton, A.4    Loftus, J.5
  • 56
    • 0031029272 scopus 로고    scopus 로고
    • A structure prediction for the ligand-binding region of the integrin β subunit: Evidence for the presence of a von Willebrand factor A domain
    • Tuckwell D., Humphries M. A structure prediction for the ligand-binding region of the integrin β subunit: evidence for the presence of a von Willebrand factor A domain. FEBS Lett. 400:1997;297-303.
    • (1997) FEBS Lett. , vol.400 , pp. 297-303
    • Tuckwell, D.1    Humphries, M.2
  • 57
    • 0028130314 scopus 로고
    • Identification of the complement iC3b binding site in the β2 integrin CR3 (CD11b/CD18)
    • Ueda T., Rieu P., Brayer J., Arnaout M.A. Identification of the complement iC3b binding site in the β2 integrin CR3 (CD11b/CD18). Proc. Natl. Acad. Sci. USA. 91:1994;10680-10684.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10680-10684
    • Ueda, T.1    Rieu, P.2    Brayer, J.3    Arnaout, M.A.4
  • 58
    • 0025734184 scopus 로고
    • Adhesive recognition sequences
    • Yamada K.M. Adhesive recognition sequences. J. Biol. Chem. 266:1991;12809-12812.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12809-12812
    • Yamada, K.M.1
  • 59
    • 0029164237 scopus 로고
    • Integrin transmembrane signaling and cytoskeletal control
    • Yamada K.M., Miyamoto S. Integrin transmembrane signaling and cytoskeletal control. Curr. Opin. Cell Biol. 7:1995;681-689.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 681-689
    • Yamada, K.M.1    Miyamoto, S.2
  • 60
    • 0028973093 scopus 로고
    • α4β1 integrin-dependent cell adhesion is regulated by a low affinity receptor pool that is conformationally responsive to ligand
    • Yednock T.A., Cannon C., Vandevert C., Goldbach E.G., Shaw G., et al. α4β1 integrin-dependent cell adhesion is regulated by a low affinity receptor pool that is conformationally responsive to ligand. J. Biol. Chem. 270:1995;28740-28750.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28740-28750
    • Yednock, T.A.1    Cannon, C.2    Vandevert, C.3    Goldbach, E.G.4    Shaw, G.5
  • 61
    • 0028241856 scopus 로고
    • Differential ligand binding specificities of recombinant CD11b/CD18 integrin I-domain
    • Zhou L., Lee D.H.S., Plescia J., Lau C.Y., Altieri D.C. Differential ligand binding specificities of recombinant CD11b/CD18 integrin I-domain. J. Biol. Chem. 269:1994;17075-17079.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17075-17079
    • Zhou, L.1    Lee, D.H.S.2    Plescia, J.3    Lau, C.Y.4    Altieri, D.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.