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A mechanism for divalent cation regulation of β3-integrins
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0029092311
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Intercellular adhesion molecule-2 (CD102) binds to the leukocyte integrin CD11b/CD18 through the A domain
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Xie J, Li R, Kotovuori P, Vermot-Desroches C, Wijdenes J, Arnaout MA, Nortamo P, Gahmberg CG: Intercellular adhesion molecule-2 (CD102) binds to the leukocyte integrin CD11b/CD18 through the A domain. J Immunol 1995, 155:3619-3628.
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Arnaout, M.A.6
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10
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0028986196
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Crystal structure of the a domain from the a subunit of integrin CR3 (CD11D/CD18)
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2+ ion in the crystal structure. Consensus hydropathy plots were used to predict the existence of an A-domain-like region in the putative integrin β subunit ligand-binding domain.
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Lee, J.-O.1
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11
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0029646107
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Two conformations of the integrin A-domain (I-domain): A pathway for activation?
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2+-occupied form in that the carboxy-terminal half of the module progressively changed pitch relative to the amino-terminal half and the carboxy-terminal helix was displaced by 10 Å relative to those domains that do not change. These findings are suggested to reflect inactive and ligand-occupied forms of the αA-domain.
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, vol.3
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Lee, J.-O.1
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12
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0028822128
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Crystal structure of the l-domain from the CD11a/CD18 (LFA-1, αLβ2) integrin
-
2+-occupied form of the integrin αL A-domain. This structure closely resembled the αM A-domain structure, the major difference being the presence of a very short version of the α5 helix in the αL A-domain.
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Qu, A.1
Leahy, D.J.2
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0027483226
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A novel divalent cation-binding site in the a domain of the β2 integrin CR3 (CD11b/CD18) is essential for ligand binding
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Michishita M, Videm V, Arnaout MA: A novel divalent cation-binding site in the A domain of the β2 integrin CR3 (CD11b/CD18) is essential for ligand binding. Cell 1993, 72:857-867.
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Michishita, M.1
Videm, V.2
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14
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0028075817
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Direct binding of collagen to the I domain of integrin α2β1 (VLA-2, CD49b/CD29) in a divalent cation-independent manner
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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 1994, 269:26006-26010.
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Kamata, T.1
Takada, Y.2
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15
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0028020563
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Functional interaction between the integrin antagonist neutrophil inhibitory factor and the I domain of CD11b/CD18
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Muchowski PJ, Zhang L, Chang ER, Soule HR, Plow EF, Moyle M: Functional interaction between the integrin antagonist neutrophil inhibitory factor and the I domain of CD11b/CD18. J Biol Chem 1994, 269:26419-26423.
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Muchowski, P.J.1
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Chang, E.R.3
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Plow, E.F.5
Moyle, M.6
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16
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0028557171
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The A-domain of β2 integrin CR3 (CD11b/CD18) is a receptor for the hookworm-derived neutrophil adhesion inhibitor NIF
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Rieu P, Ueda T, Haruta I, Sharma CP, Arnaout MA: The A-domain of β2 integrin CR3 (CD11b/CD18) is a receptor for the hookworm-derived neutrophil adhesion inhibitor NIF. J Cell Biol 1994, 127:2081-2091.
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Rieu, P.1
Ueda, T.2
Haruta, I.3
Sharma, C.P.4
Arnaout, M.A.5
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17
-
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0028130314
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Identification of the complement iC3b binding site in the β2 integrin CR3 (CD11b/CD18)
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Ueda T, Rieu P, Brayer J, Arnaout MA: Identification of the complement iC3b binding site in the β2 integrin CR3 (CD11b/CD18). Proc Natl Acad Sci USA 1994, 91:10680-10684.
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Ueda, T.1
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Brayer, J.3
Arnaout, M.A.4
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18
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0028987638
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Integrin α2 I-domain is a binding site for collagens
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Tuckwell D, Calderwood DA, Green U, Humphries MJ: Integrin α2 I-domain is a binding site for collagens. J Cell Sci 1995, 108:1629-1637.
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Tuckwell, D.1
Calderwood, D.A.2
Green, U.3
Humphries, M.J.4
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19
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0028225987
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Identification of putative ligand binding sites within I domain of integrin α2β1 (VLA-2, CD49b/CD29)
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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 1994, 269:9659-9663.
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Kamata, T.1
Puzon, W.2
Takada, Y.3
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20
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0027933588
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The role of the I domain in ligand binding of the human integrin α1β1
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Kern A, Briesewitz R, Bank I, Marcantonio EE: The role of the I domain in ligand binding of the human integrin α1β1. J Biol Chem 1994, 269:22811-22816.
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Kern, A.1
Briesewitz, R.2
Bank, I.3
Marcantonio, E.E.4
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21
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0029059228
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Identification of amino acids in the CD11a I-domain important for binding of the leukocyte function-associated antigen-1 (LFA-1) to intercellular adhesion molecule-1 (ICAM-1)
-
Edwards CP, Champe M, Gonzalez T, Wessinger ME, Spencer SA, Presta LG, Berman PW, Bodary SC: Identification of amino acids in the CD11a I-domain important for binding of the leukocyte function-associated antigen-1 (LFA-1) to intercellular adhesion molecule-1 (ICAM-1). J Biol Chem 1995, 270:12635-12640.
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Edwards, C.P.1
Champe, M.2
Gonzalez, T.3
Wessinger, M.E.4
Spencer, S.A.5
Presta, L.G.6
Berman, P.W.7
Bodary, S.C.8
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22
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0029015716
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Critical threonine and aspartic acid residues within the I domains of β2 integrins for interactions with intercellular adhesion molecule 1 (ICAM-1) and C3bi
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Kamata T, Wright R, Takada Y: Critical threonine and aspartic acid residues within the I domains of β2 integrins for interactions with intercellular adhesion molecule 1 (ICAM-1) and C3bi. J Biol Chem 1995, 270:12531-12535.
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J Biol Chem
, vol.270
, pp. 12531-12535
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Kamata, T.1
Wright, R.2
Takada, Y.3
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23
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0028803769
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Distinct ligand binding sites in the I domain of integrin αMβ2 that differentially affect a divalent cation-dependent conformation
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McGuire SL, Bajt ML: Distinct ligand binding sites in the I domain of integrin αMβ2 that differentially affect a divalent cation-dependent conformation. J Biol Chem 1995, 270:25866-25871.
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J Biol Chem
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McGuire, S.L.1
Bajt, M.L.2
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24
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0028861708
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Monoclonal antibodies that block the activity of leukocyte function-associated antigen 1 recognize three discrete epitopes in the inserted domain of CD11a
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Champe M, McIntyre BW, Berman PW: Monoclonal antibodies that block the activity of leukocyte function-associated antigen 1 recognize three discrete epitopes in the inserted domain of CD11a. J Biol Chem 1995, 270:1388-1394.
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Champe, M.1
McIntyre, B.W.2
Berman, P.W.3
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25
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0029059578
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A binding interface on the I domain of lymphocyte function-associated antigen-1 (LFA-1) required for specific interaction with intercellular adhesion molecule 1 (ICAM-1)
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Huang C, Springer TA: A binding interface on the I domain of lymphocyte function-associated antigen-1 (LFA-1) required for specific interaction with intercellular adhesion molecule 1 (ICAM-1). J Biol Chem 1995, 270:19008-19016.
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Huang, C.1
Springer, T.A.2
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26
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0029971322
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Antibodies that selectively inhibit leukocyte function-associated antigen 1 binding to intercellular adhesion molecule-3 recognize a unique epitope within the CD11 a I domain
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Binnerts ME, Van Kooyk Y, Edwards CP, Champe M, Presta L, Bodary SC, Rgdor CG, Berman PW: Antibodies that selectively inhibit leukocyte function-associated antigen 1 binding to intercellular adhesion molecule-3 recognize a unique epitope within the CD11 a I domain. J Biol Chem 1996, 271:9962-9968. Human/murine chimeras of the αL A-domain were used to map the epitopes on the A-domain to which function-blocking mAbs bind. One particular epitope, termed IdeD, was recognized by mAbs that inhibit ICAM-3, but not ICAM-1, binding to the domain. With the benefit of knowing the αL A-domain crystal structure, IdeD was shown to be spatially close to another peptide sequence, IKGN (single-letter code for amino acids), which was previously implicated in selective binding of ICAM-3. Interestingly, these sites are located on the opposite face of the αA-domain to the divalent cation binding site, suggesting that they might function allosterically to regulate ligand binding.
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(1996)
J Biol Chem
, vol.271
, pp. 9962-9968
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Binnerts, M.E.1
Van Kooyk, Y.2
Edwards, C.P.3
Champe, M.4
Presta, L.5
Bodary, S.C.6
Rgdor, C.G.7
Berman, P.W.8
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27
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0028944308
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Identification of a novel anti-integrin monoclonal antibody that recognizes a ligand-induced binding site epitope on the β1 subunit
-
Mould AP, Garratt AN, Askari JA, Akiyama SK, Humphries MJ: Identification of a novel anti-integrin monoclonal antibody that recognizes a ligand-induced binding site epitope on the β1 subunit FEBS Lett 1995, 363:118-122. The first report of an anti-β1 -LIBS mAb, 12G10. Competitive ELISA analyses showed that the epitope for this mAb overlaps with those of other previously characterized function-altering anti-β1 mAbs (residues 207-218 in the putative βA-domain). This suggests that this region of the β1 subunit is highly antigenic, conformationally flexible, and responsive to ligand binding.
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(1995)
FEBS Lett
, vol.363
, pp. 118-122
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-
Mould, A.P.1
Garratt, A.N.2
Askari, J.A.3
Akiyama, S.K.4
Humphries, M.J.5
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28
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0028858576
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Monoclonal antibody 9EG7 defines a novel β1 integrin epitope induced by soluble ligand and manganese, but inhibited by calcium
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Bazzoni G, Shin Daw-T, Buck CA, Hemler ME: Monoclonal antibody 9EG7 defines a novel β1 integrin epitope induced by soluble ligand and manganese, but inhibited by calcium. J Biol Chem 1995, 270:25570-25577. The anti-β1 mAb 9EG7 was used to define a LIBS and a cation-regulated epitope. The binding of 9EG7 was also shown to stimulate ligand binding. A model is proposed in which cation occupancy of integrins regulates integrin conformation and thereby determines ligand-binding potential.
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(1995)
J Biol Chem
, vol.270
, pp. 25570-25577
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Bazzoni, G.1
Daw-T, S.2
Buck, C.A.3
Hemler, M.E.4
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29
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0029039630
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Topography of ligand-induced binding sites, including a novel cation-sensitive epitope (AP5) at the amino terminus, of the human integrin β3 subunit
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Honda S, Tomiyama Y, Pelletier AJ, Annis D, Honda Y, Orchekowski R, Ruggeri Z, Kunicki TJ: 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 1995, 270:11947-11954.
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J Biol Chem
, vol.270
, pp. 11947-11954
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Honda, S.1
Tomiyama, Y.2
Pelletier, A.J.3
Annis, D.4
Honda, Y.5
Orchekowski, R.6
Ruggeri, Z.7
Kunicki, T.J.8
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30
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0027525561
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Long range propagation of conformational changes in integrin αIIbβS
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Du X, Gu M, Weisel JW, Nagaswami C, Bennett JS, Bowditch R, Ginsberg MH: Long range propagation of conformational changes in integrin αIIbβS. J Biol Chem 1993, 268:23087-23092.
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J Biol Chem
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Du, X.1
Gu, M.2
Weisel, J.W.3
Nagaswami, C.4
Bennett, J.S.5
Bowditch, R.6
Ginsberg, M.H.7
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31
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0029120428
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A peptide isolated from phage display libraries is a structural and functional mimic of an RGD-binding site on integrins
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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 1995, 130:1189-1196.
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J Cell Biol
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Pasqualini, R.1
Koivunen, E.2
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32
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0027248518
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Identification of a regulatory region of integrin β1 subunit using activating and inhibiting antibodies
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Takada Y, Puzon W: Identification of a regulatory region of integrin β1 subunit using activating and inhibiting antibodies. J Biol Chem 1993, 268:17597-17601.
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Takada, Y.1
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0029664954
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The inhibitory anti-β1 integrin monoclonal antibody 13 recognises an epitope that is attenuated by ligand occupancy: Evidence for allosteric inhibition of integrin function
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in press
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Mould AP, Akiyama SK, Humphries MJ: The inhibitory anti-β1 integrin monoclonal antibody 13 recognises an epitope that is attenuated by ligand occupancy: evidence for allosteric inhibition of integrin function. J Biol Chem 1996, in press. A solid-phase assay that measured integrin α5β1 -fibronectin binding was employed to assess the effects of ligand occupancy on binding of an anti-functional anti-β1 mAb to integrin α5β1. The results revealed a ligand-induced attenuation of mAb binding that was caused by a 50-fold decrease in the affinity of the mAb for the integrin. The effects of the ligand were independent of mAb concentration and therefore suggestive of an allosteric effect. As the mAb preferentially recognized the ligand-unoccupied conformation of α5β1 integrin, a model was proposed in which the ability of the mAb to inhibit ligand binding is explained by an allosteric stabilization. In addition, as ligand and mAb binding were found to be mutually exclusive, the mAb may induce a conformational change which leads to active displacement of ligand. These findings have important implications both for the location of ligand-binding sites within integrins and for the conformational changes induced by ligand occupancy.
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(1996)
J Biol Chem
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Mould, A.P.1
Akiyama, S.K.2
Humphries, M.J.3
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34
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0028900673
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Identification of putative ligand-binding sites of the integrin α4β1 (VLA-4, CD49d/CD29)
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Kamata T, Puzon W, Takada Y: Identification of putative ligand-binding sites of the integrin α4β1 (VLA-4, CD49d/CD29). Biochem J 1995, 305:945-951.
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Biochem J
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0029060141
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Molecular mapping of functional antibody binding sites of α4 integrin
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Schiffer SG, Hemlers ME, Lobb RR, Tizard R, Osbom L: Molecular mapping of functional antibody binding sites of α4 integrin. J Biol Chem 1995, 270:14270-14273.
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J Biol Chem
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Schiffer, S.G.1
Hemlers, M.E.2
Lobb, R.R.3
Tizard, R.4
Osbom, L.5
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36
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0028805249
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Critical amino acid residues for ligand binding are clustered in a predicted β-turn of the third N-terminal repeat in the integrin α4 and α5 subunits
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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 N-terminal repeat in the integrin α4 and α5 subunits. EMBO J 1995, 14:5550-5556. A large number of alanine-scanning mutations were performed in the integrin α4 subunit to localize the epitopes for function-blocking mAbs. A key site was shown to include residues 187-190. Importantly, as the equivalent sequence in the α5 subunit was also found to be recognized by inhibitory mAbs, the use of this region may be common to multiple integrins.
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EMBO J
, vol.14
, pp. 5550-5556
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Irie, A.1
Kamata, T.2
Puzon-McLaughlin, W.3
Takada, Y.4
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37
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0028054340
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A secondary structure model of the integrin α subunit N-terminal domain based on analysis of multiple alignments
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Tuckwell DS, Humphries MJ, Brass A: A secondary structure model of the integrin α subunit N-terminal domain based on analysis of multiple alignments. Cell Adhesion Commun 1994, 2:385-402.
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Cell Adhesion Commun
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Tuckwell, D.S.1
Humphries, M.J.2
Brass, A.3
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38
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0027496638
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Mutation of putative divalent cation sites in the α4 subunit of the integrin VLA-4: Distinct effects on adhesion to CS1/fibronectin, VCAM-1, and invasin
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Masumoto A, Hemler ME: Mutation of putative divalent cation sites in the α4 subunit of the integrin VLA-4: distinct effects on adhesion to CS1/fibronectin, VCAM-1, and invasin. J Cell Biol 1993, 123:245-253.
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Masumoto, A.1
Hemler, M.E.2
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39
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0029670908
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The amino-terminal one-third of αIIb defines the ligand recognition specificity of integrin αIIbβ3
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Loftus JC, Halloran CE, Ginsberg MH, Feigen LP, Zablocki JA, Smith JW: The amino-terminal one-third of αIIb defines the ligand recognition specificity of integrin αIIbβ3. J Biol Chem 1996, 271:2033-2039.
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J Biol Chem
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, pp. 2033-2039
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Loftus, J.C.1
Halloran, C.E.2
Ginsberg, M.H.3
Feigen, L.P.4
Zablocki, J.A.5
Smith, J.W.6
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40
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0029670835
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Activation of the integrin αVβ3 involves a discrete cation-binding site that regulates conformation
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Pelletier AJ, Kunicki T, Quaranta V: Activation of the integrin αVβ3 involves a discrete cation-binding site that regulates conformation. J Biol Chem 1996, 271:1364-1370.
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J Biol Chem
, vol.271
, pp. 1364-1370
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Pelletier, A.J.1
Kunicki, T.2
Quaranta, V.3
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41
-
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0028785507
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Intercellular adhesion molecule-1 dimerization and its consequences for adhesion mediated by lymphocyte function associated-1
-
Miller J, Knorr R, Ferrone M, Houdei R, Carron C, Dustin ML: Intercellular adhesion molecule-1 dimerization and its consequences for adhesion mediated by lymphocyte function associated-1. J Exp Med 1995, 182:1231-1241. Recombinant ICAM-1 is shown to be dimeric and to bind to integrin αLβ2 with high avidity. A similar dimerization was seen for cell-surface ICAM-1 as assessed by the binding of monomer-specific mAb and chemical cross-linking. Although speculative, this finding may have important implications for the stoichiometry of the binding of ICAM-1 to integrins. See also [42*].
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(1995)
J Exp Med
, vol.182
, pp. 1231-1241
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Miller, J.1
Knorr, R.2
Ferrone, M.3
Houdei, R.4
Carron, C.5
Dustin, M.L.6
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42
-
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0029013298
-
The native structure of intercellular adhesion molecule-1 (ICAM-1) is a dimer. Correlation with binding to LFA-1
-
Reilly PL, Woska JR Jr, Jeanfavre DD, McNally E, Rothlein R, Bormann BJ: The native structure of intercellular adhesion molecule-1 (ICAM-1) is a dimer. Correlation with binding to LFA-1. J Immunol 1995, 155:529-532. A very similar study to that detailed in [41*), with the same conclusions being made.
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(1995)
J Immunol
, vol.155
, pp. 529-532
-
-
Reilly, P.L.1
Woska Jr., J.R.2
Jeanfavre, D.D.3
McNally, E.4
Rothlein, R.5
Bormann, B.J.6
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43
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0028786294
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Integrin activation and cytoskeletal interaction are essential for the assembly of a fibronectin matrix
-
Wu C, Keivens VM, O'Toole TE, McDonald JA, Ginsberg MH: Integrin activation and cytoskeletal interaction are essential for the assembly of a fibronectin matrix. Cell 1995, 83:715-724.
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Cell
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Wu, C.1
Keivens, V.M.2
O'Toole, T.E.3
McDonald, J.A.4
Ginsberg, M.H.5
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44
-
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0028954797
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Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function
-
Miyamoto S, Akiyama SK, Yamada KM: Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function. Science 1995, 267:883-885. Soluble ligands and anti-integrin mAb-coated beads were used alone or in combination to demonstrate the need for receptor occupancy and clustering in integrin signalling. Both the recruitment of signalling molecules to integrins and tyrosine phosphorylation of signalling targets were found to be differentially affected by the ligands and mAbs. See also [45**].
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(1995)
Science
, vol.267
, pp. 883-885
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Miyamoto, S.1
Akiyama, S.K.2
Yamada, K.M.3
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45
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0028801218
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Integrin function: Molecular hierarchies of cytoskeletal and signaling molecules
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Miyamoto S, Teramoto H, Coso OA, Gutkind JS, Burbelo PD, Akiyama SK, Yamada KM: Integrin function: molecular hierarchies of cytoskeletal and signaling molecules. J Cell Biol 1995, 131:791-805. An extension of [44*], using the same approach to study the integrin signalling events that depend on ligand occupancy and receptor clustering. Clustering led to the recruitment of a large number of signalling molecules and the activation of the JNK (Jun kinase) pathway, but not to the accumulation of cytoskeletal proteins. Ligand occupancy, tyrosine kinase activity and cytoskeletal integrity were all required for full accumulation. This study, in conjunction with [44*], demonstrates the potential for defining and dissecting signalling hierarchies emanating from integrins.
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46
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Cooperative signaling by α5β1 and α4β1 integrins regulates metalloproteinase gene expression in fibroblasts adhering to fibronectin
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Huhtala P, Humphries MJ, McCarthy JB, Tremble PM, Werb Z, Damsky CH: Cooperative signaling by α5β1 and α4β1 integrins regulates metalloproteinase gene expression in fibroblasts adhering to fibronectin. J Cell Biol 1995, 129:867-879.
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Huhtala, P.1
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47
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Anchorage dependence, integrins, and apoptosis
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The α5β1 integrin supports survival of cells on fibronectin and up-regulates Bcl-2 expression
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Zhang Z, Vuori K, Reed JC, Ruoslahti E: The α5β1 integrin supports survival of cells on fibronectin and up-regulates Bcl-2 expression. Proc Natl Acad Sci USA 1995,92:6161-6165.
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Requirement of basement membrane for the suppression of programmed cell death in mammary epithelium
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Pullan S, Wilson J, Metcalfe A, Edwards GM, Goberdhan N, Tilly J, Hickman JA, Dive C, Streuli CH: Requirement of basement membrane for the suppression of programmed cell death in mammary epithelium. J Cell Sci 1996, 109:631-642.
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50
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α4β1 integrin-dependent cell adhesion is regulated by a low affinity receptor pool that is conformationally responsive to ligand
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Yednock TA, Cannon C, Vandevert C, Goldbach EG, Shaw G, Ellis DK, Liaw C, Fritz LC, Tanner LI: α4β1 integrin-dependent cell adhesion is regulated by a low affinity receptor pool that is conformationally responsive to ligand. J Biol Chem 1995, 270:28740-28750.
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Yednock, T.A.1
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51
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0029036091
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++ down-regulate E-cadherin and up-regulate α2β1 integrin function, activating keratinocyte migration on type I collagen
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++ down-regulate E-cadherin and up-regulate α2β1 integrin function, activating keratinocyte migration on type I collagen. J Invest Dermatol 1995, 104:768-774.
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2+ suppresses cell adhesion to osteopontin by attenuating binding affinity for integrin αVβ3
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2+ suppresses cell adhesion to osteopontin by attenuating binding affinity for integrin αVβ3. J Biol Chem 1995, 270:9917-9925.
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Hu, D.D.1
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53
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In vivo expression of alternatively spliced forms of integrin-associated protein (CD47)
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Reinhold MI, Lindberg FP, Plas D, Reynolds S, Peters MG, Brown EJ: In vivo expression of alternatively spliced forms of integrin-associated protein (CD47). J Cell Sci 1995, 108:3419-3425.
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54
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Ectopic expression of human and feline CD9 in a human B cell line confers β1 integrin-dependent motility on fibronectin and laminin substrates and enhanced tyrosine phosphorylation
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Shaw ARE, Domanska A, Mak A, Gilchrist A, Dobler K, Visser L, Poppema S, Riegel L, Letarte M, Willett BJ: Ectopic expression of human and feline CD9 in a human B cell line confers β1 integrin-dependent motility on fibronectin and laminin substrates and enhanced tyrosine phosphorylation. J Biol Chem 1995, 270:24092-24099.
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55
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Specific association of CD63 with the VLA-3 and VLA-6 integrins
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Berditchevski F, Bazzoni G, Hemler ME: Specific association of CD63 with the VLA-3 and VLA-6 integrins. J Biol Chem 1995, 270:17784-17790.
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56
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Membrane-anchored heparin-binding EGF-like growth factor (HB-EQF) and diphtheria toxin receptor-associated protein (DRAP27)/CD9 form a complex with integrin α3β1 at cell-cell contact sites
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Nakamura K, Iwamoto R, Mekeda E: Membrane-anchored heparin-binding EGF-like growth factor (HB-EQF) and diphtheria toxin receptor-associated protein (DRAP27)/CD9 form a complex with integrin α3β1 at cell-cell contact sites. J Cell Biol 1995, 129:1691-1705.
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Transendothelial migration of neutrophils involves integrinassociated protein (CD47)
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Cooper D, Lindberg FP, Gamble JR, Brown EJ, Vadas MA: Transendothelial migration of neutrophils involves integrinassociated protein (CD47). Proc Natl Acad Sci USA 1995, 92:3978-3982.
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58
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0030021514
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CO9 of mouse brain is implicated in neunte outgrowth and cell migration in vitro and is associated with the α6/β1 integrin and the neural adhesion molecule L1
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Schmidt C, Kuenemund V, Wintergerst ES, Schmitz B, Schachner M: CO9 of mouse brain is implicated in neunte outgrowth and cell migration in vitro and is associated with the α6/β1 integrin and the neural adhesion molecule L1. J Neurosci Res 1996, 43:12-31.
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Characterization of novel complexes on the cell surface between integrins and proteins with 4 transmembrane domains (TM4 proteins)
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Berditchevski F, Zutter MM, Hemler ME: Characterization of novel complexes on the cell surface between integrins and proteins with 4 transmembrane domains (TM4 proteins). Mol Biol Cell 1996. 7:193-207. Describes a comprehensive biochemical study which demonstrated a specific interaction between integrins and members of the TM4, or tetraspan, family of cell surface proteins. These interactions, which appear to be via the integrin extracellular domain, were shown to occur in cells by using chemical cross-linking. Colocalization studies also suggested an interaction of this nature in tissues.
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Berditchevski, F.1
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Hemler, M.E.3
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