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Volumn 6, Issue 1, 2012, Pages 20-29

The regulation of integrin function by divalent cations

Author keywords

ADMIDAS; Affinity; Divalent cations; Integrin; MIDAS; SyMBS

Indexed keywords

CALCIUM; DIVALENT CATION; INTEGRIN; ION;

EID: 84860360231     PISSN: 19336918     EISSN: 19336926     Source Type: Journal    
DOI: 10.4161/cam.18702     Document Type: Review
Times cited : (171)

References (105)
  • 1
    • 33750453714 scopus 로고    scopus 로고
    • Integrin ligands at a glance
    • PMID:16988024
    • Humphries JD, Byron A, Humphries MJ. Integrin ligands at a glance. J Cell Sci 2006; 119:3901-3; PMID:16988024; http://dx.doi.org/10.1242/jcs.03098
    • (2006) J Cell Sci , vol.119 , pp. 3901-3903
    • Humphries, J.D.1    Byron, A.2    Humphries, M.J.3
  • 2
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • PMID:12297042
    • Hynes RO. Integrins: bidirectional, allosteric signaling machines. Cell 2002; 110:673-87; PMID:12297042; http://dx.doi.org/10.1016/S0092-8674(02)00971-6
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 3
    • 0036696097 scopus 로고    scopus 로고
    • Integrin structure: New twists and turns in dynamic cell adhesion
    • PMID:12234368
    • Arnaout MA. Integrin structure: new twists and turns in dynamic cell adhesion. Immunol Rev 2002; 186:125-40; PMID:12234368; http://dx.doi.org/10. 1034/j.1600-065X.2002.18612.x
    • (2002) Immunol Rev , vol.186 , pp. 125-140
    • Arnaout, M.A.1
  • 4
    • 61949358716 scopus 로고    scopus 로고
    • Linking integrin conformation to function
    • PMID:19118208
    • Askari JA, Buckley PA, Mould AP, Humphries MJ. Linking integrin conformation to function. J Cell Sci 2009; 122:165-70; PMID:19118208; http://dx.doi.org/10.1242/jcs.018556
    • (2009) J Cell Sci , vol.122 , pp. 165-170
    • Askari, J.A.1    Buckley, P.A.2    Mould, A.P.3    Humphries, M.J.4
  • 5
    • 33645515261 scopus 로고    scopus 로고
    • Integrin trafficking and the control of cell migration
    • PMID:16445683
    • Caswell PT, Norman JC. Integrin trafficking and the control of cell migration. Traffic 2006; 7:14-21; PMID:16445683; http://dx.doi.org/10.1111/j. 1600-0854.2005.00362.x
    • (2006) Traffic , vol.7 , pp. 14-21
    • Caswell, P.T.1    Norman, J.C.2
  • 6
  • 7
    • 0029820264 scopus 로고    scopus 로고
    • Modulation of cell migration by integrin-mediated cytoskeletal linkages and ligand-binding affinity
    • PMID:8830782
    • Huttenlocher A, Ginsberg MH, Horwitz AF. Modulation of cell migration by integrin-mediated cytoskeletal linkages and ligand-binding affinity. J Cell Biol 1996; 134:1551-62; PMID:8830782; http://dx.doi.org/10.1083/jcb.134.6.1551
    • (1996) J Cell Biol , vol.134 , pp. 1551-1562
    • Huttenlocher, A.1    Ginsberg, M.H.2    Horwitz, A.F.3
  • 8
    • 0141865705 scopus 로고    scopus 로고
    • Talin binding to integrin β tails: A final common step in integrin activation
    • PMID:14526080
    • Tadokoro S, Shattil SJ, Eto K, Tai V, Liddington RC, de Pereda JM, et al. Talin binding to integrin β tails: a final common step in integrin activation. Science 2003; 302:103-6; PMID:14526080; http://dx.doi.org/10.1126/ science.1086652
    • (2003) Science , vol.302 , pp. 103-106
    • Tadokoro, S.1    Shattil, S.J.2    Eto, K.3    Tai, V.4    Liddington, R.C.5    De Pereda, J.M.6
  • 9
    • 34247891506 scopus 로고    scopus 로고
    • Structural basis of integrin regulation and signaling
    • PMID:17201681
    • Luo B-H, Carman CV, Springer TA. Structural basis of integrin regulation and signaling. Annu Rev Immunol 2007; 25:619-47; PMID:17201681; http://dx.doi.org/10.1146/annurev.immunol.25.022106.141618
    • (2007) Annu Rev Immunol , vol.25 , pp. 619-647
    • Luo, B.-H.1    Carman, C.V.2    Springer, T.A.3
  • 10
    • 34948882323 scopus 로고    scopus 로고
    • Requirement of α and β subunit transmembrane helix separation for integrin outside-in signaling
    • PMID:17615290
    • Zhu J, Carman CV, Kim M, Shimaoka M, Springer TA, Luo BH. Requirement of α and β subunit transmembrane helix separation for integrin outside-in signaling. Blood 2007; 110:2475-83; PMID:17615290; http://dx.doi.org/10.1182/blood-2007-03-080077
    • (2007) Blood , vol.110 , pp. 2475-2483
    • Zhu, J.1    Carman, C.V.2    Kim, M.3    Shimaoka, M.4    Springer, T.A.5    Luo, B.H.6
  • 11
    • 44449148944 scopus 로고    scopus 로고
    • The Nterminal domains of talin cooperate with the phosphotyrosine binding-like domain to activate β1 and β3 integrins
    • PMID: 18165225
    • Bouaouina M, Lad Y, Calderwood DA. The Nterminal domains of talin cooperate with the phosphotyrosine binding-like domain to activate β1 and β3 integrins. J Biol Chem 2008; 283:6118-25; PMID: 18165225; http://dx.doi.org/10.1074/jbc.M709527200
    • (2008) J Biol Chem , vol.283 , pp. 6118-6125
    • Bouaouina, M.1    Lad, Y.2    Calderwood, D.A.3
  • 12
    • 0037031906 scopus 로고    scopus 로고
    • Global conformational rearrangements in integrin extracellular domains in outside-in and inside-out signaling
    • PMID:12230977
    • Takagi J, Petre BM, Walz T, Springer TA. Global conformational rearrangements in integrin extracellular domains in outside-in and inside-out signaling. Cell 2002; 110:599-611; PMID:12230977; http://dx.doi. org/10.1016/S0092-8674(02)00935-2
    • (2002) Cell , vol.110 , pp. 599-611
    • Takagi, J.1    Petre, B.M.2    Walz, T.3    Springer, T.A.4
  • 13
    • 0030994408 scopus 로고    scopus 로고
    • Effects of buffering intracellular free calcium on neutrophil migration through three-dimensional matrices
    • PMID:9130464
    • Mandeville JT, Maxfield FR. Effects of buffering intracellular free calcium on neutrophil migration through three-dimensional matrices. J Cell Physiol 1997; 171:168-78; PMID:9130464; http://dx.doi. org/10.1002/(SICI)1097- 4652(199705)171:2〈168:: AID-JCP7〉3.0.CO;2-M
    • (1997) J Cell Physiol , vol.171 , pp. 168-178
    • Mandeville, J.T.1    Maxfield, F.R.2
  • 14
    • 10244224019 scopus 로고    scopus 로고
    • Functional and structural correlations of individual αIIbβ3 molecules
    • PMID:15319287
    • Litvinov RI, Nagaswami C, Vilaire G, Shuman H, Bennett JS, Weisel JW. Functional and structural correlations of individual αIIbβ3 molecules. Blood 2004; 104:3979-85; PMID:15319287; http://dx.doi. org/10.1182/blood-2004-04-1411
    • (2004) Blood , vol.104 , pp. 3979-3985
    • Litvinov, R.I.1    Nagaswami, C.2    Vilaire, G.3    Shuman, H.4    Bennett, J.S.5    Weisel, J.W.6
  • 15
    • 14744273494 scopus 로고    scopus 로고
    • The three-dimensional structure of integrins and their ligands, and conformational regulation of cell adhesion
    • PMID:15500858
    • Springer TA, Wang J-h. The three-dimensional structure of integrins and their ligands, and conformational regulation of cell adhesion. Adv Protein Chem 2004; 68:29-63; PMID:15500858; http://dx.doi.org/10. 1016/S0065-3233(04)68002-8
    • (2004) Adv Protein Chem , vol.68 , pp. 29-63
    • Springer, T.A.1    Wang, J.-H.2
  • 16
    • 34248215265 scopus 로고    scopus 로고
    • Involvement of α6β4 integrin in the mechanisms that regulate breast cancer progression
    • PMID:17319974
    • Bon G, Folgiero V, Di Carlo S, Sacchi A, Falcioni R. Involvement of α6β4 integrin in the mechanisms that regulate breast cancer progression. Breast Cancer Res 2007; 9:203; PMID:17319974; http://dx.doi.org/10. 1186/bcr1651
    • (2007) Breast Cancer Res , vol.9 , pp. 203
    • Bon, G.1    Folgiero, V.2    Di Carlo, S.3    Sacchi, A.4    Falcioni, R.5
  • 17
    • 64049108887 scopus 로고    scopus 로고
    • Increased expression of mucosal addressin cell adhesion molecule 1 in the duodenum of patients with active celiac disease is associated with depletion of integrinα4β7-positive T cells in blood
    • PMID:19157500
    • Di Sabatino A, Rovedatti L, Rosado MM, Carsetti R, Corazza GR, MacDonald TT. Increased expression of mucosal addressin cell adhesion molecule 1 in the duodenum of patients with active celiac disease is associated with depletion of integrinα4β7-positive T cells in blood. Hum Pathol 2009; 40:699-704; PMID:19157500; http://dx.doi.org/10.1016/j.humpath. 2008.10.014
    • (2009) Hum Pathol , vol.40 , pp. 699-704
    • Di Sabatino, A.1    Rovedatti, L.2    Rosado, M.M.3    Carsetti, R.4    Corazza, G.R.5    MacDonald, T.T.6
  • 18
    • 0029686918 scopus 로고    scopus 로고
    • Tumor angiogenesis and the role of vascular cell integrin αVβ3
    • PMID:8791129
    • Varner JA, Cheresh DA. Tumor angiogenesis and the role of vascular cell integrin αVβ3. Important Adv Oncol 1996; 69-87; PMID:8791129
    • (1996) Important Adv Oncol , pp. 69-87
    • Varner, J.A.1    Cheresh, D.A.2
  • 19
    • 0028983485 scopus 로고
    • Involvement of α1 and α4 integrins in gut mucosal injury of graft-versus-host disease
    • PMID:7495725
    • Tanaka T, Ohtsuka Y, Yagita H, Shiratori Y, Omata M, Okumura K. Involvement of α1 and α4 integrins in gut mucosal injury of graft-versus-host disease. Int Immunol 1995; 7:1183-9; PMID:7495725; http://dx. doi.org/10.1093/intimm/7.8.1183
    • (1995) Int Immunol , vol.7 , pp. 1183-1189
    • Tanaka, T.1    Ohtsuka, Y.2    Yagita, H.3    Shiratori, Y.4    Omata, M.5    Okumura, K.6
  • 20
    • 58149087246 scopus 로고    scopus 로고
    • Roles of integrins in tumor angiogenesis and lymphangiogenesis
    • PMID:19093788
    • Garmy-Susini B, Varner JA. Roles of integrins in tumor angiogenesis and lymphangiogenesis. Lymphat Res Biol 2008; 6:155-63; PMID:19093788; http://dx. doi.org/10.1089/lrb.2008.1011
    • (2008) Lymphat Res Biol , vol.6 , pp. 155-163
    • Garmy-Susini, B.1    Varner, J.A.2
  • 21
    • 0037413240 scopus 로고    scopus 로고
    • α4 integrins as therapeutic targets in autoimmune disease
    • PMID:12510047
    • von Andrian UH, Engelhardt B. α4 integrins as therapeutic targets in autoimmune disease. N Engl J Med 2003; 348:68-72; PMID:12510047; http://dx. doi.org/10.1056/NEJMe020157
    • (2003) N Engl J Med , vol.348 , pp. 68-72
    • Von Andrian, U.H.1    Engelhardt, B.2
  • 23
    • 34548288408 scopus 로고    scopus 로고
    • The connection between metal ion affinity and ligand affinity in integrin I domains
    • PMID: 17702677
    • Vorup-Jensen T, Waldron TT, Astrof N, Shimaoka M, Springer TA. The connection between metal ion affinity and ligand affinity in integrin I domains. Biochim Biophys Acta 2007; 1774:1148-55; PMID: 17702677
    • (2007) Biochim Biophys Acta , vol.1774 , pp. 1148-1155
    • Vorup-Jensen, T.1    Waldron, T.T.2    Astrof, N.3    Shimaoka, M.4    Springer, T.A.5
  • 24
    • 0034068356 scopus 로고    scopus 로고
    • Integrins: Structure and functions
    • PMID: 10779172
    • Berman AE, Kozlova NI. Integrins: structure and functions. Membr Cell Biol 2000; 13:207-44; PMID: 10779172
    • (2000) Membr Cell Biol , vol.13 , pp. 207-244
    • Berman, A.E.1    Kozlova, N.I.2
  • 25
    • 76349099822 scopus 로고    scopus 로고
    • Structure of an integrin with an αI domain, complement receptor type 4
    • PMID:20033057
    • Xie C, Zhu J, Chen X, Mi L, Nishida N, Springer TA.Structure of an integrin with an αI domain, complement receptor type 4. EMBO J 2010; 29:666-79; PMID:20033057; http://dx.doi.org/10.1038/emboj. 2009.367
    • (2010) EMBO J , vol.29 , pp. 666-679
    • Xie, C.1    Zhu, J.2    Chen, X.3    Mi, L.4    Nishida, N.5    Springer, T.A.6
  • 26
    • 69449084406 scopus 로고    scopus 로고
    • Crystal structure of the complete integrin αVβ3 ectodomain plus an α/β transmembrane fragment
    • PMID:19704023
    • Xiong JP, Mahalingham B, Alonso JL, Borrelli LA, Rui X, Anand S, et al. Crystal structure of the complete integrin αVβ3 ectodomain plus an α/β transmembrane fragment. J Cell Biol 2009; 186:589-600; PMID:19704023; http://dx.doi.org/10.1083/jcb. 200905085
    • (2009) J Cell Biol , vol.186 , pp. 589-600
    • Xiong, J.P.1    Mahalingham, B.2    Alonso, J.L.3    Borrelli, L.A.4    Rui, X.5    Anand, S.6
  • 27
    • 57749116060 scopus 로고    scopus 로고
    • Structure of a complete integrin ectodomain in a physiologic resting state and activation and deactivation by applied forces
    • PMID:19111664
    • Zhu J, Luo BH, Xiao T, Zhang C, Nishida N, Springer TA. Structure of a complete integrin ectodomain in a physiologic resting state and activation and deactivation by applied forces. Mol Cell 2008; 32:849-61; PMID:19111664; http://dx.doi.org/10. 1016/j.molcel.2008.11.018
    • (2008) Mol Cell , vol.32 , pp. 849-861
    • Zhu, J.1    Luo, B.H.2    Xiao, T.3    Zhang, C.4    Nishida, N.5    Springer, T.A.6
  • 28
    • 0035850669 scopus 로고    scopus 로고
    • Crystal structure of the extracellular segment of integrin αVβ3
    • PMID:11546839
    • Xiong JP, Stehle T, Diefenbach B, Zhang R, Dunker R, Scott DL, et al. Crystal structure of the extracellular segment of integrin αVβ3. Science 2001; 294:339-45; PMID:11546839; http://dx.doi.org/10.1126/science. 1064535
    • (2001) Science , vol.294 , pp. 339-345
    • Xiong, J.P.1    Stehle, T.2    Diefenbach, B.3    Zhang, R.4    Dunker, R.5    Scott, D.L.6
  • 29
    • 0035932996 scopus 로고    scopus 로고
    • Reversibly locking a protein fold in an active conformation with a disulfide bond: Integrin αL I domains with high affinity and antagonist activity in vivo
    • PMID:11353828
    • Shimaoka M, Lu C, Palframan R, von Andrian UH, Takagi J, Springer TA. Reversibly locking a protein fold in an active conformation with a disulfide bond: integrin αL I domains with high affinity and antagonist activity in vivo. Proc Natl Acad Sci USA 2001; 98:6009-14; PMID:11353828; http://dx.doi.org/10. 1073/pnas.101130498
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 6009-6014
    • Shimaoka, M.1    Lu, C.2    Palframan, R.3    Von Andrian, U.H.4    Takagi, J.5    Springer, T.A.6
  • 30
    • 8544259562 scopus 로고    scopus 로고
    • Structural basis for allostery in integrins and binding to fibrinogen-mimetic therapeutics
    • PMID:15378069
    • Xiao T, Takagi J, Coller BS, Wang JH, Springer TA. Structural basis for allostery in integrins and binding to fibrinogen-mimetic therapeutics. Nature 2004; 432:59-67; PMID:15378069; http://dx.doi.org/10. 1038/nature02976
    • (2004) Nature , vol.432 , pp. 59-67
    • Xiao, T.1    Takagi, J.2    Coller, B.S.3    Wang, J.H.4    Springer, T.A.5
  • 31
    • 57749106677 scopus 로고    scopus 로고
    • Distinct roles of β1 metal ion-dependent adhesion site (MIDAS), adjacent to MIDAS (ADMIDAS), and ligand-associated metal-binding site (LIMBS) cation-binding sites in ligand recognition by integrin α2β1
    • PMID:18820259
    • Valdramidou D, Humphries MJ, Mould AP. Distinct roles of β1 metal ion-dependent adhesion site (MIDAS), adjacent to MIDAS (ADMIDAS), and ligand-associated metal-binding site (LIMBS) cation-binding sites in ligand recognition by integrin α2β1. J Biol Chem 2008; 283:32704-14; PMID:18820259; http://dx.doi.org/10.1074/jbc.M802066200
    • (2008) J Biol Chem , vol.283 , pp. 32704-32714
    • Valdramidou, D.1    Humphries, M.J.2    Mould, A.P.3
  • 32
    • 0141721496 scopus 로고    scopus 로고
    • Integrins, cations and ligands: Making the connection
    • PMID: 12871301
    • Xiong JP, Stehle T, Goodman SL, Arnaout MA. Integrins, cations and ligands: making the connection. J Thromb Haemost 2003; 1:1642-54; PMID: 12871301; http://dx.doi.org/10.1046/j.1538-7836. 2003.00277.x
    • (2003) J Thromb Haemost , vol.1 , pp. 1642-1654
    • Xiong, J.P.1    Stehle, T.2    Goodman, S.L.3    Arnaout, M.A.4
  • 33
    • 0025787344 scopus 로고
    • Ca2+-dependent structural transitions of the platelet glycoprotein IIb-IIIa complex. Preparation of stable glycoprotein IIb and IIIa monomers
    • PMID:1869535
    • Steiner B, Parise LV, Leung B, Phillips DR. Ca2+-dependent structural transitions of the platelet glycoprotein IIb-IIIa complex. Preparation of stable glycoprotein IIb and IIIa monomers. J Biol Chem 1991; 266:14986-91; PMID:1869535
    • (1991) J Biol Chem , vol.266 , pp. 14986-14991
    • Steiner, B.1    Parise, L.V.2    Leung, B.3    Phillips, D.R.4
  • 34
    • 0029797963 scopus 로고    scopus 로고
    • Inherited mutations within the calcium-binding sites of the integrin αIIb subunit (platelet glycoprotein IIb). Effects of the amino acid side chain and the amino acid position on cation binding
    • PMID:8925838
    • Jackson DE, Poncz M, Holyst MT, Newman PJ. Inherited mutations within the calcium-binding sites of the integrin αIIb subunit (platelet glycoprotein IIb). Effects of the amino acid side chain and the amino acid position on cation binding. Eur J Biochem 1996; 240:280-7; PMID:8925838; http://dx.doi.org/10. 1111/j.1432-1033.1996.0280h.x
    • (1996) Eur J Biochem , vol.240 , pp. 280-287
    • Jackson, D.E.1    Poncz, M.2    Holyst, M.T.3    Newman, P.J.4
  • 35
    • 0019403970 scopus 로고
    • The formation of Ca2+ dependent complexes of platelet membrane glycoproteins IIb and IIIa in solution as determined by crossed immunoelectrophoreisis
    • PMID:6454451
    • Kunicki TJ, Pidard D, Rosa J-P, Nurden AT. The formation of Ca2+ dependent complexes of platelet membrane glycoproteins IIb and IIIa in solution as determined by crossed immunoelectrophoreisis. Blood 1981; 58:268-78; PMID:6454451
    • (1981) Blood , vol.58 , pp. 268-278
    • Kunicki, T.J.1    Pidard, D.2    Rosa, J.-P.3    Nurden, A.T.4
  • 36
    • 0022982040 scopus 로고
    • Divalent cation regulation of the surface orientation of platelet membrane glycoprotein IIb: Correlation with fibrinogen binding function and definition of a novel variant of Glanzmann's thrombasthenia
    • PMID:2428841
    • Ginsberg MH, Lightsey A, Kunicki TJ, Kaufmann A, Marguerie G, Plow EF. Divalent cation regulation of the surface orientation of platelet membrane glycoprotein IIb: Correlation with fibrinogen binding function and definition of a novel variant of Glanzmann's thrombasthenia. J Clin Invest 1986; 78: 1103-11; PMID:2428841; http://dx.doi.org/10.1172/ JCI112667
    • (1986) J Clin Invest , vol.78 , pp. 1103-1111
    • Ginsberg, M.H.1    Lightsey, A.2    Kunicki, T.J.3    Kaufmann, A.4    Marguerie, G.5    Plow, E.F.6
  • 37
    • 0023189463 scopus 로고
    • Protein sequence of endothelial glycoprotein IIIa derived from a cDNA clone. Identity with platelet glycoprotein IIIa and similarity to "integrin"
    • PMID:3494014
    • Fitzgerald LA, Steiner B, Rall SC, Jr., Lo S, Phillips DR. Protein sequence of endothelial glycoprotein IIIa derived from a cDNA clone. Identity with platelet glycoprotein IIIa and similarity to "integrin". J Biol Chem 1987; 262:3936-9; PMID:3494014
    • (1987) J Biol Chem , vol.262 , pp. 3936-3939
    • Fitzgerald, L.A.1    Steiner, B.2    Rall Jr., S.C.3    Lo, S.4    Phillips, D.R.5
  • 38
    • 0024523286 scopus 로고
    • The membrane glycoprotein Ia-IIa (VLA- 2) complex mediates the Mg2+-dependent adhesion of platelets to collagen
    • PMID:2715183
    • Staatz WD, Rajpara SM, Wayner EA, Carter WG, Santoro SA. The membrane glycoprotein Ia-IIa (VLA- 2) complex mediates the Mg2+-dependent adhesion of platelets to collagen. J Cell Biol 1989; 108:1917-24; PMID:2715183; http://dx.doi.org/10.1083/jcb.108.5.1917
    • (1989) J Cell Biol , vol.108 , pp. 1917-1924
    • Staatz, W.D.1    Rajpara, S.M.2    Wayner, E.A.3    Carter, W.G.4    Santoro, S.A.5
  • 39
    • 0026601096 scopus 로고
    • Divalent cation regulation of the function of the leukocyte integrin LFA-1
    • PMID: 1346139
    • Dransfield I, Cabanas C, Craig A, Hogg N. Divalent cation regulation of the function of the leukocyte integrin LFA-1. J Cell Biol 1992; 116:219-26; PMID: 1346139; http://dx.doi.org/10.1083/jcb.116.1.219
    • (1992) J Cell Biol , vol.116 , pp. 219-226
    • Dransfield, I.1    Cabanas, C.2    Craig, A.3    Hogg, N.4
  • 40
    • 0019464862 scopus 로고
    • Anticoagulant and calcium-binding properties of high molecular weight derivatives of human fibrinogen, produced by plasmin (fragments X)
    • PMID:6453618
    • Nieuwenhuizen W, Gravesen M. Anticoagulant and calcium-binding properties of high molecular weight derivatives of human fibrinogen, produced by plasmin (fragments X). Biochim Biophys Acta 1981; 668:81-8; PMID:6453618
    • (1981) Biochim Biophys Acta , vol.668 , pp. 81-88
    • Nieuwenhuizen, W.1    Gravesen, M.2
  • 41
    • 0026601096 scopus 로고
    • Divalent cation regulation of the function of the leukocyte integrin LFA-1
    • PMID: 1346139
    • Dransfield I, Cabañas C, Craig A, Hogg N. Divalent cation regulation of the function of the leukocyte integrin LFA-1. J Cell Biol 1992; 116:219-26; PMID: 1346139; http://dx.doi.org/10.1083/jcb.116.1.219
    • (1992) J Cell Biol , vol.116 , pp. 219-226
    • Dransfield, I.1    Cabañas, C.2    Craig, A.3    Hogg, N.4
  • 42
    • 0028986791 scopus 로고
    • Ca2+ suppresses cell adhesion to osteopontin by attenuating binding affinity for integrin αVβ3
    • PMID:7537271
    • Hu DD, Hoyer JR, Smith JW. Ca2+ suppresses cell adhesion to osteopontin by attenuating binding affinity for integrin αVβ3. J Biol Chem 1995; 270:9917-25; PMID:7537271; http://dx.doi.org/10.1074/jbc. 270.17.9917
    • (1995) J Biol Chem , vol.270 , pp. 9917-9925
    • Hu, D.D.1    Hoyer, J.R.2    Smith, J.W.3
  • 43
    • 0027601069 scopus 로고
    • Role of intracellular Ca2+ levels in the regulation of CD11a/CD18 mediated cell adhesion
    • PMID:7915956
    • van Kooyk Y, Weder P, Heije K, De Waal Malefijt R, Figdor CG. Role of intracellular Ca2+ levels in the regulation of CD11a/CD18 mediated cell adhesion. Cell Adhes Commun 1993; 1:21-32; PMID:7915956; http://dx.doi.org/10. 3109/15419069309095679
    • (1993) Cell Adhes Commun , vol.1 , pp. 21-32
    • Van Kooyk, Y.1    Weder, P.2    Heije, K.3    De Waal Malefijt, R.4    Figdor, C.G.5
  • 44
    • 0034636864 scopus 로고    scopus 로고
    • Micromolar Ca2+ concentrations are essential for Mg2+-dependent binding of collagen by the integrin α2β1 in human platelets
    • PMID:10827198
    • Onley DJ, Knight CG, Tuckwell DS, Barnes MJ, Farndale RW. Micromolar Ca2+ concentrations are essential for Mg2+-dependent binding of collagen by the integrin α2β1 in human platelets. J Biol Chem 2000; 275:24560-4; PMID:10827198; http://dx.doi. org/10.1074/jbc.M004111200
    • (2000) J Biol Chem , vol.275 , pp. 24560-24564
    • Onley, D.J.1    Knight, C.G.2    Tuckwell, D.S.3    Barnes, M.J.4    Farndale, R.W.5
  • 45
    • 0032528432 scopus 로고    scopus 로고
    • Molecular regulation of the interaction between leukocyte function-associated antigen-1 and soluble ICAM-1 by divalent metal cations
    • PMID:9670961
    • Labadia ME, Jeanfavre DD, Caviness GO, Morelock MM. Molecular regulation of the interaction between leukocyte function-associated antigen-1 and soluble ICAM-1 by divalent metal cations. J Immunol 1998; 161:836-42; PMID:9670961
    • (1998) J Immunol , vol.161 , pp. 836-842
    • Labadia, M.E.1    Jeanfavre, D.D.2    Caviness, G.O.3    Morelock, M.M.4
  • 46
    • 0034694962 scopus 로고    scopus 로고
    • The regulation of integrin function by Ca2+
    • PMID:11108953
    • Leitinger B, McDowall A, Stanley P, Hogg N. The regulation of integrin function by Ca2+. Biochim Biophys Acta 2000; 1498:91-8; PMID:11108953; http://dx.doi.org/10.1016/S0167-4889(00)00086-0
    • (2000) Biochim Biophys Acta , vol.1498 , pp. 91-98
    • Leitinger, B.1    McDowall, A.2    Stanley, P.3    Hogg, N.4
  • 47
    • 0030272101 scopus 로고    scopus 로고
    • Integrin activation: The link between ligand binding and signal transduction
    • PMID:8939662
    • Humphries MJ. Integrin activation: The link between ligand binding and signal transduction. Curr Opin Cell Biol 1996; 8:632-40; PMID:8939662; http://dx. doi.org/10.1016/S0955-0674(96)80104-9
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 632-640
    • Humphries, M.J.1
  • 48
    • 33751158321 scopus 로고
    • Characterization of cation-binding sequences in the platelet integrin GPIIb-IIIa (αIIbβ3) by terbium luminescence
    • PMID:7522557
    • Cierniewski CSHT, Smith JW, Plow EF. Characterization of cation-binding sequences in the platelet integrin GPIIb-IIIa (αIIbβ3) by terbium luminescence. Biochemistry 1994; 33:12238-46; PMID:7522557; http://dx.doi.org/ 10.1021/bi00206a029
    • (1994) Biochemistry , vol.33 , pp. 12238-12246
    • Cierniewski, C.1    Smith, J.W.2    Plow, E.F.3
  • 49
    • 0025908304 scopus 로고
    • Calcium binding to human platelet integrin GPIIb/IIIa and to its constituent glycoproteins: Effects of lipids and temperature
    • PMID:2039481
    • Rivas GA, Gonzalez-Rodriguez J. Calcium binding to human platelet integrin GPIIb/IIIa and to its constituent glycoproteins: Effects of lipids and temperature. Biochem J 1991; 276:35-40; PMID:2039481
    • (1991) Biochem J , vol.276 , pp. 35-40
    • Rivas, G.A.1    Gonzalez-Rodriguez, J.2
  • 50
    • 0037192811 scopus 로고    scopus 로고
    • Identification and characterization of two cation binding sites in the integrin β3 subunit
    • PMID:11796735
    • Cierniewska-Cieslak A, Cierniewski CS, Blecka K, Papierak M, Michalec L, Zhang L, et al. Identification and characterization of two cation binding sites in the integrin β3 subunit. J Biol Chem 2002; 277:11126- 34; PMID:11796735; http://dx.doi.org/10.1074/jbc. M112388200
    • (2002) J Biol Chem , vol.277 , pp. 11126-11134
    • Cierniewska-Cieslak, A.1    Cierniewski, C.S.2    Blecka, K.3    Papierak, M.4    Michalec, L.5    Zhang, L.6
  • 51
    • 0035965303 scopus 로고    scopus 로고
    • Evidence that ligand and metal ion binding to integrin α4β1 are regulated through a coupled equilibrium
    • PMID:11473127
    • Chen LL, Whitty A, Scott D, Lee WC, Cornebise M, Adams SP, et al. Evidence that ligand and metal ion binding to integrin α4β1 are regulated through a coupled equilibrium. J Biol Chem 2001; 276:36520-9; PMID:11473127; http://dx.doi.org/10.1074/jbc. M106216200
    • (2001) J Biol Chem , vol.276 , pp. 36520-36529
    • Chen, L.L.1    Whitty, A.2    Scott, D.3    Lee, W.C.4    Cornebise, M.5    Adams, S.P.6
  • 52
    • 0037443402 scopus 로고    scopus 로고
    • Two novel mutations in the aIIb calcium-binding domains identify hydrophobic regions essential for αIIbβ3 biogenesis
    • PMID:12424194
    • Mitchell WB, Li JH, Singh F, Michelson AD, Bussel J, Coller BS, et al. Two novel mutations in the aIIb calcium-binding domains identify hydrophobic regions essential for αIIbβ3 biogenesis. Blood 2003; 101: 2268-76; PMID:12424194; http://dx.doi.org/10. 1182/blood-2002-07-2266
    • (2003) Blood , vol.101 , pp. 2268-2276
    • Mitchell, W.B.1    Li, J.H.2    Singh, F.3    Michelson, A.D.4    Bussel, J.5    Coller, B.S.6
  • 53
    • 0026643364 scopus 로고
    • Homology modelling of integrin EF-hands. Evidence for widespread use of a conserved cation-binding site
    • PMID:1322124
    • Tuckwell DS, Brass A, Humphries MJ. Homology modelling of integrin EF-hands. Evidence for widespread use of a conserved cation-binding site. Biochem J 1992; 285:325-31; PMID:1322124
    • (1992) Biochem J , vol.285 , pp. 325-331
    • Tuckwell, D.S.1    Brass, A.2    Humphries, M.J.3
  • 54
    • 0034604295 scopus 로고    scopus 로고
    • A novel Ca2+ binding beta hairpin loop better resembles integrin sequence motifs than the EF hand
    • PMID:10975518
    • Springer TA, Jing H, Takagi J. A novel Ca2+ binding beta hairpin loop better resembles integrin sequence motifs than the EF hand. Cell 2000; 102:275-7; PMID:10975518; http://dx.doi.org/10.1016/S0092- 8674(00)00033-7
    • (2000) Cell , vol.102 , pp. 275-277
    • Springer, T.A.1    Jing, H.2    Takagi, J.3
  • 55
    • 0031013031 scopus 로고    scopus 로고
    • Folding of the N-terminal, ligand-binding region of integrin α-subunits into a beta-propeller domain
    • PMID:8990162
    • Springer TA. Folding of the N-terminal, ligand-binding region of integrin α-subunits into a beta-propeller domain. Proc Natl Acad Sci USA 1997; 94:65-72; PMID:8990162; http://dx.doi.org/10. 1073/pnas.94.1.65
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 65-72
    • Springer, T.A.1
  • 56
    • 0026035464 scopus 로고
    • A discrete sequence in a platelet integrin is involved in ligand recognition
    • PMID: 2002847
    • D'Souza SE, Ginsberg MH, Matsueda GR, Plow EF. A discrete sequence in a platelet integrin is involved in ligand recognition. Nature 1991; 350:66-8; PMID: 2002847; http://dx.doi.org/10.1038/350066a0
    • (1991) Nature , vol.350 , pp. 66-68
    • D'Souza, S.E.1    Ginsberg, M.H.2    Matsueda, G.R.3    Plow, E.F.4
  • 57
    • 0026586249 scopus 로고
    • Ca2+-binding properties of the platelet glycoprotein IIb ligand-interacting domain
    • PMID:1730629
    • Gulino D, Boudignon C, Zhang L, Concord E, Rabiet M-J, Marguerie G. Ca2+-binding properties of the platelet glycoprotein IIb ligand-interacting domain. J Biol Chem 1992; 267:1001-7; PMID:1730629
    • (1992) J Biol Chem , vol.267 , pp. 1001-1007
    • Gulino, D.1    Boudignon, C.2    Zhang, L.3    Concord, E.4    Rabiet, M.-J.5    Marguerie, G.6
  • 58
    • 0029670908 scopus 로고    scopus 로고
    • The amino-terminal one-third of αIIb defines the ligand recognition specificity of integrin αIIbβ3
    • PMID:8567656
    • 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; 271:2033-9; PMID:8567656; http://dx.doi.org/10.1074/jbc.271.4. 2033
    • (1996) J Biol Chem , vol.271 , pp. 2033-2039
    • Loftus, J.C.1    Halloran, C.E.2    Ginsberg, M.H.3    Feigen, L.P.4    Zablocki, J.A.5    Smith, J.W.6
  • 59
    • 0027496638 scopus 로고
    • Mutation of putative divalent cation sites in the a4 subunit of the integrin VLA-4; distinct effects on adhesion to CS1/fibronectin, VCAM-1, and invasin
    • PMID:7691827
    • Masumoto A, Hemler ME. Mutation of putative divalent cation sites in the a4 subunit of the integrin VLA-4; distinct effects on adhesion to CS1/fibronectin, VCAM-1, and invasin. J Cell Biol 1993; 123:245- 53; PMID:7691827; http://dx.doi.org/10.1083/jcb. 123.1.245
    • (1993) J Cell Biol , vol.123 , pp. 245-253
    • Masumoto, A.1    Hemler, M.E.2
  • 60
    • 0028123329 scopus 로고
    • Glanzmann thrombasthenia secondary to a Gly273 - Asp mutation adjacent to the first calcium-binding domain of platelet glycoprotein IIb
    • PMID:8282784
    • Poncz M, Rifat S, Coller BS, Newman PJ, Shattil SJ, Parrella T, et al. Glanzmann thrombasthenia secondary to a Gly273 - Asp mutation adjacent to the first calcium-binding domain of platelet glycoprotein IIb. J Clin Invest 1994; 93:172-9; PMID:8282784; http:// dx.doi.org/10.1172/JCI116942
    • (1994) J Clin Invest , vol.93 , pp. 172-179
    • Poncz, M.1    Rifat, S.2    Coller, B.S.3    Newman, P.J.4    Shattil, S.J.5    Parrella, T.6
  • 61
    • 0028071221 scopus 로고
    • A single amino acid substitution flanking the fourth calcium binding domain of aIIb prevents maturation of the αIIbβ3 integrin complex
    • PMID:7508443
    • Wilcox DA, Wautier JL, Pidard D, Newman PJ. A single amino acid substitution flanking the fourth calcium binding domain of aIIb prevents maturation of the αIIbβ3 integrin complex. J Biol Chem 1994; 269:4450-7; PMID:7508443
    • (1994) J Biol Chem , vol.269 , pp. 4450-4457
    • Wilcox, D.A.1    Wautier, J.L.2    Pidard, D.3    Newman, P.J.4
  • 62
    • 0028951764 scopus 로고
    • Glanzmann thrombasthenia resulting from a single amino acid substitution between the second and third calcium-binding domains of GPIIb
    • PMID:7706461
    • Wilcox DA, Paddock CM, Lyman S, Gill JC, Newman PJ. Glanzmann thrombasthenia resulting from a single amino acid substitution between the second and third calcium-binding domains of GPIIb. J Clin Invest 1995; 95:1553-60; PMID:7706461; http://dx.doi.org/10.1172/JCI117828
    • (1995) J Clin Invest , vol.95 , pp. 1553-1560
    • Wilcox, D.A.1    Paddock, C.M.2    Lyman, S.3    Gill, J.C.4    Newman, P.J.5
  • 63
    • 0029947855 scopus 로고    scopus 로고
    • Glanzmann thrombasthenia due to a two amino acid deletion in the fourth calcium-binding domain of αIIb: Demonstration of the importance of calcium-binding domains in the conformation of αIIbβ3
    • PMID:8704171
    • Basani RB, Vilaire G, Shattil SJ, Kolodziej MA, Bennett JS, Poncz M. Glanzmann thrombasthenia due to a two amino acid deletion in the fourth calcium-binding domain of αIIb: demonstration of the importance of calcium-binding domains in the conformation of αIIbβ3. Blood 1996; 88:167-73; PMID:8704171
    • (1996) Blood , vol.88 , pp. 167-173
    • Basani, R.B.1    Vilaire, G.2    Shattil, S.J.3    Kolodziej, M.A.4    Bennett, J.S.5    Poncz, M.6
  • 64
    • 0029658260 scopus 로고    scopus 로고
    • A mutant (Arg327→His) GPIIb associated to thrombasthenia exerts a dominant negative effect in stably transfected CHO cells
    • PMID:8883261
    • Ferrer M, Fernandez-Pinel M, Gonzalez-Manchon C, Gonzalez J, Ayuso MS, Parrilla R. A mutant (Arg327→His) GPIIb associated to thrombasthenia exerts a dominant negative effect in stably transfected CHO cells. Thromb Haemost 1996; 76:292-301; PMID:8883261
    • (1996) Thromb Haemost , vol.76 , pp. 292-301
    • Ferrer, M.1    Fernandez-Pinel, M.2    Gonzalez-Manchon, C.3    Gonzalez, J.4    Ayuso, M.S.5    Parrilla, R.6
  • 65
    • 7444240182 scopus 로고    scopus 로고
    • The integrin a subunit leg extends at a Ca2+-dependent epitope in the thigh/genu interface upon activation
    • PMID:15494438
    • Xie C, Shimaoka M, Xiao T, Schwab P, Klickstein LB, Springer TA. The integrin a subunit leg extends at a Ca2+-dependent epitope in the thigh/genu interface upon activation. Proc Natl Acad Sci USA 2004; 101:15422-7; PMID:15494438; http://dx.doi.org/10. 1073/pnas.0406680101
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 15422-15427
    • Xie, C.1    Shimaoka, M.2    Xiao, T.3    Schwab, P.4    Klickstein, L.B.5    Springer, T.A.6
  • 66
    • 0027530684 scopus 로고
    • The I domain is a major recognition site on the leukocyte integrin Mac-1 (CD11b/CD18) for four distinct adhesion ligands
    • PMID:7679388
    • Diamond MS, Garcia-Aguilar J, Bickford JK, Corbi AL, Springer TA. The I domain is a major recognition site on the leukocyte integrin Mac-1 (CD11b/CD18) for four distinct adhesion ligands. J Cell Biol 1993; 120:1031-43; PMID:7679388; http://dx.doi.org/10. 1083/jcb.120.4.1031
    • (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
  • 67
    • 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
    • PMID:8458080
    • 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; 72:857-67; PMID:8458080; http://dx.doi.org/10.1016/0092- 8674(93)90575-B
    • (1993) Cell , vol.72 , pp. 857-867
    • Michishita, M.1    Videm, V.2    Arnaout, M.A.3
  • 68
    • 0037428080 scopus 로고    scopus 로고
    • Structures of the aL I domain and its complex with ICAM-1 reveal a shape-shifting pathway for integrin regulation
    • PMID:12526797
    • Shimaoka M, Xiao T, Liu JH, Yang Y, Dong Y, Jun CD, et al. Structures of the aL I domain and its complex with ICAM-1 reveal a shape-shifting pathway for integrin regulation. Cell 2003; 112:99-111; PMID:12526797; http://dx.doi.org/10. 1016/S0092- 8674(02)01257-6
    • (2003) Cell , vol.112 , pp. 99-111
    • Shimaoka, M.1    Xiao, T.2    Liu, J.H.3    Yang, Y.4    Dong, Y.5    Jun, C.D.6
  • 69
    • 14744276916 scopus 로고    scopus 로고
    • An atomic resolution view of ICAM recognition in a complex between the binding domains of ICAM-3 and integrin αLβ2
    • PMID:15728350
    • Song G, Yang Y, Liu JH, Casasnovas JM, Shimaoka M, Springer TA, et al. An atomic resolution view of ICAM recognition in a complex between the binding domains of ICAM-3 and integrin αLβ2. Proc Natl Acad Sci USA 2005; 102:3366-71; PMID:15728350; http://dx.doi.org/10.1073/pnas.0500200102
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 3366-3371
    • Song, G.1    Yang, Y.2    Liu, J.H.3    Casasnovas, J.M.4    Shimaoka, M.5    Springer, T.A.6
  • 70
    • 0028986196 scopus 로고
    • Crystal structure of the A domain from the α subunit of integrin CR3 (CD11b/CD18)
    • PMID:7867070
    • Lee JO, Rieu P, Arnaout MA, Liddington R. Crystal structure of the A domain from the α subunit of integrin CR3 (CD11b/CD18). Cell 1995; 80:631-8; PMID:7867070; http://dx.doi.org/10.1016/0092- 8674(95)90517-0
    • (1995) Cell , vol.80 , pp. 631-638
    • Lee, J.O.1    Rieu, P.2    Arnaout, M.A.3    Liddington, R.4
  • 71
    • 0034737296 scopus 로고    scopus 로고
    • Structural basis of collagen recognition by integrin α2β1
    • PMID:10778855
    • Emsley J, Knight CG, Farndale RW, Barnes MJ, Liddington RC. Structural basis of collagen recognition by integrin α2β1. Cell 2000; 101:47-56; PMID:10778855; http://dx.doi.org/10.1016/S0092- 8674(00)80622-4
    • (2000) Cell , vol.101 , pp. 47-56
    • Emsley, J.1    Knight, C.G.2    Farndale, R.W.3    Barnes, M.J.4    Liddington, R.C.5
  • 72
    • 0029646107 scopus 로고
    • Two conformations of the integrin A-domain (Idomain): A pathway for activation?
    • PMID:8747460
    • Lee J-O, Bankston LA, Arnaout MA, Liddington RC. Two conformations of the integrin A-domain (Idomain): a pathway for activation? Structure 1995; 3:1333-40; PMID:8747460; http://dx.doi.org/10. 1016/S0969-2126(01)00271-4
    • (1995) Structure , vol.3 , pp. 1333-1340
    • Lee, J.-O.1    Bankston, L.A.2    Arnaout, M.A.3    Liddington, R.C.4
  • 73
    • 0037023363 scopus 로고    scopus 로고
    • Crystal structure of the extracellular segment of integrin αVβ3 in complex with an Arg-Gly-Asp ligand
    • PMID:11884718
    • Xiong JP, Stehle T, Zhang R, Joachimiak A, Frech M, Goodman SL, et al. Crystal structure of the extracellular segment of integrin αVβ3 in complex with an Arg-Gly-Asp ligand. Science 2002; 296:151-5; PMID:11884718; http://dx.doi.org/10.1126/science. 1069040
    • (2002) Science , vol.296 , pp. 151-155
    • Xiong, J.P.1    Stehle, T.2    Zhang, R.3    Joachimiak, A.4    Frech, M.5    Goodman, S.L.6
  • 74
    • 0034624058 scopus 로고    scopus 로고
    • An isoleucine-based allosteric switch controls affinity and shape shifting in integrin CD11b A-domain
    • PMID:11034990
    • Xiong J-P, Li R, Essafi M, Stehle T, Arnaout MA. An isoleucine-based allosteric switch controls affinity and shape shifting in integrin CD11b A-domain. J Biol Chem 2000; 275:38762-7; PMID:11034990; http:// dx.doi.org/10.1074/jbc.C000563200
    • (2000) J Biol Chem , vol.275 , pp. 38762-38767
    • Xiong, J.-P.1    Li, R.2    Essafi, M.3    Stehle, T.4    Arnaout, M.A.5
  • 75
    • 0029664968 scopus 로고    scopus 로고
    • An allosteric Ca2+ binding site on the β3-integrins that regulates the dissociation rate for RGD ligands
    • PMID:8702970
    • Hu DD, Barbas CF, Smith JW. An allosteric Ca2+ binding site on the β3-integrins that regulates the dissociation rate for RGD ligands. J Biol Chem 1996; 271:21745-51; PMID:8702970; http://dx.doi.org/10. 1074/jbc.271.36.21745
    • (1996) J Biol Chem , vol.271 , pp. 21745-21751
    • Hu, D.D.1    Barbas, C.F.2    Smith, J.W.3
  • 76
    • 0141625303 scopus 로고    scopus 로고
    • Structure of integrin α5β1 in complex with fibronectin
    • PMID:12970173
    • Takagi J, Strokovich K, Springer TA, Walz T. Structure of integrin α5β1 in complex with fibronectin. EMBO J 2003; 22:4607-15; PMID:12970173; http://dx.doi.org/10.1093/emboj/cdg445
    • (2003) EMBO J , vol.22 , pp. 4607-4615
    • Takagi, J.1    Strokovich, K.2    Springer, T.A.3    Walz, T.4
  • 77
    • 8544259562 scopus 로고    scopus 로고
    • Structural basis for allostery in integrins and binding of ligand-mimetic therapeutics to the platelet receptor for fibrinogen
    • PMID: 15378069
    • Xiao T, Takagi J, Wang J-h, Coller BS, Springer TA. Structural basis for allostery in integrins and binding of ligand-mimetic therapeutics to the platelet receptor for fibrinogen. Nature 2004; 432:59-67; PMID: 15378069; http://dx.doi.org/10.1038/nature02976
    • (2004) Nature , vol.432 , pp. 59-67
    • Xiao, T.1    Takagi, J.2    Wang, J.-H.3    Coller, B.S.4    Springer, T.A.5
  • 78
    • 79952940482 scopus 로고    scopus 로고
    • Regulation of integrin αIIbβ3 ligand binding and signaling by the metal ion binding sites in the β I domain
    • PMID:21309594
    • Raborn J, Wang W, Luo BH. Regulation of integrin αIIbβ3 ligand binding and signaling by the metal ion binding sites in the β I domain. Biochemistry 2011; 50:2084-91; PMID:21309594; http://dx.doi.org/10.1021/ bi2000092
    • (2011) Biochemistry , vol.50 , pp. 2084-2091
    • Raborn, J.1    Wang, W.2    Luo, B.H.3
  • 79
    • 0344628802 scopus 로고    scopus 로고
    • Bistable regulation of integrin adhesiveness by a bipolar metal ion cluster
    • PMID: 14608374
    • Chen J, Salas A, Springer TA. Bistable regulation of integrin adhesiveness by a bipolar metal ion cluster. Nat Struct Biol 2003; 10:995-1001; PMID: 14608374; http://dx.doi.org/10.1038/nsb1011
    • (2003) Nat Struct Biol , vol.10 , pp. 995-1001
    • Chen, J.1    Salas, A.2    Springer, T.A.3
  • 80
    • 11244258886 scopus 로고    scopus 로고
    • The relative influence of metal ion binding sites in the I-like domain and the interface with the hybrid domain on rolling and firm adhesion by integrin α4β7
    • PMID:15448154
    • Chen J, Takagi J, Xie C, Xiao T, Luo BH, Springer TA. The relative influence of metal ion binding sites in the I-like domain and the interface with the hybrid domain on rolling and firm adhesion by integrin α4β7. J Biol Chem 2004; 279:55556-61; PMID:15448154; http://dx.doi.org/10.1074/jbc. M407773200
    • (2004) J Biol Chem , vol.279 , pp. 55556-55561
    • Chen, J.1    Takagi, J.2    Xie, C.3    Xiao, T.4    Luo, B.H.5    Springer, T.A.6
  • 81
    • 0347695986 scopus 로고    scopus 로고
    • Role of ADMIDAS cation-binding site in ligand recognition by integrin α5β1
    • PMID:14532288
    • Mould AP, Barton SJ, Askari JA, Craig SE, Humphries MJ. Role of ADMIDAS cation-binding site in ligand recognition by integrin α5β1. J Biol Chem 2003; 278:51622-9; PMID:14532288; http://dx.doi.org/10. 1074/jbc.M306655200
    • (2003) J Biol Chem , vol.278 , pp. 51622-51629
    • Mould, A.P.1    Barton, S.J.2    Askari, J.A.3    Craig, S.E.4    Humphries, M.J.5
  • 82
    • 0036796740 scopus 로고    scopus 로고
    • Essay from the Genome Annotation Series: Distribution and Evolution of the von Willebrand/Integrin A domain: A widely dispersed domain with roles in cell adhesion and elsewhere
    • PMID:12388743
    • Whittaker CA, Hynes RO. Essay from the Genome Annotation Series: Distribution and Evolution of the von Willebrand/Integrin A domain: a widely dispersed domain with roles in cell adhesion and elsewhere. Mol Biol Cell 2002; 13:3369-87; PMID:12388743; http:// dx.doi.org/10.1091/mbc.E02-05-0259
    • (2002) Mol Biol Cell , vol.13 , pp. 3369-3387
    • Whittaker, C.A.1    Hynes, R.O.2
  • 83
    • 0034710157 scopus 로고    scopus 로고
    • The evolution of cell adhesion
    • PMID:10908592
    • Hynes RO, Zhao Q. The evolution of cell adhesion. J Cell Biol 2000; 150:F89-96; PMID:10908592; http:// dx.doi.org/10.1083/jcb.150.2.F89
    • (2000) J Cell Biol , vol.150
    • Hynes, R.O.1    Zhao, Q.2
  • 84
    • 0036089390 scopus 로고    scopus 로고
    • Conformational regulation of integrin structure and function
    • PMID:11988479
    • Shimaoka M, Takagi J, Springer TA. Conformational regulation of integrin structure and function. Annu Rev Biophys Biomol Struct 2002; 31:485-516; PMID:11988479; http://dx.doi.org/10.1146/annurev. biophys.31.101101.140922
    • (2002) Annu Rev Biophys Biomol Struct , vol.31 , pp. 485-516
    • Shimaoka, M.1    Takagi, J.2    Springer, T.A.3
  • 85
    • 0034625083 scopus 로고    scopus 로고
    • NMR and mutagenesis evidence for an I domain allosteric site that regulates lymphocyte function-associated antigen 1 ligand binding
    • PMID:10805782
    • Huth JR, Olejniczak ET, Mendoza R, Liang H, Harris EA, Lupher ML, Jr., et al. NMR and mutagenesis evidence for an I domain allosteric site that regulates lymphocyte function-associated antigen 1 ligand binding. Proc Natl Acad Sci USA 2000; 97:5231-6; PMID:10805782; http://dx.doi.org/10.1073/pnas.97. 10.5231
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 5231-5236
    • Huth, J.R.1    Olejniczak, E.T.2    Mendoza, R.3    Liang, H.4    Harris, E.A.5    Lupher Jr., M.L.6
  • 86
    • 0037076494 scopus 로고    scopus 로고
    • Does the integrin αA domain act as a ligand for its βA domain?
    • PMID: 12015130
    • Alonso JL, Essafi M, Xiong JP, Stehle T, Arnaout MA. Does the integrin αA domain act as a ligand for its βA domain? Curr Biol 2002; 12:R340-2; PMID: 12015130; http://dx.doi.org/10.1016/S0960-9822 (02)00852-7
    • (2002) Curr Biol , vol.12
    • Alonso, J.L.1    Essafi, M.2    Xiong, J.P.3    Stehle, T.4    Arnaout, M.A.5
  • 87
    • 1542357680 scopus 로고    scopus 로고
    • Intersubunit signal transmission in integrins by a receptor-like interaction with a pull spring
    • PMID:14978279
    • Yang W, Shimaoka M, Salas A, Takagi J, Springer TA. Intersubunit signal transmission in integrins by a receptor-like interaction with a pull spring. Proc Natl Acad Sci USA 2004; 101:2906-11; PMID:14978279; http://dx.doi.org/10. 1073/pnas.0307340101
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 2906-2911
    • Yang, W.1    Shimaoka, M.2    Salas, A.3    Takagi, J.4    Springer, T.A.5
  • 88
    • 0035094475 scopus 로고    scopus 로고
    • Geometry of metal-ligand interactions in proteins
    • PMID:11223517
    • Harding MM. Geometry of metal-ligand interactions in proteins. Acta Crystallogr D Biol Crystallogr 2001; 57:401-11; PMID:11223517; http://dx.doi.org/10. 1107/S0907444900019168
    • (2001) Acta Crystallogr D Biol Crystallogr , vol.57 , pp. 401-411
    • Harding, M.M.1
  • 89
    • 78049367272 scopus 로고    scopus 로고
    • Rolling cell adhesion
    • PMID:19575676
    • McEver RP, Zhu C. Rolling cell adhesion. Annu Rev Cell Dev Biol 2010; 26:363-96; PMID:19575676; http://dx.doi.org/10.1146/annurev.cellbio.042308. 113238
    • (2010) Annu Rev Cell Dev Biol , vol.26 , pp. 363-396
    • McEver, R.P.1    Zhu, C.2
  • 90
    • 0027990819 scopus 로고
    • Mutation of a ligand binding domain of β3 integrin: Integral role of oxygenated residues in αIIbβ3 (GPIIb-IIIa) receptor function
    • PMID:7520434
    • Bajt ML, Loftus JC. Mutation of a ligand binding domain of β3 integrin: integral role of oxygenated residues in αIIbβ3 (GPIIb-IIIa) receptor function. J Biol Chem 1994; 269:20913-9; PMID:7520434
    • (1994) J Biol Chem , vol.269 , pp. 20913-20919
    • Bajt, M.L.1    Loftus, J.C.2
  • 91
    • 33748431400 scopus 로고    scopus 로고
    • Regulation of outside-in signaling and affinity by the β2 I domain of integrin αLβ2
    • PMID:16920795
    • Chen J, Yang W, Kim M, Carman CV, Springer TA. Regulation of outside-in signaling and affinity by the β2 I domain of integrin αLβ2. Proc Natl Acad Sci USA 2006; 103:13062-7; PMID:16920795; http://dx.doi. org/10.1073/pnas.0605666103
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 13062-13067
    • Chen, J.1    Yang, W.2    Kim, M.3    Carman, C.V.4    Springer, T.A.5
  • 92
    • 34848856081 scopus 로고    scopus 로고
    • Aberrant activation of integrin α4β7 suppresses lymphocyte migration to the gut
    • PMID:17786243
    • Park EJ, Mora JR, Carman CV, Chen J, Sasaki Y, Cheng G, et al. Aberrant activation of integrin α4β7 suppresses lymphocyte migration to the gut. J Clin Invest 2007; 117:2526-38; PMID:17786243; http:// dx.doi.org/10.1172/JCI31570
    • (2007) J Clin Invest , vol.117 , pp. 2526-2538
    • Park, E.J.1    Mora, J.R.2    Carman, C.V.3    Chen, J.4    Sasaki, Y.5    Cheng, G.6
  • 93
    • 44349114473 scopus 로고    scopus 로고
    • Functional and computational studies of the ligand-associated metal binding site of β3 integrins
    • PMID:18175315
    • Murcia M, Jirouskova M, Li J, Coller BS, Filizola M. Functional and computational studies of the ligand-associated metal binding site of β3 integrins. Proteins 2008; 71:1779-91; PMID:18175315; http://dx.doi. org/10.1002/prot.21859
    • (2008) Proteins , vol.71 , pp. 1779-1791
    • Murcia, M.1    Jirouskova, M.2    Li, J.3    Coller, B.S.4    Filizola, M.5
  • 94
    • 0029786892 scopus 로고    scopus 로고
    • Ligand binding to integrin αIIbβ3 is dependent on a MIDAS-like domain in the β3 subunit
    • PMID: 8703003
    • Tozer EC, Liddington RC, Sutcliffe MJ, Smeeton AH, Loftus JC. Ligand binding to integrin αIIbβ3 is dependent on a MIDAS-like domain in the β3 subunit. J Biol Chem 1996; 271:21978-84; PMID: 8703003; http://dx.doi.org/10.1074/jbc.271.36.21978
    • (1996) J Biol Chem , vol.271 , pp. 21978-21984
    • Tozer, E.C.1    Liddington, R.C.2    Sutcliffe, M.J.3    Smeeton, A.H.4    Loftus, J.C.5
  • 95
    • 0036221518 scopus 로고    scopus 로고
    • Identification of critical residues for ligand binding in the integrin β3 I-domain by site-directed mutagenesis
    • PMID:12008962
    • Yamanouchi J, Hato T, Tamura T, Fujita S. Identification of critical residues for ligand binding in the integrin β3 I-domain by site-directed mutagenesis. Thromb Haemost 2002; 87:756-62; PMID:12008962
    • (2002) Thromb Haemost , vol.87 , pp. 756-762
    • Yamanouchi, J.1    Hato, T.2    Tamura, T.3    Fujita, S.4
  • 96
    • 0031055333 scopus 로고    scopus 로고
    • A genetic analysis of integrin function: Glanzmann thrombasthenia in vitro
    • PMID:9050889
    • Baker EK, Tozer EC, Pfaff M, Shattil SJ, Loftus JC, Ginsberg MH. A genetic analysis of integrin function: Glanzmann thrombasthenia in vitro. Proc Natl Acad Sci USA 1997; 94:1973-8; PMID:9050889; http://dx. doi.org/10.1073/ pnas.94.5.1973
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 1973-1978
    • Baker, E.K.1    Tozer, E.C.2    Pfaff, M.3    Shattil, S.J.4    Loftus, J.C.5    Ginsberg, M.H.6
  • 97
    • 78650724558 scopus 로고    scopus 로고
    • Cation-p interaction regulates ligand-binding affinity and signaling of integrin α4β7
    • PMID:21098296
    • Pan Y, Zhang K, Qi J, Yue J, Springer TA, Chen J. Cation-p interaction regulates ligand-binding affinity and signaling of integrin α4β7. Proc Natl Acad Sci USA 2010; 107:21388-93; PMID:21098296; http:// dx.doi.org/10.1073/pnas.1015487107
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 21388-21393
    • Pan, Y.1    Zhang, K.2    Qi, J.3    Yue, J.4    Springer, T.A.5    Chen, J.6
  • 98
    • 0036499161 scopus 로고    scopus 로고
    • The role of the CPNKEKEC sequence in the β2 subunit I domain in regulation of integrin αLβ2 (LFA-1)
    • PMID:11859118
    • Kamata T, Tieu KK, Tarui T, Puzon-McLaughlin W, Hogg N, Takada Y. The role of the CPNKEKEC sequence in the β2 subunit I domain in regulation of integrin αLβ2 (LFA-1). J Immunol 2002; 168:2296-301; PMID:11859118
    • (2002) J Immunol , vol.168 , pp. 2296-2301
    • Kamata, T.1    Tieu, K.K.2    Tarui, T.3    Puzon-McLaughlin, W.4    Hogg, N.5    Takada, Y.6
  • 99
    • 1842684991 scopus 로고    scopus 로고
    • Rolling adhesion through an extended conformation of integrin αLβ2 and relation to α I and β I-like domain interaction
    • PMID:15084269
    • Salas A, Shimaoka M, Kogan AN, Harwood C, von Andrian UH, Springer TA. Rolling adhesion through an extended conformation of integrin αLβ2 and relation to α I and β I-like domain interaction. Immunity 2004; 20:393-406; PMID:15084269; http://dx.doi.org/10.1016/S1074-7613(04)00082-2
    • (2004) Immunity , vol.20 , pp. 393-406
    • Salas, A.1    Shimaoka, M.2    Kogan, A.N.3    Harwood, C.4    Von Andrian, U.H.5    Springer, T.A.6
  • 100
    • 0023644247 scopus 로고
    • Purified intercellular adhesion molecule-1 (ICAM-1) is a ligand for lymphocyte function-associated antigen 1 (LFA-1)
    • PMID:3315233
    • Marlin SD, Springer TA. Purified intercellular adhesion molecule-1 (ICAM-1) is a ligand for lymphocyte function-associated antigen 1 (LFA-1). Cell 1987; 51: 813-9; PMID:3315233; http://dx.doi.org/10.1016/ 0092-8674(87)90104-8
    • (1987) Cell , vol.51 , pp. 813-819
    • Marlin, S.D.1    Springer, T.A.2
  • 101
    • 0028970566 scopus 로고
    • Regulation of integrin α5β 1-fibronectin interactions by divalent cations. Evidence for distinct classes of binding sites for Mn2+, Mg2+, and Ca2+
    • PMID:7592835
    • Mould AP, Akiyama SK, Humphries MJ. Regulation of integrin α5β 1-fibronectin interactions by divalent cations. Evidence for distinct classes of binding sites for Mn2+, Mg2+, and Ca2+. J Biol Chem 1995; 270:26270-7; PMID:7592835
    • (1995) J Biol Chem , vol.270 , pp. 26270-26277
    • Mould, A.P.1    Akiyama, S.K.2    Humphries, M.J.3
  • 102
    • 0033406615 scopus 로고    scopus 로고
    • Fine mapping of inhibitory anti-α5 monoclonal antibody epitopes that differentially affect integrin-ligand binding
    • PMID:10567237
    • Burrows L, Clark K, Mould AP, Humphries MJ. Fine mapping of inhibitory anti-α5 monoclonal antibody epitopes that differentially affect integrin-ligand binding. Biochem J 1999; 344:527-33; PMID:10567237; http://dx.doi.org/10.1042/0264-6021:3440527
    • (1999) Biochem J , vol.344 , pp. 527-533
    • Burrows, L.1    Clark, K.2    Mould, A.P.3    Humphries, M.J.4
  • 103
    • 0141960077 scopus 로고    scopus 로고
    • Structure of an integrin-ligand complex deduced from solution X-ray scattering and site-directed mutagenesis
    • PMID:12871973
    • Mould AP, Symonds EJ, Buckley PA, Grossmann JG, McEwan PA, Barton SJ, et al. Structure of an integrin-ligand complex deduced from solution X-ray scattering and site-directed mutagenesis. J Biol Chem 2003; 278:39993-9; PMID:12871973; http://dx.doi.org/10. 1074/jbc.M304627200
    • (2003) J Biol Chem , vol.278 , pp. 39993-39999
    • Mould, A.P.1    Symonds, E.J.2    Buckley, P.A.3    Grossmann, J.G.4    McEwan, P.A.5    Barton, S.J.6
  • 104
    • 33747344492 scopus 로고    scopus 로고
    • The specificity and function of the metal-binding sites in the integrin β3 A-domain
    • PMID:16723352
    • Pesho MM, Bledzka K, Michalec L, Cierniewski CS, Plow EF. The specificity and function of the metal-binding sites in the integrin β3 A-domain. J Biol Chem 2006; 281:23034-41; PMID:16723352; http://dx.doi. org/10.1074/jbc. M602856200
    • (2006) J Biol Chem , vol.281 , pp. 23034-23041
    • Pesho, M.M.1    Bledzka, K.2    Michalec, L.3    Cierniewski, C.S.4    Plow, E.F.5
  • 105
    • 0029036091 scopus 로고
    • Changes in the concentrations of extracellular Mg2+ and Ca2+ down-regulate E-cadherin and up-regulate α2β1 integrin function, activating keratinocyte migration on type I collagen
    • PMID:7537775
    • Grzesiak JJ, Pierschbacher MD. Changes in the concentrations of extracellular Mg2+ and Ca2+ down-regulate E-cadherin and up-regulate α2β1 integrin function, activating keratinocyte migration on type I collagen. J Invest Dermatol 1995; 104:768-74; PMID:7537775; http://dx.doi.org/ 10.1111/1523-1747.ep12606983
    • (1995) J Invest Dermatol , vol.104 , pp. 768-774
    • Grzesiak, J.J.1    Pierschbacher, M.D.2


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