메뉴 건너뛰기




Volumn 27, Issue , 2011, Pages 321-345

Regulation of integrin activation

Author keywords

Cell adhesion; Cell migration; Integrin; Nanodisc; Signal transduction; Transmembrane domain

Indexed keywords

BETA INTEGRIN; BINDING PROTEIN; CALCIUM; CELL PROTEIN; FILAMIN; GUANOSINE TRIPHOSPHATE; INTEGRIN; INTEGRIN BINDING PROTEIN 1; INTEGRIN CYTOPLASMIC DOMAIN ASSOCIATED PROTEIN 1; INTEGRIN LINKED KINASE; KINDLIN; MEMBRANE PROTEIN; MIGFILIN; RAP1 PROTEIN; UNCLASSIFIED DRUG;

EID: 80053329700     PISSN: 10810706     EISSN: 15308995     Source Type: Book Series    
DOI: 10.1146/annurev-cellbio-100109-104104     Document Type: Article
Times cited : (352)

References (144)
  • 1
    • 67650716492 scopus 로고    scopus 로고
    • The ins and outs of leukocyte integrin signaling
    • Abram CL, Lowell CA. 2009. The ins and outs of leukocyte integrin signaling. Annu. Rev. Immunol. 27:339-62
    • (2009) Annu. Rev. Immunol. , vol.27 , pp. 339-362
    • Abram, C.L.1    Lowell, C.A.2
  • 2
    • 16844381981 scopus 로고    scopus 로고
    • Three-dimensional em structure of the ectodomain of integrin αvβ3 in a complex with fibronectin
    • Adair BD, Xiong JP, Maddock C, Goodman SL, Arnaout MA, Yeager M. 2005. Three-dimensional EM structure of the ectodomain of integrin αVβ3 in a complex with fibronectin. J. Cell Biol. 168:1109-18
    • (2005) J. Cell Biol. , vol.168 , pp. 1109-1118
    • Adair, B.D.1    Xiong, J.P.2    Maddock, C.3    Goodman, S.L.4    Arnaout, M.A.5    Yeager, M.6
  • 5
    • 50849132538 scopus 로고    scopus 로고
    • Cells on the run: Shear-regulated integrin activation in leukocyte rolling and arrest on endothelial cells
    • Alon R, Ley K. 2008. Cells on the run: shear-regulated integrin activation in leukocyte rolling and arrest on endothelial cells. Curr. Opin. Cell Biol. 20:525-32
    • (2008) Curr. Opin. Cell Biol. , vol.20 , pp. 525-532
    • Alon, R.1    Ley, K.2
  • 6
    • 70450222316 scopus 로고    scopus 로고
    • The structure of an integrin/talin complex reveals the basis of inside-out signal transduction
    • Anthis NJ, Wegener KL, Ye F, Kim C, Goult BT, et al. 2009. The structure of an integrin/talin complex reveals the basis of inside-out signal transduction. EMBO J. 28:3623-32
    • (2009) EMBO J. , vol.28 , pp. 3623-3632
    • Anthis, N.J.1    Wegener, K.L.2    Ye, F.3    Kim, C.4    Goult, B.T.5
  • 7
    • 0033601259 scopus 로고    scopus 로고
    • Determination of the border between the transmembrane and cytoplasmic domains of human integrin subunits
    • Armulik A, Nilsson I, von Heijne G, Johansson S. 1999. Determination of the border between the transmembrane and cytoplasmic domains of human integrin subunits. J. Biol. Chem. 274:37030-34
    • (1999) J. Biol. Chem. , vol.274 , pp. 37030-37034
    • Armulik, A.1    Nilsson, I.2    Von Heijne, G.3    Johansson, S.4
  • 9
    • 0024846571 scopus 로고
    • Activation-dependent redistribution of the adhesion plaque protein, talin, in intact human platelets
    • DOI 10.1083/jcb.109.6.3333
    • Beckerle MC, Miller DE, Bertagnolli ME, Locke SJ. 1989. Activation-dependent redistribution of the adhesion plaque protein, talin, in intact human platelets. J. Cell Biol. 109:3333-46 (Pubitemid 20017983)
    • (1989) Journal of Cell Biology , vol.109 , Issue.6 , pp. 3333-3346
    • Beckerle, M.C.1    Miller, D.E.2    Bertagnolli, M.E.3    Locke, S.J.4
  • 10
    • 0036220127 scopus 로고    scopus 로고
    • Cysteine-rich module structure reveals a fulcrum for integrin rearrangement upon activation
    • DOI 10.1038/nsb779
    • Beglova N, Blacklow SC, Takagi J, Springer TA. 2002. Cysteine-rich module structure reveals a fulcrum for integrin rearrangement upon activation. Nat. Struct. Biol. 9:282-87 (Pubitemid 34289901)
    • (2002) Nature Structural Biology , vol.9 , Issue.4 , pp. 282-287
    • Beglova, N.1    Blacklow, S.C.2    Takagi, J.3    Springer, T.A.4
  • 11
    • 0034739854 scopus 로고    scopus 로고
    • Activated R-Ras, Rac1, PI 3-kinase and PKCε can each restore cell spreading inhibited by isolated integrin β1 cytoplasmic domains
    • DOI 10.1083/jcb.151.7.1549
    • Berrier AL, Mastrangelo AM, Downward J, Ginsberg M, LaFlamme SE. 2000. Activated R-ras, Rac1, PI 3-kinase and PKCε can each restore cell spreading inhibited by isolated integrin β1 cytoplasmic domains. J. Cell Biol. 151:1549-60 (Pubitemid 32047602)
    • (2000) Journal of Cell Biology , vol.151 , Issue.7 , pp. 1549-1560
    • Berrier, A.L.1    Mastrangelo, A.M.2    Downward, J.3    Ginsberg, M.4    LaFlamme, S.E.5
  • 14
    • 77953317401 scopus 로고    scopus 로고
    • The integrin coactivator kindlin-3 is expressed and functional in a non-hematopoietic cell, the endothelial cell
    • Bialkowska K, Ma YQ, Bledzka K, Sossey-Alaoui K, Izem L, et al. 2010. The integrin coactivator kindlin-3 is expressed and functional in a non-hematopoietic cell, the endothelial cell. J. Biol. Chem. 285:18640-49
    • (2010) J. Biol. Chem. , vol.285 , pp. 18640-18649
    • Bialkowska, K.1    Ma, Y.Q.2    Bledzka, K.3    Sossey-Alaoui, K.4    Izem, L.5
  • 15
    • 0034865567 scopus 로고    scopus 로고
    • A functional comparison of mutations in integrin β cytoplasmic domains: Effects on the regulation of tyrosine phosphorylation, cell spreading, cell attachment and β1 integrin conformation
    • Bodeau AL, Berrier AL, Mastrangelo AM, Martinez R, LaFlamme SE. 2001. A functional comparison of mutations in integrin βcytoplasmic domains: effects on the regulation of tyrosine phosphorylation, cell spreading, cell attachment and β1 integrin conformation. J. Cell Sci. 114:2795-807 (Pubitemid 32785458)
    • (2001) Journal of Cell Science , vol.114 , Issue.15 , pp. 2795-2807
    • Bodeau, A.L.1    Berrier, A.L.2    Mastrangelo, A.M.3    Martinez, R.4    LaFlamme, S.E.5
  • 19
    • 0033213922 scopus 로고    scopus 로고
    • The talin head domain binds to integrin βsubunit cytoplasmic tails and regulates integrin activation
    • Calderwood DA, Zent R, Grant R, Rees DJ, Hynes RO, Ginsberg MH. 1999. The talin head domain binds to integrin βsubunit cytoplasmic tails and regulates integrin activation. J. Biol. Chem. 274:28071-74
    • (1999) J. Biol. Chem. , vol.274 , pp. 28071-28074
    • Calderwood, D.A.1    Zent, R.2    Grant, R.3    Rees, D.J.4    Hynes, R.O.5    Ginsberg, M.H.6
  • 20
    • 0030924021 scopus 로고    scopus 로고
    • 1 integrin
    • DOI 10.1083/jcb.138.5.1149
    • Chang DD, Wong C, Smith H, Liu J. 1997. ICAP-1, a novel β1 integrin cytoplasmic domain-associated protein, binds to a conserved and functionally important NPXY sequence motif of β1 integrin. J. Cell Biol. 138:1149-57 (Pubitemid 27386463)
    • (1997) Journal of Cell Biology , vol.138 , Issue.5 , pp. 1149-1157
    • Chang, D.D.1    Wong, C.2    Smith, H.3    Liu, J.4
  • 25
    • 52649163308 scopus 로고    scopus 로고
    • CalDAG-GEFI and protein kinase C represent alternative pathways leading to activation of integrin αiIbβ3 in platelets
    • Cifuni SM, Wagner DD, Bergmeier W. 2008. CalDAG-GEFI and protein kinase C represent alternative pathways leading to activation of integrin αIIbβ3 in platelets. Blood 112:1696-703
    • (2008) Blood , vol.112 , pp. 1696-703
    • Cifuni, S.M.1    Wagner, D.D.2    Bergmeier, W.3
  • 26
    • 28344436780 scopus 로고    scopus 로고
    • Protease-activated receptors in hemostasis, thrombosis and vascular biology
    • DOI 10.1111/j.1538-7836.2005.01377.x
    • Coughlin SR. 2005. Protease-activated receptors in hemostasis, thrombosis and vascular biology. J. Thromb. Haemost. 3:1800-14 (Pubitemid 41716567)
    • (2005) Journal of Thrombosis and Haemostasis , vol.3 , Issue.8 , pp. 1800-1814
    • Coughlin, S.R.1
  • 27
    • 67650288199 scopus 로고    scopus 로고
    • Biochemical and structural properties of the integrin-associated cytoskeletal protein talin
    • CritchleyDR. 2009. Biochemical and structural properties of the integrin-associated cytoskeletal protein talin. Annu. Rev. Biophys. 38:235-54
    • (2009) Annu. Rev. Biophys. , vol.38 , pp. 235-254
    • Critchley, D.R.1
  • 29
    • 55549097150 scopus 로고    scopus 로고
    • Characterization of calcium-and integrinbinding protein 1 (CIB1) knockout platelets: Potential compensation by CIB family members
    • Denofrio JC, Yuan W, Temple BR, Gentry HR, Parise LV. 2008. Characterization of calcium-and integrinbinding protein 1 (CIB1) knockout platelets: potential compensation by CIB family members. Thromb. Haemost. 100:847-56
    • (2008) Thromb. Haemost. , vol.100 , pp. 847-856
    • Denofrio, J.C.1    Yuan, W.2    Temple, B.R.3    Gentry, H.R.4    Parise, L.V.5
  • 33
    • 77957779535 scopus 로고    scopus 로고
    • The structure of the talin head reveals a novel extended conformation of the FERM domain
    • Elliott PR, Goult BT, Kopp PM, Bate N, Grossmann JG, et al. 2010. The structure of the talin head reveals a novel extended conformation of the FERM domain. Structure 18:1289-99
    • (2010) Structure , vol.18 , pp. 1289-1299
    • Elliott, P.R.1    Goult, B.T.2    Kopp, P.M.3    Bate, N.4    Grossmann, J.G.5
  • 34
    • 0030611604 scopus 로고    scopus 로고
    • Integrin αIIβ3 reconstituted into lipid bilayers is nonclustered in its activated state but clusters after fibrinogen binding
    • DOI 10.1021/bi9702187
    • Erb EM, Tangemann K, Bohrmann B, Muller B, Engel J. 1997. Integrin αIIbβ3 reconstituted into lipid bilayers is nonclustered in its activated state but clusters after fibrinogen binding. Biochemistry 36:7395-402 (Pubitemid 27262361)
    • (1997) Biochemistry , vol.36 , Issue.24 , pp. 7395-7402
    • Erb, E.-M.1    Tangemann, K.2    Bohrmann, B.3    Muller, B.4    Engel, J.5
  • 35
    • 0031014969 scopus 로고    scopus 로고
    • 2+-mediated activation of Rap1 in human platelets
    • DOI 10.1093/emboj/16.2.252
    • Franke B, Akkerman JW, Bos JL. 1997. Rapid Ca2+-mediated activation of Rap1 in human platelets. EMBO J. 16:252-59 (Pubitemid 27049383)
    • (1997) EMBO Journal , vol.16 , Issue.2 , pp. 252-259
    • Franke, B.1    Akkerman, J.-W.N.2    Bos, J.L.3
  • 37
    • 59149097344 scopus 로고    scopus 로고
    • Mechanically activated integrin switch controls α5β1 function
    • Friedland JC, Lee MH, Boettiger D. 2009. Mechanically activated integrin switch controls α5β1 function. Science 323:642-44
    • (2009) Science , vol.323 , pp. 642-644
    • Friedland, J.C.1    Lee, M.H.2    Boettiger, D.3
  • 38
    • 71149097258 scopus 로고    scopus 로고
    • The pseudoactive site of ILK is essential for its binding to α-parvin and localization to focal adhesions
    • Fukuda K, Gupta S, Chen K, Wu C, Qin J. 2009. The pseudoactive site of ILK is essential for its binding to α-parvin and localization to focal adhesions. Mol. Cell 36:819-30
    • (2009) Mol. Cell , vol.36 , pp. 819-830
    • Fukuda, K.1    Gupta, S.2    Chen, K.3    Wu, C.4    Qin, J.5
  • 41
    • 77956510396 scopus 로고    scopus 로고
    • Central region of talin has a unique fold that binds vinculin and actin
    • Gingras AR, Bate N, Goult BT, Patel B, Kopp PM, et al. 2010. Central region of talin has a unique fold that binds vinculin and actin. J. Biol. Chem. 285:29577-87
    • (2010) J. Biol. Chem. , vol.285 , pp. 29577-29587
    • Gingras, A.R.1    Bate, N.2    Goult, B.T.3    Patel, B.4    Kopp, P.M.5
  • 43
    • 18944403970 scopus 로고    scopus 로고
    • A coiled-coil structure of the αiIbβ3 integrin transmembrane and cytoplasmic domains in its resting state
    • Gottschalk KE. 2005. A coiled-coil structure of the αIIbβ3 integrin transmembrane and cytoplasmic domains in its resting state. Structure 13:703-12
    • (2005) Structure , vol.13 , pp. 703-712
    • Gottschalk, K.E.1
  • 44
    • 77949566587 scopus 로고    scopus 로고
    • Structure of a double ubiquitin-like domain in the talin head: A role in integrin activation
    • Goult BT, Bouaouina M, Elliott PR, Bate N, Patel B, et al. 2010. Structure of a double ubiquitin-like domain in the talin head: a role in integrin activation. EMBO J. 29:1069-80
    • (2010) EMBO J. , vol.29 , pp. 1069-1080
    • Goult, B.T.1    Bouaouina, M.2    Elliott, P.R.3    Bate, N.4    Patel, B.5
  • 45
    • 79551647521 scopus 로고    scopus 로고
    • Talin-dependent integrin activation is required for fibrin clot retraction by platelets
    • Haling JR, Monkley SJ, Critchley DR, Petrich BG. 2011. Talin-dependent integrin activation is required for fibrin clot retraction by platelets. Blood 117:1718-22
    • (2011) Blood , vol.117 , pp. 1718-1722
    • Haling, J.R.1    Monkley, S.J.2    Critchley, D.R.3    Petrich, B.G.4
  • 48
    • 66449119343 scopus 로고    scopus 로고
    • Kindlin-1 and-2 directly bind the C-terminal region of βintegrin cytoplasmic tails and exert integrin-specific activation effects
    • Harburger DS, Bouaouina M, Calderwood DA. 2009. Kindlin-1 and-2 directly bind the C-terminal region of βintegrin cytoplasmic tails and exert integrin-specific activation effects. J. Biol. Chem. 284:11485-97
    • (2009) J. Biol. Chem. , vol.284 , pp. 11485-11497
    • Harburger, D.S.1    Bouaouina, M.2    Calderwood, D.A.3
  • 52
    • 33751517699 scopus 로고    scopus 로고
    • Disabled-2 is a novel αIIb-integrin-binding protein that negatively regulates platelet-fibrinogen interactions and platelet aggregation
    • DOI 10.1242/jcs.03195
    • Huang CL, Cheng JC, Stern A, Hsieh JT, Liao CH, Tseng CP. 2006. Disabled-2 is a novel αIIb-integrinbinding protein that negatively regulates platelet-fibrinogen interactions and platelet aggregation. J. Cell Sci. 119:4420-30 (Pubitemid 44830641)
    • (2006) Journal of Cell Science , vol.119 , Issue.21 , pp. 4420-4430
    • Huang, C.-L.1    Cheng, J.-C.2    Stern, A.3    Hsieh, J.-T.4    Liao, C.-H.5    Tseng, C.-P.6
  • 53
    • 0029966310 scopus 로고    scopus 로고
    • Breaking the integrin hinge. A defined structural constraint regulates integrin signaling
    • Hughes PE, Diaz-Gonzalez F, Leong L, Wu C, McDonald JA, et al. 1996. Breaking the integrin hinge. A defined structural constraint regulates integrin signaling. J. Biol. Chem. 271:6571-74
    • (1996) J. Biol. Chem. , vol.271 , pp. 6571-6574
    • Hughes, P.E.1    Diaz-Gonzalez, F.2    Leong, L.3    Wu, C.4    McDonald, J.A.5
  • 54
    • 0029048813 scopus 로고
    • The conserved membrane-proximal region of an integrin cytoplasmic domain specifies ligand binding affinity
    • Hughes PE, O'Toole TE, Ylanne J, Shattil SJ, Ginsberg MH. 1995. The conserved membrane-proximal region of an integrin cytoplasmic domain specifies ligand binding affinity. J. Biol. Chem. 270:12411-17
    • (1995) J. Biol. Chem. , vol.270 , pp. 12411-12417
    • Hughes, P.E.1    O'Toole, T.E.2    Ylanne, J.3    Shattil, S.J.4    Ginsberg, M.H.5
  • 55
    • 0030909050 scopus 로고    scopus 로고
    • Suppression of integrin activation: A novel function of a Ras/Raf- initiated MAP kinase pathway
    • DOI 10.1016/S0092-8674(00)81892-9
    • Hughes PE, Renshaw MW, Pfaff M, Forsyth J, Keivens VM, et al. 1997. Suppression of integrin activation: a novel function of a Ras/Raf-initiated MAP kinase pathway. Cell 88:521-30 (Pubitemid 27154417)
    • (1997) Cell , vol.88 , Issue.4 , pp. 521-530
    • Hughes, P.E.1    Renshaw, M.W.2    Pfaff, M.3    Forsyth, J.4    Keivens, V.M.5    Schwartz, M.A.6    Ginsberg, M.H.7
  • 57
    • 0035850915 scopus 로고    scopus 로고
    • Structure. An anthropomorphic integrin
    • Humphries MJ, Mold AP. 2001. Structure. An anthropomorphic integrin. Science 294:316-17
    • (2001) Science , vol.294 , pp. 316-317
    • Humphries, M.J.1    Mold, A.P.2
  • 58
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • DOI 10.1016/S0092-8674(02)00971-6
    • Hynes RO. 2002. Integrins: bidirectional, allosteric signaling machines. Cell 110:673-87 (Pubitemid 35283958)
    • (2002) Cell , vol.110 , Issue.6 , pp. 673-687
    • Hynes, R.O.1
  • 59
    • 63249102905 scopus 로고    scopus 로고
    • Migfilin, a molecular switch in regulation of integrin activation
    • Ithychanda SS, Das M, Ma YQ, Ding K, Wang X, et al. 2009a. Migfilin, a molecular switch in regulation of integrin activation. J. Biol. Chem. 284:4713-22
    • (2009) J. Biol. Chem. , vol.284 , pp. 4713-4722
    • Ithychanda, S.S.1    Das, M.2    Ma, Y.Q.3    Ding, K.4    Wang, X.5
  • 60
    • 71749121849 scopus 로고    scopus 로고
    • Identification and characterization of multiple similar ligand-binding repeats in filamin: Implication on filamin-mediated receptor clustering and crosstalk
    • Ithychanda SS, Hsu D, Li H, Yan L, Liu DD, et al. 2009b. Identification and characterization of multiple similar ligand-binding repeats in filamin: implication on filamin-mediated receptor clustering and crosstalk. J. Biol. Chem. 284:35113-21
    • (2009) J. Biol. Chem. , vol.284 , pp. 35113-35121
    • Ithychanda, S.S.1    Hsu, D.2    Li, H.3    Yan, L.4    Liu, D.D.5
  • 61
    • 33747872565 scopus 로고    scopus 로고
    • Analyzing the mechanism of Rap1 activation in platelets: Rap1 activation is related to the release reaction mediated through the collagen receptor GPVI
    • DOI 10.1016/j.thromres.2005.11.002, PII S0049384805004342
    • Jung SM, Ohnuma M, Watanabe N, Sonoda M, Handa M, Moroi M. 2006. Analyzing the mechanism of Rap1 activation in platelets: Rap1 activation is related to the release reaction mediated through the collagen receptor GPVI. Thromb. Res. 118:509-21 (Pubitemid 44292806)
    • (2006) Thrombosis Research , vol.118 , Issue.4 , pp. 509-521
    • Jung, S.M.1    Ohnuma, M.2    Watanabe, N.3    Sonoda, M.4    Handa, M.5    Moroi, M.6
  • 62
    • 77957777260 scopus 로고    scopus 로고
    • The structure of the talin/integrin complex at a lipid bilayer: An NMR and MD simulation study
    • Kalli AC, Wegener KL, Goult BT, Anthis NJ, Campbell ID, Sansom MS. 2010. The structure of the talin/integrin complex at a lipid bilayer: an NMR and MD simulation study. Structure 18:1280-88
    • (2010) Structure , vol.18 , pp. 1280-1288
    • Kalli, A.C.1    Wegener, K.L.2    Goult, B.T.3    Anthis, N.J.4    Campbell, I.D.5    Sansom, M.S.6
  • 64
    • 0034284386 scopus 로고    scopus 로고
    • How proteins adapt to a membrane-water interface
    • DOI 10.1016/S0968-0004(00)01626-1, PII S0968000400016261
    • Killian JA, von Heijne G. 2000. How proteins adapt to a membrane-water interface. Trends Biochem. Sci. 25:429-34 (Pubitemid 30662410)
    • (2000) Trends in Biochemical Sciences , vol.25 , Issue.9 , pp. 429-434
    • Killian, J.A.1    Von Heijne, G.2
  • 65
    • 66549097709 scopus 로고    scopus 로고
    • Interactions of platelet integrinαIIb andβ3 transmembrane domains in mammalian cell membranes and their role in integrin activation
    • KimC, Lau TL, Ulmer TS, GinsbergMH. 2009. Interactions of platelet integrinαIIb andβ3 transmembrane domains in mammalian cell membranes and their role in integrin activation. Blood 113:4747-53
    • (2009) Blood , vol.113 , pp. 4747-4753
    • Kim, C.1    Lau, T.L.2    Ulmer, T.S.3    Ginsberg, M.H.4
  • 66
    • 0042681786 scopus 로고    scopus 로고
    • Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins
    • DOI 10.1126/science.1084174
    • Kim M, Carman CV, Springer TA. 2003. Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins. Science 301:1720-25 (Pubitemid 37174365)
    • (2003) Science , vol.301 , Issue.5640 , pp. 1720-1725
    • Kim, M.1    Carman, C.V.2    Springer, T.A.3
  • 67
    • 1342346591 scopus 로고    scopus 로고
    • The kindler syndrome protein is regulated by transforming growth factor-β and involved in integrin-mediated adhesion
    • DOI 10.1074/jbc.M307978200
    • Kloeker S, Major MB, Calderwood DA, Ginsberg MH, Jones DA, Beckerle MC. 2004. The Kindler syndrome protein is regulated by transforming growth factor-βand involved in integrin-mediated adhesion. J. Biol. Chem. 279:6824-33 (Pubitemid 38248824)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.8 , pp. 6824-6833
    • Kloeker, S.1    Major, M.B.2    Calderwood, D.A.3    Ginsberg, M.H.4    Jones, D.A.5    Beckerle, M.C.6
  • 70
    • 58049193581 scopus 로고    scopus 로고
    • Structural basis of the migfilin-filamin interaction and competition with integrin βtails
    • Lad Y, Jiang P, Ruskamo S, Harburger DS, Ylanne J, et al. 2008. Structural basis of the migfilin-filamin interaction and competition with integrin βtails. J. Biol. Chem. 283:35154-63
    • (2008) J. Biol. Chem. , vol.283 , pp. 35154-35163
    • Lad, Y.1    Jiang, P.2    Ruskamo, S.3    Harburger, D.S.4    Ylanne, J.5
  • 72
    • 0027994108 scopus 로고
    • Single subunit chimeric integrins as mimics and inhibitors of endogenous integrin functions in receptor localization, cell spreading and migration, and matrix assembly
    • DOI 10.1083/jcb.126.5.1287
    • LaFlamme SE, Thomas LA, Yamada SS, Yamada KM. 1994. Single subunit chimeric integrins as mimics and inhibitors of endogenous integrin functions in receptor localization, cell spreading and migration, and matrix assembly. J. Cell Biol. 126:1287-98 (Pubitemid 24266560)
    • (1994) Journal of Cell Biology , vol.126 , Issue.5 , pp. 1287-1298
    • LaFlamme, S.E.1    Thomas, L.A.2    Yamada, S.S.3    Yamada, K.M.4
  • 74
    • 70350064314 scopus 로고    scopus 로고
    • Integrin-linked kinase is an adaptor with essential functions during mouse development
    • Lange A, Wickstrom SA, Jakobson M, Zent R, Sainio K, Fassler R. 2009. Integrin-linked kinase is an adaptor with essential functions during mouse development. Nature 461:1002-6
    • (2009) Nature , vol.461 , pp. 1002-6
    • Lange, A.1    Wickstrom, S.A.2    Jakobson, M.3    Zent, R.4    Sainio, K.5    Fassler, R.6
  • 75
    • 47049087659 scopus 로고    scopus 로고
    • Structure of the integrin αiIb transmembrane segment
    • Lau TL, Dua V, Ulmer TS. 2008a. Structure of the integrin αIIb transmembrane segment. J. Biol. Chem. 283:16162-68
    • (2008) J. Biol. Chem. , vol.283 , pp. 16162-16168
    • Lau, T.L.1    Dua, V.2    Ulmer, T.S.3
  • 76
    • 65649127175 scopus 로고    scopus 로고
    • The structure of the integrin αiIbβ3 transmembrane complex explains integrin transmembrane signaling
    • Lau TL, Kim C, Ginsberg MH, Ulmer TS. 2009. The structure of the integrin αIIbβ3 transmembrane complex explains integrin transmembrane signaling. EMBO J. 28:1351-61
    • (2009) EMBO J. , vol.28 , pp. 1351-1361
    • Lau, T.L.1    Kim, C.2    Ginsberg, M.H.3    Ulmer, T.S.4
  • 77
    • 41449108071 scopus 로고    scopus 로고
    • Structure of the integrin β3 transmembrane segment in phospholipid bicelles and detergent micelles
    • DOI 10.1021/bi800107a
    • Lau TL, Partridge AW, Ginsberg MH, Ulmer TS. 2008b. Structure of the integrin β3 transmembrane segment in phospholipid bicelles and detergent micelles. Biochemistry 47:4008-16 (Pubitemid 351458115)
    • (2008) Biochemistry , vol.47 , Issue.13 , pp. 4008-4016
    • Lau, T.-L.1    Partridge, A.W.2    Ginsberg, M.H.3    Ulmer, T.S.4
  • 78
  • 81
    • 0037207135 scopus 로고    scopus 로고
    • Characterization of the monomeric form of the transmembrane and cytoplasmic domains of the integrin β3 subunit by NMR spectroscopy
    • DOI 10.1021/bi026822l
    • Li R, Babu CR, Valentine K, Lear JD, Wand AJ, et al. 2002. Characterization of the monomeric form of the transmembrane and cytoplasmic domains of the integrin β3 subunit by NMR spectroscopy. Biochemistry 41:15618-24 (Pubitemid 36062466)
    • (2002) Biochemistry , vol.41 , Issue.52 , pp. 15618-15624
    • Li, R.1    Babu, C.R.2    Valentine, K.3    Lear, J.D.4    Wand, A.J.5    Bennett, J.S.6    DeGrado, W.F.7
  • 85
    • 0035805633 scopus 로고    scopus 로고
    • Association of the membrane proximal regions of the α and β subunit cytoplasmic domains constrains an integrin in the inactive state
    • Lu C, Takagi J, Springer TA. 2001. Association of the membrane proximal regions of the α and β subunit cytoplasmic domains constrains an integrin in the inactive state. J. Biol. Chem. 276:14642-48
    • (2001) J. Biol. Chem. , vol.276 , pp. 14642-14648
    • Lu, C.1    Takagi, J.2    Springer, T.A.3
  • 87
    • 16644396938 scopus 로고    scopus 로고
    • A specific interface between integrin transmembrane helices and affinity for ligand
    • Luo BH, Springer TA, Takagi J. 2004. A specific interface between integrin transmembrane helices and affinity for ligand. PLoS Biol. 2:e153
    • (2004) PLoS Biol. , vol.2
    • Luo, B.H.1    Springer, T.A.2    Takagi, J.3
  • 88
    • 43149085289 scopus 로고    scopus 로고
    • 3 integrins
    • DOI 10.1083/jcb.200710196
    • Ma YQ, Qin J, Wu C, Plow EF. 2008. Kindlin-2 (Mig-2): a co-activator ofβ3 integrins. J. Cell Biol. 181:439-46 (Pubitemid 351645034)
    • (2008) Journal of Cell Biology , vol.181 , Issue.3 , pp. 439-446
    • Ma, Y.-Q.1    Qin, J.2    Wu, C.3    Plow, E.F.4
  • 89
    • 0037076211 scopus 로고    scopus 로고
    • C. elegans PAT-4/ILK functions as an adaptor protein within integrin adhesion complexes
    • DOI 10.1016/S0960-9822(02)00810-2, PII S0960982202008102
    • Mackinnon AC, Qadota H, Norman KR, Moerman DG, Williams BD. 2002. C. elegans PAT-4/ILK functions as an adaptor protein within integrin adhesion complexes. Curr. Biol. 12:787-97 (Pubitemid 34514364)
    • (2002) Current Biology , vol.12 , Issue.10 , pp. 787-797
    • Mackinnon A.Craig1    Qadota, H.2    Norman, K.R.3    Moerman, D.G.4    Williams, B.D.5
  • 90
    • 61949240364 scopus 로고    scopus 로고
    • A point mutation in KINDLIN3 ablates activation of three integrin subfamilies in humans
    • Malinin NL, Zhang L, Choi J, Ciocea A, Razorenova O, et al. 2009. A point mutation in KINDLIN3 ablates activation of three integrin subfamilies in humans. Nat. Med. 15:313-18
    • (2009) Nat. Med. , vol.15 , pp. 313-318
    • Malinin, N.L.1    Zhang, L.2    Choi, J.3    Ciocea, A.4    Razorenova, O.5
  • 91
    • 77954755706 scopus 로고    scopus 로고
    • Two mutations in the KINDLIN3 gene of a new leukocyte adhesion deficiency III patient reveal distinct effects on leukocyte function in vitro
    • McDowall A, Svensson L, Stanley P, Patzak I, Chakravarty P, et al. 2010. Two mutations in the KINDLIN3 gene of a new leukocyte adhesion deficiency III patient reveal distinct effects on leukocyte function in vitro. Blood 115:4834-42
    • (2010) Blood , vol.115 , pp. 4834-4842
    • McDowall, A.1    Svensson, L.2    Stanley, P.3    Patzak, I.4    Chakravarty, P.5
  • 93
    • 0028954797 scopus 로고
    • Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function
    • Miyamoto S, Akiyama SK, Yamada KM. 1995. Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function. Science 267:883-85
    • (1995) Science , vol.267 , pp. 883-885
    • Miyamoto, S.1    Akiyama, S.K.2    Yamada, K.M.3
  • 95
    • 55249083592 scopus 로고    scopus 로고
    • Kindlin-3: A new gene involved in the pathogenesis of LAD-III
    • Mory A, Feigelson SW, Yarali N, Kilic SS, Bayhan GI, et al. 2008. Kindlin-3: a new gene involved in the pathogenesis of LAD-III. Blood 112:2591.
    • (2008) Blood , vol.112 , pp. 2591
    • Mory, A.1    Feigelson, S.W.2    Yarali, N.3    Kilic, S.S.4    Bayhan, G.I.5
  • 96
    • 61949352480 scopus 로고    scopus 로고
    • Kindlin-3 is required for β2 integrinmediated leukocyte adhesion to endothelial cells
    • Moser M, Bauer M, Schmid S, Ruppert R, Schmidt S, et al. 2009a. Kindlin-3 is required for β2 integrinmediated leukocyte adhesion to endothelial cells. Nat. Med. 15:300-5
    • (2009) Nat. Med. , vol.15 , pp. 300-305
    • Moser, M.1    Bauer, M.2    Schmid, S.3    Ruppert, R.4    Schmidt, S.5
  • 97
    • 66149128873 scopus 로고    scopus 로고
    • The tail of integrins, talin, and kindlins
    • Moser M, Legate KR, Zent R, Fassler R. 2009b. The tail of integrins, talin, and kindlins. Science 324:895-99
    • (2009) Science , vol.324 , pp. 895-899
    • Moser, M.1    Legate, K.R.2    Zent, R.3    Fassler, R.4
  • 98
    • 40449133970 scopus 로고    scopus 로고
    • Kindlin-3 is essential for integrin activation and platelet aggregation
    • DOI 10.1038/nm1722, PII NM1722
    • Moser M, Nieswandt B, Ussar S, Pozgajova M, Fassler R. 2008. Kindlin-3 is essential for integrin activation and platelet aggregation. Nat. Med. 14:325-30 (Pubitemid 351347914)
    • (2008) Nature Medicine , vol.14 , Issue.3 , pp. 325-330
    • Moser, M.1    Nieswandt, B.2    Ussar, S.3    Pozgajova, M.4    Fassler, R.5
  • 99
    • 0031046185 scopus 로고    scopus 로고
    • Identification of a novel calcium-binding protein that interacts with the integrin α(IIb) cytoplasmic domain
    • DOI 10.1074/jbc.272.8.4651
    • Naik UP, Patel PM, Parise LV. 1997. Identification of a novel calcium-binding protein that interacts with the integrin αIIb cytoplasmic domain. J. Biol. Chem. 272:4651-54 (Pubitemid 27090004)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.8 , pp. 4651-4654
    • Naik, U.P.1    Patel, P.M.2    Parise, L.V.3
  • 100
    • 33847639732 scopus 로고    scopus 로고
    • Applications of phospholipid bilayer nanodiscs in the study of membranes and membrane proteins
    • DOI 10.1021/bi602371n
    • Nath A, Atkins WM, Sligar SG. 2007. Applications of phospholipid bilayer nanodiscs in the study of membranes and membrane proteins. Biochemistry 46:2059-69 (Pubitemid 46355317)
    • (2007) Biochemistry , vol.46 , Issue.8 , pp. 2059-2069
    • Nath, A.1    Atkins, W.M.2    Sligar, S.G.3
  • 101
    • 37549029679 scopus 로고    scopus 로고
    • Loss of talin1 in platelets abrogates integrin activation, platelet aggregation, and thrombus formation in vitro and in vivo
    • Nieswandt B, Moser M, Pleines I, Varga-Szabo D, Monkley S, et al. 2007. Loss of talin1 in platelets abrogates integrin activation, platelet aggregation, and thrombus formation in vitro and in vivo. J. Exp. Med. 204:3113-18
    • (2007) J. Exp. Med. , vol.204 , pp. 3113-3118
    • Nieswandt, B.1    Moser, M.2    Pleines, I.3    Varga-Szabo, D.4    Monkley, S.5
  • 102
    • 0038494921 scopus 로고    scopus 로고
    • Platelet-collagen interaction: Is GPVI the central receptor?
    • DOI 10.1182/blood-2002-12-3882
    • Nieswandt B, Watson SP. 2003 Platelet-collagen interaction: is GPVI the central receptor? Blood 102:449-61 (Pubitemid 36841960)
    • (2003) Blood , vol.102 , Issue.2 , pp. 449-461
    • Nieswandt, B.1    Watson, S.P.2
  • 103
    • 0035968234 scopus 로고    scopus 로고
    • Integrin-linked kinase (ILK) binding to paxillin LD1 motif regulates ILK localization to focal adhesions
    • Nikolopoulos SN, Turner CE. 2001. Integrin-linked kinase (ILK) binding to paxillin LD1 motif regulates ILK localization to focal adhesions. J. Biol. Chem. 276:23499-505
    • (2001) J. Biol. Chem. , vol.276 , pp. 23499-23505
    • Nikolopoulos, S.N.1    Turner, C.E.2
  • 104
    • 0037059789 scopus 로고    scopus 로고
    • Molecular dissection of actopaxin-integrin-linked kinase-paxillin interactions and their role in subcellular localization
    • DOI 10.1074/jbc.M108612200
    • Nikolopoulos SN, Turner CE. 2002. Molecular dissection of actopaxin-integrin-linked kinase-paxillin interactions and their role in subcellular localization. J. Biol. Chem. 277:1568-75 (Pubitemid 34968915)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.2 , pp. 1568-1575
    • Nikolopoulos, S.N.1    Turner, C.E.2
  • 106
    • 0030756508 scopus 로고    scopus 로고
    • Defective platelet activation in Gα(q)-deficient mice
    • DOI 10.1038/38284
    • Offermanns S, Toombs CF, Hu YH, Simon MI. 1997. Defective platelet activation in Gαq-deficient mice. Nature 389:183-86 (Pubitemid 27400600)
    • (1997) Nature , vol.389 , Issue.6647 , pp. 183-186
    • Offermanns, S.1    Toombs, C.F.2    Hu, Y.-H.3    Simon, M.I.4
  • 107
    • 14844323604 scopus 로고    scopus 로고
    • Transmembrane domain helix packing stabilizes integrin αIIbβ3 in the low affinity state
    • DOI 10.1074/jbc.M412701200
    • Partridge AW, Liu S, Kim S, Bowie JU, Ginsberg MH. 2005. Transmembrane domain helix packing stabilizes integrin αIIbβ3 in the low affinity state. J. Biol. Chem. 280:7294-300 (Pubitemid 40341287)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.8 , pp. 7294-7300
    • Partridge, A.W.1    Liu, S.2    Kim, S.3    Bowie, J.U.4    Ginsberg, M.H.5
  • 108
    • 0036306621 scopus 로고    scopus 로고
    • Evidence that the platelet integrin αIIbβ3 is regulated by the integrin-linked kinase, ILK, in a PI3-kinase dependent pathway
    • Pasquet JM, Noury M, Nurden AT. 2002. Evidence that the platelet integrin αIIbβ3 is regulated by the integrin-linked kinase, IL K, in a PI3-kinase dependent pathway. Thromb. Haemost. 88:115-22 (Pubitemid 34752276)
    • (2002) Thrombosis and Haemostasis , vol.88 , Issue.1 , pp. 115-122
    • Pasquet, J.-M.1    Noury, M.2    Nurden, A.T.3
  • 109
    • 77956412906 scopus 로고    scopus 로고
    • Dissecting the molecular architecture of integrin adhesion sites by cryo-electron tomography
    • Patla I, Volberg T, Elad N, Hirschfeld-Warneken V, Grashoff C, et al. 2010. Dissecting the molecular architecture of integrin adhesion sites by cryo-electron tomography. Nat. Cell Biol. 12:909-15
    • (2010) Nat. Cell Biol. , vol.12 , pp. 909-915
    • Patla, I.1    Volberg, T.2    Elad, N.3    Hirschfeld-Warneken, V.4    Grashoff, C.5
  • 111
    • 37549064277 scopus 로고    scopus 로고
    • Talin is required for integrinmediated platelet function in hemostasis and thrombosis
    • Petrich BG, Marchese P, Ruggeri ZM, Spiess S, Weichert RA, et al. 2007b. Talin is required for integrinmediated platelet function in hemostasis and thrombosis. J. Exp. Med. 204:3103-11
    • (2007) J. Exp. Med. , vol.204 , pp. 3103-3111
    • Petrich, B.G.1    Marchese, P.2    Ruggeri, Z.M.3    Spiess, S.4    Weichert, R.A.5
  • 112
    • 0842285677 scopus 로고    scopus 로고
    • Signaling by ephrinB1 and Eph kinases in platelets promotes Rap1 activation, platelet adhesion, and aggregation via effector pathways that do not require phosphorylation of ephrinB1
    • DOI 10.1182/blood-2003-06-1781
    • Prevost N, Woulfe DS, Tognolini M, Tanaka T, Jian W, et al. 2004. Signaling by ephrinB1 and Eph kinases in platelets promotes Rap1 activation, platelet adhesion, and aggregation via effector pathways that do not require phosphorylation of ephrinB1. Blood 103:1348-55 (Pubitemid 38168647)
    • (2004) Blood , vol.103 , Issue.4 , pp. 1348-1355
    • Prevost, N.1    Woulfe, D.S.2    Tognolini, M.3    Tanaka, T.4    Jian, W.5    Fortna, R.R.6    Jiang, H.7    Brass, L.F.8
  • 113
    • 33750337536 scopus 로고    scopus 로고
    • How the headpiece hinge angle is opened: New insights into the dynamics of integrin activation
    • DOI 10.1083/jcb.200602071
    • Puklin-Faucher E, Gao M, Schulten K, Vogel V. 2006. How the headpiece hinge angle is opened: new insights into the dynamics of integrin activation. J. Cell Biol. 175:349-60 (Pubitemid 44631428)
    • (2006) Journal of Cell Biology , vol.175 , Issue.2 , pp. 349-360
    • Puklin-Faucher, E.1    Gao, M.2    Schulten, K.3    Vogel, V.4
  • 114
    • 0034632070 scopus 로고    scopus 로고
    • The UNC-112 gene in Caenorhabditis elegans encodes a novel component of cell-matrix adhesion structures required for integrin localization in the muscle cell membrane
    • DOI 10.1083/jcb.150.1.253
    • Rogalski TM, Mullen GP, Gilbert MM, Williams BD, Moerman DG. 2000. The UNC-112 gene in Caenorhabditis elegans encodes a novel component of cell-matrix adhesion structures required for integrin localization in the muscle cell membrane. J. Cell Biol. 150:253-64 (Pubitemid 30480998)
    • (2000) Journal of Cell Biology , vol.150 , Issue.1 , pp. 253-264
    • Rogalski, T.M.1    Mullen, G.P.2    Gilbert, M.M.3    Williams, B.D.4    Moerman, D.G.5
  • 115
    • 0032523064 scopus 로고    scopus 로고
    • Integrin signaling: The platelet paradigm
    • Shattil SJ, Kashiwagi H, Pampori N. 1998. Integrin signaling: the platelet paradigm. Blood 91:2645-57 (Pubitemid 28227512)
    • (1998) Blood , vol.91 , Issue.8 , pp. 2645-2657
    • Shattil, S.J.1    Kashiwagi, H.2    Pampori, N.3
  • 117
    • 4444264392 scopus 로고    scopus 로고
    • Integrins: Dynamic scaffolds for adhesion and signaling in platelets
    • DOI 10.1182/blood-2004-04-1257
    • Shattil SJ, Newman PJ. 2004. Integrins: dynamic scaffolds for adhesion and signaling in platelets. Blood 104:1606-15 (Pubitemid 39202265)
    • (2004) Blood , vol.104 , Issue.6 , pp. 1606-1615
    • Shattil, S.J.1    Newman, P.J.2
  • 118
    • 61949086409 scopus 로고    scopus 로고
    • Leukocyte adhesion deficiency-III is caused by mutations in KINDLIN3 affecting integrin activation
    • Svensson L, Howarth K, McDowall A, Patzak I, Evans R, et al. 2009. Leukocyte adhesion deficiency-III is caused by mutations in KINDLIN3 affecting integrin activation. Nat. Med. 15:306-12
    • (2009) Nat. Med. , vol.15 , pp. 306-312
    • Svensson, L.1    Howarth, K.2    McDowall, A.3    Patzak, I.4    Evans, R.5
  • 120
    • 0037031906 scopus 로고    scopus 로고
    • Global conformational rearrangements in integrin extracellular domains in outside-in and inside-out signaling
    • Takagi J, Petre BM, Walz T, Springer TA. 2002. Global conformational rearrangements in integrin extracellular domains in outside-in and inside-out signaling. Cell 110:599-11
    • (2002) Cell , vol.110 , pp. 599-511
    • Takagi, J.1    Petre, B.M.2    Walz, T.3    Springer, T.A.4
  • 121
    • 33744829519 scopus 로고    scopus 로고
    • An interaction between integrin and the talin FERM domain mediates integrin activation but not linkage to the cytoskeleton
    • DOI 10.1038/ncb1411, PII N1411
    • Tanentzapf G, Brown NH. 2006. An interaction between integrin and the talin FERM domain mediates integrin activation but not linkage to the cytoskeleton. Nat. Cell Biol. 8:601-6 (Pubitemid 43827353)
    • (2006) Nature Cell Biology , vol.8 , Issue.6 , pp. 601-606
    • Tanentzapf, G.1    Brown, N.H.2
  • 122
    • 0037418837 scopus 로고    scopus 로고
    • Migfilin and Mig-2 link focal adhesions to filamin and the actin cytoskeleton and function in cell shape modulation
    • DOI 10.1016/S0092-8674(03)00163-6
    • Tu Y, Wu S, Shi X, Chen K, Wu C. 2003. Migfilin and Mig-2 link focal adhesions to filamin and the actin cytoskeleton and function in cell shape modulation. Cell 113:37-47 (Pubitemid 36411958)
    • (2003) Cell , vol.113 , Issue.1 , pp. 37-47
    • Tu, Y.1    Wu, S.2    Shi, X.3    Chen, K.4    Wu, C.5
  • 123
    • 58149388333 scopus 로고    scopus 로고
    • A dual role for integrin-linked kinase in platelets: Regulating integrin function and α-granule secretion
    • Tucker KL, Sage T, Stevens JM, Jordan PA, Jones S, et al. 2008. A dual role for integrin-linked kinase in platelets: regulating integrin function and α-granule secretion. Blood 112:4523-31
    • (2008) Blood , vol.112 , pp. 4523-4531
    • Tucker, K.L.1    Sage, T.2    Stevens, J.M.3    Jordan, P.A.4    Jones, S.5
  • 124
    • 0035954396 scopus 로고    scopus 로고
    • NMR analysis of structure and dynamics of the cytosolic tails of integrin αIIβ3 in aqueous solution
    • Ulmer TS, Yaspan B, Ginsberg MH, Campbell ID. 2001. NMR analysis of structure and dynamics of the cytosolic tails of integrin αIIbβ3 in aqueous solution. Biochemistry 40:7498-508 (Pubitemid 32578014)
    • (2001) Biochemistry , vol.40 , Issue.25 , pp. 7498-7508
    • Ulmer, T.S.1    Yaspan, B.2    Ginsberg, M.H.3    Campbell, I.D.4
  • 125
    • 58149154658 scopus 로고    scopus 로고
    • Loss of Kindlin-1 causes skin atrophy and lethal neonatal intestinal epithelial dysfunction
    • Ussar S, Moser M, Widmaier M, Rognoni E, Harrer C, et al. 2008. Loss of Kindlin-1 causes skin atrophy and lethal neonatal intestinal epithelial dysfunction. PLoS Genet. 4:e1000289
    • (2008) PLoS Genet. , vol.4
    • Ussar, S.1    Moser, M.2    Widmaier, M.3    Rognoni, E.4    Harrer, C.5
  • 126
    • 0037031551 scopus 로고    scopus 로고
    • 3 "inside-out" activation as regulated by its cytoplasmic face
    • DOI 10.1016/S0092-8674(02)00906-6
    • Vinogradova O, Velyvis A, Velyviene A, Hu B, Haas T, et al. 2002. A structural mechanism of integrin αIIbβ3 "inside-out" activation as regulated by its cytoplasmic face. Cell 110:587-97 (Pubitemid 35247839)
    • (2002) Cell , vol.110 , Issue.5 , pp. 587-597
    • Vinogradova, O.1    Velyvis, A.2    Velyviene, A.3    Hu, B.4    Haas, T.A.5    Plow, E.F.6    Qin, J.7
  • 132
    • 3042708179 scopus 로고    scopus 로고
    • The PINCH-ILK-parvin complexes: Assembly, functions and regulation
    • DOI 10.1016/j.bbamcr.2004.01.006, PII S0167488904000965
    • Wu C. 2004. The PINCH-ILK-parvin complexes: assembly, functions and regulation. Biochim. Biophys. Acta 1692:55-62 (Pubitemid 38891767)
    • (2004) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1692 , Issue.2-3 , pp. 55-62
    • Wu, C.1
  • 134
    • 0037023363 scopus 로고    scopus 로고
    • Crystal structure of the extracellular segment of integrin αVβ3 in complex with an Arg-Gly-Asp ligand
    • DOI 10.1126/science.1069040
    • Xiong JP, Stehle T, Zhang R, Joachimiak A, Frech M, et al. 2002. Crystal structure of the extracellular segment of integrin αVβ3 in complex with an Arg-Gly-Asp ligand. Science 296:151-55 (Pubitemid 34280076)
    • (2002) Science , vol.296 , Issue.5565 , pp. 151-155
    • Xiong, J.-P.1    Stehle, T.2    Zhang, R.3    Joachimiak, A.4    Frech, M.5    Goodman, S.L.6    Arnaout, M.A.7
  • 135
    • 0031929760 scopus 로고    scopus 로고
    • Vinculin knockout results in heart and brain defects during embryonic development
    • XuW, Baribault H, AdamsonED. 1998. Vinculin knockout results in heart and brain defects during embryonic development. Development 125:327-37 (Pubitemid 28064445)
    • (1998) Development , vol.125 , Issue.2 , pp. 327-337
    • Xu, W.1    Baribault, H.2    Adamson, E.D.3
  • 136
    • 75749154495 scopus 로고    scopus 로고
    • Recreation of the terminal events in physiological integrin activation
    • Ye F, Hu G, Taylor D, Ratnikov B, Bobkov AA, et al. 2010. Recreation of the terminal events in physiological integrin activation. J. Cell Biol. 188:157-73
    • (2010) J. Cell Biol. , vol.188 , pp. 157-173
    • Ye, F.1    Hu, G.2    Taylor, D.3    Ratnikov, B.4    Bobkov, A.A.5
  • 137
    • 42649140589 scopus 로고    scopus 로고
    • Integrin αiIbβ3 in a membrane environment remains the same height after Mn2+ activation when observed by cryoelectron tomography
    • Ye F, Liu J, Winkler H, Taylor KA. 2008. Integrin αIIbβ3 in a membrane environment remains the same height after Mn2+ activation when observed by cryoelectron tomography. J. Mol. Biol. 378:976-86
    • (2008) J. Mol. Biol. , vol.378 , pp. 976-986
    • Ye, F.1    Liu, J.2    Winkler, H.3    Taylor, K.A.4
  • 138
    • 0027263655 scopus 로고
    • Distinct functions of integrin α and β subunit cytoplasmic domains in cell spreading and formation of focal adhesions
    • Ylanne J, Chen Y, O'Toole TE, Loftus JC, Takada Y, Ginsberg MH. 1993. Distinct functions of integrin α and β subunit cytoplasmic domains in cell spreading and formation of focal adhesions. J. Cell Biol. 122:223-33 (Pubitemid 23188813)
    • (1993) Journal of Cell Biology , vol.122 , Issue.1 , pp. 223-233
    • Ylanne, J.1    Chen, Y.2    O'Toole, T.E.3    Loftus, J.C.4    Takada, Y.5    Ginsberg, M.H.6
  • 140
    • 0035809918 scopus 로고    scopus 로고
    • Drosophila integrin-linked kinase is required at sites of integrin adhesion to link the cytoskeleton to the plasma membrane
    • DOI 10.1083/jcb.152.5.1007
    • Zervas CG, Gregory SL, Brown NH. 2001. Drosophila integrin-linked kinase is required at sites of integrin adhesion to link the cytoskeleton to the plasma membrane. J. Cell Biol. 152:1007-18 (Pubitemid 34286076)
    • (2001) Journal of Cell Biology , vol.152 , Issue.5 , pp. 1007-1018
    • Zervas, C.G.1    Gregory, S.L.2    Brown, N.H.3
  • 141
    • 0032590074 scopus 로고    scopus 로고
    • 1 cytoplasmic domain with ICAP-1 protein
    • DOI 10.1074/jbc.274.1.11
    • Zhang XA, Hemler ME. 1999. Interaction of the integrin β1 cytoplasmic domain with ICAP-1 protein. J. Biol. Chem. 274:11-19 (Pubitemid 29035023)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.1 , pp. 11-19
    • Zhang, X.A.1    Hemler, M.E.2
  • 142
    • 34948882323 scopus 로고    scopus 로고
    • Requirement of α and β subunit transmembrane helix separation for integrin outside-in signaling
    • DOI 10.1182/blood-2007-03-080077
    • Zhu J, Carman CV, Kim M, Shimaoka M, Springer TA, Luo BH. 2007. Requirement of α and β subunit transmembrane helix separation for integrin outside-in signaling. Blood 110:2475-83 (Pubitemid 47523169)
    • (2007) Blood , vol.110 , Issue.7 , pp. 2475-2483
    • Zhu, J.1    Carman, C.V.2    Kim, M.3    Shimaoka, M.4    Springer, T.A.5    Luo, B.-H.6
  • 143
    • 64749101260 scopus 로고    scopus 로고
    • The structure of a receptor with two associating transmembrane domains on the cell surface: Integrin αiIbβ3
    • Zhu J, Luo BH, Barth P, Schonbrun J, Baker D, Springer TA. 2009. The structure of a receptor with two associating transmembrane domains on the cell surface: integrin αIIbβ3. Mol. Cell 34:234-49
    • (2009) Mol. Cell , vol.34 , pp. 234-249
    • Zhu, J.1    Luo, B.H.2    Barth, P.3    Schonbrun, J.4    Baker, D.5    Springer, T.A.6
  • 144
    • 57749116060 scopus 로고    scopus 로고
    • Structure of a complete integrin ectodomain in a physiologic resting state and activation and deactivation by applied forces
    • Zhu J, Luo BH, Xiao T, Zhang C, Nishida N, Springer TA. 2008. Structure of a complete integrin ectodomain in a physiologic resting state and activation and deactivation by applied forces. Mol. Cell 32:849-61
    • (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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.