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Volumn 119, Issue 1, 2012, Pages 26-33

Reconstruction of integrin activation

Author keywords

[No Author keywords available]

Indexed keywords

G PROTEIN COUPLED RECEPTOR; INTEGRIN; INTEGRIN RECEPTOR; LACTOSE PERMEASE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;

EID: 84862924585     PISSN: 00064971     EISSN: 15280020     Source Type: Journal    
DOI: 10.1182/blood-2011-04-292128     Document Type: Review
Times cited : (98)

References (120)
  • 1
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • DOI 10.1016/S0092-8674(02)00971-6
    • Hynes RO. Integrins: bidirectional, allosteric signaling machines. Cell. 2002;110(6):673-687. (Pubitemid 35283958)
    • (2002) Cell , vol.110 , Issue.6 , pp. 673-687
    • Hynes, R.O.1
  • 2
    • 54049152026 scopus 로고    scopus 로고
    • The GPIIb/IIIa (integrin alphaIIbbeta3) odyssey: A technology-driven saga of a receptor with twists, turns, and even a bend
    • Coller BS, Shattil SJ. The GPIIb/IIIa (integrin alphaIIbbeta3) odyssey: a technology-driven saga of a receptor with twists, turns, and even a bend. Blood. 2008;112(8):3011-3025.
    • (2008) Blood , vol.112 , Issue.8 , pp. 3011-3025
    • Coller, B.S.1    Shattil, S.J.2
  • 3
    • 0032523064 scopus 로고    scopus 로고
    • Integrin signaling: The platelet paradigm
    • Shattil SJ, Kashiwagi H, Pampori N. Integrin signaling: the platelet paradigm. Blood. 1998;91(8): 2645-2657. (Pubitemid 28227512)
    • (1998) Blood , vol.91 , Issue.8 , pp. 2645-2657
    • Shattil, S.J.1    Kashiwagi, H.2    Pampori, N.3
  • 4
    • 77949862490 scopus 로고    scopus 로고
    • The final steps of integrin activation: The end game
    • Shattil SJ, Kim C, Ginsberg MH. The final steps of integrin activation: the end game. Nat Rev Mol Cell Biol. 2010;11(4):288-300.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , Issue.4 , pp. 288-300
    • Shattil, S.J.1    Kim, C.2    Ginsberg, M.H.3
  • 5
    • 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. Integrins: dynamic scaffolds for adhesion and signaling in platelets. Blood. 2004;104(6):1606-1615. (Pubitemid 39202265)
    • (2004) Blood , vol.104 , Issue.6 , pp. 1606-1615
    • Shattil, S.J.1    Newman, P.J.2
  • 6
    • 0034663430 scopus 로고    scopus 로고
    • Thrombasthenic mice generated by replacement of the integrin alpha(IIb) gene: Demonstration that transcriptional activation of this megakaryocytic locus precedes lineage commitment
    • Tronik-Le Roux D, Roullot V, Poujol C, Kortulewski T, Nurden P, Marguerie G. Thrombasthenic mice generated by replacement of the integrin alpha(IIb) gene: demonstration that transcriptional activation of this megakaryocytic locus precedes lineage commitment. Blood. 2000; 96(4):1399-1408. (Pubitemid 30658470)
    • (2000) Blood , vol.96 , Issue.4 , pp. 1399-1408
    • Tronik-Le, R.D.1    Roullot, V.2    Poujol, C.3    Kortulewski, T.4    Nurden, P.5    Marguerie, G.6
  • 7
    • 0034568429 scopus 로고    scopus 로고
    • Glanzmann thrombasthenia: Integrin alpha IIb beta 3 deficiency
    • Tomiyama Y. Glanzmann thrombasthenia: integrin alpha IIb beta 3 deficiency. Int J Hematol. 2000;72(4):448-454.
    • (2000) Int J Hematol , vol.72 , Issue.4 , pp. 448-454
    • Tomiyama, Y.1
  • 9
    • 0028028267 scopus 로고
    • Glanzmann thrombasthenia: New insights from an historical perspective
    • Coller BS, Seligsohn U, Peretz H, Newman PJ. Glanzmann thrombasthenia: new insights from an historical perspective. Semin Hematol. 1994; 31(4):301-311. (Pubitemid 24325182)
    • (1994) Seminars in Hematology , vol.31 , Issue.4 , pp. 301-311
    • Coller, B.S.1    Seligsohn, U.2    Peretz, H.3    Newman, P.J.4
  • 10
    • 0030664425 scopus 로고    scopus 로고
    • 3 complex
    • .Wang R, Shattil SJ, Ambruso DR, Newman PJ. Truncation of the cytoplasmic domain of beta3 in a variant form of Glanzmann thrombasthenia abrogates signaling through the integrin alpha(IIb)beta3 complex. J Clin Invest. 1997; 100(9):2393-2403. (Pubitemid 27500165)
    • (1997) Journal of Clinical Investigation , vol.100 , Issue.9 , pp. 2393-2403
    • Wang, R.1    Shattil, S.J.2    Ambruso, D.R.3    Newman, P.J.4
  • 11
    • 0026614923 scopus 로고
    • Ser-752->Pro mutation in the cytoplasmic domain of integrin beta 3 subunit and defective activation of platelet integrin alpha IIb beta 3 (glycoprotein IIb-IIIa) in a variant of Glanzmann thrombasthenia
    • Chen YP, Djaffar I, Pidard D, et al. Ser-752->Pro mutation in the cytoplasmic domain of integrin beta 3 subunit and defective activation of platelet integrin alpha IIb beta 3 (glycoprotein IIb-IIIa) in a variant of Glanzmann thrombasthenia. Proc Natl Acad Sci U S A. 1992;89(21):10169-10173.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , Issue.21 , pp. 10169-10173
    • Chen, Y.P.1    Djaffar, I.2    Pidard, D.3
  • 12
    • 0034233731 scopus 로고    scopus 로고
    • Genetic analysis of integrin function in man: LAD-1 and other syndromes
    • DOI 10.1016/S0945-053X(00)00066-4, PII S0945053X00000664
    • Hogg N, Bates PA. Genetic analysis of integrin function in man: LAD-1 and other syndromes. Matrix Biol. 2000;19(3):211-222. (Pubitemid 30601754)
    • (2000) Matrix Biology , vol.19 , Issue.3 , pp. 211-222
    • Hogg, N.1    Bates, P.A.2
  • 13
    • 61949086409 scopus 로고    scopus 로고
    • Leukocyte adhesion deficiency-III is caused by mutations in KINDLIN3 affecting integrin activation
    • Svensson L, Howarth K, McDowall A, et al. Leukocyte adhesion deficiency-III is caused by mutations in KINDLIN3 affecting integrin activation. Nat Med. 2009;15(3):306-312.
    • (2009) Nat Med , vol.15 , Issue.3 , pp. 306-312
    • Svensson, L.1    Howarth, K.2    McDowall, A.3
  • 14
    • 61949240364 scopus 로고    scopus 로고
    • A point mutation in KINDLIN3 ablates activation of three integrin subfamilies in humans
    • Malinin NL, Zhang L, Choi J, et al. A point mutation in KINDLIN3 ablates activation of three integrin subfamilies in humans. Nat Med. 2009;15(3): 313-318.
    • (2009) Nat Med , vol.15 , Issue.3 , pp. 313-318
    • Malinin, N.L.1    Zhang, L.2    Choi, J.3
  • 15
    • 66549121768 scopus 로고    scopus 로고
    • LAD-1/variant syndrome is caused by mutations in FERMT3
    • Kuijpers TW, van de Vijver E, Weterman MA, et al. LAD-1/variant syndrome is caused by mutations in FERMT3. Blood. 2009;113(19):4740- 4746.
    • (2009) Blood , vol.113 , Issue.19 , pp. 4740-4746
    • Kuijpers, T.W.1    Van De Vijver, E.2    Weterman, M.A.3
  • 16
    • 0141670816 scopus 로고    scopus 로고
    • LAD-III, a novel group of leukocyte integrin activation deficiencies
    • DOI 10.1016/j.it.2003.08.001
    • Alon R, Etzioni A. LAD-III, a novel group of leukocyte integrin activation deficiencies. Trends Immunol. 2003;24(10):561-566. (Pubitemid 37205208)
    • (2003) Trends in Immunology , vol.24 , Issue.10 , pp. 561-566
    • Alon, R.1    Etzioni, A.2
  • 17
    • 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, et al. Two mutations in the KINDLIN3 gene of a new leukocyte adhesion deficiency III patient reveal distinct effects on leukocyte function in vitro. Blood. 2010; 115(23):4834-4842.
    • (2010) Blood , vol.115 , Issue.23 , pp. 4834-4842
    • McDowall, A.1    Svensson, L.2    Stanley, P.3
  • 19
    • 70450225549 scopus 로고    scopus 로고
    • Kindler syndrome pathogenesis and fermitin family homologue 1 (kindlin-1) function
    • D'Souza MA, Kimble RM, McMillan JR. Kindler syndrome pathogenesis and fermitin family homologue 1 (kindlin-1) function. Dermatol Clin. 2010;28(1):115-118.
    • (2010) Dermatol Clin , vol.28 , Issue.1 , pp. 115-118
    • D'Souza, M.A.1    Kimble, R.M.2    McMillan, J.R.3
  • 27
    • 0032568695 scopus 로고    scopus 로고
    • 1-ATPase is a highly efficient molecular motor that rotates with discrete 120 degree steps
    • DOI 10.1016/S0092-8674(00)81456-7
    • Yasuda R, Noji H, Kinosita K Jr, Yoshida M. F1-ATPase is a highly efficient molecular motor that rotates with discrete 120 degree steps. Cell. 1998;93(7):1117-1124. (Pubitemid 28307417)
    • (1998) Cell , vol.93 , Issue.7 , pp. 1117-1124
    • Yasuda, R.1    Noji, H.2    Kinosita Jr., K.3    Yoshida, M.4
  • 28
    • 0030934380 scopus 로고    scopus 로고
    • Direct observation of the rotation of F1-ATPase
    • Noji H, Yasuda R, Yoshida M, Kinosita K Jr. Direct observation of the rotation of F1-ATPase. Nature. 1997;386(6622):299-302.
    • (1997) Nature , vol.386 , Issue.6622 , pp. 299-302
    • Noji, H.1    Yasuda, R.2    Yoshida, M.3    Kinosita Jr., K.4
  • 30
    • 64149100431 scopus 로고    scopus 로고
    • RIAM activates integrins by linking talin to ras GTPase membrane-targeting sequences
    • Lee HS, Lim CJ, Puzon-McLaughlinW, Shattil SJ, Ginsberg MH. RIAM activates integrins by linking talin to ras GTPase membrane-targeting sequences. J Biol Chem. 2009;284(8):5119-5127.
    • (2009) J Biol Chem , vol.284 , Issue.8 , pp. 5119-5127
    • Lee, H.S.1    Lim, C.J.2    Puzon-McLaughlin, W.3    Shattil, S.J.4    Ginsberg, M.H.5
  • 32
    • 8544259562 scopus 로고    scopus 로고
    • Structural basis for allostery in integrins and binding to fibrinogen-mimetic therapeutics
    • DOI 10.1038/nature02976
    • 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(7013):59-67. (Pubitemid 39490825)
    • (2004) Nature , vol.432 , Issue.7013 , pp. 59-67
    • Xia, T.1    Takagi, J.2    Coller, B.S.3    Wang, J.-H.4    Springer, T.A.5
  • 34
    • 0037023363 scopus 로고    scopus 로고
    • Crystal structure of the extracellular segment of integrin alphaVbeta3 in complex with an Arg-Gly-Asp ligand
    • DOI 10.1126/science.1069040
    • Xiong JP, Stehle T, Zhang R, et al. Crystal structure of the extracellular segment of integrin alpha Vbeta3 in complex with an Arg-Gly-Asp ligand. Science. 2002;296(5565):151-155. (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
  • 35
    • 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. Structure of a complete integrin ectodomain in a physiologic resting state and activation and deactivation by applied forces. Mol Cell. 2008;32(6):849-861.
    • (2008) Mol Cell , vol.32 , Issue.6 , pp. 849-861
    • Zhu, J.1    Luo, B.H.2    Xiao, T.3    Zhang, C.4    Nishida, N.5    Springer, T.A.6
  • 36
    • 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, et al. The structure of an integrin/talin complex reveals the basis of inside-out signal transduction. EMBO J. 2009; 28(22):3623-3632.
    • (2009) EMBO J , vol.28 , Issue.22 , pp. 3623-3632
    • Anthis, N.J.1    Wegener, K.L.2    Ye, F.3
  • 37
    • 65649127175 scopus 로고    scopus 로고
    • The structure of the integrin alphaIIbbeta3 transmembrane complex explains integrin transmembrane signalling
    • Lau TL, Kim C, Ginsberg MH, Ulmer TS. The structure of the integrin alphaIIbbeta3 transmembrane complex explains integrin transmembrane signalling. EMBO J. 2009;28(9):1351-1361.
    • (2009) EMBO J , vol.28 , Issue.9 , pp. 1351-1361
    • Lau, T.L.1    Kim, C.2    Ginsberg, M.H.3    Ulmer, T.S.4
  • 39
    • 16844381981 scopus 로고    scopus 로고
    • Three-dimensional EM structure of the ectodomain of integrin-alphaV-beta3 in a complex with fibronectin
    • Adair BD, Xiong JP, Maddock C, Goodman SL, Arnaout MA, Yeager M. Three-dimensional EM structure of the ectodomain of integrin-alphaV-beta3 in a complex with fibronectin. J Cell Biol. 2005;168(7):1109-1118.
    • (2005) J Cell Biol , vol.168 , Issue.7 , 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
  • 40
    • 77957034686 scopus 로고    scopus 로고
    • Requirement of open headpiece conformation for activation of leukocyte integrin alphaXbeta2
    • Chen X, Xie C, Nishida N, Li Z,Walz T, Springer TA. Requirement of open headpiece conformation for activation of leukocyte integrin alphaXbeta2. Proc Natl Acad Sci U S A. 2010;107(33):14727-14732.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , Issue.33 , pp. 14727-14732
    • Chen, X.1    Xie, C.2    Nishida, N.3    Li, Z.4    Walz, T.5    Springer, T.A.6
  • 41
    • 33749522074 scopus 로고    scopus 로고
    • 2 Integrins by Conversion from Bent to Extended Conformations
    • DOI 10.1016/j.immuni.2006.07.016, PII S1074761306004274
    • Nishida N, Xie C, Shimaoka M, Cheng Y, Walz T, Springer TA. Activation of leukocyte beta2 integrins by conversion from bent to extended conformations. Immunity. 2006;25(4):583-594. (Pubitemid 44529036)
    • (2006) Immunity , vol.25 , Issue.4 , pp. 583-594
    • Nishida, N.1    Xie, C.2    Shimaoka, M.3    Cheng, Y.4    Walz, T.5    Springer, T.A.6
  • 42
    • 0037031906 scopus 로고    scopus 로고
    • Global conformational earrangements in integrin extracellular domains in outside-in and inside-out signaling
    • DOI 10.1016/S0092-8674(02)00935-2
    • Takagi J, Petre BM, Walz T, Springer TA. Global conformational rearrangements in integrin extra-cellular domains in outside-in and inside-out signaling. Cell. 2002;110(5):599-611. (Pubitemid 35247840)
    • (2002) Cell , vol.110 , Issue.5 , pp. 599-611
    • Takagi, J.1    Petre, B.M.2    Walz, T.3    Springer, T.A.4
  • 43
    • 75749154495 scopus 로고    scopus 로고
    • Re-creation of the terminal events in physiological integrin activation
    • Ye F, Hu G, Taylor D, et al. Re-creation of the terminal events in physiological integrin activation. J Cell Biol. 2010;188(1):157-173.
    • (2010) J Cell Biol , vol.188 , Issue.1 , pp. 157-173
    • Ye, F.1    Hu, G.2    Taylor, D.3
  • 44
    • 0025519981 scopus 로고
    • Affinity modulation of the alpha IIb beta 3 integrin (platelet GPIIb-IIIa) is an intrinsic property of the receptor
    • O'Toole TE, Loftus JC, Du XP, et al. Affinity modulation of the alpha IIb beta 3 integrin (platelet GPIIb-IIIa) is an intrinsic property of the receptor. Cell Regul. 1990;1(12):883-893.
    • (1990) Cell Regul , vol.1 , Issue.12 , pp. 883-893
    • O'Toole, T.E.1    Loftus, J.C.2    Du, X.P.3
  • 45
    • 0033213922 scopus 로고    scopus 로고
    • The Talin head domain binds to integrin beta subunit cytoplasmic tails and regulates integrin activation
    • Calderwood DA, Zent R, Grant R, Rees DJ, Hynes RO, Ginsberg MH. The Talin head domain binds to integrin beta subunit cytoplasmic tails and regulates integrin activation. J Biol Chem. 1999;274(40):28071-28074.
    • (1999) J Biol Chem , vol.274 , Issue.40 , 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
  • 47
    • 46149093439 scopus 로고    scopus 로고
    • Structural Basis for the Autoinhibition of Talin in Regulating Integrin Activation
    • DOI 10.1016/j.molcel.2008.06.011, PII S1097276508004292
    • Goksoy E, Ma YQ, Wang X, et al. Structural basis for the autoinhibition of talin in regulating integrin activation. Mol Cell. 2008;31(1):124-133. (Pubitemid 351905930)
    • (2008) Molecular Cell , vol.31 , Issue.1 , pp. 124-133
    • Goksoy, E.1    Ma, Y.-Q.2    Wang, X.3    Kong, X.4    Perera, D.5    Plow, E.F.6    Qin, J.7
  • 49
    • 61949352480 scopus 로고    scopus 로고
    • Kindlin-3 is required for beta2 integrin-mediated leukocyte adhesion to endothelial cells
    • Moser M, Bauer M, Schmid S, et al. Kindlin-3 is required for beta2 integrin-mediated leukocyte adhesion to endothelial cells. Nat Med. 2009; 15(3):300-305.
    • (2009) Nat Med , vol.15 , Issue.3 , pp. 300-305
    • Moser, M.1    Bauer, M.2    Schmid, S.3
  • 50
    • 58149154658 scopus 로고    scopus 로고
    • Loss of Kindlin-1 causes skin atrophy and lethal neonatal intestinal epithelial dysfunction
    • Ussar S, Moser M, Widmaier M, et al. Loss of Kindlin-1 causes skin atrophy and lethal neonatal intestinal epithelial dysfunction. PLoS Genet. 2008;4(12):e1000289.
    • (2008) PLoS Genet , vol.4 , Issue.12
    • Ussar, S.1    Moser, M.2    Widmaier, M.3
  • 51
    • 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. Kindlin-3 is essential for integrin activation and platelet aggregation. Nat Med. 2008; 14(3):325-330. (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
  • 54
    • 1342346591 scopus 로고    scopus 로고
    • The Kindler Syndrome Protein Is Regulated by Transforming Growth Factor-beta and Involved in Integrin-mediated Adhesion
    • DOI 10.1074/jbc.M307978200
    • Kloeker S, Major MB, Calderwood DA, Ginsberg MH, Jones DA, Beckerle MC. The Kindler syndrome protein is regulated by transforming growth factor-beta and involved in integrin-mediated adhesion. J Biol Chem. 2004;279(8): 6824-6833. (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
  • 55
    • 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. Migfilin and Mig-2 link focal adhesions to filamin and the actin cytoskeleton and function in cell shape modulation. Cell. 2003;113(1):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
  • 56
    • 66449119343 scopus 로고    scopus 로고
    • Kindlin-1 and -2 directly bind the C-terminal region of beta integrin cytoplasmic tails and exert integrin-specific activation effects
    • Harburger DS, Bouaouina M, Calderwood DA. Kindlin-1 and -2 directly bind the C-terminal region of beta integrin cytoplasmic tails and exert integrin-specific activation effects. J Biol Chem. 2009;284(17):11485-11497.
    • (2009) J Biol Chem , vol.284 , Issue.17 , pp. 11485-11497
    • Harburger, D.S.1    Bouaouina, M.2    Calderwood, D.A.3
  • 57
    • 43149085289 scopus 로고    scopus 로고
    • 3 integrins
    • DOI 10.1083/jcb.200710196
    • Ma YQ, Qin J, Wu C, Plow EF. Kindlin-2 (Mig-2): a co-activator of beta3 integrins. J Cell Biol. 2008; 181(3):439-446. (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
  • 58
    • 77957269801 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of integrin beta3 regulates kindlin-2 binding and integrin activation
    • Bledzka K, Bialkowska K, Nie H, et al. Tyrosine phosphorylation of integrin beta3 regulates kindlin-2 binding and integrin activation. J Biol Chem. 2010;285(40):30370-30374.
    • (2010) J Biol Chem , vol.285 , Issue.40 , pp. 30370-30374
    • Bledzka, K.1    Bialkowska, K.2    Nie, H.3
  • 61
    • 42649140589 scopus 로고    scopus 로고
    • Integrin alpha IIb beta 3 in a membrane environment remains the same height after Mn2+ activation when observed by cryoelectron tomography
    • Ye F, Liu J, Winkler H, Taylor KA. Integrin alpha IIb beta 3 in a membrane environment remains the same height after Mn2+ activation when observed by cryoelectron tomography. J Mol Biol. 2008;378(5):976-986.
    • (2008) J Mol Biol , vol.378 , Issue.5 , pp. 976-986
    • Ye, F.1    Liu, J.2    Winkler, H.3    Taylor, K.A.4
  • 62
    • 0023730954 scopus 로고
    • Regulation of the fibronectin receptor affinity by divalent cations
    • Gailit J, Ruoslahti E. Regulation of the fibronectin receptor affinity by divalent cations. J Biol Chem. 1988;263(26):12927-12932.
    • (1988) J Biol Chem , vol.263 , Issue.26 , pp. 12927-12932
    • Gailit, J.1    Ruoslahti, E.2
  • 63
    • 0021918205 scopus 로고
    • Platelet membrane glycoprotein IIb-IIIa complex incorporated into phospholipid vesicles. Preparation and morphology
    • Parise LV, Phillips DR. Platelet membrane glycoprotein IIb-IIIa complex incorporated into phospholipid vesicles: preparation and morphology. J Biol Chem. 1985;260(3):1750-1756. (Pubitemid 15145454)
    • (1985) Journal of Biological Chemistry , vol.260 , Issue.3 , pp. 1750-1756
    • Parise, L.V.1    Phillips, D.R.2
  • 64
    • 0022226524 scopus 로고
    • Reconstitution of the purified platelet fibrinogen receptor: Fibrinogen binding properties of the glycoprotein IIb-IIIa complex
    • Parise LV, Phillips DR. Reconstitution of the purified platelet fibrinogen receptor: fibrinogen binding properties of the glycoprotein IIb-IIIa complex. J Biol Chem. 1985;260(19):10698-10707. (Pubitemid 16252251)
    • (1985) Journal of Biological Chemistry , vol.260 , Issue.19 , pp. 10698-10707
    • Parise, L.V.1    Phillips, D.R.2
  • 66
    • 2342450625 scopus 로고    scopus 로고
    • Electrostatic force microscopy analysis of lipid miscibility in two-component monolayers
    • Goodman T, Bussmann E, Williams C, Taveras M, Britt D. Electrostatic force microscopy analysis of lipid miscibility in two-component monolayers. Langmuir. 2004;20(9):3684-3689.
    • (2004) Langmuir , vol.20 , Issue.9 , pp. 3684-3689
    • Goodman, T.1    Bussmann, E.2    Williams, C.3    Taveras, M.4    Britt, D.5
  • 67
    • 0023003807 scopus 로고
    • Lipid miscibility and size increase of vesicles composed of two phosphatidylcholines
    • DOI 10.1016/0005-2736(86)90266-X
    • Massari S, Colonna R. Lipid miscibility and size increase of vesicles composed of two phosphatidylcholines. Biochim Biophys Acta. 1986;863(2): 264-276. (Pubitemid 17219336)
    • (1986) Biochimica et Biophysica Acta - Biomembranes , vol.863 , Issue.2 , pp. 264-276
    • Massari, S.1    Colonna, R.2
  • 68
    • 0021057433 scopus 로고
    • Fibrinogen binding to human platelet plasma membranes. Identification of two steps requiring divalent cations
    • Phillips DR, Baughan AK. Fibrinogen binding to human platelet plasma membranes: identification of two steps requiring divalent cations. J Biol Chem. 1983;258(17):10240-10246. (Pubitemid 14241180)
    • (1983) Journal of Biological Chemistry , vol.258 , Issue.17 , pp. 10240-10246
    • Phillips, D.R.1    Baughan, A.K.2
  • 69
    • 0021337959 scopus 로고
    • 2+ on the surface of platelets
    • Brass LF, Shattil SJ. Identification and function of the high affinity binding sites for Ca2+ on the surface of platelets. J Clin Invest. 1984;73(3):626-632. (Pubitemid 14156841)
    • (1984) Journal of Clinical Investigation , vol.73 , Issue.3 , pp. 626-632
    • Brass, L.F.1    Shattil, S.J.2
  • 70
    • 0026020583 scopus 로고
    • Receptor functions for the integrin VLA-3: Fibronectin, collagen, and laminin binding are differentially influenced by ARG-GLY-ASP peptide and by divalent cations
    • Elices MJ, Urry LA, Hemler ME. Receptor functions for the integrin VLA-3: fibronectin, collagen, and laminin binding are differentially influenced by Arg-Gly-Asp peptide and by divalent cations. J Cell Biol. 1991;112(1):169-181. (Pubitemid 21909609)
    • (1991) Journal of Cell Biology , vol.112 , Issue.1 , pp. 169-181
    • Elices, M.J.1    Urry, L.A.2    Hemler, M.E.3
  • 71
    • 0025761341 scopus 로고
    • Manganese ion elicits a binding activity of placenta vitronectin receptor to fibronectin cell-binding domain
    • Yanai T, Shimo-Oka T, Ii I. Manganese ion elicits a binding activity of placenta vitronectin receptor to fibronectin cell-binding domain. Cell Struct Funct. 1991;16(2):149-156.
    • (1991) Cell Struct Funct , vol.16 , Issue.2 , pp. 149-156
    • Yanai, T.1    Shimo-Oka, T.2    Ii, I.3
  • 72
    • 0026601096 scopus 로고
    • Divalent cation regulation of the function of the leukocyte integrin LFA-1
    • 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(1):219-226.
    • (1992) J Cell Biol , vol.116 , Issue.1 , pp. 219-226
    • Dransfield, I.1    Cabanas, C.2    Craig, A.3    Hogg, N.4
  • 73
    • 0025009813 scopus 로고
    • Cation-dependent changes in the binding specificity of the platelet receptor GPIIb/IIIa
    • Kirchhofer D, Gailit J, Ruoslahti E, Grzesiak J, Pierschbacher MD. Cation-dependent changes in the binding specificity of the platelet receptor GPIIb/IIIa. J Biol Chem. 1990;265(30):18525-18530.
    • (1990) J Biol Chem , vol.265 , Issue.30 , pp. 18525-18530
    • Kirchhofer, D.1    Gailit, J.2    Ruoslahti, E.3    Grzesiak, J.4    Pierschbacher, M.D.5
  • 74
    • 0023812375 scopus 로고
    • Laminin receptor on platelets is the integrin VLA-6
    • Sonnenberg A, Modderman PW, Hogervorst F. Laminin receptor on platelets is the integrin VLA-6. Nature. 1988;336(6198):487-489.
    • (1988) Nature , vol.336 , Issue.6198 , pp. 487-489
    • Sonnenberg, A.1    Modderman, P.W.2    Hogervorst, F.3
  • 75
    • 0027268377 scopus 로고
    • Interaction of type IV collagen with the isolated integrins alpha1beta1 and alpha2beta1
    • Kern A, Eble J, Golbik R, Kuhn K. Interaction of type IV collagen with the isolated integrins alpha 1 beta 1 and alpha 2 beta 1. Eur J Biochem. 1993;215(1):151-159. (Pubitemid 23211136)
    • (1993) European Journal of Biochemistry , vol.215 , Issue.1 , pp. 151-159
    • Kern, A.1    Eble, J.2    Golbik, R.3    Kuhn, K.4
  • 76
    • 0027442097 scopus 로고
    • + T lymphocyte adhesion to ICAM-1, fibronectin, VCAM-1, and invasin
    • Shimizu Y, Mobley JL. Distinct divalent cation requirements for integrin-mediated CD4+ T lymphocyte adhesion to ICAM-1, fibronectin, VCAM-1, and invasin. J Immunol. 1993;151(8): 4106-4115. (Pubitemid 23298743)
    • (1993) Journal of Immunology , vol.151 , Issue.8 , pp. 4106-4115
    • Shimizu, Y.1    Mobley, J.L.2
  • 78
    • 0032478739 scopus 로고    scopus 로고
    • 1 integrin chain
    • DOI 10.1074/jbc.273.14.7981
    • Ni H, Li A, Simonsen N, Wilkins JA. Integrin activation by dithiothreitol or Mn2+ induces a ligand-occupied conformation and exposure of a novel NH2-terminal regulatory site on the beta1 integrin chain. J Biol Chem. 1998;273(14):7981-7987. (Pubitemid 28168847)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.14 , pp. 7981-7987
    • Ni, H.1    Li, A.2    Simonsen, N.3    Wilkins, J.A.4
  • 79
    • 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. Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins. Science. 2003;301(5640): 1720-1725. (Pubitemid 37174365)
    • (2003) Science , vol.301 , Issue.5640 , pp. 1720-1725
    • Kim, M.1    Carman, C.V.2    Springer, T.A.3
  • 81
    • 21644476221 scopus 로고    scopus 로고
    • Membrane-proximal alpha/beta stalk interactions differentially regulate integrin activation
    • DOI 10.1074/jbc.M409548200
    • Kamata T, Handa M, Sato Y, Ikeda Y, Aiso S. Membrane-proximal alpha/beta stalk interactions differentially regulate integrin activation. J Biol Chem. 2005;280(26):24775-24783. (Pubitemid 40934568)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.26 , pp. 24775-24783
    • Kamata, T.1    Handa, M.2    Sato, Y.3    Ikeda, Y.4    Aiso, S.5
  • 83
    • 0026063230 scopus 로고
    • 3 (glycoprotein IIb-IIIa) alter receptor affinity, specificity, and function
    • Frelinger AL 3rd, Du XP, Plow EF, Ginsberg MH. Monoclonal antibodies to ligand-occupied conformers of integrin alpha IIb beta 3 (glycoprotein IIb-IIIa) alter receptor affinity, specificity, and function. J Biol Chem. 1991;266(26):17106-17111. (Pubitemid 21907912)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.26 , pp. 17106-17111
    • Frelinger III, A.L.1    Du, X.2    Plow, E.F.3    Ginsberg, M.H.4
  • 89
    • 66549097709 scopus 로고    scopus 로고
    • Interactions of platelet integrin alphaIIb and beta3 transmembrane domains in mammalian cell membranes and their role in integrin activation
    • Kim C, Lau TL, Ulmer TS, Ginsberg MH. Interactions of platelet integrin alphaIIb and beta3 transmembrane domains in mammalian cell membranes and their role in integrin activation. Blood. 2009;113(19):4747-4753.
    • (2009) Blood , vol.113 , Issue.19 , pp. 4747-4753
    • Kim, C.1    Lau, T.L.2    Ulmer, T.S.3    Ginsberg, M.H.4
  • 91
    • 0036283479 scopus 로고    scopus 로고
    • Redox control of integrin adhesion receptors
    • DOI 10.1016/S0076-6879(02)53045-7
    • Smith JW, Yan B, Landry F, Lombardo CR. Redox control of integrin adhesion receptors. Methods Enzymol. 2002;353:156-163. (Pubitemid 34625589)
    • (2002) Methods in Enzymology , vol.353 , pp. 156-163
    • Smith, J.W.1    Yan, B.2    Landry, F.3    Lombardo, C.R.4
  • 92
    • 0034704162 scopus 로고    scopus 로고
    • A redox site involved in integrin activation
    • DOI 10.1074/jbc.M007041200
    • Yan B, Smith JW. A redox site involved in integrin activation. J Biol Chem. 2000;275(51):39964-39972. (Pubitemid 32064618)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.51 , pp. 39964-39972
    • Yan, B.1    Smith, J.W.2
  • 93
    • 3543024456 scopus 로고    scopus 로고
    • 1-integrin affinity by reducing agents: "Inside-out" signaling is independent of and additive to reduction-regulated integrin activation
    • DOI 10.1074/jbc.M404387200
    • Chigaev A, Zwartz GJ, Buranda T, Edwards BS, Prossnitz ER, Sklar LA. Conformational regulation of alpha 4 beta 1-integrin affinity by reducing agents: "inside-out" signaling is independent of and additive to reduction-regulated integrin activation. J Biol Chem. 2004;279(31):32435-32443. (Pubitemid 39014698)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.31 , pp. 32435-32443
    • Chigaev, A.1    Zwartz, G.J.2    Buranda, T.3    Edwards, B.S.4    Prossnitz, E.R.5    Sklar, L.A.6
  • 95
    • 0026503815 scopus 로고
    • Immobilized Arg-Gly-Asp (RGD) peptides of varying lengths as structural probes of the platelet glycoprotein IIb/IIIa receptor
    • Beer JH, Springer KT, Coller BS. Immobilized Arg-Gly-Asp (RGD) peptides of varying lengths as structural probes of the platelet glycoprotein IIb/IIIa receptor. Blood. 1992;79(1):117-128.
    • (1992) Blood , vol.79 , Issue.1 , pp. 117-128
    • Beer, J.H.1    Springer, K.T.2    Coller, B.S.3
  • 97
    • 67650621363 scopus 로고    scopus 로고
    • Negative regulation of activated alpha-2 integrins during thrombopoiesis
    • Zou Z, Schmaier AA, Cheng L, et al. Negative regulation of activated alpha-2 integrins during thrombopoiesis. Blood. 2009;113(25):6428-6439.
    • (2009) Blood , vol.113 , Issue.25 , pp. 6428-6439
    • Zou, Z.1    Schmaier, A.A.2    Cheng, L.3
  • 98
    • 0031181648 scopus 로고    scopus 로고
    • The alpha Subunit Cytoplasmic Domain Regulates the Assembly and Adhesiveness of Integrin Lymphocyte Function-Associated Antigen-1
    • Lu CF, Springer TA. The alpha subunit cytoplasmic domain regulates the assembly and adhesiveness of integrin lymphocyte function-associated antigen-1. J Immunol. 1997;159(1): 268-278. (Pubitemid 127493709)
    • (1997) Journal of Immunology , vol.159 , Issue.1 , pp. 268-278
    • Lu, C.-F.1    Springer, T.A.2
  • 100
    • 0029966310 scopus 로고    scopus 로고
    • Breaking the integrin hinge: A defined structural constraint regulates integrin signaling
    • Hughes PE, Diaz-Gonzalez F, Leong L, et al. Breaking the integrin hinge: a defined structural constraint regulates integrin signaling. J Biol Chem. 1996;271(12):6571-6574.
    • (1996) J Biol Chem , vol.271 , Issue.12 , pp. 6571-6574
    • Hughes, P.E.1    Diaz-Gonzalez, F.2    Leong, L.3
  • 104
  • 106
    • 0029646107 scopus 로고
    • Two conformations of the integrin A-domain (I-domain): A pathway for activation?
    • DOI 10.1016/S0969-2126(01)00271-4
    • Lee JO, Bankston LA, Arnaout MA, Liddington RC. Two conformations of the integrin A-domain (I-domain): a pathway for activation? Structure. 1995;3(12):1333-1340. (Pubitemid 3012265)
    • (1995) Structure , vol.3 , Issue.12 , pp. 1333-1340
    • Lee, J.-O.H.1    Bankston, L.A.2    Arnaout, M.A.3    Liddington, R.C.4
  • 107
    • 3042602113 scopus 로고    scopus 로고
    • 1 integrin antibodies that stabilize the low affinity state by preventing the swing-out of the hybrid domain
    • DOI 10.1074/jbc.M404354200
    • Luo BH, Strokovich K, Walz T, Springer TA, Takagi J. Allosteric beta1 integrin antibodies that stabilize the low affinity state by preventing the swing-out of the hybrid domain. J Biol Chem. 2004;279(26):27466-27471. (Pubitemid 38812586)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.26 , pp. 27466-27471
    • Luo, B.-H.1    Strokovich, K.2    Walz, T.3    Springer, T.A.4    Takagi, J.5
  • 108
    • 0141625303 scopus 로고    scopus 로고
    • 1 in complex with fibronectin
    • DOI 10.1093/emboj/cdg445
    • Takagi J, Strokovich K, Springer TA, Walz T. Structure of integrin alpha5beta1 in complex with fibronectin. EMBO J. 2003;22(18):4607-4615. (Pubitemid 37162897)
    • (2003) EMBO Journal , vol.22 , Issue.18 , pp. 4607-4615
    • Takagi, J.1    Strokovich, K.2    Springer, T.A.3    Walz, T.4
  • 110
    • 0032517824 scopus 로고    scopus 로고
    • 2+-complexed crystal structures
    • DOI 10.1083/jcb.143.6.1523
    • Li R, Rieu P, Griffith DL, Scott D, Arnaout MA. Two functional states of the CD11b A-domain: correlations with key features of two Mn2+-complexed crystal structures. J Cell Biol. 1998;143(6): 1523-1534. (Pubitemid 29006500)
    • (1998) Journal of Cell Biology , vol.143 , Issue.6 , pp. 1523-1534
    • Li, R.1    Rieu, P.2    Griffith, D.L.3    Scott, D.4    Arnaout, M.A.5
  • 111
    • 0033900165 scopus 로고    scopus 로고
    • Computational design of an integrin I domain stabilized in the open high affinity conformation
    • DOI 10.1038/77978
    • Shimaoka M, Shifman JM, Jing H, Takagi J, Mayo SL, Springer TA. Computational design of an integrin I domain stabilized in the open high affinity conformation. Nat Struct Biol. 2000;7(8):674-678. (Pubitemid 30636680)
    • (2000) Nature Structural Biology , vol.7 , Issue.8 , pp. 674-678
    • Shimaoka, M.1    Shifman, J.M.2    Jing, H.3    Takagi, J.4    Mayo, S.L.5    Springer, T.A.6
  • 113
    • 63649083644 scopus 로고    scopus 로고
    • Rationally designed integrin beta3 mutants stabilized in the high affinity conformation
    • Luo BH, Karanicolas J, Harmacek LD, Baker D, Springer TA. Rationally designed integrin beta3 mutants stabilized in the high affinity conformation. J Biol Chem. 2009;284(6):3917-3924.
    • (2009) J Biol Chem , vol.284 , Issue.6 , pp. 3917-3924
    • Luo, B.H.1    Karanicolas, J.2    Harmacek, L.D.3    Baker, D.4    Springer, T.A.5
  • 118
    • 1642305349 scopus 로고    scopus 로고
    • 3 Integrin I-like Domain into High and Low Affinity Conformations with Disulfides
    • DOI 10.1074/jbc.M312732200
    • Luo BH, Takagi J, Springer TA. Locking the beta3 integrin I-like domain into high and low affinity conformations with disulfides. J Biol Chem. 2004; 279(11):10215-10221. (Pubitemid 38372626)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.11 , pp. 10215-10221
    • Luo, B.-H.1    Takagi, J.2    Springer, T.A.3
  • 119
    • 77952931584 scopus 로고    scopus 로고
    • Effects of limiting extension at the alphaIIb genu on ligand binding to integrin alphaIIbbeta3
    • Blue R, Li J, Steinberger J, Murcia M, Filizola M, Coller BS. Effects of limiting extension at the alphaIIb genu on ligand binding to integrin alphaIIbbeta3. J Biol Chem. 2010;285(23):17604-17613.
    • (2010) J Biol Chem , vol.285 , Issue.23 , pp. 17604-17613
    • Blue, R.1    Li, J.2    Steinberger, J.3    Murcia, M.4    Filizola, M.5    Coller, B.S.6
  • 120
    • 66149128873 scopus 로고    scopus 로고
    • The tail of integrins, talin, and kindlins
    • Moser M, Legate KR, Zent R, Fassler R. The tail of integrins, talin, and kindlins. Science. 2009; 324(5929):895-899.
    • (2009) Science , vol.324 , Issue.5929 , pp. 895-899
    • Moser, M.1    Legate, K.R.2    Zent, R.3    Fassler, R.4


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