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Volumn 118, Issue 23, 2011, Pages 5996-6005

Glanzmann thrombasthenia: A review of ITGA2B and ITGB3 defects with emphasis on variants, phenotypic variability, and mouse models

Author keywords

[No Author keywords available]

Indexed keywords

BLOOD CLOTTING FACTOR 7; FIBRIN; FIBRINOGEN RECEPTOR; PROTEIN ITGA2B; PROTEIN ITGB3; RECOMBINANT BLOOD CLOTTING FACTOR 7; UNCLASSIFIED DRUG; VITRONECTIN RECEPTOR;

EID: 82955207656     PISSN: 00064971     EISSN: 15280020     Source Type: Journal    
DOI: 10.1182/blood-2011-07-365635     Document Type: Review
Times cited : (203)

References (104)
  • 1
    • 0025253068 scopus 로고
    • Glanzmann's thrombasthenia: The spectrum of clinical disease
    • George JN, Caen JP, Nurden AT. Glanzmann's thrombasthenia: the spectrum of clinical disease. Blood. 1990;75(7):1383-1395. (Pubitemid 20114873)
    • (1990) Blood , vol.75 , Issue.7 , pp. 1383-1395
    • George, J.N.1    Caen, J.P.2    Nurden, A.T.3
  • 2
    • 33646803323 scopus 로고    scopus 로고
    • Inherited abnormalities of the platelet membrane: Glanzmann thrombasthenia, Bernard-Soulier syndrome, and other disorders
    • Colman RW, Marder VJ, Clowes AW, George JN, Goldhaber S, eds. (4th ed). Philadelphia, PA: Lippincott, Williams & Wilkins;
    • Nurden AT, George JN. Inherited abnormalities of the platelet membrane: Glanzmann thrombasthenia, Bernard-Soulier syndrome, and other disorders. In: Colman RW, Marder VJ, Clowes AW, George JN, Goldhaber S, eds. Hemostasis and Thrombosis (4th ed). Philadelphia, PA: Lippincott, Williams & Wilkins; 2006:987-1010.
    • (2006) Hemostasis and Thrombosis , pp. 987-1010
    • Nurden, A.T.1    George, J.N.2
  • 3
    • 54049152026 scopus 로고    scopus 로고
    • The GPIIb/IIIa (integrin alphaIIbß3) odyssey: A technology-driven saga of a receptor with twists and turns and even a bend
    • Coller BS, Shattil SJ. The GPIIb/IIIa (integrin alphaIIbß3) odyssey: a technology-driven saga of a receptor with twists and 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
  • 4
    • 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;432:59-67. (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
  • 5
    • 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
  • 6
    • 72949119124 scopus 로고    scopus 로고
    • Integrins in cancer: Biological implications and therapeutic opportunities
    • Desgrosellier JS, Cheresh DA. Integrins in cancer: biological implications and therapeutic opportunities. Nat Rev Cancer. 2010;10(1):9-22.
    • (2010) Nat Rev Cancer , vol.10 , Issue.1 , pp. 9-22
    • Desgrosellier, J.S.1    Cheresh, D.A.2
  • 8
    • 77951625288 scopus 로고    scopus 로고
    • Dissection of platelet and myeloid cell defects by conditional targeting of the beta3-integrin subunit
    • Morgan EA, Schneider JG, Baroni TE, et al. Dissection of platelet and myeloid cell defects by conditional targeting of the beta3-integrin subunit. FASEB J. 2010;24(4):1117-1127.
    • (2010) FASEB J , vol.24 , Issue.4 , pp. 1117-1127
    • Morgan, E.A.1    Schneider, J.G.2    Baroni, T.E.3
  • 9
    • 34247896877 scopus 로고    scopus 로고
    • Glanzmann thrombasthenia
    • Nurden AT. Glanzmann thrombasthenia. Orphanet J Rare Dis. 2006;1:10-18.
    • (2006) Orphanet J Rare Dis , vol.1 , pp. 10-18
    • Nurden, A.T.1
  • 10
    • 0026024976 scopus 로고
    • Platelet vitronectin receptor expression differentiates Iraqi-Jewish from Arab patients with Glanzmann's thrombasthenia in Israel
    • Coller BS, Cheresh DA, Asch E, Seligsohn U. Platelet vitronectin receptor expression differentiates Iraqi-Jewish from Arab patients with Glanzmann's thrombasthenia in Israel. Blood. 1991;77(1):75-83.
    • (1991) Blood , vol.77 , Issue.1 , pp. 75-83
    • Coller, B.S.1    Cheresh, D.A.2    Asch, E.3    Seligsohn, U.4
  • 11
    • 0038445927 scopus 로고    scopus 로고
    • The glycoprotein IIb molecule is expressed on early murine hematopoietic progenitors and regulates their numbers in sites of hematopoiesis
    • DOI 10.1016/S1074-7613(03)00173-0
    • Emambokus NR, Frampton J. The glycoprotein IIb molecule is expressed on early murine hematopoietic progenitors and regulates their numbers in sites of hematopoiesis. Immunity. 2003;19(1):33-45. (Pubitemid 36859899)
    • (2003) Immunity , vol.19 , Issue.1 , pp. 33-45
    • Emambokus, N.R.1    Frampton, J.2
  • 12
    • 33645504401 scopus 로고    scopus 로고
    • AlphaIIbbeta3 biogenesis is controlled by engagement of alphaIIb in the calnexin cycle via the N15-linked glycan
    • Mitchell WB, Li JH, French DL, Coller BS. alphaIIbbeta3 biogenesis is controlled by engagement of alphaIIb in the calnexin cycle via the N15-linked glycan. Blood. 2006;107(7):2713-2719.
    • (2006) Blood , vol.107 , Issue.7 , pp. 2713-2719
    • Mitchell, W.B.1    Li, J.H.2    French, D.L.3    Coller, B.S.4
  • 13
    • 0028071221 scopus 로고
    • A single amino acid substitution flanking the fourth calcium binding domain of alphaIIb prevents maturation of the alphaIIbbeta3 integrin complex
    • Wilcox DA, Wautier JL, Pidard D, Newman PJ. A single amino acid substitution flanking the fourth calcium binding domain of alphaIIb prevents maturation of the alphaIIbbeta3 integrin complex. J Biol Chem. 1994;269(6):4450-4457.
    • (1994) J Biol Chem , vol.269 , Issue.6 , pp. 4450-4457
    • Wilcox, D.A.1    Wautier, J.L.2    Pidard, D.3    Newman, P.J.4
  • 14
    • 29244462341 scopus 로고    scopus 로고
    • 3 from endoplasmic reticulum to Golgi
    • DOI 10.1111/j.1538-7836.2005.01593.x
    • Nelson EJR, Li J, Mitchell WN, Chandy M, Srivastava A, Coller BS. Three novel beta-propeller mutations causing Glanzmann thrombasthenia result in production of normally stable pro-alphaIIb but variably impaired progression of pro-alphaIIbbeta3 from endoplasmic reticulum to Golgi. J Thromb Haemost. 2005;3(12):2773-2783. (Pubitemid 41819807)
    • (2005) Journal of Thrombosis and Haemostasis , vol.3 , Issue.12 , pp. 2773-2783
    • Nelson, E.J.R.1    Li, J.2    Mitchell, W.B.3    Chandy, M.4    Srivastava, A.5    Coller, B.S.6
  • 15
    • 18844388451 scopus 로고    scopus 로고
    • A novel homozygous splice junction mutation in GPIIb associated with alternative splicing, nonsense-mediated decay of GPIIbmRNA, and type II Glanzmann's thrombasthenia
    • Gonzalez-Manchon C, Arias-Salgado EG, Butta N, et al. A novel homozygous splice junction mutation in GPIIb associated with alternative splicing, nonsense-mediated decay of GPIIbmRNA, and type II Glanzmann's thrombasthenia. J Thromb Haemost. 2003;1(5):1071-1078.
    • (2003) J Thromb Haemost , vol.1 , Issue.5 , pp. 1071-1078
    • Gonzalez-Manchon, C.1    Arias-Salgado, E.G.2    Butta, N.3
  • 16
    • 78650952649 scopus 로고    scopus 로고
    • An alphaIIb mutation in patients with Glanzmann thrombasthenia located in the N-terminus of blade 1 of the beta-propeller (Asn2Asp) disrupts a calcium binding site in blade 6
    • Mansour W, Einav Y, Hauschner H, Koren A, Seligsohn U, Rosenberg N. An alphaIIb mutation in patients with Glanzmann thrombasthenia located in the N-terminus of blade 1 of the beta-propeller (Asn2Asp) disrupts a calcium binding site in blade 6. J Thromb Haemost. 2011;9(1):192-200.
    • (2011) J Thromb Haemost , vol.9 , Issue.1 , pp. 192-200
    • Mansour, W.1    Einav, Y.2    Hauschner, H.3    Koren, A.4    Seligsohn, U.5    Rosenberg, N.6
  • 18
    • 33645786359 scopus 로고    scopus 로고
    • Molecular diversity of Glanzmann thrombasthenia in Southern India: New insights into mRNA splicing and structure-function correlations of alphaIIbbeta3 integrin (ITGA2B, ITGB3)
    • Peretz H, Rosenberg N, Landau M, et al. Molecular diversity of Glanzmann thrombasthenia in Southern India: new insights into mRNA splicing and structure-function correlations of alphaIIbbeta3 integrin (ITGA2B, ITGB3). Hum Mutat. 2006;27(4):359-369.
    • (2006) Hum Mutat , vol.27 , Issue.4 , pp. 359-369
    • Peretz, H.1    Rosenberg, N.2    Landau, M.3
  • 19
    • 70449399296 scopus 로고    scopus 로고
    • Molecular defects in ITGA2B and ITGB3 genes in patients with Glanzmann's thrombasthenia
    • Kannan M,Ahmad F, Yadav B, Kumar R, Choudry VP, Saxena R. Molecular defects in ITGA2B and ITGB3 genes in patients with Glanzmann's thrombasthenia. J Thromb Haemost. 2009;7(11):1878-1885.
    • (2009) J Thromb Haemost , vol.7 , Issue.11 , pp. 1878-1885
    • Kannan, M.1    Ahmad, F.2    Yadav, B.3    Kumar, R.4    Choudry, V.P.5    Saxena, R.6
  • 21
    • 0035914422 scopus 로고    scopus 로고
    • Probing conformation changes in the I-like domain and the cysteine-rich repeat of human beta3 integrins following disulfide bond disruption by cysteine mutations
    • Chen P, Melchior C, Brons NHC, Schlegel N, Caen J, Kieffer N. Probing conformation changes in the I-like domain and the cysteine-rich repeat of human beta3 integrins following disulfide bond disruption by cysteine mutations. J Biol Chem. 2001;276(42):38628-38635.
    • (2001) J Biol Chem , vol.276 , Issue.42 , pp. 38628-38635
    • Chen, P.1    Melchior, C.2    Brons, N.H.C.3    Schlegel, N.4    Caen, J.5    Kieffer, N.6
  • 22
    • 18744407550 scopus 로고    scopus 로고
    • Dissociation between fibrinogen and fibrin interaction with platelets in patients with different subtypes of Glanzmann's thrombasthenia: Studies in an ex vivo perfusion chamber model
    • DOI 10.1046/j.1365-2141.2002.03966.x
    • Hainaud P, Brouland J-P, André P, et al. Dissociation between fibrinogen and fibrin interaction with platelets in patients with different subtypes of Glanzmann's thrombasthenia: studies in an ex vivo perfusion chamber model. Br J Haematol. 2002;119(4):998-1004. (Pubitemid 35469170)
    • (2002) British Journal of Haematology , vol.119 , Issue.4 , pp. 998-1004
    • Hainaud, P.1    Brouland, J.-P.2    Andre, P.3    Simoneau, G.4    Sollier, C.B.D.5    Drouet, L.6    Caen, J.7    Bellucci, S.8
  • 24
    • 0025838830 scopus 로고
    • Platelet fibrinogen and vitronectin in Glanzmann thrombasthenia: Evidence consistent with specific roles for glycoprotein IIb/IIIa and alphavbeta3 integrins in platelet protein trafficking
    • Coller BS, Seligsohn U, West SM, Scudder LE, Norton KJ. Platelet fibrinogen and vitronectin in Glanzmann thrombasthenia: evidence consistent with specific roles for glycoprotein IIb/IIIa and alphavbeta3 integrins in platelet protein trafficking. Blood. 1991;78(10):2603-2610.
    • (1991) Blood , vol.78 , Issue.10 , pp. 2603-2610
    • Coller, B.S.1    Seligsohn, U.2    West, S.M.3    Scudder, L.E.4    Norton, K.J.5
  • 25
    • 0031052323 scopus 로고    scopus 로고
    • 3) in human platelets and megakaryocytes reveals an intracellular pool and labelling of the alpha-granule membrane
    • Poujol C, Nurden AT, Nurden P. Ultrastructural analysis of the distribution of the vitronectin receptor (alphavbeta3) in human platelets and megakaryocytes reveals an intracellular pool and labelling of the alpha-granule membrane. Br J Haematol. 1997;96(4):823-835. (Pubitemid 27115880)
    • (1997) British Journal of Haematology , vol.96 , Issue.4 , pp. 823-835
    • Poujol, C.1    Nurden, A.T.2    Nurden, P.3
  • 26
    • 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
  • 27
    • 0036464723 scopus 로고    scopus 로고
    • Missense mutations in the beta3 subunit have a different impact on the expression and function between alphaIIbbeta3 and alphavbeta3
    • Tadokoro S, Tomiyama Y, Honda S, et al. Missense mutations in the beta3 subunit have a different impact on the expression and function between alphaIIbbeta3 and alphavbeta3. Blood. 2002;99(3):931-938.
    • (2002) Blood , vol.99 , Issue.3 , pp. 931-938
    • Tadokoro, S.1    Tomiyama, Y.2    Honda, S.3
  • 28
    • 0035657707 scopus 로고    scopus 로고
    • A naturally occurring point mutation in the beta3 integrin MIDAS-like domain affects differently alphaVbeta3 and alphaIIbbeta3 receptor function
    • Morel-Kopp M-C, Melchior C, Chen P, et al. A naturally occurring point mutation in the beta3 integrin MIDAS-like domain affects differently alphavbeta3 and alphaIIbbeta3 receptor function. Thromb Haemost. 2001;86(6):1425-1434. (Pubitemid 34007515)
    • (2001) Thrombosis and Haemostasis , vol.86 , Issue.6 , pp. 1425-1434
    • Morel-Kopp, M.-C.1    Melchior, C.2    Chen, P.3    Ammerlaan, W.4    Lecompte, T.5    Kaplan, C.6    Kieffer, N.7
  • 29
    • 77953928506 scopus 로고    scopus 로고
    • A unique interaction between alphaIIb and beta3 in the head region is essential for outside-in signaling-related functions of alphaIIbbeta3 integrin
    • Hauschner H, Landau M, Seligsohn U, Rosenberg N. A unique interaction between alphaIIb and beta3 in the head region is essential for outside-in signaling-related functions of alphaIIbbeta3 integrin. Blood. 2010;115(22):4542-4550.
    • (2010) Blood , vol.115 , Issue.22 , pp. 4542-4550
    • Hauschner, H.1    Landau, M.2    Seligsohn, U.3    Rosenberg, N.4
  • 30
    • 0025222435 scopus 로고
    • Analysis of platelet aggregation disorders based on flow cytometric analysis of membrane glycoprotein IIb-IIIa with conformation-specific monoclonal antibodies
    • Ginsberg MH, Frelinger AL, Lam SC-T, et al. Analysis of platelet aggregation disorders based on flow cytometric analysis of membrane glycoprotein IIb-IIIa with conformation-specific monoclonal antibodies. Blood. 1990;76(10):2017-2023.
    • (1990) Blood , vol.76 , Issue.10 , pp. 2017-2023
    • Ginsberg, M.H.1    Frelinger, A.L.2    Lam, S.C.-T.3
  • 31
    • 0025062149 scopus 로고
    • A beta3 mutation abolishes ligand binding and alters divalent cation-dependent conformation
    • Loftus JC, O'Toole TE, Plow EF, Glass A, Frelinger AL 3rd, Ginsberg MH. A beta3 mutation abolishes ligand binding and alters divalent cation-dependent conformation. Science. 1990;249(4971):915-918.
    • (1990) Science , vol.249 , Issue.4971 , pp. 915-918
    • Loftus, J.C.1    O'Toole, T.E.2    Plow, E.F.3    Glass, A.4    Frelinger III, A.L.5    Ginsberg, M.H.6
  • 32
    • 0027990819 scopus 로고
    • Mutation of a ligand binding domain of beta3 integrin: Integral role of oxygenated residues in alphaIIbbeta3 (GPIIb-IIIa) receptor function
    • Bajt ML, Loftus JC. Mutation of a ligand binding domain of beta3 integrin: integral role of oxygenated residues in alphaIIbbeta3 (GPIIb-IIIa) receptor function. J Biol Chem. 1994;269(33):20913-20919.
    • (1994) J Biol Chem , vol.269 , Issue.33 , pp. 20913-20919
    • Bajt, M.L.1    Loftus, J.C.2
  • 33
    • 0023104863 scopus 로고
    • A variant of Glanzmann's thrombasthenia with abnormal glycoprotein IIb-IIIa complexes in the platelet membrane
    • Nurden AT, Rosa J-P, Fournier D, et al. A variant of Glanzmann's thrombasthenia with abnormal glycoprotein IIb-IIIa complexes in the platelet membrane. J Clin Invest. 1987;79:962-969. (Pubitemid 17050925)
    • (1987) Journal of Clinical Investigation , vol.79 , Issue.3 , pp. 962-969
    • Nurden, A.T.1    Rosa, J.-P.2    Fournier, D.3
  • 34
    • 0026761286 scopus 로고
    • A spontaneous mutation of integrin alphaIIbbeta3 (platelet glycoprotein IIb-IIIa) helps define a ligand binding site
    • Bajt ML, Ginsberg MH, Frelinger AL, Berndt MC, Loftus JC. A spontaneous mutation of integrin alphaIIbbeta3 (platelet glycoprotein IIb-IIIa) helps define a ligand binding site. J Biol Chem. 1992;267(6):3789-3794.
    • (1992) J Biol Chem , vol.267 , Issue.6 , pp. 3789-3794
    • Bajt, M.L.1    Ginsberg, M.H.2    Frelinger, A.L.3    Berndt, M.C.4    Loftus, J.C.5
  • 36
    • 50249106884 scopus 로고    scopus 로고
    • Structural basis for distinctive recognition of fibrinogen gammaC peptide by the platelet integrin alphaIIbbeta3
    • Springer TA, Zhu J, Xiao T. Structural basis for distinctive recognition of fibrinogen gammaC peptide by the platelet integrin alphaIIbbeta3. J Cell Biol. 2008;182(4):791-800.
    • (2008) J Cell Biol , vol.182 , Issue.4 , pp. 791-800
    • Springer, T.A.1    Zhu, J.2    Xiao, T.3
  • 37
    • 79952940482 scopus 로고    scopus 로고
    • Regulation of integrin alphaIIbbeta3 ligand binding and signaling by the metal ion binding sites in the beta1 domain
    • Raborn J, Wang W, Luo B-H. Regulation of integrin alphaIIbbeta3 ligand binding and signaling by the metal ion binding sites in the beta1 domain. Biochemistry. 2011;50:2084-2091.
    • (2011) Biochemistry , vol.50 , pp. 2084-2091
    • Raborn, J.1    Wang, W.2    Luo, B.-H.3
  • 38
    • 0031595456 scopus 로고    scopus 로고
    • 3 complex that retains partial function in a novel form of type II Glanzmann thrombasthenia
    • Jackson DE, White MM, Jennings LK, Newman PJ. A Ser162->Leu mutation within glycoprotein (GP)IIIa (integrin beta3) results in an unstable alphaIIbbeta3 complex that retains partial function in a novel form of type II Glanzmann thrombasthenia. Thromb Haemost. 1998;80(1):42-48. (Pubitemid 28353496)
    • (1998) Thrombosis and Haemostasis , vol.80 , Issue.1 , pp. 42-48
    • Jackson, D.E.1    White, M.M.2    Jennings, L.K.3    Newman, P.J.4
  • 39
    • 0034234624 scopus 로고    scopus 로고
    • 3 complex that binds fibrin but not fibrinogen
    • .Ward CM, Kestin AS, Newman PJ. A Leu262Pro mutation in the integrin beta3 subunit results in an alphaIIbbeta3 complex that binds fibrin but not fibrinogen. Blood. 2000;96(1):161-169. (Pubitemid 30456466)
    • (2000) Blood , vol.96 , Issue.1 , pp. 161-169
    • Ward, C.M.1    Kestin, A.S.2    Newman, P.J.3
  • 40
    • 10444285227 scopus 로고    scopus 로고
    • A novel Ser123Pro substitution in the MIDAS domain of integrin 3 associated with variant Glanzmann's thrombasthenia in an Indian patient
    • Nair S, Ghosh K, Shetty S, Mohanty D. A novel Ser123Pro substitution in the MIDAS domain of integrin beta3 associated with variant Glanzmann's thrombasthenia in an Indian patient. Haematologica. 2004;89(12):1529-1530. (Pubitemid 39643524)
    • (2004) Haematologica , vol.89 , Issue.12 , pp. 1529-1530
    • Nair, S.1    Ghosh, K.2    Shetty, S.3    Mohanty, D.4
  • 41
    • 0026614923 scopus 로고
    • Ser-752->Pro mutation in the cytoplasmic domain of integrin beta3 subunit and defective activation of platelet integrin alphaIIbbeta3 (glycoprotein IIb-IIIa) in a variant of Glanzmann thrombasthenia
    • Chen Y-P, Djaffar I, Pidard D, et al. Ser-752->Pro mutation in the cytoplasmic domain of integrin beta3 subunit and defective activation of platelet integrin alphaIIbbeta3 (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
  • 42
    • 0035982903 scopus 로고    scopus 로고
    • 752 > Pro substitution in the cytoplasmic domain of beta3 in a Glanzmann thrombasthenia variant fails to prevent interactions between the alphaIIbbeta3 integrin and the platelet granule pool of fibrinogen
    • DOI 10.1046/j.1365-2141.2002.03758.x
    • Nurden P, Poujol C, Winckler J, Combrie R, Caen JP, Nurden AT. A Ser752->Pro substitution in the cytoplasmic domain of beta3 in a Glanzmann thrombasthenia variant fails to prevent interactions between the alphaIIbbeta3 integrin and the platelet granule pool of fibrinogen. Br J Haematol. 2002;118(4):1143-1151. (Pubitemid 35025983)
    • (2002) British Journal of Haematology , vol.118 , Issue.4 , pp. 1143-1151
    • Nurden, P.1    Poujol, C.2    Winckler, J.3    Combrie, R.4    Caen, J.P.5    Nurden, A.T.6
  • 43
    • 0028146157 scopus 로고
    • 752->P) impairs bidirectional signaling through alphaIIbß3 (platelet glycoprotein IIb-IIIa)
    • 752->P) impairs bidirectional signaling through alphaIIbß3 (platelet glycoprotein IIb-IIIa). Blood. 1994;84(6):1857-1865.
    • (1994) Blood , vol.84 , Issue.6 , pp. 1857-1865
    • Chen, Y.-P.1    O'Toole, T.E.2    Ylänne, J.3    Rosa, J.-P.4    Ginsberg, M.H.5
  • 44
    • 0031003706 scopus 로고    scopus 로고
    • 3 cytoplasmic domain in triggering focal adhesion kinase phosphorylation
    • DOI 10.1074/jbc.272.12.7892
    • Tahiliani PD, Singh L, Auer KL, LaFlamme SE. The role of conserved amino acid motifs within the integrin beta3 cytoplasmic domain in triggering focal adhesion kinase phosphorylation. J Biol Chem. 1997;272(12):7892-7898. (Pubitemid 27137349)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.12 , pp. 7892-7898
    • Tahiliani, P.D.1    Singh, L.2    Auer, K.L.3    LaFlamme, S.E.4
  • 45
    • 0029833463 scopus 로고    scopus 로고
    • Serine 752 in the cytoplasmic domain of the beta3 integrin subunit is not required for alphavbeta3 postreceptor signaling events
    • Kieffer N, Melchior C, Guinet JM, Michels S, Gouon V, Bron N. Serine 752 in the cytoplasmic domain of the beta3 integrin subunit is not required for alphavbeta3 postreceptor signaling events. Cell Adhes Commun. 1996;4(1):25-39. (Pubitemid 26325330)
    • (1996) Cell Adhesion and Communication , vol.4 , Issue.1 , pp. 25-39
    • Kieffer, N.1
  • 46
    • 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
  • 47
    • 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 alphaIIbbeta3 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
  • 48
    • 53449089830 scopus 로고    scopus 로고
    • Identification of FcγRIIa as the ITAM-bearing receptor mediating alphaIIbbeta3 outside-in integrin signaling in human platelets
    • Boylan B, Gao C, Rathore V, Gill JC, Newman DK, Newman PJ. Identification of FcγRIIa as the ITAM-bearing receptor mediating alphaIIbbeta3 outside-in integrin signaling in human platelets. Blood. 2008;112(7):2780-2786.
    • (2008) Blood , vol.112 , Issue.7 , pp. 2780-2786
    • Boylan, B.1    Gao, C.2    Rathore, V.3    Gill, J.C.4    Newman, D.K.5    Newman, P.J.6
  • 49
    • 0035353156 scopus 로고    scopus 로고
    • Competition between normal (674C) and mutant (674R) subunits: Role of the molecular chaperone BiP in the processing of GPIIb-IIIa complexes
    • Arias-Salgado EG, Butta N, Gonzalez-Manchon C, Larrucea S, Ayuso MS, Parrilla R. Competition between normal (674C) and mutant (674R) subunits: role of the molecular chaperone BiP in the processing of GPIIb-IIIa complexes. Blood. 2001;97(9):2640-2647.
    • (2001) Blood , vol.97 , Issue.9 , pp. 2640-2647
    • Arias-Salgado, E.G.1    Butta, N.2    Gonzalez-Manchon, C.3    Larrucea, S.4    Ayuso, M.S.5    Parrilla, R.6
  • 51
    • 0012954418 scopus 로고    scopus 로고
    • 3 function for soluble ligands but retains its ability for mediating cell adhesion and clot retraction: Comparison with other mutations causing ligand-binding defects
    • DOI 10.1182/blood-2002-07-2144
    • Kiyoi T, Tomiyama Y, Honda S, et al. A naturally occurring Tyr143His alphaIIb mutation abolishes alphaIIbbeta3 function for soluble ligands but retains its ability for mediating cell adhesion and clot retraction: comparison with other mutations causing ligand-binding defects. Blood. 2003;101(9):3485- 3491. (Pubitemid 36857931)
    • (2003) Blood , vol.101 , Issue.9 , pp. 3485-3491
    • Kiyoi, T.1    Tomiyama, Y.2    Honda, S.3    Tadokoro, S.4    Arai, M.5    Kashiwagi, H.6    Kosugi, S.7    Kato, H.8    Kurata, Y.9    Matsuzawa, Y.10
  • 52
    • 9144221480 scopus 로고    scopus 로고
    • Glanzmann thrombasthenia Frankfurt I is associated with a point mutation Thr176IIe in the N-terminal region of alphaIIb subunit integrin
    • DOI 10.1160/TH04-03-0170
    • .Westrup D, Santoso S, Follert-Hagenorff K, et al. Glanzmann thrombasthenia Frankfurt I is associated with a point mutation Thr176Ile in the Nterminal region of alphaIIb subunit integrin. Thromb Haemost. 2004;92(5):1040-1051. (Pubitemid 39545528)
    • (2004) Thrombosis and Haemostasis , vol.92 , Issue.5 , pp. 1040-1051
    • Westrup, D.1    Santoso, S.2    Follert-Hagendorff, K.3    Bassus, S.4    Just, M.5    Jablonka, B.6    Kirchmaier, C.M.7
  • 54
    • 67649373064 scopus 로고    scopus 로고
    • The novel S527F mutation in the integrin beta3 chain induces a high affinity alphaIIbbeta3 receptor by hindering adoption of the bent conformation
    • Vanhoorelbeke K, De Meyer SF, Pareyn SF, et al. The novel S527F mutation in the integrin beta3 chain induces a high affinity alphaIIbbeta3 receptor by hindering adoption of the bent conformation. J Biol Chem. 2009;284(22):14914- 14920.
    • (2009) J Biol Chem , vol.284 , Issue.22 , pp. 14914-14920
    • Vanhoorelbeke, K.1    De Meyer, S.F.2    Pareyn, S.F.3
  • 55
    • 1642504824 scopus 로고    scopus 로고
    • Critical cysteine residues for regulation of integrin alphaIIbbeta3 are clustered in the epidermal growth factor domains of the beta3 subunit
    • DOI 10.1042/BJ20031701
    • Kamata T, Ambo H, Puzon-McLaughlin W, et al. Critical cysteine residues for regulation of integrin alphaIIbbeta3 are clustered in the epidermal growth factor domains of the beta3 subunit. Biochem J. 2004;378(3):1079-1082. (Pubitemid 38406889)
    • (2004) Biochemical Journal , vol.378 , Issue.3 , pp. 1079-1082
    • Kamata, T.1    Ambo, H.2    Puzon-McLaughlin, W.3    Tieu, K.K.4    Handa, M.5    Ikeda, Y.6    Takada, Y.7
  • 56
    • 36949001794 scopus 로고    scopus 로고
    • Disulfide bond disruption by a beta3-Cys549Arg mutation in six Jordanian families with Glanzmann thrombasthenia causes diminished production of constitutively active alphaIIbbeta3
    • DOI 10.1160/TH07-04-0248
    • Mor-Cohen R, Rosenberg N, Peretz H, et al. Disulfide bond disruption by a beta3-Cys549Arg mutation in six Jordanian families with Glanzmann thrombasthenia causes diminished production of constitutively active alphaIIbbeta3. Thromb Haemost. 2007;98(6):1257-1265. (Pubitemid 350239098)
    • (2007) Thrombosis and Haemostasis , vol.98 , Issue.6 , pp. 1257-1265
    • Mor-Cohen, R.1    Rosenberg, N.2    Peretz, H.3    Landau, M.4    Coller, B.S.5    Awidi, A.6    Seligsohn, U.7
  • 57
    • 0035889152 scopus 로고    scopus 로고
    • A point mutation in the cysteine-rich domain of glycoprotein (GP) IIIa results in the expression of a GPIIb-IIIa (alphaIIbbeta3) integrin locked in a high affinity state and a Glanzmann thrombasthenia-like phenotype
    • Ruiz C, Liu CY, Sun QH, et al. A point mutation in the cysteine-rich domain of glycoprotein (GP) IIIa results in the expression of a GPIIb-IIIa (alphaIIbbeta3) integrin locked in a high affinity state and a Glanzmann thrombasthenia-like phenotype. Blood. 2001;98(8):2432-2441.
    • (2001) Blood , vol.98 , Issue.8 , pp. 2432-2441
    • Ruiz, C.1    Liu, C.Y.2    Sun, Q.H.3
  • 59
    • 10444283433 scopus 로고    scopus 로고
    • 3-subunit: (Met124Val)beta 3 alters the subunit dimerization rendering a decreased number of constitutive active alphaIIbbeta3 receptors
    • DOI 10.1160/TH04-06-0380
    • Gonzalez-Manchon C, Butta N, Larrucea S, et al. A variant thrombasthenic phenotype associated with compound heterozygosity of integrin beta3-subunit: (Met124Val)beta3 alters the subunit dimerization rendering a decreased number of constitutive active alphaIIbbeta3 receptors. Thromb Haemost. 2004;92(6):1377-1386. (Pubitemid 39642550)
    • (2004) Thrombosis and Haemostasis , vol.92 , Issue.6 , pp. 1377-1386
    • Gonzalez-Manchon, C.1    Butta, N.2    Larrucea, S.3    Arias-Salgado, E.G.4    Alonso, S.5    Lopez, A.6    Parrilla, R.7
  • 60
    • 0026772036 scopus 로고
    • A defect of platelet aggregation associated with an abnormal distribution of glycoprotein IIb-IIIa complexes within the platelet: The cause of a lifelong bleeding disorder
    • Hardisty R, Pidard D, Cox A, et al. A defect of platelet aggregation associated with an abnormal distribution of glycoprotein IIb-IIIa complexes within the platelet: the cause of a lifelong bleeding disorder. Blood. 1992;80(3):696-708.
    • (1992) Blood , vol.80 , Issue.3 , pp. 696-708
    • Hardisty, R.1    Pidard, D.2    Cox, A.3
  • 61
    • 0032402117 scopus 로고    scopus 로고
    • R to Q amino acid substitution in the GFFKR sequence of the cytoplasmic domain of the integrin alpha(IIb) subunit in a patient with a Glanzmann's thrombasthenia-like syndrome
    • Peyruchaud O, Nurden AT, Milet S, et al. R to Q substitution in the GFFKR sequence of the cytoplasmic domain of the integrin alphaIIb subunit in a patient with a Glanzmann's thrombasthenia-like syndrome. Blood. 1998;92(11):4178-4187. (Pubitemid 28544333)
    • (1998) Blood , vol.92 , Issue.11 , pp. 4178-4187
    • Peyruchaud, O.1    Nurden, A.T.2    Milet, S.3    Macchi, L.4    Pannochia, A.5    Bray, P.F.6    Kieffer, N.7    Bourre, F.8
  • 62
    • 81755178910 scopus 로고    scopus 로고
    • Glanzmann thrombasthenia-like syndromes associated with macrothrombocytopenias and mutations in the genes encoding the alphaIIbbeta3 integrin
    • Nurden AT, Pillois X, Fiore M, Heilig R, Nurden P. Glanzmann thrombasthenia-like syndromes associated with macrothrombocytopenias and mutations in the genes encoding the alphaIIbbeta3 integrin. Semin Thromb Hemost. 2011;37(6):698-706.
    • (2011) Semin Thromb Hemost , vol.37 , Issue.6 , pp. 698-706
    • Nurden, A.T.1    Pillois, X.2    Fiore, M.3    Heilig, R.4    Nurden, P.5
  • 63
    • 79956280665 scopus 로고    scopus 로고
    • Heterozygous ITGA2B R995W mutation inducing constitutive activation of the alphaIIbbeta3 receptor affects proplatelet formation and causes congenital macrothrombocytopenia
    • Kunishima S, Kashiwagi H, Otsu M, et al. Heterozygous ITGA2B R995W mutation inducing constitutive activation of the alphaIIbbeta3 receptor affects proplatelet formation and causes congenital macrothrombocytopenia. Blood. 2011;117(20):5479-5484.
    • (2011) Blood , vol.117 , Issue.20 , pp. 5479-5484
    • Kunishima, S.1    Kashiwagi, H.2    Otsu, M.3
  • 64
    • 70449566822 scopus 로고    scopus 로고
    • Structure of an integrin alphaIIbbeta3 transmembrane-cytoplasmic heterocomplex provides insight into integrin activation
    • Yang J, Ma YQ, Page RC, Misra S, Plow EF, Qin J. Structure of an integrin alphaIIbbeta3 transmembrane-cytoplasmic heterocomplex provides insight into integrin activation. Proc Natl Acad Sci U S A. 2009;106(42):17729-17734.
    • (2009) Proc Natl Acad Sci U S A. , vol.106 , Issue.42 , pp. 17729-17734
    • Yang, J.1    Ma, Y.Q.2    Page, R.C.3    Misra, S.4    Plow, E.F.5    Qin, J.6
  • 65
    • 43549096235 scopus 로고    scopus 로고
    • A nonsynonymous SNP in the ITGB3 gene disrupts the conserved membrane proximal cytoplasmic salt bridge in the alphaIIbbeta3 integrin and cosegregates dominantly with abnormal proplatelet formation and macrothrombocytopenia
    • Ghevaert C, Salamann A, Watkins NA, et al. A nonsynonymous SNP in the ITGB3 gene disrupts the conserved membrane proximal cytoplasmic salt bridge in the alphaIIbbeta3 integrin and cosegregates dominantly with abnormal proplatelet formation and macrothrombocytopenia. Blood. 2008;111(7):3407-3414.
    • (2008) Blood , vol.111 , Issue.7 , pp. 3407-3414
    • Ghevaert, C.1    Salamann, A.2    Watkins, N.A.3
  • 66
    • 66049160883 scopus 로고    scopus 로고
    • Dominant inheritance of a novel integrin beta3 mutation associated with a hereditary macrothrombocytopenia and platelet dysfunction in two Italian families
    • Gresele P, Falcinelli E, Giannini S, et al. Dominant inheritance of a novel integrin beta3 mutation associated with a hereditary macrothrombocytopenia and platelet dysfunction in two Italian families. Haematologica. 2009;94(5):663-669.
    • (2009) Haematologica , vol.94 , Issue.5 , pp. 663-669
    • Gresele, P.1    Falcinelli, E.2    Giannini, S.3
  • 67
    • 77954507827 scopus 로고    scopus 로고
    • L1718P mutation in the membrane-proximal cytoplasmic tail of beta3 promotes abnormal alphaIIbbeta3 clustering and lipid domain coalescence, and associates with a thrombasthenia-like phenotype
    • Jayo A, Conde I, Lastres P, et al. L1718P mutation in the membrane-proximal cytoplasmic tail of beta3 promotes abnormal alphaIIbbeta3 clustering and lipid domain coalescence, and associates with a thrombasthenia-like phenotype. Haematologica. 2010;95(7):1158-1166.
    • (2010) Haematologica , vol.95 , Issue.7 , pp. 1158-1166
    • Jayo, A.1    Conde, I.2    Lastres, P.3
  • 71
    • 66549121768 scopus 로고    scopus 로고
    • LAD-1/variant syndrome is caused by mutations in FERMT3
    • KuijpersTW, van de Vijver E,Weterman MAJ, 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.J.3
  • 72
    • 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
  • 73
    • 77953233840 scopus 로고    scopus 로고
    • Kindlins in FERM adhesion
    • Malinin BL, Plow EF, Byzova TV. Kindlins in FERM adhesion. Blood. 2010;115(20):4011-4017.
    • (2010) Blood , vol.115 , Issue.20 , pp. 4011-4017
    • Malinin, B.L.1    Plow, E.F.2    Byzova, T.V.3
  • 74
    • 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
  • 75
    • 77953317401 scopus 로고    scopus 로고
    • The integrin co-activator kindlin-3 is expressed and functional in a non-hematopoietic cell, the endothelial cell
    • Bialkowska K, Ma Y-Q, Bledzka K, et al. The integrin co-activator kindlin-3 is expressed and functional in a non-hematopoietic cell, the endothelial cell. J Biol Chem. 2010;285(24):18640-18649.
    • (2010) J Biol Chem , vol.285 , Issue.24 , pp. 18640-18649
    • Bialkowska, K.1    Ma, Y.-Q.2    Bledzka, K.3
  • 76
    • 0346102708 scopus 로고    scopus 로고
    • Glanzmann's thrombasthenia: Modulation of clinical phenotype by alpha2C807T gene polymorphism
    • D'Andrea G, Margaglione M. Glanzmann's Thrombasthenia Italian Team (GLATIT). Glanzmann's thrombasthenia: modulation of clinical phenotype by alpha2C807T gene polymorphism. Haematologica. 2003;88(12):1378-1382. (Pubitemid 38029721)
    • (2003) Haematologica , vol.88 , Issue.12 , pp. 1378-1382
    • D'Andrea, G.1    Margaglione, M.2
  • 77
    • 0141561924 scopus 로고    scopus 로고
    • The role of platelets in venous thrombosis: A patient with Glanzmann's thrombasthenia and factor V Leiden mutation suffering from deep vein thrombosis
    • ten Cate H, Brandjes DPM, Smits PHM, Van Mourik JA. The role of platelets in venous thrombosis: a patient with Glanzmann's thrombasthenia and factor V Leiden mutation suffering from deep vein thrombosis. J Thromb Haemost. 2003;1(2):394-395.
    • (2003) J Thromb Haemost , vol.1 , Issue.2 , pp. 394-395
    • Ten Cate, H.1    Brandjes, D.P.M.2    Smits, P.H.M.3    Van Mourik, J.A.4
  • 78
    • 0036436932 scopus 로고    scopus 로고
    • Human platelet alloantigen polymorphism in Glanzmann's thrombasthenia and its impact on the severity of the disease
    • DOI 10.1046/j.1365-2141.2002.03864.x
    • Ghosh K, Kulkarni B, Nair S, Shetty S, Mohanty D. Human platelet alloantigen polymorphism in Glanzmann's thrombasthenia and its impact on the severity of the disease. Br J Haematol. 2002;119(2):348-353. (Pubitemid 35365480)
    • (2002) British Journal of Haematology , vol.119 , Issue.2 , pp. 348-353
    • Ghosh, K.1    Kulkarni, B.2    Nair, S.3    Shetty, S.4    Mohanty, D.5
  • 79
    • 0642372604 scopus 로고    scopus 로고
    • Analysis of platelet membrane glycoprotein polymorphisms in Glanzmann thrombasthenia showed the French gypsy mutation in the alphaIIb gene to be strongly linked to the HPA-1b polymorphism in beta3
    • Jacquelin B, Tuleja E, Kunicki TJ, Nurden P, Nurden AT. Analysis of platelet membrane glycoprotein polymorphisms in Glanzmann thrombasthenia showed the French gypsy mutation in the alphaIIb gene to be strongly linked to the HPA-1b polymorphism in beta3. J Thromb Haemost. 2003;1(3):573-575.
    • (2003) J Thromb Haemost , vol.1 , Issue.3 , pp. 573-575
    • Jacquelin, B.1    Tuleja, E.2    Kunicki, T.J.3    Nurden, P.4    Nurden, A.T.5
  • 80
    • 77957935532 scopus 로고    scopus 로고
    • The genetics of normal platelet reactivity
    • Kunicki TJ, Nugent DJ. The genetics of normal platelet reactivity. Blood. 2010;116(15):2627-2634.
    • (2010) Blood , vol.116 , Issue.15 , pp. 2627-2634
    • Kunicki, T.J.1    Nugent, D.J.2
  • 81
    • 77951708287 scopus 로고    scopus 로고
    • Deadly allies: The fatal interplay between platelets and metastasizing cancer cells
    • Erpenbeck L, Schön MP. Deadly allies: the fatal interplay between platelets and metastasizing cancer cells. Blood. 2010;115(17):3427-3436.
    • (2010) Blood , vol.115 , Issue.17 , pp. 3427-3436
    • Erpenbeck, L.1    Schön, M.P.2
  • 83
    • 45549098345 scopus 로고    scopus 로고
    • 3 complex senses bacterial lipopeptides via vitronectin
    • DOI 10.1038/ni.1618, PII NI.1618
    • Gerold G, Ajaz KA, Bienert M, Laws H-J, Zychlinsky A, L de Diego JL.Atoll-like receptor 2-integrin beta3 complex senses bacterial lipopeptides via vitronectin. Nat Immunol. 2008;9(7):761-768. (Pubitemid 351859159)
    • (2008) Nature Immunology , vol.9 , Issue.7 , pp. 761-768
    • Gerold, G.1    Ajaj, K.A.2    Bienert, M.3    Laws, H.-J.4    Zychlinsky, A.5    De Diego, J.L.6
  • 84
    • 4644247875 scopus 로고    scopus 로고
    • Presentation and pattern of symptoms in 382 patients with glanzmann thrombasthenia in Iran
    • DOI 10.1002/ajh.20159
    • Toogeh G, Sharifian R, Lak M, Safeea R, Artoni A, Peyvandi F. Presentation and patterns of symptoms in 382 patients with Glanzmann thrombasthenia in Iran. Am J Hematol. 2004;77(2):198-199. (Pubitemid 39281870)
    • (2004) American Journal of Hematology , vol.77 , Issue.2 , pp. 198-199
    • Toogeh, G.1    Sharifian, R.2    Lak, M.3    Safaee, R.4    Artoni, A.5    Peyvandi, F.6
  • 87
    • 9244231286 scopus 로고    scopus 로고
    • Elevated Flk1 (vascular endothelial growth factor receptor 2) signaling mediates enhanced angiogenesis in beta3-integrin-deficient mice
    • Reynolds AR, Reynolds LE, Nagel TE, et al. Elevated Flk1 (vascular endothelial growth factor receptor 2) signaling mediates enhanced angiogenesis in beta3-integrin-deficient mice. Cancer Res. 2004;64(23):8343-8350.
    • (2004) Cancer Res , vol.64 , Issue.23 , pp. 8343-8350
    • Reynolds, A.R.1    Reynolds, L.E.2    Nagel, T.E.3
  • 89
    • 33847350777 scopus 로고    scopus 로고
    • Cooperation between VEGF and beta3 integrin during cardiac vascular development
    • DOI 10.1182/blood-2005-10-038893
    • .Weis SM, Lindquist JN, Barnes LA, et al. Cooperation between VEGF and beta3 integrin during cardiac vascular development. Blood. 2007;109(5):1962- 1970. (Pubitemid 46348193)
    • (2007) Blood , vol.109 , Issue.5 , pp. 1962-1970
    • Weis, S.M.1    Lindquist, J.N.2    Barnes, L.A.3    Lutu-Fuga, K.M.4    Cui, J.5    Wood, M.R.6    Cheresh, D.A.7
  • 91
    • 36348980445 scopus 로고    scopus 로고
    • Macrophage beta3 integrin suppresses hyperlipidemia-induced inflammation by modulating TNFalpha expression
    • DOI 10.1161/ATVBAHA.107.153650
    • Schneider JG, Zhu Y, Coleman T, Semenkovich CF. Macrophage beta3 integrin suppresses hyperlipidemia-induced inflammation by modulating TNFalpha expression. Arterioscler Thromb Vasc Biol. 2007;27(12):2699-2706. (Pubitemid 350158925)
    • (2007) Arteriosclerosis, Thrombosis, and Vascular Biology , vol.27 , Issue.12 , pp. 2699-2706
    • Schneider, J.G.1    Zhu, Y.2    Coleman, T.3    Semenkovich, C.F.4
  • 97
    • 0023946733 scopus 로고
    • Role of adhesive proteins in platelet tumour interaction in vitro and metastasis formation in vivo
    • Karpatkin S, Pearlstein E, Ambrogio C, Coller BS. Role of adhesive proteins in platelet tumour interaction in vitro and metastasis formation in vivo. J Clin Invest. 1988;81(4):1012-1019.
    • (1988) J Clin Invest , vol.81 , Issue.4 , pp. 1012-1019
    • Karpatkin, S.1    Pearlstein, E.2    Ambrogio, C.3    Coller, B.S.4
  • 99
    • 79952435385 scopus 로고    scopus 로고
    • Kindlin-3-mediated signaling from multiple integrin classes is required for osteoclast-mediated bone resorption
    • Schmidt S, Nakchbandi I, Ruppert R, et al. Kindlin-3-mediated signaling from multiple integrin classes is required for osteoclast-mediated bone resorption. J Cell Biol. 2011;192(5):883-897.
    • (2011) J Cell Biol , vol.192 , Issue.5 , pp. 883-897
    • Schmidt, S.1    Nakchbandi, I.2    Ruppert, R.3
  • 100
    • 79951574616 scopus 로고    scopus 로고
    • Absence of preference for social novelty and increased grooming in integrin beta3 knockout mice: Initial studies and future directions
    • Carter MD, Shah CR, Muller CL, Crawley JN, Carneiro AM, Veenstra-VanderWeele J. Absence of preference for social novelty and increased grooming in integrin beta3 knockout mice: initial studies and future directions. Autism Res. 2011;4:(1):57-67.
    • (2011) Autism Res , vol.4 , Issue.1 , pp. 57-67
    • Carter, M.D.1    Shah, C.R.2    Muller, C.L.3    Crawley, J.N.4    Carneiro, A.M.5    Veenstra-VanderWeele, J.6
  • 101
    • 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, Marguérie G. Thrombasthenic mice generated by replacement of the integrin alphaIIb 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
  • 102
    • 15244352092 scopus 로고    scopus 로고
    • GPIIb (CD41) integrin is expressed on mast cells and influences their adhesion properties
    • DOI 10.1016/j.exphem.2005.01.011
    • Berlanga O, Emambokus N, Frampton J. GPIIb (CD41) integrin is expressed on mast cells and influences their adhesion properties. Exp Hematol. 2005;33(4):403-412. (Pubitemid 40387622)
    • (2005) Experimental Hematology , vol.33 , Issue.4 , pp. 403-412
    • Berlanga, O.1    Emambokus, N.2    Frampton, J.3
  • 103
    • 79251575575 scopus 로고    scopus 로고
    • Von Willebrand factor-mediated platelet adhesion is critical for deep vein thrombosis in mouse models
    • Brill A, Fuchs TA, Chauhan AK, et al. von Willebrand factor-mediated platelet adhesion is critical for deep vein thrombosis in mouse models. Blood. 2011;117(4):1400-1407.
    • (2011) Blood , vol.117 , Issue.4 , pp. 1400-1407
    • Brill, A.1    Fuchs, T.A.2    Chauhan, A.K.3


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