메뉴 건너뛰기




Volumn 30, Issue 23, 2011, Pages 4712-4727

Regulation of integrin affinity on cell surfaces

Author keywords

CD11a CD18; ICAM 1; Lymphocyte functionassociated antigen 1 (LFA 1); Metal ion dependent adhesion site (MIDAS); Stromal cell derived factor (SDF)

Indexed keywords

CELL ADHESION MOLECULE; INTEGRIN; LYMPHOCYTE FUNCTION ASSOCIATED ANTIGEN 1; T LYMPHOCYTE RECEPTOR;

EID: 82455189778     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.1038/emboj.2011.333     Document Type: Article
Times cited : (145)

References (75)
  • 2
    • 33745912405 scopus 로고    scopus 로고
    • A time- and cost-efficient system for high-level protein production in mammalian cells
    • Aricescu AR, Lu W, Jones EY (2006) A time- and cost-efficient system for high-level protein production in mammalian cells. Acta Crystallogr D Biol Crystallogr 62(Part 10): 1243-1250
    • (2006) Acta Crystallogr D Biol Crystallogr , vol.62 , Issue.PART 10 , pp. 1243-1250
    • Aricescu, A.R.1    Lu, W.2    Jones, E.Y.3
  • 3
    • 0036220127 scopus 로고    scopus 로고
    • Cysteine-rich module structure reveals a fulcrum for integrin rearrangement upon activation
    • 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: 282-287
    • (2002) Nat Struct Biol , vol.9 , pp. 282-287
    • Beglova, N.1    Blacklow, S.C.2    Takagi, J.3    Springer, T.A.4
  • 5
    • 77957034686 scopus 로고    scopus 로고
    • Requirement of open headpiece conformation for activation of leukocyte integrin aXb2
    • Chen X, Xie C, Nishida N, Li Z, Walz T, Springer TA (2010) Requirement of open headpiece conformation for activation of leukocyte integrin aXb2. Proc Natl Acad Sci USA 107: 14727-14732
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 14727-14732
    • Chen, X.1    Xie, C.2    Nishida, N.3    Li, Z.4    Walz, T.5    Springer, T.A.6
  • 6
    • 0034507687 scopus 로고    scopus 로고
    • Chemokines trigger immediate β2 integrin affinity and mobility changes: Differential regulation and roles in lymphocyte arrest under flow
    • Constantin G, Majeed M, Giagulli C, Piccib L, Kim JY, Butcher EC, Laudanna C (2000) Chemokines trigger immediate β2 integrin affinity and mobility changes: differential regulation and roles in lymphocyte arrest under flow. Immunity 13: 759-769
    • (2000) Immunity , vol.13 , pp. 759-769
    • Constantin, G.1    Majeed, M.2    Giagulli, C.3    Piccib, L.4    Kim, J.Y.5    Butcher, E.C.6    Laudanna, C.7
  • 7
    • 0026601096 scopus 로고
    • Divalent cation regulation of the function of the leukocyte integrin LFA-1
    • Dransfield I, Cabañas C, Craig A, Hogg N (1992) Divalent cation regulation of the function of the leukocyte integrin LFA-1. J Cell Biol 116: 219-226
    • (1992) J Cell Biol , vol.116 , pp. 219-226
    • Dransfield, I.1    Cabañas, C.2    Craig, A.3    Hogg, N.4
  • 8
    • 0024814732 scopus 로고
    • 2+ binding epitope on leukocyte integrin alpha subunits
    • 2+ binding epitope on leukocyte integrin alpha subunits. EMBO J 8: 3759-3765
    • (1989) EMBO J , vol.8 , pp. 3759-3765
    • Dransfield, I.1    Hogg, N.2
  • 9
    • 0035005829 scopus 로고    scopus 로고
    • A novel anti-CD18mAb recognizes an activation-related epitope and induces a high-affinity conformation in leukocyte integrins
    • Drbal K, Angelisova P, Cerny J, Hilgert I, Horejsi V (2001) A novel anti-CD18mAb recognizes an activation-related epitope and induces a high-affinity conformation in leukocyte integrins. Immunobiology 203: 687-698
    • (2001) Immunobiology , vol.203 , pp. 687-698
    • Drbal, K.1    Angelisova, P.2    Cerny, J.3    Hilgert, I.4    Horejsi, V.5
  • 11
    • 0024443411 scopus 로고
    • T cell receptor cross-linking transiently stimulates adhesiveness through LFA-1
    • Dustin ML, Springer TA (1989) T cell receptor cross-linking transiently stimulates adhesiveness through LFA-1. Nature 341: 619-624
    • (1989) Nature , vol.341 , pp. 619-624
    • Dustin, M.L.1    Springer, T.A.2
  • 13
    • 78650661881 scopus 로고    scopus 로고
    • Occupancy of lymphocyte LFA-1 by surface-immobilized ICAM-1 is critical for TCR- but not for chemokine-triggered LFA-1 conversion to an open headpiece high-affinity state
    • Feigelson SW, Pasvolsky R, Cemerski S, Shulman Z, Grabovsky V, Ilani T, Sagiv A, Lemaitre F, Laudanna C, Shaw AS, Alon R (2010) Occupancy of lymphocyte LFA-1 by surface-immobilized ICAM-1 is critical for TCR- but not for chemokine-triggered LFA-1 conversion to an open headpiece high-affinity state. J Immunol 185: 7394-7404
    • (2010) J Immunol , vol.185 , pp. 7394-7404
    • Feigelson, S.W.1    Pasvolsky, R.2    Cemerski, S.3    Shulman, Z.4    Grabovsky, V.5    Ilani, T.6    Sagiv, A.7    Lemaitre, F.8    Laudanna, C.9    Shaw, A.S.10    Alon, R.11
  • 16
    • 0031571726 scopus 로고    scopus 로고
    • Low affinity of cell surface lymphocyte function-associated antigen-1 (LFA-1) generates selectivity for cell-cell interactions
    • Ganpule G, Knorr R, Miller JM, Carron CP, Dustin ML (1997) Low affinity of cell surface lymphocyte function-associated antigen-1 (LFA-1) generates selectivity for cell-cell interactions. J Immunol 159: 2685-2692
    • (1997) J Immunol , vol.159 , pp. 2685-2692
    • Ganpule, G.1    Knorr, R.2    Miller, J.M.3    Carron, C.P.4    Dustin, M.L.5
  • 18
    • 78049354941 scopus 로고    scopus 로고
    • Tethering of intercellular adhesion molecule on target cells is required for LFA-1-dependent NK cell adhesion and granule polarization
    • Gross CC, Brzostowski JA, Liu D, Long EO (2010) Tethering of intercellular adhesion molecule on target cells is required for LFA-1-dependent NK cell adhesion and granule polarization. J Immunol 185: 2918-2926
    • (2010) J Immunol , vol.185 , pp. 2918-2926
    • Gross, C.C.1    Brzostowski, J.A.2    Liu, D.3    Long, E.O.4
  • 19
    • 0025806144 scopus 로고
    • Regulation of adhesion to ICAM-1 by the cytoplasmic domain of LFA-1 integrin b subunit
    • Hibbs ML, Xu H, Stacker SA, Springer TA (1991) Regulation of adhesion to ICAM-1 by the cytoplasmic domain of LFA-1 integrin b subunit. Science 251: 1611-1613
    • (1991) Science , vol.251 , pp. 1611-1613
    • Hibbs, M.L.1    Xu, H.2    Stacker, S.A.3    Springer, T.A.4
  • 20
  • 22
    • 33645808241 scopus 로고    scopus 로고
    • Directed evolution to probe protein allostery and integrin i domains of 200 000-fold higher affinity
    • Jin M, Song G, Kim Y-S, Astrof N, Shimaoka M, Wittrup D, Springer TA (2006) Directed evolution to probe protein allostery and integrin I domains of 200 000-fold higher affinity. Proc Natl Acad USA 103: 5758-5763
    • (2006) Proc Natl Acad USA , vol.103 , pp. 5758-5763
    • Jin, M.1    Song, G.2    Kim, Y.-S.3    Astrof, N.4    Shimaoka, M.5    Wittrup, D.6    Springer, T.A.7
  • 23
    • 38049136514 scopus 로고    scopus 로고
    • Mechanisms for segregating T cell receptor and adhesion molecules during immunological synapse formation in Jurkat T cells
    • Kaizuka Y, Douglass AD, Varma R, Dustin ML, Vale RD (2007) Mechanisms for segregating T cell receptor and adhesion molecules during immunological synapse formation in Jurkat T cells. Proc Natl Acad USA 104: 20296-20301
    • (2007) Proc Natl Acad USA , vol.104 , pp. 20296-20301
    • Kaizuka, Y.1    Douglass, A.D.2    Varma, R.3    Dustin, M.L.4    Vale, R.D.5
  • 25
    • 0042681786 scopus 로고    scopus 로고
    • Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins
    • Kim M, Carman CV, Springer TA (2003) Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins. Science 301: 1720-1725
    • (2003) Science , vol.301 , pp. 1720-1725
    • Kim, M.1    Carman, C.V.2    Springer, T.A.3
  • 26
    • 11244274075 scopus 로고    scopus 로고
    • The primacy of affinity over clustering in regulation of adhesiveness of the integrin aLb2
    • Kim M, Carman CV, Yang W, Salas A, Springer TA (2004) The primacy of affinity over clustering in regulation of adhesiveness of the integrin aLb2. J Cell Biol 167: 1241-1253
    • (2004) J Cell Biol , vol.167 , pp. 1241-1253
    • Kim, M.1    Carman, C.V.2    Yang, W.3    Salas, A.4    Springer, T.A.5
  • 27
    • 0029913643 scopus 로고    scopus 로고
    • Adhesionactivating phorbol ester increases the mobility of leukocyte integrin LFA-1 in cultured lymphocytes
    • Kucik DF, Dustin ML, Miller JM, Brown EJ (1996) Adhesionactivating phorbol ester increases the mobility of leukocyte integrin LFA-1 in cultured lymphocytes. J Clin Invest 97: 2139-2144
    • (1996) J Clin Invest , vol.97 , pp. 2139-2144
    • Kucik, D.F.1    Dustin, M.L.2    Miller, J.M.3    Brown, E.J.4
  • 28
    • 0018701862 scopus 로고
    • Monoclonal antibodies defining distinctive human T cell surface antigens
    • Kung PC, Goldstein G, Reinherz EL, Schlossman SF (1979) Monoclonal antibodies defining distinctive human T cell surface antigens. Science NY 206: 347-349
    • (1979) Science NY , vol.206 , pp. 347-349
    • Kung, P.C.1    Goldstein, G.2    Reinherz, E.L.3    Schlossman, S.F.4
  • 30
    • 65649127175 scopus 로고    scopus 로고
    • The structure of the integrin aIIbb3 transmembrane complex explains integrin transmembrane signalling
    • Lau TL, Kim C, Ginsberg MH, Ulmer TS (2009) The structure of the integrin aIIbb3 transmembrane complex explains integrin transmembrane signalling. EMBO J 9: 1351-1361
    • (2009) EMBO J , vol.9 , pp. 1351-1361
    • Lau, T.L.1    Kim, C.2    Ginsberg, M.H.3    Ulmer, T.S.4
  • 31
    • 0028986196 scopus 로고
    • Crystal structure of the A domain from the a subunit of integrin CR3 (CD11b/ CD18)
    • Lee J-O, Rieu P, Arnaout MA, Liddington R (1995) Crystal structure of the A domain from the a subunit of integrin CR3 (CD11b/ CD18). Cell 80: 631-638
    • (1995) Cell , vol.80 , pp. 631-638
    • Lee, J.-O.1    Rieu, P.2    Arnaout, M.A.3    Liddington, R.4
  • 32
    • 34548241344 scopus 로고    scopus 로고
    • The cytosolic protein talin induces an intermediate affinity integrin aLb2
    • Li YF, Tang RH, Puan KJ, Law SK, Tan SM (2007) The cytosolic protein talin induces an intermediate affinity integrin aLb2. J Biol Chem 282: 24310-24319
    • (2007) J Biol Chem , vol.282 , pp. 24310-24319
    • Li, Y.F.1    Tang, R.H.2    Puan, K.J.3    Law, S.K.4    Tan, S.M.5
  • 33
    • 0027364840 scopus 로고
    • Direct evidence for two affinity states for lymphocyte functionassociated antigen 1 on activated T cells
    • Lollo BA, Chan KW, Hanson EM, Moy VT, Brian AA (1993) Direct evidence for two affinity states for lymphocyte functionassociated antigen 1 on activated T cells. J Biol Chem 268: 21693-21700
    • (1993) J Biol Chem , vol.268 , pp. 21693-21700
    • Lollo, B.A.1    Chan, K.W.2    Hanson, E.M.3    Moy, V.T.4    Brian, A.A.5
  • 34
    • 0035341132 scopus 로고    scopus 로고
    • Epitope mapping of antibodies to the C-terminal region of the integrin β2 subunit reveals regions that become exposed upon receptor activation
    • Lu C, Ferzly M, Takagi J, Springer TA (2001a) Epitope mapping of antibodies to the C-terminal region of the integrin β2 subunit reveals regions that become exposed upon receptor activation. J Immunol 166: 5629-5637
    • (2001) J Immunol , vol.166 , pp. 5629-5637
    • Lu, C.1    Ferzly, M.2    Takagi, J.3    Springer, T.A.4
  • 36
    • 4644342292 scopus 로고    scopus 로고
    • The binding sites for competitive antagonistic, allosteric antagonistic, and agonistic antibodies to the i domain of integrin LFA-1
    • Lu C, Shimaoka M, Salas A, Springer TA (2004) The binding sites for competitive antagonistic, allosteric antagonistic, and agonistic antibodies to the I domain of integrin LFA-1. J Immunol 173: 3972-3978
    • (2004) J Immunol , vol.173 , pp. 3972-3978
    • Lu, C.1    Shimaoka, M.2    Salas, A.3    Springer, T.A.4
  • 38
    • 0031181648 scopus 로고    scopus 로고
    • The alpha subunit cytoplasmic domain regulates the assembly and adhesiveness of integrin lymphocyte function-associated antigen-1 (LFA-1)
    • Lu C, Springer TA (1997) The alpha subunit cytoplasmic domain regulates the assembly and adhesiveness of integrin lymphocyte function-associated antigen-1 (LFA-1). J Immunol 159: 268-278
    • (1997) J Immunol , vol.159 , pp. 268-278
    • Lu, C.1    Springer, T.A.2
  • 40
    • 34247891506 scopus 로고    scopus 로고
    • Structural basis of integrin regulation and signaling
    • Luo B-H, Carman CV, Springer TA (2007) Structural basis of integrin regulation and signaling. Annu Rev Immunol 25: 619-647
    • (2007) Annu Rev Immunol , vol.25 , pp. 619-647
    • Luo, B.-H.1    Carman, C.V.2    Springer, T.A.3
  • 41
    • 0347717903 scopus 로고    scopus 로고
    • T-cell priming by dendritic cells in lymph nodes occurs in three distinct phases
    • Mempel TR, Henrickson SE, Von Andrian UH (2004) T-cell priming by dendritic cells in lymph nodes occurs in three distinct phases. Nature 427: 154-159
    • (2004) Nature , vol.427 , pp. 154-159
    • Mempel, T.R.1    Henrickson, S.E.2    Von Andrian, U.H.3
  • 42
    • 66149128873 scopus 로고    scopus 로고
    • The tail of integrins, Talin and Kindlins
    • Moser M, Legate KR, Zent R, Fassler R (2009) The tail of integrins, Talin and Kindlins. Science 234: 895-899
    • (2009) Science , vol.234 , pp. 895-899
    • Moser, M.1    Legate, K.R.2    Zent, R.3    Fassler, R.4
  • 43
    • 33749522074 scopus 로고    scopus 로고
    • Activation of leukocyte b2 integrins by conversion from bent to extended conformations
    • Nishida N, Xie C, Shimaoka M, Cheng Y, Walz T, Springer TA (2006) Activation of leukocyte b2 integrins by conversion from bent to extended conformations. Immunity 25: 583-594
    • (2006) Immunity , vol.25 , pp. 583-594
    • Nishida, N.1    Xie, C.2    Shimaoka, M.3    Cheng, Y.4    Walz, T.5    Springer, T.A.6
  • 44
    • 0029004083 scopus 로고
    • Activation of LFA-1 (CD11a/CD18) and Mac-1 (CD11b/CD18) mimicked by an antibody directed against CD18
    • Petruzzelli L, Maduzia L, Springer TA (1995) Activation of LFA-1 (CD11a/CD18) and Mac-1 (CD11b/CD18) mimicked by an antibody directed against CD18. J Immunol 155: 854-866
    • (1995) J Immunol , vol.155 , pp. 854-866
    • Petruzzelli, L.1    Maduzia, L.2    Springer, T.A.3
  • 45
    • 0037109074 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: High-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline- inducible N-acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line
    • Reeves PJ, Callewaert N, Contreras R, Khorana HG (2002) Structure and function in rhodopsin: high-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline- inducible N- acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line. Proc Natl Acad Sci USA 99: 13419-13424
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 13419-13424
    • Reeves, P.J.1    Callewaert, N.2    Contreras, R.3    Khorana, H.G.4
  • 46
    • 0026557165 scopus 로고
    • Antibody against the Leu-cam b-chain (CD18) promotes both LFA-1-and CR3-dependent adhesion events
    • Robinson MK, Andrew D, Rosen H, Brown D, Ortlepp S, Stephens P, Butcher EC (1992) Antibody against the Leu-cam b-chain (CD18) promotes both LFA-1-and CR3-dependent adhesion events. J Immunol 148: 1080-1085
    • (1992) J Immunol , vol.148 , pp. 1080-1085
    • Robinson, M.K.1    Andrew, D.2    Rosen, H.3    Brown, D.4    Ortlepp, S.5    Stephens, P.6    Butcher, E.C.7
  • 47
    • 1842684991 scopus 로고    scopus 로고
    • Rolling adhesion through an extended conformation of integrin aLb2 and relation to a i and b I-like domain interaction
    • Salas A, Shimaoka M, Kogan AN, Harwood C, von Andrian UH, Springer TA (2004) Rolling adhesion through an extended conformation of integrin aLb2 and relation to a I and b I-like domain interaction. Immunity 20: 393-406
    • (2004) Immunity , vol.20 , pp. 393-406
    • Salas, A.1    Shimaoka, M.2    Kogan, A.N.3    Harwood, C.4    Von Andrian, U.H.5    Springer, T.A.6
  • 50
    • 35648936537 scopus 로고    scopus 로고
    • A structural hypothesis for the transition between bent and extended conformations of the leukocyte b2 integrins
    • Shi M, Foo SY, Tan SM, Mitchell EP, Law SK, Lescar J (2007) A structural hypothesis for the transition between bent and extended conformations of the leukocyte b2 integrins. J Biol Chem 282: 30198-30206
    • (2007) J Biol Chem , vol.282 , pp. 30198-30206
    • Shi, M.1    Foo, S.Y.2    Tan, S.M.3    Mitchell, E.P.4    Law, S.K.5    Lescar, J.6
  • 51
    • 24044494270 scopus 로고    scopus 로고
    • The crystal structure of the plexin-semaphorin-integrin domain/hybrid domain/I-EGF1 segment from the human integrin b2 subunit at 1.8-A resolution
    • Shi M, Sundramurthy K, Liu B, Tan SM, Law SK, Lescar J (2005) The crystal structure of the plexin-semaphorin-integrin domain/hybrid domain/I-EGF1 segment from the human integrin b2 subunit at 1.8-A resolution. J Biol Chem 280: 30586-30593
    • (2005) J Biol Chem , vol.280 , pp. 30586-30593
    • Shi, M.1    Sundramurthy, K.2    Liu, B.3    Tan, S.M.4    Law, S.K.5    Lescar, J.6
  • 53
    • 0035932996 scopus 로고    scopus 로고
    • Reversibly locking a protein fold in an active conformation with a disulfide bond: Integrin aL i domains with high affinity and antagonist activity in vivo
    • Shimaoka M, Lu C, Palframan R, von Andrian UH, Takagi J, Springer TA (2001) Reversibly locking a protein fold in an active conformation with a disulfide bond: integrin aL I domains with high affinity and antagonist activity in vivo. Proc Natl Acad Sci USA 98: 6009-6014
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 6009-6014
    • Shimaoka, M.1    Lu, C.2    Palframan, R.3    Von Andrian, U.H.4    Takagi, J.5    Springer, T.A.6
  • 54
    • 0141746138 scopus 로고    scopus 로고
    • Small molecule integrin antagonists that bind to the β2 subunit I-like domain and activate signals in one direction and block them in another
    • Shimaoka M, Salas A, Yang W, Weitz-Schmidt G, Springer TA (2003a) Small molecule integrin antagonists that bind to the β2 subunit I-like domain and activate signals in one direction and block them in another. Immunity 19: 391-402
    • (2003) Immunity , vol.19 , pp. 391-402
    • Shimaoka, M.1    Salas, A.2    Yang, W.3    Weitz-Schmidt, G.4    Springer, T.A.5
  • 55
    • 0142026204 scopus 로고    scopus 로고
    • Therapeutic antagonists and the conformational regulation of integrin structure and function
    • Shimaoka M, Springer TA (2003) Therapeutic antagonists and the conformational regulation of integrin structure and function. Nat Rev Drug Disc 2: 703-716
    • (2003) Nat Rev Drug Disc , vol.2 , pp. 703-716
    • Shimaoka, M.1    Springer, T.A.2
  • 59
    • 0018758819 scopus 로고
    • Mac-1: A macrophage differentiation antigen identified by monoclonal antibody
    • Springer TA, Galfre G, Secher DS, Milstein C (1979) Mac-1: a macrophage differentiation antigen identified by monoclonal antibody. Eur J Immunol 9: 301-306
    • (1979) Eur J Immunol , vol.9 , pp. 301-306
    • Springer, T.A.1    Galfre, G.2    Secher, D.S.3    Milstein, C.4
  • 60
    • 38049063929 scopus 로고    scopus 로고
    • Intermediate-affinity LFA-1 binds alpha-actinin-1 to control migration at the leading edge of the T cell
    • Stanley P, Smith A, McDowall A, Nicol A, Zicha D, Hogg N (2008) Intermediate-affinity LFA-1 binds alpha-actinin-1 to control migration at the leading edge of the T cell. EMBO J 27: 62-75
    • (2008) EMBO J , vol.27 , pp. 62-75
    • Stanley, P.1    Smith, A.2    McDowall, A.3    Nicol, A.4    Zicha, D.5    Hogg, N.6
  • 61
    • 0030028039 scopus 로고    scopus 로고
    • T cell adhesion to intercellular adhesion molecule-1 (ICAM-1) is controlled by cell spreading and the activation of integrin LFA-1
    • Stewart MP, Cabanas C, Hogg N (1996) T cell adhesion to intercellular adhesion molecule-1 (ICAM-1) is controlled by cell spreading and the activation of integrin LFA-1. J Immunol 156: 1810-1817
    • (1996) J Immunol , vol.156 , pp. 1810-1817
    • Stewart, M.P.1    Cabanas, C.2    Hogg, N.3
  • 62
    • 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: 599-611
    • (2002) Cell , vol.110 , pp. 599-611
    • Takagi, J.1    Petre, B.M.2    Walz, T.3    Springer, T.A.4
  • 63
    • 23844442497 scopus 로고    scopus 로고
    • Epitope mapping of monoclonal antibody to integrin aLb2 hybrid domain suggests different requirements of affinity states for intercellular adhesion molecules (ICAM)-1 and ICAM-3 binding
    • Tang RH, Tng E, Law SK, Tan SM (2005) Epitope mapping of monoclonal antibody to integrin aLb2 hybrid domain suggests different requirements of affinity states for intercellular adhesion molecules (ICAM)-1 and ICAM-3 binding. J Biol Chem 280: 29208-29216
    • (2005) J Biol Chem , vol.280 , pp. 29208-29216
    • Tang, R.H.1    Tng, E.2    Law, S.K.3    Tan, S.M.4
  • 64
    • 44449139065 scopus 로고    scopus 로고
    • Intercellular adhesion molecule-3 binding of integrin aLb2 requires both extension and opening of the integrin headpiece
    • Tang XY, Li YF, Tan SM (2008) Intercellular adhesion molecule-3 binding of integrin aLb2 requires both extension and opening of the integrin headpiece. J Immunol 180: 4793-4804
    • (2008) J Immunol , vol.180 , pp. 4793-4804
    • Tang, X.Y.1    Li, Y.F.2    Tan, S.M.3
  • 65
    • 0033578822 scopus 로고    scopus 로고
    • The actin cytoskeleton regulates LFA-1 ligand binding through avidity rather than affinity changes
    • van Kooyk Y, van Vliet SJ, Figdor CG (1999) The actin cytoskeleton regulates LFA-1 ligand binding through avidity rather than affinity changes. J Biol Chem 274: 26869-26877
    • (1999) J Biol Chem , vol.274 , pp. 26869-26877
    • Van Kooyk, Y.1    Van Vliet, S.J.2    Figdor, C.G.3
  • 68
    • 8544259562 scopus 로고    scopus 로고
    • Structural basis for allostery in integrins and binding of fibrinogen-mimetic therapeutics
    • Xiao T, Takagi J, Wang J-h, Coller BS, Springer TA (2004) Structural basis for allostery in integrins and binding of fibrinogen-mimetic therapeutics. Nature 432: 59-67
    • (2004) Nature , vol.432 , pp. 59-67
    • Xiao, T.1    Takagi, J.2    J-H, W.3    Coller, B.S.4    Springer, T.A.5
  • 69
    • 76349099822 scopus 로고    scopus 로고
    • Structure of an integrin with an a i domain, complement receptor type 4
    • Xie C, Zhu J, Chen X, Mi L, Nishida N, Springer TA (2010) Structure of an integrin with an a I domain, complement receptor type 4. EMBO J 29: 666-679
    • (2010) EMBO J , vol.29 , pp. 666-679
    • Xie, C.1    Zhu, J.2    Chen, X.3    Mi, L.4    Nishida, N.5    Springer, T.A.6
  • 72
    • 1542357680 scopus 로고    scopus 로고
    • Intersubunit signal transmission in integrins by a receptor-like interaction with a pull spring
    • Yang W, Shimaoka M, Salas A, Takagi J, Springer TA (2004) Intersubunit signal transmission in integrins by a receptor-like interaction with a pull spring. Proc Natl Acad Sci USA 101: 2906-2911
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 2906-2911
    • Yang, W.1    Shimaoka, M.2    Salas, A.3    Takagi, J.4    Springer, T.A.5
  • 75
    • 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: 849-861
    • (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.