메뉴 건너뛰기




Volumn 64, Issue 1, 2009, Pages 133-156

Cytoskeletal interactions with leukocyte and endothelial cell adhesion molecules

Author keywords

[No Author keywords available]

Indexed keywords


EID: 80054020965     PISSN: 10635823     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1063-5823(09)64005-9     Document Type: Article
Times cited : (1)

References (127)
  • 1
    • 67650716492 scopus 로고    scopus 로고
    • The ins and outs of leukocyte integrin signaling
    • Abram, C. L., & Lowell, C. A. (2009). The ins and outs of leukocyte integrin signaling. Annual Review of Immunology, 27, 339-362.
    • (2009) Annual Review of Immunology , vol.27 , pp. 339-362
    • Abram, C.L.1    Lowell, C.A.2
  • 2
    • 29144447527 scopus 로고    scopus 로고
    • Alpha4beta1-dependent adhesion strengthening under mechanical strain is regulated by paxillin association with the alpha4-cytoplasmic domain
    • Alon, R., Feigelson, S. W., Manevich, E., Rose, D. M., Schmitz, J., Overby, D. R., et al. (2005). Alpha4beta1-dependent adhesion strengthening under mechanical strain is regulated by paxillin association with the alpha4-cytoplasmic domain. Journal of Cell Biology, 171, 1073-1084.
    • (2005) Journal of Cell Biology , vol.171 , pp. 1073-1084
    • Alon, R.1    Feigelson, S.W.2    Manevich, E.3    Rose, D.M.4    Schmitz, J.5    Overby, D.R.6
  • 3
    • 50849132538 scopus 로고    scopus 로고
    • Cells on the run: Shear-regulated integrin activation in leukocyte rolling and arrest on endothelial cells
    • Alon, R., & Ley, K. (2008). Cells on the run: Shear-regulated integrin activation in leukocyte rolling and arrest on endothelial cells. Current Opinion in Cell Biology, 20, 525-532.
    • (2008) Current Opinion in Cell Biology , vol.20 , pp. 525-532
    • Alon, R.1    Ley, K.2
  • 5
    • 34447336931 scopus 로고    scopus 로고
    • Functional insights on the polarized redistribution of leukocyte integrins and their ligands during leukocyte migration and immune interactions
    • Barreiro, O., de la Fuente, H., Mittelbrunn, M., & Sanchez-Madrid, F. (2007). Functional insights on the polarized redistribution of leukocyte integrins and their ligands during leukocyte migration and immune interactions. Immunological Reviews, 218, 147-164.
    • (2007) Immunological Reviews , vol.218 , pp. 147-164
    • Barreiro, O.1    de la Fuente, H.2    Mittelbrunn, M.3    Sanchez-Madrid, F.4
  • 6
    • 0037166942 scopus 로고    scopus 로고
    • Dynamic interaction of VCAM-1 and ICAM-1 with moesin and ezrin in a novel endothelial docking structure for adherent leukocytes
    • Barreiro, O., Yanez-Mo, M., Serrador, J. M., Montoya, M. C., Vicente-Manzanares, M., Tejedor, R., et al. (2002). Dynamic interaction of VCAM-1 and ICAM-1 with moesin and ezrin in a novel endothelial docking structure for adherent leukocytes. Journal of Cell Biology, 157, 1233-1245.
    • (2002) Journal of Cell Biology , vol.157 , pp. 1233-1245
    • Barreiro, O.1    Yanez-Mo, M.2    Serrador, J.M.3    Montoya, M.C.4    Vicente-Manzanares, M.5    Tejedor, R.6
  • 7
    • 58549086016 scopus 로고    scopus 로고
    • Regulation of conformer-specific activation of the integrin LFA-1 by a chemokinetriggered Rho signaling module
    • Bolomini-Vittori, M., Montresor, A., Giagulli, C., Staunton, D., Rossi, B., Martinello, M., et al. (2009). Regulation of conformer-specific activation of the integrin LFA-1 by a chemokinetriggered Rho signaling module. Nature Immunology, 10, 185-194.
    • (2009) Nature Immunology , vol.10 , pp. 185-194
    • Bolomini-Vittori, M.1    Montresor, A.2    Giagulli, C.3    Staunton, D.4    Rossi, B.5    Martinello, M.6
  • 8
    • 0030812812 scopus 로고    scopus 로고
    • Maintenance of human T cell anergy: Blocking of IL-2 gene transcription by activated Rap1
    • Boussiotis, V. A., Freeman, G. J., Berezovskaya, A., Barber, D. L., & Nadler, L. M. (1997). Maintenance of human T cell anergy: Blocking of IL-2 gene transcription by activated Rap1. Science, 278, 124-128.
    • (1997) Science , vol.278 , pp. 124-128
    • Boussiotis, V.A.1    Freeman, G.J.2    Berezovskaya, A.3    Barber, D.L.4    Nadler, L.M.5
  • 10
    • 3242705077 scopus 로고    scopus 로고
    • RhoA, Rac1, and Cdc42 exert distinct effects on epithelial barrier via selective structural and biochemical modulation of junctional proteins and F-actin
    • Bruewer, M., Hopkins, A. M., Hobert, M. E., Nusrat, A., & Madara, J. L. (2004). RhoA, Rac1, and Cdc42 exert distinct effects on epithelial barrier via selective structural and biochemical modulation of junctional proteins and F-actin. American Journal of Physiology: Cell Physiology, 287, C327-C335.
    • (2004) American Journal of Physiology: Cell Physiology , vol.287
    • Bruewer, M.1    Hopkins, A.M.2    Hobert, M.E.3    Nusrat, A.4    Madara, J.L.5
  • 11
    • 33747091892 scopus 로고    scopus 로고
    • Cytoskeletal regulation couples LFA-1 conformational changes to receptor lateral mobility and clustering
    • Cairo, C. W., Mirchev, R., & Golan, D. E. (2006). Cytoskeletal regulation couples LFA-1 conformational changes to receptor lateral mobility and clustering. Immunity, 25, 297-308.
    • (2006) Immunity , vol.25 , pp. 297-308
    • Cairo, C.W.1    Mirchev, R.2    Golan, D.E.3
  • 15
    • 47249143701 scopus 로고    scopus 로고
    • Integrin-associated proteins as potential therapeutic targets
    • Cantor, J. M., Ginsberg, M. H., & Rose, D. M. (2008). Integrin-associated proteins as potential therapeutic targets. Immunological Reviews, 223, 236-251.
    • (2008) Immunological Reviews , vol.223 , pp. 236-251
    • Cantor, J.M.1    Ginsberg, M.H.2    Rose, D.M.3
  • 16
    • 0026672861 scopus 로고
    • Association of intercellular adhesion molecule-1 (ICAM-1) with actin-containing cytoskeleton and alpha-actinin
    • Carpen, O., Pallai, P., Staunton, D., & Springer, T. A. (1992). Association of intercellular adhesion molecule-1 (ICAM-1) with actin-containing cytoskeleton and alpha-actinin. Journal of Cell Biology, 118, 1223-1234.
    • (1992) Journal of Cell Biology , vol.118 , pp. 1223-1234
    • Carpen, O.1    Pallai, P.2    Staunton, D.3    Springer, T.A.4
  • 17
    • 0030924021 scopus 로고    scopus 로고
    • ICAP-1, a novel beta1 integrin cytoplasmic domain-associated protein, binds to a conserved and functionally important NPXY sequence motif of beta1 integrin
    • Chang, D. D., Wong, C., Smith, H., & Liu, J. (1997). ICAP-1, a novel beta1 integrin cytoplasmic domain-associated protein, binds to a conserved and functionally important NPXY sequence motif of beta1 integrin. Journal of Cell Biology, 138, 1149-1157.
    • (1997) Journal of Cell Biology , vol.138 , pp. 1149-1157
    • Chang, D.D.1    Wong, C.2    Smith, H.3    Liu, J.4
  • 18
    • 11244352382 scopus 로고    scopus 로고
    • Interaction between insulin-like growth factor-I receptor and alphaVbeta3 integrin linked signaling pathways: Cellular responses to changes in multiple signaling inputs
    • Clemmons, D. R., & Maile, L. A. (2005). Interaction between insulin-like growth factor-I receptor and alphaVbeta3 integrin linked signaling pathways: Cellular responses to changes in multiple signaling inputs. Molecular Endocrinology, 19, 1-11.
    • (2005) Molecular Endocrinology , vol.19 , pp. 1-11
    • Clemmons, D.R.1    Maile, L.A.2
  • 19
    • 47249111609 scopus 로고    scopus 로고
    • Chemokine signaling and integrin activation in lymphocyte migration into the inflamed brain
    • Constantin, G. (2008). Chemokine signaling and integrin activation in lymphocyte migration into the inflamed brain. Journal of Neuroimmunology, 198, 20-26.
    • (2008) Journal of Neuroimmunology , vol.198 , pp. 20-26
    • Constantin, G.1
  • 20
    • 67650288199 scopus 로고    scopus 로고
    • Biochemical and structural properties of the integrin-associated cytoskeletal protein talin
    • Critchley, D. R. (2009). Biochemical and structural properties of the integrin-associated cytoskeletal protein talin. Annual Review of Biophysics, 38, 235-254.
    • (2009) Annual Review of Biophysics , vol.38 , pp. 235-254
    • Critchley, D.R.1
  • 21
    • 67649969524 scopus 로고    scopus 로고
    • An integrin-{alpha}4-14-3-3{zeta}-paxillin ternary complex mediates localised Cdc42 activity and accelerates cell migration
    • Deakin, N. O., Bass, M. D., Warwood, S., Schoelermann, J., Mostafavi-Pour, Z., Knight, D., et al. (2009). An integrin-{alpha}4-14-3-3{zeta}-paxillin ternary complex mediates localised Cdc42 activity and accelerates cell migration. Journal of Cell Science, 122, 1654-1664.
    • (2009) Journal of Cell Science , vol.122 , pp. 1654-1664
    • Deakin, N.O.1    Bass, M.D.2    Warwood, S.3    Schoelermann, J.4    Mostafavi-Pour, Z.5    Knight, D.6
  • 23
    • 0035494494 scopus 로고    scopus 로고
    • Cytoplasmic anchorage of L-selectin controls leukocyte capture and rolling by increasing the mechanical stability of the selectin tether
    • Dwir, O., Kansas, G. S., & Alon, R. (2001). Cytoplasmic anchorage of L-selectin controls leukocyte capture and rolling by increasing the mechanical stability of the selectin tether. Journal of Cell Biology, 155, 145-156.
    • (2001) Journal of Cell Biology , vol.155 , pp. 145-156
    • Dwir, O.1    Kansas, G.S.2    Alon, R.3
  • 24
    • 33646431420 scopus 로고    scopus 로고
    • Shedding of lymphocyte function-associated antigen-1 (LFA-1) in a human inflammatory response
    • Evans, B. J., McDowall, A., Taylor, P. C., Hogg, N., Haskard, D. O., & Landis, R. C. (2006). Shedding of lymphocyte function-associated antigen-1 (LFA-1) in a human inflammatory response. Blood, 107, 3593-3599.
    • (2006) Blood , vol.107 , pp. 3593-3599
    • Evans, B.J.1    McDowall, A.2    Taylor, P.C.3    Hogg, N.4    Haskard, D.O.5    Landis, R.C.6
  • 27
    • 27944476021 scopus 로고    scopus 로고
    • Specific integrin alpha and beta chain phosphorylations regulate LFA-1 activation through affinity-dependent and -independent mechanisms
    • Fagerholm, S. C., Hilden, T. J., Nurmi, S. M., & Gahmberg, C. G. (2005). Specific integrin alpha and beta chain phosphorylations regulate LFA-1 activation through affinity-dependent and -independent mechanisms. Journal of Cell Biology, 171, 705-715.
    • (2005) Journal of Cell Biology , vol.171 , pp. 705-715
    • Fagerholm, S.C.1    Hilden, T.J.2    Nurmi, S.M.3    Gahmberg, C.G.4
  • 29
    • 42449138333 scopus 로고    scopus 로고
    • RhoA activation and actin reorganization involved in endothelial CAM-mediated endocytosis of anti-PECAM carriers: Critical role for tyrosine 686 in the cytoplasmic tail of PECAM-1
    • Garnacho, C., Shuvaev, V., Thomas, A., McKenna, L., Sun, J., Koval, M., et al. (2008). RhoA activation and actin reorganization involved in endothelial CAM-mediated endocytosis of anti-PECAM carriers: Critical role for tyrosine 686 in the cytoplasmic tail of PECAM-1. Blood, 111, 3024-3033.
    • (2008) Blood , vol.111 , pp. 3024-3033
    • Garnacho, C.1    Shuvaev, V.2    Thomas, A.3    McKenna, L.4    Sun, J.5    Koval, M.6
  • 30
    • 0034213074 scopus 로고    scopus 로고
    • Cytohesin-1 regulates beta-2 integrin-mediated adhesion through both ARF-GEF function and interaction with LFA-1
    • Geiger, C., Nagel, W., Boehm, T., van Kooyk, Y., Figdor, C. G., Kremmer, E., et al. (2000). Cytohesin-1 regulates beta-2 integrin-mediated adhesion through both ARF-GEF function and interaction with LFA-1. EMBO Journal, 19, 2525-2536.
    • (2000) EMBO Journal , vol.19 , pp. 2525-2536
    • Geiger, C.1    Nagel, W.2    Boehm, T.3    van Kooyk, Y.4    Figdor, C.G.5    Kremmer, E.6
  • 34
    • 18944403970 scopus 로고    scopus 로고
    • A coiled-coil structure of the alphaIIbbeta3 integrin transmembrane and cytoplasmic domains in its resting state
    • Gottschalk, K. E. (2005). A coiled-coil structure of the alphaIIbbeta3 integrin transmembrane and cytoplasmic domains in its resting state. Structure, 13, 703-712.
    • (2005) Structure , vol.13 , pp. 703-712
    • Gottschalk, K.E.1
  • 35
    • 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, D. S., Bouaouina, M., & Calderwood, D. A. (2009). Kindlin-1 and -2 directly bind the C-terminal region of beta integrin cytoplasmic tails and exert integrin-specific activation effects. Journal of Biological Chemistry, 284, 11485-11497.
    • (2009) Journal of Biological Chemistry , vol.284 , pp. 11485-11497
    • Harburger, D.S.1    Bouaouina, M.2    Calderwood, D.A.3
  • 36
    • 0029908326 scopus 로고    scopus 로고
    • Binding of the cytoplasmic domain of intercellular adhesion molecule-2 (ICAM-2) to alphaactinin
    • Heiska, L., Kantor, C., Parr, T., Critchley, D. R., Vilja, P., Gahmberg, C. G., et al. (1996). Binding of the cytoplasmic domain of intercellular adhesion molecule-2 (ICAM-2) to alphaactinin. Journal of Biological Chemistry, 271, 26214-26219.
    • (1996) Journal of Biological Chemistry , vol.271 , pp. 26214-26219
    • Heiska, L.1    Kantor, C.2    Parr, T.3    Critchley, D.R.4    Vilja, P.5    Gahmberg, C.G.6
  • 39
    • 0022534722 scopus 로고
    • Interaction of plasma membrane fibronectin receptor with talin-A transmembrane linkage
    • Horwitz, A., Duggan, K., Buck, C., Beckerle, M. C., & Burridge, K. (1986). Interaction of plasma membrane fibronectin receptor with talin-A transmembrane linkage. Nature, 320, 531-533.
    • (1986) Nature , vol.320 , pp. 531-533
    • Horwitz, A.1    Duggan, K.2    Buck, C.3    Beckerle, M.C.4    Burridge, K.5
  • 41
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • Hynes, R. O. (2002). Integrins: Bidirectional, allosteric signaling machines. Cell, 110, 673-687.
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 43
    • 0037127291 scopus 로고    scopus 로고
    • The cytoplasmic tail of L-selectin interacts with members of the ezrin-radixin-moesin (ERM) family of proteins: Cell activation-dependent binding of moesin but not ezrin
    • Ivetic, A., Deka, J., Ridley, A., & Ager, A. (2002). The cytoplasmic tail of L-selectin interacts with members of the ezrin-radixin-moesin (ERM) family of proteins: Cell activation-dependent binding of moesin but not ezrin. Journal of Biological Chemistry, 277, 2321-2329.
    • (2002) Journal of Biological Chemistry , vol.277 , pp. 2321-2329
    • Ivetic, A.1    Deka, J.2    Ridley, A.3    Ager, A.4
  • 44
    • 4043079958 scopus 로고    scopus 로고
    • Mutagenesis of the ezrin-radixin-moesin binding domain of L-selectin tail affects shedding, microvillar positioning, and leukocyte tethering
    • Ivetic, A., Florey, O., Deka, J., Haskard, D. O., Ager, A., & Ridley, A. J. (2004). Mutagenesis of the ezrin-radixin-moesin binding domain of L-selectin tail affects shedding, microvillar positioning, and leukocyte tethering. Journal of Biological Chemistry, 279, 33263-33272.
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 33263-33272
    • Ivetic, A.1    Florey, O.2    Deka, J.3    Haskard, D.O.4    Ager, A.5    Ridley, A.J.6
  • 45
    • 0027509819 scopus 로고
    • Regulation of leukocyte rolling and adhesion to high endothelial venules through the cytoplasmic domain of L-selectin
    • Kansas, G. S., Ley, K., Munro, J. M., & Tedder, T. F. (1993). Regulation of leukocyte rolling and adhesion to high endothelial venules through the cytoplasmic domain of L-selectin. Journal of Experimental Medicine, 177, 833-838.
    • (1993) Journal of Experimental Medicine , vol.177 , pp. 833-838
    • Kansas, G.S.1    Ley, K.2    Munro, J.M.3    Tedder, T.F.4
  • 46
    • 0030010583 scopus 로고    scopus 로고
    • The cytoplasmic domains of E- and P-selectin do not constitutively interact with alpha-actinin and are not essential for leukocyte adhesion
    • Kansas, G. S., & Pavalko, F. M. (1996). The cytoplasmic domains of E- and P-selectin do not constitutively interact with alpha-actinin and are not essential for leukocyte adhesion. Journal of Immunology, 157, 321-325.
    • (1996) Journal of Immunology , vol.157 , pp. 321-325
    • Kansas, G.S.1    Pavalko, F.M.2
  • 48
    • 0034004457 scopus 로고    scopus 로고
    • Rap1 is a potent activation signal for leukocyte function-associated antigen 1 distinct from protein kinase C and phosphatidylinositol-3-OH kinase
    • Katagiri, K., Hattori, M., Minato, N., Irie, S., Takatsu, K., & Kinashi, T. (2000). Rap1 is a potent activation signal for leukocyte function-associated antigen 1 distinct from protein kinase C and phosphatidylinositol-3-OH kinase. Molecular Cell Biology, 20, 1956-1969.
    • (2000) Molecular Cell Biology , vol.20 , pp. 1956-1969
    • Katagiri, K.1    Hattori, M.2    Minato, N.3    Irie, S.4    Takatsu, K.5    Kinashi, T.6
  • 49
    • 0042490495 scopus 로고    scopus 로고
    • RAPL, a Rap1-binding molecule that mediates Rap1-induced adhesion through spatial regulation of LFA-1
    • Katagiri, K., Maeda, A., Shimonaka, M., & Kinashi, T. (2003). RAPL, a Rap1-binding molecule that mediates Rap1-induced adhesion through spatial regulation of LFA-1. Nature Immunology, 4, 741-748.
    • (2003) Nature Immunology , vol.4 , pp. 741-748
    • Katagiri, K.1    Maeda, A.2    Shimonaka, M.3    Kinashi, T.4
  • 50
    • 65649085856 scopus 로고    scopus 로고
    • In vitro and in vivo characterization of molecular interactions between calmodulin, ezrin/radixin/moesin, and L-selectin
    • Killock, D. J., Parsons, M., Zarrouk, M., Ameer-Beg, S. M., Ridley, A. J., Haskard, D. O., et al. (2009). In vitro and in vivo characterization of molecular interactions between calmodulin, ezrin/radixin/moesin, and L-selectin. Journal of Biological Chemistry, 284, 8833-8845.
    • (2009) Journal of Biological Chemistry , vol.284 , pp. 8833-8845
    • Killock, D.J.1    Parsons, M.2    Zarrouk, M.3    Ameer-Beg, S.M.4    Ridley, A.J.5    Haskard, D.O.6
  • 51
    • 0042681786 scopus 로고    scopus 로고
    • Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins
    • Kim, M., Carman, C. V., & Springer, T. A. (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
  • 52
    • 21844450244 scopus 로고    scopus 로고
    • Intracellular signalling controlling integrin activation in lymphocytes
    • Kinashi, T. (2005). Intracellular signalling controlling integrin activation in lymphocytes. Nature Reviews Immunology, 5, 546-559.
    • (2005) Nature Reviews Immunology , vol.5 , pp. 546-559
    • Kinashi, T.1
  • 53
    • 2342597085 scopus 로고    scopus 로고
    • Regulation of lymphocyte adhesion and migration by the small GTPase Rap1 and its effector molecule, RAPL
    • Kinashi, T., & Katagiri, K. (2004). Regulation of lymphocyte adhesion and migration by the small GTPase Rap1 and its effector molecule, RAPL. Immunology Letters, 93, 1-5.
    • (2004) Immunology Letters , vol.93 , pp. 1-5
    • Kinashi, T.1    Katagiri, K.2
  • 54
    • 34447335816 scopus 로고    scopus 로고
    • Guanine nucleotide exchange factors of the cytohesin family and their roles in signal transduction
    • Kolanus, W. (2007). Guanine nucleotide exchange factors of the cytohesin family and their roles in signal transduction. Immunological Reviews, 218, 102-113.
    • (2007) Immunological Reviews , vol.218 , pp. 102-113
    • Kolanus, W.1
  • 55
    • 0030602819 scopus 로고    scopus 로고
    • Alpha L beta 2 integrin/LFA-1 binding to ICAM-1 induced by cytohesin-1, a cytoplasmic regulatory molecule
    • Kolanus, W., Nagel, W., Schiller, B., Zeitlmann, L., Godar, S., Stockinger, H., et al. (1996). Alpha L beta 2 integrin/LFA-1 binding to ICAM-1 induced by cytohesin-1, a cytoplasmic regulatory molecule. Cell, 86, 233-242.
    • (1996) Cell , vol.86 , pp. 233-242
    • Kolanus, W.1    Nagel, W.2    Schiller, B.3    Zeitlmann, L.4    Godar, S.5    Stockinger, H.6
  • 56
    • 57049169143 scopus 로고    scopus 로고
    • Kindlins: Essential regulators of integrin signalling and cell-matrix adhesion
    • Larjava, H., Plow, E. F., & Wu, C. (2008). Kindlins: Essential regulators of integrin signalling and cell-matrix adhesion. EMBO Reports, 9, 1203-1208.
    • (2008) EMBO Reports , vol.9 , pp. 1203-1208
    • Larjava, H.1    Plow, E.F.2    Wu, C.3
  • 57
    • 61449213806 scopus 로고    scopus 로고
    • Mechanisms that regulate adaptor binding to beta-integrin cytoplasmic tails
    • Legate, K. R., & Fassler, R. (2009). Mechanisms that regulate adaptor binding to beta-integrin cytoplasmic tails. Journal of Cell Science, 122, 187-198.
    • (2009) Journal of Cell Science , vol.122 , pp. 187-198
    • Legate, K.R.1    Fassler, R.2
  • 58
    • 23844460509 scopus 로고    scopus 로고
    • Rap1-GTP is a negative regulator of Th cell function and promotes the generation of CD4+CD103+ regulatory T cells in vivo
    • Li, L., Greenwald, R. J., Lafuente, E. M., Tzachanis, D., Berezovskaya, A., Freeman, G. J., et al. (2005). Rap1-GTP is a negative regulator of Th cell function and promotes the generation of CD4{thorn}CD103{thorn} regulatory T cells in vivo. Journal of Immunology, 175, 3133-3139.
    • (2005) Journal of Immunology , vol.175 , pp. 3133-3139
    • Li, L.1    Greenwald, R.J.2    Lafuente, E.M.3    Tzachanis, D.4    Berezovskaya, A.5    Freeman, G.J.6
  • 59
    • 0033539801 scopus 로고    scopus 로고
    • Binding of paxillin to alpha4 integrins modifies integrin-dependent biological responses
    • Liu, S., Thomas, S. M., Woodside, D. G., Rose, D. M., Kiosses, W. B., Pfaff, M., et al. (1999). Binding of paxillin to alpha4 integrins modifies integrin-dependent biological responses. Nature, 402, 676-681.
    • (1999) Nature , vol.402 , pp. 676-681
    • Liu, S.1    Thomas, S.M.2    Woodside, D.G.3    Rose, D.M.4    Kiosses, W.B.5    Pfaff, M.6
  • 60
  • 61
    • 61949240364 scopus 로고    scopus 로고
    • A point mutation in KINDLIN3 ablates activation of three integrin subfamilies in humans
    • Malinin, N. L., Zhang, L., Choi, J., Ciocea, A., Razorenova, O., Ma, Y. Q., et al. (2009). A point mutation in KINDLIN3 ablates activation of three integrin subfamilies in humans. Nature Medicine, 15, 313-318.
    • (2009) Nature Medicine , vol.15 , pp. 313-318
    • Malinin, N.L.1    Zhang, L.2    Choi, J.3    Ciocea, A.4    Razorenova, O.5    Ma, Y.Q.6
  • 62
    • 42249092270 scopus 로고    scopus 로고
    • Leukocyte transmigration requires kinesin-mediated microtubule-dependent membrane trafficking from the lateral border recycling compartment
    • Mamdouh, Z., Kreitzer, G. E., & Muller, W. A. (2008). Leukocyte transmigration requires kinesin-mediated microtubule-dependent membrane trafficking from the lateral border recycling compartment. Journal of Experimental Medicine, 205, 951-966.
    • (2008) Journal of Experimental Medicine , vol.205 , pp. 951-966
    • Mamdouh, Z.1    Kreitzer, G.E.2    Muller, W.A.3
  • 66
    • 33645162400 scopus 로고    scopus 로고
    • Lymphocyte transcellular migration occurs through recruitment of endothelial ICAM-1 to caveola- and F-actin-rich domains
    • Millan, J., Hewlett, L., Glyn, M., Toomre, D., Clark, P., & Ridley, A. J. (2006). Lymphocyte transcellular migration occurs through recruitment of endothelial ICAM-1 to caveola- and F-actin-rich domains. Nature Cell Biology, 8, 113-123.
    • (2006) Nature Cell Biology , vol.8 , pp. 113-123
    • Millan, J.1    Hewlett, L.2    Glyn, M.3    Toomre, D.4    Clark, P.5    Ridley, A.J.6
  • 67
    • 52649135450 scopus 로고    scopus 로고
    • Separable requirements for cytoplasmic domain of PSGL-1 in leukocyte rolling and signaling under flow
    • Miner, J. J., Xia, L., Yago, T., Kappelmayer, J., Liu, Z., Klopocki, A. G., et al. (2008). Separable requirements for cytoplasmic domain of PSGL-1 in leukocyte rolling and signaling under flow. Blood, 112, 2035-2045.
    • (2008) Blood , vol.112 , pp. 2035-2045
    • Miner, J.J.1    Xia, L.2    Yago, T.3    Kappelmayer, J.4    Liu, Z.5    Klopocki, A.G.6
  • 68
    • 62149083068 scopus 로고    scopus 로고
    • The immunoglobulin-like cell adhesion molecule hepaCAM modulates cell adhesion and motility through direct interaction with the actin cytoskeleton
    • Moh, M. C., Tian, Q., Zhang, T., Lee, L. H., & Shen, S. (2009). The immunoglobulin-like cell adhesion molecule hepaCAM modulates cell adhesion and motility through direct interaction with the actin cytoskeleton. Journal of Cell Physiology, 219, 382-391.
    • (2009) Journal of Cell Physiology , vol.219 , pp. 382-391
    • Moh, M.C.1    Tian, Q.2    Zhang, T.3    Lee, L.H.4    Shen, S.5
  • 69
    • 22844449001 scopus 로고    scopus 로고
    • Structural and functional analyses of a novel ig-like cell adhesion molecule, hepaCAM, in the human breast carcinoma MCF7 cells
    • Moh, M. C., Zhang, C., Luo, C., Lee, L. H., & Shen, S. (2005). Structural and functional analyses of a novel ig-like cell adhesion molecule, hepaCAM, in the human breast carcinoma MCF7 cells. Journal of Biological Chemistry, 280, 27366-27374.
    • (2005) Journal of Biological Chemistry , vol.280 , pp. 27366-27374
    • Moh, M.C.1    Zhang, C.2    Luo, C.3    Lee, L.H.4    Shen, S.5
  • 70
    • 34447301486 scopus 로고    scopus 로고
    • Small GTPases and LFA-1 reciprocally modulate adhesion and signaling
    • Mor, A., Dustin, M. L., & Philips, M. R. (2007). Small GTPases and LFA-1 reciprocally modulate adhesion and signaling. Immunological Reviews, 218, 114-125.
    • (2007) Immunological Reviews , vol.218 , pp. 114-125
    • Mor, A.1    Dustin, M.L.2    Philips, M.R.3
  • 71
    • 61949352480 scopus 로고    scopus 로고
    • Kindlin-3 is required for beta2 integrin-mediated leukocyte adhesion to endothelial cells
    • Moser, M., Bauer, M., Schmid, S., Ruppert, R., Schmidt, S., Sixt, M., et al. (2009a). Kindlin-3 is required for beta2 integrin-mediated leukocyte adhesion to endothelial cells. Nature Medicine, 15, 300-305.
    • (2009) Nature Medicine , vol.15 , pp. 300-305
    • Moser, M.1    Bauer, M.2    Schmid, S.3    Ruppert, R.4    Schmidt, S.5    Sixt, M.6
  • 72
    • 66149128873 scopus 로고    scopus 로고
    • The tail of integrins, talin, and kindlins
    • Moser, M., Legate, K. R., Zent, R., & Fassler, R. (2009b). The tail of integrins, talin, and kindlins. Science, 324, 895-899.
    • (2009) Science , vol.324 , pp. 895-899
    • Moser, M.1    Legate, K.R.2    Zent, R.3    Fassler, R.4
  • 73
    • 40449133970 scopus 로고    scopus 로고
    • Kindlin-3 is essential for integrin activation and platelet aggregation
    • Moser, M., Nieswandt, B., Ussar, S., Pozgajova, M., & Fassler, R. (2008). Kindlin-3 is essential for integrin activation and platelet aggregation. Nature Medicine, 14, 325-330.
    • (2008) Nature Medicine , vol.14 , pp. 325-330
    • Moser, M.1    Nieswandt, B.2    Ussar, S.3    Pozgajova, M.4    Fassler, R.5
  • 74
    • 0031828870 scopus 로고    scopus 로고
    • The PH domain and the polybasic c domain of cytohesin-1 cooperate specifically in plasma membrane association and cellular function
    • Nagel, W., Schilcher, P., Zeitlmann, L., & Kolanus, W. (1998a). The PH domain and the polybasic c domain of cytohesin-1 cooperate specifically in plasma membrane association and cellular function. Molecular Biology of the Cell, 9, 1981-1994.
    • (1998) Molecular Biology of the Cell , vol.9 , pp. 1981-1994
    • Nagel, W.1    Schilcher, P.2    Zeitlmann, L.3    Kolanus, W.4
  • 75
    • 0032511031 scopus 로고    scopus 로고
    • Phosphoinositide 3-OH kinase activates the beta2 integrin adhesion pathway and induces membrane recruitment of cytohesin-1
    • Nagel, W., Zeitlmann, L., Schilcher, P., Geiger, C., Kolanus, J., & Kolanus, W. (1998b). Phosphoinositide 3-OH kinase activates the beta2 integrin adhesion pathway and induces membrane recruitment of cytohesin-1. Journal of Biological Chemistry, 273, 14853-14861.
    • (1998) Journal of Biological Chemistry , vol.273 , pp. 14853-14861
    • Nagel, W.1    Zeitlmann, L.2    Schilcher, P.3    Geiger, C.4    Kolanus, J.5    Kolanus, W.6
  • 78
    • 0026779479 scopus 로고
    • Activation-dependent changes in human plateletPECAM-1: Phosphorylation, cytoskeletal association, and surface membrane redistribution
    • Newman, P. J., Hillery, C. A., Albrecht, R., Parise, L. V., Berndt, M. C., Mazurov, A. V., et al. (1992). Activation-dependent changes in human plateletPECAM-1: Phosphorylation, cytoskeletal association, and surface membrane redistribution. Journal ofCell Biology, 119, 239-246.
    • (1992) Journal ofCell Biology , vol.119 , pp. 239-246
    • Newman, P.J.1    Hillery, C.A.2    Albrecht, R.3    Parise, L.V.4    Berndt, M.C.5    Mazurov, A.V.6
  • 79
    • 34250820373 scopus 로고    scopus 로고
    • Numb controls integrin endocytosis for directional cell migration with aPKC and PAR-3
    • Nishimura, T., & Kaibuchi, K. (2007). Numb controls integrin endocytosis for directional cell migration with aPKC and PAR-3. Developmental Cell, 13, 15-28.
    • (2007) Developmental Cell , vol.13 , pp. 15-28
    • Nishimura, T.1    Kaibuchi, K.2
  • 80
    • 14844323604 scopus 로고    scopus 로고
    • Transmembrane domain helix packing stabilizes integrin alphaIIbbeta3 in the low affinity state
    • Partridge, A. W., Liu, S., Kim, S., Bowie, J. U., & Ginsberg, M. H. (2005). Transmembrane domain helix packing stabilizes integrin alphaIIbbeta3 in the low affinity state. Journal of Biological Chemistry, 280, 7294-7300.
    • (2005) Journal of Biological Chemistry , vol.280 , pp. 7294-7300
    • Partridge, A.W.1    Liu, S.2    Kim, S.3    Bowie, J.U.4    Ginsberg, M.H.5
  • 81
    • 60849107267 scopus 로고    scopus 로고
    • The role of cell adhesion molecules in the progression of colorectal cancer and the development of liver metastasis
    • Paschos, K. A., Canovas, D., & Bird, N. C. (2009). The role of cell adhesion molecules in the progression of colorectal cancer and the development of liver metastasis. Cellular Signalling, 21, 665-674.
    • (2009) Cellular Signalling , vol.21 , pp. 665-674
    • Paschos, K.A.1    Canovas, D.2    Bird, N.C.3
  • 82
    • 0027317933 scopus 로고
    • Activation of human neutrophils induces an interaction between the integrin beta 2-subunit (CD18) and the actin binding protein alpha-actinin
    • Pavalko, F. M., & LaRoche, S. M. (1993). Activation of human neutrophils induces an interaction between the integrin beta 2-subunit (CD18) and the actin binding protein alpha-actinin. Journal of Immunology, 151, 3795-3807.
    • (1993) Journal of Immunology , vol.151 , pp. 3795-3807
    • Pavalko, F.M.1    LaRoche, S.M.2
  • 83
    • 0029074732 scopus 로고
    • The cytoplasmic domain of L-selectin interacts with cytoskeletal proteins via alphaactinin: Receptor positioning in microvilli does not require interaction with alpha-actinin
    • Pavalko, F. M., Walker, D. M., Graham, L., Goheen, M., Doerschuk, C. M., & Kansas, G. S. (1995). The cytoplasmic domain of L-selectin interacts with cytoskeletal proteins via alphaactinin: Receptor positioning in microvilli does not require interaction with alpha-actinin. Journal of Cell Biology, 129, 1155-1164.
    • (1995) Journal of Cell Biology , vol.129 , pp. 1155-1164
    • Pavalko, F.M.1    Walker, D.M.2    Graham, L.3    Goheen, M.4    Doerschuk, C.M.5    Kansas, G.S.6
  • 84
    • 33748680506 scopus 로고    scopus 로고
    • Simvastatin inhibits the migration and adhesion of monocytic cells and disorganizes the cytoskeleton of activated endothelial cells
    • Pozo, M., de Nicolas, R., Egido, J., & Gonzalez-Cabrero, J. (2006). Simvastatin inhibits the migration and adhesion of monocytic cells and disorganizes the cytoskeleton of activated endothelial cells. European Journal of Pharmacology, 548, 53-63.
    • (2006) European Journal of Pharmacology , vol.548 , pp. 53-63
    • Pozo, M.1    de Nicolas, R.2    Egido, J.3    Gonzalez-Cabrero, J.4
  • 85
    • 34248576321 scopus 로고    scopus 로고
    • Modulation of tight junction barrier function by outer membrane proteins of enteropathogenic Escherichia coli: Role of F-actin and junctional adhesion molecule-1
    • Puthenedam, M., Williams, P. H., Lakshmi, B. S., & Balakrishnan, A. (2007). Modulation of tight junction barrier function by outer membrane proteins of enteropathogenic Escherichia coli: Role of F-actin and junctional adhesion molecule-1. Cell Biology International, 31, 836-844.
    • (2007) Cell Biology International , vol.31 , pp. 836-844
    • Puthenedam, M.1    Williams, P.H.2    Lakshmi, B.S.3    Balakrishnan, A.4
  • 87
    • 67651089939 scopus 로고    scopus 로고
    • Cytohesin-1 controls the activation of RhoA and modulates integrin-dependent adhesion and migration of dendritic cells
    • Quast, T., Tappertzhofen, B., Schild, C., Grell, J., Czeloth, N., Forster, R., et al. (2009). Cytohesin-1 controls the activation of RhoA and modulates integrin-dependent adhesion and migration of dendritic cells. Blood, 113, 5801-5810.
    • (2009) Blood , vol.113 , pp. 5801-5810
    • Quast, T.1    Tappertzhofen, B.2    Schild, C.3    Grell, J.4    Czeloth, N.5    Forster, R.6
  • 90
    • 34447314985 scopus 로고    scopus 로고
    • Integrin modulation and signaling in leukocyte adhesion and migration
    • Rose, D. M., Alon, R., & Ginsberg, M. H. (2007). Integrin modulation and signaling in leukocyte adhesion and migration. Immunological Reviews, 218, 126-134.
    • (2007) Immunological Reviews , vol.218 , pp. 126-134
    • Rose, D.M.1    Alon, R.2    Ginsberg, M.H.3
  • 91
    • 0036696904 scopus 로고    scopus 로고
    • Alpha4 integrins and the immune response
    • Rose, D. M., Han, J., & Ginsberg, M. H. (2002). Alpha4 integrins and the immune response. Immunological Reviews, 186, 118-124.
    • (2002) Immunological Reviews , vol.186 , pp. 118-124
    • Rose, D.M.1    Han, J.2    Ginsberg, M.H.3
  • 92
    • 0032509204 scopus 로고    scopus 로고
    • Cytoskeletal interactions with the leukocyte integrin beta2 cytoplasmic tail. activation-dependent regulation of associations with talin and alpha-actinin [In Process Citation]
    • Sampath, R., Gallagher, P. J., & Pavalko, F. M. (1998). Cytoskeletal interactions with the leukocyte integrin beta2 cytoplasmic tail. activation-dependent regulation of associations with talin and alpha-actinin [In Process Citation]. Journal of Biological Chemistry, 273, 33588-33594.
    • (1998) Journal of Biological Chemistry , vol.273 , pp. 33588-33594
    • Sampath, R.1    Gallagher, P.J.2    Pavalko, F.M.3
  • 93
    • 1642396353 scopus 로고    scopus 로고
    • Involvement of transmembrane domain interactions in signal transduction by alpha/beta integrins
    • Schneider, D., & Engelman, D. M. (2004). Involvement of transmembrane domain interactions in signal transduction by alpha/beta integrins. Journal of Biological Chemistry, 279, 9840-9846.
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 9840-9846
    • Schneider, D.1    Engelman, D.M.2
  • 94
    • 0036009116 scopus 로고    scopus 로고
    • Rap1A positively regulates T cells via integrin activation rather than inhibiting lymphocyte signaling
    • Sebzda, E., Bracke, M., Tugal, T., Hogg, N., & Cantrell, D. A. (2002). Rap1A positively regulates T cells via integrin activation rather than inhibiting lymphocyte signaling. Nature Immunology, 3, 251-258.
    • (2002) Nature Immunology , vol.3 , pp. 251-258
    • Sebzda, E.1    Bracke, M.2    Tugal, T.3    Hogg, N.4    Cantrell, D.A.5
  • 96
    • 0346732920 scopus 로고    scopus 로고
    • Signal-dependent distribution of cell surface P-selectin in clathrin-coated pits affects leukocyte rolling under flow
    • Setiadi, H., & McEver, R. P. (2003). Signal-dependent distribution of cell surface P-selectin in clathrin-coated pits affects leukocyte rolling under flow. Journal of Cell Biology, 163, 1385-1395.
    • (2003) Journal of Cell Biology , vol.163 , pp. 1385-1395
    • Setiadi, H.1    McEver, R.P.2
  • 97
    • 41349095230 scopus 로고    scopus 로고
    • Clustering endothelial E-selectin in clathrin-coated pits and lipid rafts enhances leukocyte adhesion under flow
    • Setiadi, H., & McEver, R. P. (2008). Clustering endothelial E-selectin in clathrin-coated pits and lipid rafts enhances leukocyte adhesion under flow. Blood, 111, 1989-1998.
    • (2008) Blood , vol.111 , pp. 1989-1998
    • Setiadi, H.1    McEver, R.P.2
  • 98
    • 0028958438 scopus 로고
    • Direct interaction of filamin (ABP-280) with the beta 2-integrin subunit CD18
    • Sharma, C. P., Ezzell, R. M., & Arnaout, M. A. (1995). Direct interaction of filamin (ABP-280) with the beta 2-integrin subunit CD18. Journal of Immunology, 154, 3461-3470.
    • (1995) Journal of Immunology , vol.154 , pp. 3461-3470
    • Sharma, C.P.1    Ezzell, R.M.2    Arnaout, M.A.3
  • 99
    • 0033197965 scopus 로고    scopus 로고
    • Signaling functions of L-selectin in neutrophils: Alterations in the cytoskeleton and colocalization with CD18
    • Simon, S. I., Cherapanov, V., Nadra, I., Waddell, T. K., Seo, S. M., Wang, Q., et al. (1999). Signaling functions of L-selectin in neutrophils: Alterations in the cytoskeleton and colocalization with CD18. Journal of Immunology, 163, 2891-2901.
    • (1999) Journal of Immunology , vol.163 , pp. 2891-2901
    • Simon, S.I.1    Cherapanov, V.2    Nadra, I.3    Waddell, T.K.4    Seo, S.M.5    Wang, Q.6
  • 100
    • 58849140051 scopus 로고    scopus 로고
    • Leucocyte recruitment under fluid shear: Mechanical and molecular regulation within the inflammatory synapse
    • Simon, S. I., Sarantos, M. R., Green, C. E., & Schaff, U. Y. (2009). Leucocyte recruitment under fluid shear: Mechanical and molecular regulation within the inflammatory synapse. Clinical and Experimental Pharmacology & Physiology, 36, 217-224.
    • (2009) Clinical and Experimental Pharmacology & Physiology , vol.36 , pp. 217-224
    • Simon, S.I.1    Sarantos, M.R.2    Green, C.E.3    Schaff, U.Y.4
  • 104
    • 0037097835 scopus 로고    scopus 로고
    • Attachment of the PSGL-1 cytoplasmic domain to the actin cytoskeleton is essential for leukocyte rolling on P-selectin
    • Snapp, K. R., Heitzig, C. E., & Kansas, G. S. (2002). Attachment of the PSGL-1 cytoplasmic domain to the actin cytoskeleton is essential for leukocyte rolling on P-selectin. Blood, 99, 4494-4502.
    • (2002) Blood , vol.99 , pp. 4494-4502
    • Snapp, K.R.1    Heitzig, C.E.2    Kansas, G.S.3
  • 105
    • 25844435342 scopus 로고    scopus 로고
    • Myosin-X: A molecular motor at the cell's fingertips
    • Sousa, A. D., & Cheney, R. E. (2005). Myosin-X: A molecular motor at the cell's fingertips. Trends in Cell Biology, 15, 533-539.
    • (2005) Trends in Cell Biology , vol.15 , pp. 533-539
    • Sousa, A.D.1    Cheney, R.E.2
  • 106
    • 38049063929 scopus 로고    scopus 로고
    • Intermediateaffinity 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). Intermediateaffinity LFA-1 binds alpha-actinin-1 to control migration at the leading edge of the T cell. EMBO Journal, 27, 62-75.
    • (2008) EMBO Journal , vol.27 , pp. 62-75
    • Stanley, P.1    Smith, A.2    McDowall, A.3    Nicol, A.4    Zicha, D.5    Hogg, N.6
  • 107
    • 61949086409 scopus 로고    scopus 로고
    • Leukocyte adhesion deficiency-III is caused by mutations in KINDLIN3 affecting integrin activation
    • Svensson, L., Howarth, K., McDowall, A., Patzak, I., Evans, R., Ussar, S., et al. (2009). Leukocyte adhesion deficiency-III is caused by mutations in KINDLIN3 affecting integrin activation. Nature Medicine, 15, 306-312.
    • (2009) Nature Medicine , vol.15 , pp. 306-312
    • Svensson, L.1    Howarth, K.2    McDowall, A.3    Patzak, I.4    Evans, R.5    Ussar, S.6
  • 108
    • 0141865705 scopus 로고    scopus 로고
    • Talin binding to integrin beta tails: A final common step in integrin activation
    • Tadokoro, S., Shattil, S. J., Eto, K., Tai, V., Liddington, R. C., de Pereda, J. M., et al. (2003). Talin binding to integrin beta tails: A final common step in integrin activation. Science, 302, 103-106.
    • (2003) Science , vol.302 , pp. 103-106
    • Tadokoro, S.1    Shattil, S.J.2    Eto, K.3    Tai, V.4    Liddington, R.C.5    de Pereda, J.M.6
  • 109
    • 0141625303 scopus 로고    scopus 로고
    • Structure of integrin alpha5beta1 in complex with fibronectin
    • Takagi, J., Strokovich, K., Springer, T. A., & Walz, T. (2003). Structure of integrin alpha5beta1 in complex with fibronectin. EMBO Journal, 22, 4607-4615.
    • (2003) EMBO Journal , vol.22 , pp. 4607-4615
    • Takagi, J.1    Strokovich, K.2    Springer, T.A.3    Walz, T.4
  • 111
    • 52649141494 scopus 로고    scopus 로고
    • Beta2 integrin phosphorylation on Thr758 acts as a molecular switch to regulate 14-3-3 and filamin binding
    • Takala, H., Nurminen, E., Nurmi, S. M., Aatonen, M., Strandin, T., Takatalo, M., et al. (2008). Beta2 integrin phosphorylation on Thr758 acts as a molecular switch to regulate 14-3-3 and filamin binding. Blood, 112, 1853-1862.
    • (2008) Blood , vol.112 , pp. 1853-1862
    • Takala, H.1    Nurminen, E.2    Nurmi, S.M.3    Aatonen, M.4    Strandin, T.5    Takatalo, M.6
  • 112
    • 0037100270 scopus 로고    scopus 로고
    • Intercellular adhesion molecule (ICAM)-1, but not ICAM-2, activates RhoA and stimulates c-fos and rhoA transcription in endothelial cells
    • Thompson, P. W., Randi, A. M., & Ridley, A. J. (2002). Intercellular adhesion molecule (ICAM)-1, but not ICAM-2, activates RhoA and stimulates c-fos and rhoA transcription in endothelial cells. Journal of Immunology, 169, 1007-1013.
    • (2002) Journal of Immunology , vol.169 , pp. 1007-1013
    • Thompson, P.W.1    Randi, A.M.2    Ridley, A.J.3
  • 113
    • 18644377589 scopus 로고    scopus 로고
    • ITAM-based interaction of ERM proteins with Syk mediates signaling by the leukocyte adhesion receptor PSGL-1
    • Urzainqui, A., Serrador, J. M., Viedma, F., Yanez-Mo, M., Rodriguez, A., Corbi, A. L., et al. (2002). ITAM-based interaction of ERM proteins with Syk mediates signaling by the leukocyte adhesion receptor PSGL-1. Immunity, 17, 401-412.
    • (2002) Immunity , vol.17 , pp. 401-412
    • Urzainqui, A.1    Serrador, J.M.2    Viedma, F.3    Yanez-Mo, M.4    Rodriguez, A.5    Corbi, A.L.6
  • 114
    • 64849099993 scopus 로고    scopus 로고
    • Endothelial adapter proteins in leukocyte transmigration
    • van Buul, J. D., & Hordijk, P. L. (2009). Endothelial adapter proteins in leukocyte transmigration. Thrombosis and Haemostasis, 101, 649-655.
    • (2009) Thrombosis and Haemostasis , vol.101 , pp. 649-655
    • van Buul, J.D.1    Hordijk, P.L.2
  • 115
    • 15744393717 scopus 로고    scopus 로고
    • The role of the cytoskeleton in cellular adhesion molecule expression in tumor necrosis factor-stimulated endothelial cells
    • VandenBerg, E., Reid, M. D., Edwards, J. D., & Davis, H. W. (2004). The role of the cytoskeleton in cellular adhesion molecule expression in tumor necrosis factor-stimulated endothelial cells. Journal of Cell Biochemistry, 91, 926-937.
    • (2004) Journal of Cell Biochemistry , vol.91 , pp. 926-937
    • VandenBerg, E.1    Reid, M.D.2    Edwards, J.D.3    Davis, H.W.4
  • 117
    • 0037031551 scopus 로고    scopus 로고
    • A structural mechanism of integrin alpha(IIb)beta(3) "inside-out" activation as regulated by its cytoplasmic face
    • Vinogradova, O., Velyvis, A., Velyviene, A., Hu, B., Haas, T., Plow, E., et al. (2002). A structural mechanism of integrin alpha(IIb)beta(3) "inside-out" activation as regulated by its cytoplasmic face. Cell, 110, 587-597.
    • (2002) Cell , vol.110 , pp. 587-597
    • Vinogradova, O.1    Velyvis, A.2    Velyviene, A.3    Hu, B.4    Haas, T.5    Plow, E.6
  • 118
    • 33646240152 scopus 로고    scopus 로고
    • Engagement of PSGL-1 enhances beta(2)-integrin-involved adhesion of neutrophils to recombinant ICAM-1
    • Wang, X. G., Cheng, Y. P., & Ba, X. Q. (2006). Engagement of PSGL-1 enhances beta(2)-integrin-involved adhesion of neutrophils to recombinant ICAM-1. Acta Pharmacologica Sinica, 27, 617-622.
    • (2006) Acta Pharmacologica Sinica , vol.27 , pp. 617-622
    • Wang, X.G.1    Cheng, Y.P.2    Ba, X.Q.3
  • 119
    • 0035846547 scopus 로고    scopus 로고
    • Cytohesin-1 is a dynamic regulator of distinct LFA-1 functions in leukocyte arrest and transmigration triggered by chemokines
    • Weber, K. S., Weber, C., Ostermann, G., Dierks, H., Nagel, W., & Kolanus, W. (2001). Cytohesin-1 is a dynamic regulator of distinct LFA-1 functions in leukocyte arrest and transmigration triggered by chemokines. Current Biology, 11, 1969-1974.
    • (2001) Current Biology , vol.11 , pp. 1969-1974
    • Weber, K.S.1    Weber, C.2    Ostermann, G.3    Dierks, H.4    Nagel, W.5    Kolanus, W.6
  • 121
    • 80055114178 scopus 로고    scopus 로고
    • Analysis of physiologic E-selectin-mediated leukocyte rolling on microvascular endothelium
    • Wiese, G., Barthel, S. R., & Dimitroff, C. J. (2009). Analysis of physiologic E-selectin-mediated leukocyte rolling on microvascular endothelium. Journal of Visualized Experiments, 24,.
    • (2009) Journal of Visualized Experiments , vol.24
    • Wiese, G.1    Barthel, S.R.2    Dimitroff, C.J.3
  • 122
    • 0032528336 scopus 로고    scopus 로고
    • Phosphorylation of the cytoplasmic domain of E-selectin is regulated during leukocyte- endothelial adhesion
    • Yoshida, M., Szente, B. E., Kiely, J. M., Rosenzweig, A., & Gimbrone, M. A., Jr. (1998). Phosphorylation of the cytoplasmic domain of E-selectin is regulated during leukocyte- endothelial adhesion. Journal of Immunology, 161, 933-941.
    • (1998) Journal of Immunology , vol.161 , pp. 933-941
    • Yoshida, M.1    Szente, B.E.2    Kiely, J.M.3    Rosenzweig, A.4    Gimbrone Jr., M.A.5
  • 123
    • 0029937785 scopus 로고    scopus 로고
    • Leukocyte adhesion to vascular endothelium induces E-selectin linkage to the actin cytoskeleton
    • Yoshida, M., Westlin, W. F., Wang, N., Ingber, D. E., Rosenzweig, A., Resnick, N., et al. (1996). Leukocyte adhesion to vascular endothelium induces E-selectin linkage to the actin cytoskeleton. Journal of Cell Biology, 133, 445-455.
    • (1996) Journal of Cell Biology , vol.133 , pp. 445-455
    • Yoshida, M.1    Westlin, W.F.2    Wang, N.3    Ingber, D.E.4    Rosenzweig, A.5    Resnick, N.6
  • 124
    • 38749113918 scopus 로고    scopus 로고
    • Mechanisms and consequences of neutrophil interaction with the endothelium
    • Zarbock, A., & Ley, K. (2008). Mechanisms and consequences of neutrophil interaction with the endothelium. American Journal of Pathology, 172, 1-7.
    • (2008) American Journal of Pathology , vol.172 , pp. 1-7
    • Zarbock, A.1    Ley, K.2
  • 125
    • 64249148490 scopus 로고    scopus 로고
    • Neutrophil adhesion and activation under flow
    • Zarbock, A., & Ley, K. (2009). Neutrophil adhesion and activation under flow. Microcirculation, 16, 31-42.
    • (2009) Microcirculation , vol.16 , pp. 31-42
    • Zarbock, A.1    Ley, K.2
  • 126
    • 2942705683 scopus 로고    scopus 로고
    • Myosin-X provides a motor-based link between integrins and the cytoskeleton
    • Zhang, H., Berg, J. S., Li, Z., Wang, Y., Lang, P., Sousa, A. D., et al. (2004). Myosin-X provides a motor-based link between integrins and the cytoskeleton. Nature Cell Biology, 6, 523-531.
    • (2004) Nature Cell Biology , vol.6 , pp. 523-531
    • Zhang, H.1    Berg, J.S.2    Li, Z.3    Wang, Y.4    Lang, P.5    Sousa, A.D.6
  • 127
    • 34948882323 scopus 로고    scopus 로고
    • Requirement of alpha and beta subunit transmembrane helix separation for integrin outside-in signaling
    • Zhu, J., Carman, C. V., Kim, M., Shimaoka, M., Springer, T. A., & Luo, B. H. (2007). Requirement of alpha and beta subunit transmembrane helix separation for integrin outside-in signaling. Blood, 110, 2475-2483.
    • (2007) Blood , vol.110 , pp. 2475-2483
    • Zhu, J.1    Carman, C.V.2    Kim, M.3    Shimaoka, M.4    Springer, T.A.5    Luo, B.H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.