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Volumn 68, Issue 1, 2015, Pages 24.5.1-24.5.31

Supported Lipid Bilayer Technology for the Study of Cellular Interfaces

Author keywords

CHOs cells; diffusion; liposome extrusion; protein engineering; recombinant transmembrane proteins; signal transduction; supported lipid bilayers; suspension CHO cells; synapse

Indexed keywords

1,2 DIOLEOYL SN GLYCERO 3 PHOSPHOETHANOLAMINE N (CAP BIOTINYL); 1,2 DIOLEOYL SN GLYCERO 3 [[N (5 AMINO 1 CARBOXYPENTYL)IMINODIACETIC ACID]SUCCINYL]; BIOTIN; GLYCEROPHOSPHOLIPID; LIPOSOME; MEMBRANE PROTEIN; UNCLASSIFIED DRUG; LIPID BILAYER; RECOMBINANT PROTEIN;

EID: 84995942648     PISSN: 19342500     EISSN: 19342616     Source Type: Journal    
DOI: 10.1002/0471143030.cb2405s68     Document Type: Article
Times cited : (15)

References (69)
  • 1
    • 84864139002 scopus 로고    scopus 로고
    • Integration of the movement of signaling microclusters with cellular motility in immunological synapses
    • Beemiller, P, Jacobelli, J, and Krummel, M.F. 2012. Integration of the movement of signaling microclusters with cellular motility in immunological synapses. Nat. Immunol. 13:787-795.
    • (2012) Nat. Immunol. , vol.13 , pp. 787-795
    • Beemiller, P.1    Jacobelli, J.2    Krummel, M.F.3
  • 2
    • 0028085838 scopus 로고
    • Cytoplasmic tail deletion of T cell receptor (TCR) beta-chain results in its surface expression as glycosylphosphatidylinositol-anchored polypeptide on mature T cells in the absence of TCR-alpha
    • Bell, L.M, Solomon, K.R, Gold, J.P, and Tan, K.N. 1994. Cytoplasmic tail deletion of T cell receptor (TCR) beta-chain results in its surface expression as glycosylphosphatidylinositol-anchored polypeptide on mature T cells in the absence of TCR-alpha. J. Biol. Chem. 269:22758-22763.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22758-22763
    • Bell, L.M.1    Solomon, K.R.2    Gold, J.P.3    Tan, K.N.4
  • 3
    • 85062765049 scopus 로고    scopus 로고
    • Actin and agonist MHC-peptide complex-dependent T cell receptor microclusters as scaffolds for signaling
    • Campi, G, Varma, R, and Dustin, M.L. 2005. Actin and agonist MHC-peptide complex-dependent T cell receptor microclusters as scaffolds for signaling. J. Exp. Med. 202:1031-1036.
    • (2005) J. Exp. Med. , vol.202 , pp. 1031-1036
    • Campi, G.1    Varma, R.2    Dustin, M.L.3
  • 4
    • 2442467885 scopus 로고    scopus 로고
    • LFA-1/ICAM-1 interaction lowers the threshold of B cell activation by facilitating B cell adhesion and synapse formation
    • Carrasco, Y.R, Fleire, S.J, Cameron, T, Dustin, M.L, and Batista, F.D. 2004. LFA-1/ICAM-1 interaction lowers the threshold of B cell activation by facilitating B cell adhesion and synapse formation. Immunity 20:589-599.
    • (2004) Immunity , vol.20 , pp. 589-599
    • Carrasco, Y.R.1    Fleire, S.J.2    Cameron, T.3    Dustin, M.L.4    Batista, F.D.5
  • 7
    • 84863740148 scopus 로고    scopus 로고
    • A TIRF microscopy technique for real-time, simultaneous imaging of the TCR and its associated signaling proteins
    • Crites, T.J, Chen, L, and Varma, R. 2012. A TIRF microscopy technique for real-time, simultaneous imaging of the TCR and its associated signaling proteins. J. Vis. Exp. 3892. doi: 10.3791/3892
    • (2012) J. Vis. Exp. , vol.3892
    • Crites, T.J.1    Chen, L.2    Varma, R.3
  • 9
    • 84914689850 scopus 로고    scopus 로고
    • Ligand-mediated friction determines morphodynamics of spreading T Cells
    • Dillard, P, Varma, R, Sengupta, K, and Limozin, L. 2014. Ligand-mediated friction determines morphodynamics of spreading T Cells. Biophys. J. 107:2629-2638.
    • (2014) Biophys. J. , vol.107 , pp. 2629-2638
    • Dillard, P.1    Varma, R.2    Sengupta, K.3    Limozin, L.4
  • 10
    • 0030916178 scopus 로고    scopus 로고
    • Adhesive bond dynamics in contacts between T lymphocytes and glass-supported planar bilayers reconstituted with the immunoglobulin-related adhesion molecule CD58
    • Dustin, M.L. 1997. Adhesive bond dynamics in contacts between T lymphocytes and glass-supported planar bilayers reconstituted with the immunoglobulin-related adhesion molecule CD58. J. Biol. Chem. 272:15782-15788.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15782-15788
    • Dustin, M.L.1
  • 11
    • 69249202271 scopus 로고    scopus 로고
    • Supported bilayers at the vanguard of immune cell activation studies
    • Dustin, M.L. 2009. Supported bilayers at the vanguard of immune cell activation studies. J. Struct. Biol. 168:152-160.
    • (2009) J. Struct. Biol. , vol.168 , pp. 152-160
    • Dustin, M.L.1
  • 12
    • 0030239667 scopus 로고    scopus 로고
    • TCR-mediated adhesion of T cell hybridomas to planar bilayers containing purified MHC class II/peptide complexes and receptor shedding during detachment
    • Dustin, M.L, Miller, J.M, Ranganath, S, Vignali, D.A, Viner, N.J, Nelson, C.A, and Unanue, E.R. 1996. TCR-mediated adhesion of T cell hybridomas to planar bilayers containing purified MHC class II/peptide complexes and receptor shedding during detachment. Eur. J. Immunol. 157:2014-2021.
    • (1996) Eur. J. Immunol. , vol.157 , pp. 2014-2021
    • Dustin, M.L.1    Miller, J.M.2    Ranganath, S.3    Vignali, D.A.4    Viner, N.J.5    Nelson, C.A.6    Unanue, E.R.7
  • 14
    • 77957258701 scopus 로고    scopus 로고
    • Supported planar bilayers for study of the immunological synapse
    • Dustin, M.L, Starr, T, Varma, R, and Thomas, V.K. 2007. Supported planar bilayers for study of the immunological synapse. Curr. Protoc. Immunol. 76:18.13.1-18.13.35.
    • (2007) Curr. Protoc. Immunol. , vol.76 , pp. 18.13.1-18.13.35
    • Dustin, M.L.1    Starr, T.2    Varma, R.3    Thomas, V.K.4
  • 15
    • 0032409445 scopus 로고    scopus 로고
    • Sequence properties of GPI-anchored proteins near the omega-site: Constraints for the polypeptide binding site of the putative transamidase
    • Eisenhaber, B, Bork, P, and Eisenhaber, F. 1998. Sequence properties of GPI-anchored proteins near the omega-site: Constraints for the polypeptide binding site of the putative transamidase. Protein Eng. 11:1155-1161.
    • (1998) Protein Eng. , vol.11 , pp. 1155-1161
    • Eisenhaber, B.1    Bork, P.2    Eisenhaber, F.3
  • 16
    • 0033600935 scopus 로고    scopus 로고
    • Prediction of potential GPI-modification sites in proprotein sequences
    • Eisenhaber, B, Bork, P, and Eisenhaber, F. 1999. Prediction of potential GPI-modification sites in proprotein sequences. J. Mol. Biol. 292:741-758.
    • (1999) J. Mol. Biol. , vol.292 , pp. 741-758
    • Eisenhaber, B.1    Bork, P.2    Eisenhaber, F.3
  • 17
    • 59849088541 scopus 로고    scopus 로고
    • Studying cell-to-cell interactions: An easy method of tethering ligands on artificial membranes
    • Fleire, S.J. and Batista, F.D. 2009. Studying cell-to-cell interactions: An easy method of tethering ligands on artificial membranes. Methods Mol. Biol. 462:145-154.
    • (2009) Methods Mol. Biol. , vol.462 , pp. 145-154
    • Fleire, S.J.1    Batista, F.D.2
  • 18
  • 19
    • 84907829271 scopus 로고    scopus 로고
    • Phosphatase CD45 both positively and negatively regulates T cell receptor phosphorylation in reconstituted membrane protein clusters
    • Furlan, G, Minowa, T, Hanagata, N, Kataoka-Hamai, C, and Kaizuka, Y. 2014. Phosphatase CD45 both positively and negatively regulates T cell receptor phosphorylation in reconstituted membrane protein clusters. J. Biol. Chem. 289:28514-28525.
    • (2014) J. Biol. Chem. , vol.289 , pp. 28514-28525
    • Furlan, G.1    Minowa, T.2    Hanagata, N.3    Kataoka-Hamai, C.4    Kaizuka, Y.5
  • 20
    • 67849125074 scopus 로고    scopus 로고
    • One-dimensional SDS gel electrophoresis of proteins
    • Gallagher, S.R. 2007. One-dimensional SDS gel electrophoresis of proteins. Curr. Protoc. Cell Biol. 37:6.1.1-6.1.38.
    • (2007) Curr. Protoc. Cell Biol. , vol.37 , pp. 6.1.1-6.1.38
    • Gallagher, S.R.1
  • 22
    • 51649092841 scopus 로고    scopus 로고
    • Quantitative fluorescence microscopy using supported lipid bilayer standards
    • Galush, W.J, Nye, J.A, and Groves, J.T. 2008. Quantitative fluorescence microscopy using supported lipid bilayer standards. Biophys. J. 95:2512-2519.
    • (2008) Biophys. J. , vol.95 , pp. 2512-2519
    • Galush, W.J.1    Nye, J.A.2    Groves, J.T.3
  • 24
    • 0142134858 scopus 로고    scopus 로고
    • Supported planar bilayers in studies on immune cell adhesion and communication
    • Groves, J.T. and Dustin, M.L. 2003. Supported planar bilayers in studies on immune cell adhesion and communication. J. Immunol. Methods 278:19-32.
    • (2003) J. Immunol. Methods , vol.278 , pp. 19-32
    • Groves, J.T.1    Dustin, M.L.2
  • 28
    • 67349114397 scopus 로고    scopus 로고
    • T cell antigen receptor signaling and immunological synapse stability require myosin IIA
    • Ilani, T, Vasiliver-Shamis, G, Vardhana, S, Bretscher, A, and Dustin, M.L. 2009. T cell antigen receptor signaling and immunological synapse stability require myosin IIA. Nat. Immunol. 10:531-539.
    • (2009) Nat. Immunol. , vol.10 , pp. 531-539
    • Ilani, T.1    Vasiliver-Shamis, G.2    Vardhana, S.3    Bretscher, A.4    Dustin, M.L.5
  • 29
    • 0029845009 scopus 로고    scopus 로고
    • Domains of the TCR beta-chain required for early thymocyte development
    • Jacobs, H, Iacomini, J, van de Ven, M, Tonegawa, S, and Berns, A. 1996. Domains of the TCR beta-chain required for early thymocyte development. J. Exp. Med. 184:1833-1843.
    • (1996) J. Exp. Med. , vol.184 , pp. 1833-1843
    • Jacobs, H.1    Iacomini, J.2    van de Ven, M.3    Tonegawa, S.4    Berns, A.5
  • 30
    • 0025062267 scopus 로고
    • On the species specificity of the interaction of LFA-1 with intercellular adhesion molecules
    • Johnston, S.C, Dustin, M.L, Hibbs, M.L, and Springer, T.A. 1990. On the species specificity of the interaction of LFA-1 with intercellular adhesion molecules. Eur. J. Immunol. 145:1181-1187.
    • (1990) Eur. J. Immunol. , vol.145 , pp. 1181-1187
    • Johnston, S.C.1    Dustin, M.L.2    Hibbs, M.L.3    Springer, T.A.4
  • 31
    • 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, A.D, Varma, R, Dustin, M.L, and Vale, R.D. 2007. Mechanisms for segregating T cell receptor and adhesion molecules during immunological synapse formation in Jurkat T cells. Proc. Natl. Acad. Sci. U.S.A. 104:20296-20301.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 20296-20301
    • Kaizuka, Y.1    Douglass, A.D.2    Varma, R.3    Dustin, M.L.4    Vale, R.D.5
  • 32
    • 0028233838 scopus 로고
    • Production of soluble MHC class II proteins with covalently bound single peptides
    • Kozono, H, White, J, Clements, J, Marrack, P, and Kappler, J. 1994. Production of soluble MHC class II proteins with covalently bound single peptides. Nature 369:151-154.
    • (1994) Nature , vol.369 , pp. 151-154
    • Kozono, H.1    White, J.2    Clements, J.3    Marrack, P.4    Kappler, J.5
  • 33
    • 17844364513 scopus 로고    scopus 로고
    • Paradigm shift of the plasma membrane concept from the two-dimensional continuum fluid to the partitioned fluid: High-speed single-molecule tracking of membrane molecules
    • Kusumi, A, Nakada, C, Ritchie, K, Murase, K, Suzuki, K, Murakoshi, H, Kasai, R.S, Kondo, J, and Fujiwara, T. 2005. Paradigm shift of the plasma membrane concept from the two-dimensional continuum fluid to the partitioned fluid: High-speed single-molecule tracking of membrane molecules. Annu. Rev. Biophys. Biomol. Struct. 34:351-378.
    • (2005) Annu. Rev. Biophys. Biomol. Struct. , vol.34 , pp. 351-378
    • Kusumi, A.1    Nakada, C.2    Ritchie, K.3    Murase, K.4    Suzuki, K.5    Murakoshi, H.6    Kasai, R.S.7    Kondo, J.8    Fujiwara, T.9
  • 34
    • 84888095370 scopus 로고    scopus 로고
    • Annular PIP3 accumulation controls actin architecture and modulates cytotoxicity at the immunological synapse
    • Le Floc'h, A, Tanaka, Y, Bantilan, N.S, Voisinne, G, Altan-Bonnet, G, Fukui, Y, and Huse, M. 2013. Annular PIP3 accumulation controls actin architecture and modulates cytotoxicity at the immunological synapse. J. Exp. Med.210:2721-2737.
    • (2013) J. Exp. Med , vol.210 , pp. 2721-2737
    • Le Floc'h, A.1    Tanaka, Y.2    Bantilan, N.S.3    Voisinne, G.4    Altan-Bonnet, G.5    Fukui, Y.6    Huse, M.7
  • 35
    • 0030668877 scopus 로고    scopus 로고
    • Simple affinity purification of antibodies using in vivo biotinylation of a fusion protein
    • Lesley, S.A. and Groskreutz, D.J. 1997. Simple affinity purification of antibodies using in vivo biotinylation of a fusion protein. J. Immunol. Methods 207:147-155.
    • (1997) J. Immunol. Methods , vol.207 , pp. 147-155
    • Lesley, S.A.1    Groskreutz, D.J.2
  • 36
    • 80755166293 scopus 로고    scopus 로고
    • Supported membrane formation, characterization, functionalization, and patterning for application in biological science and technology
    • Lin, W.C, Yu, C.H, Triffo, S, and Groves, J.T. 2010. Supported membrane formation, characterization, functionalization, and patterning for application in biological science and technology. Curr. Protoc. Chem. Biol. 2:235-269.
    • (2010) Curr. Protoc. Chem. Biol. , vol.2 , pp. 235-269
    • Lin, W.C.1    Yu, C.H.2    Triffo, S.3    Groves, J.T.4
  • 40
    • 0022531311 scopus 로고
    • Supported planar membranes in studies of cell-cell recognition in the immune system
    • McConnell, H.M, Watts, T.H, Weis, R.M, and Brian, A.A. 1986. Supported planar membranes in studies of cell-cell recognition in the immune system. Biochim. Biophys. Acta 864:95-106.
    • (1986) Biochim. Biophys. Acta , vol.864 , pp. 95-106
    • McConnell, H.M.1    Watts, T.H.2    Weis, R.M.3    Brian, A.A.4
  • 41
    • 0025776390 scopus 로고
    • Cytoplasmic tail deletion converts membrane immunoglobulin to a phosphatidylinositol-linked form lacking signaling and efficient antigen internalization functions
    • Mitchell, R.N, Shaw, A.C, Weaver, Y.K, Leder, P, and Abbas, A.K. 1991. Cytoplasmic tail deletion converts membrane immunoglobulin to a phosphatidylinositol-linked form lacking signaling and efficient antigen internalization functions. J. Biol. Chem. 266:8856-8860.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8856-8860
    • Mitchell, R.N.1    Shaw, A.C.2    Weaver, Y.K.3    Leder, P.4    Abbas, A.K.5
  • 42
    • 27944442353 scopus 로고    scopus 로고
    • Altered TCR signaling from geometrically repatterned immunological synapses
    • Mossman, K.D, Campi, G, Groves, J.T, and Dustin, M.L. 2005. Altered TCR signaling from geometrically repatterned immunological synapses. Science 310:1191-1193.
    • (2005) Science , vol.310 , pp. 1191-1193
    • Mossman, K.D.1    Campi, G.2    Groves, J.T.3    Dustin, M.L.4
  • 43
    • 84879694222 scopus 로고    scopus 로고
    • B cells use mechanical energy to discriminate antigen affinities
    • Natkanski, E, Lee, W.Y, Mistry, B, Casal, A, Molloy, J.E, and Tolar, P. 2013. B cells use mechanical energy to discriminate antigen affinities. Science 340:1587-1590.
    • (2013) Science , vol.340 , pp. 1587-1590
    • Natkanski, E.1    Lee, W.Y.2    Mistry, B.3    Casal, A.4    Molloy, J.E.5    Tolar, P.6
  • 44
    • 42449096835 scopus 로고    scopus 로고
    • Kinetic control of histidine-tagged protein surface density on supported lipid bilayers
    • Nye, J.A. and Groves, J.T. 2008. Kinetic control of histidine-tagged protein surface density on supported lipid bilayers. Langmuir 24:4145-4149.
    • (2008) Langmuir , vol.24 , pp. 4145-4149
    • Nye, J.A.1    Groves, J.T.2
  • 45
    • 84880089372 scopus 로고    scopus 로고
    • Direct single molecule measurement of TCR triggering by agonist pMHC in living primary T cells
    • O'Donoghue, G.P, Pielak, R.M, Smoligovets, A.A, Lin, J.J, and Groves, J.T. 2013. Direct single molecule measurement of TCR triggering by agonist pMHC in living primary T cells. eLife 2:e00778.
    • (2013) eLife , vol.2
    • O'Donoghue, G.P.1    Pielak, R.M.2    Smoligovets, A.A.3    Lin, J.J.4    Groves, J.T.5
  • 46
    • 84949224109 scopus 로고    scopus 로고
    • Basic techniques in mammalian cell tissue culture
    • Phelan, K. and May, K.M. 2015. Basic techniques in mammalian cell tissue culture. Curr. Protoc. Cell Biol. 66:1.1.1-1.1.22.
    • (2015) Curr. Protoc. Cell Biol. , vol.66 , pp. 1.1.1-1.1.22
    • Phelan, K.1    May, K.M.2
  • 47
    • 0033578388 scopus 로고    scopus 로고
    • An inverse relationship between T cell receptor affinity and antigen dose during CD4+ T cell responses in vivo and in vitro
    • Rees, W, Bender, J, Teague, T.K, Kedl, R.M, Crawford, F, Marrack, P, and Kappler, J. 1999. An inverse relationship between T cell receptor affinity and antigen dose during CD4+ T cell responses in vivo and in vitro. Proc. Natl. Acad. Sci. 96:9781-9786.
    • (1999) Proc. Natl. Acad. Sci. , vol.96 , pp. 9781-9786
    • Rees, W.1    Bender, J.2    Teague, T.K.3    Kedl, R.M.4    Crawford, F.5    Marrack, P.6    Kappler, J.7
  • 49
    • 0029979998 scopus 로고    scopus 로고
    • Role of chain pairing for the production of functional soluble IA major histocompatibility complex class II molecules
    • Scott, C.A, Garcia, K.C, Carbone, F.R, Wilson, I.A, and Teyton, L. 1996. Role of chain pairing for the production of functional soluble IA major histocompatibility complex class II molecules. J. Exp. Med. 183:2087-2095.
    • (1996) J. Exp. Med. , vol.183 , pp. 2087-2095
    • Scott, C.A.1    Garcia, K.C.2    Carbone, F.R.3    Wilson, I.A.4    Teyton, L.5
  • 50
    • 34147200105 scopus 로고    scopus 로고
    • Cell adhesion and growth to Peptide-patterned supported lipid membranes
    • Stroumpoulis, D, Zhang, H, Rubalcava, L, Gliem, J, and Tirrell, M. 2007. Cell adhesion and growth to Peptide-patterned supported lipid membranes. Langmuir 23:3849-3856.
    • (2007) Langmuir , vol.23 , pp. 3849-3856
    • Stroumpoulis, D.1    Zhang, H.2    Rubalcava, L.3    Gliem, J.4    Tirrell, M.5
  • 51
    • 0022687436 scopus 로고
    • Lateral diffusion of specific antibodies bound to lipid monolayers on alkylated substrates
    • Subramaniam, S, Seul, M, and McConnell, H.M. 1986. Lateral diffusion of specific antibodies bound to lipid monolayers on alkylated substrates. Proc. Natl. Acad. Sci. U.S.A. 83:1169-1173.
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 1169-1173
    • Subramaniam, S.1    Seul, M.2    McConnell, H.M.3
  • 53
    • 36248948115 scopus 로고    scopus 로고
    • Issues of ligand accessibility and mobility in initial cell attachment
    • Thid, D, Bally, M, Holm, K, Chessari, S, Tosatti, S, Textor, M, and Gold, J. 2007. Issues of ligand accessibility and mobility in initial cell attachment. Langmuir 23:11693-11704.
    • (2007) Langmuir , vol.23 , pp. 11693-11704
    • Thid, D.1    Bally, M.2    Holm, K.3    Chessari, S.4    Tosatti, S.5    Textor, M.6    Gold, J.7
  • 54
    • 58149247765 scopus 로고    scopus 로고
    • The constant region of the membrane immunoglobulin mediates B cell-receptor clustering and signaling in response to membrane antigens
    • Tolar, P, Hanna, J, Krueger, P.D, and Pierce, S.K. 2009. The constant region of the membrane immunoglobulin mediates B cell-receptor clustering and signaling in response to membrane antigens. Immunity 30:44-55.
    • (2009) Immunity , vol.30 , pp. 44-55
    • Tolar, P.1    Hanna, J.2    Krueger, P.D.3    Pierce, S.K.4
  • 55
    • 80055115517 scopus 로고    scopus 로고
    • Supported planar bilayers for the formation of study of immunological synapses and kinapse
    • Vardhana, S. and Dustin, M. 2008. Supported planar bilayers for the formation of study of immunological synapses and kinapse. J. Vis. Exp. pii:947. doi: 10.3791/947.
    • (2008) J. Vis. Exp. , vol.pii , pp. 947
    • Vardhana, S.1    Dustin, M.2
  • 56
    • 0029071688 scopus 로고
    • Soluble mouse major histocompatibility complex class II molecules produced in Drosophila cells
    • Wallny, H.J, Sollami, G, and Karjalainen, K. 1995. Soluble mouse major histocompatibility complex class II molecules produced in Drosophila cells. Eur. J. Immunol. 25:1262-1266.
    • (1995) Eur. J. Immunol. , vol.25 , pp. 1262-1266
    • Wallny, H.J.1    Sollami, G.2    Karjalainen, K.3
  • 58
    • 0021811620 scopus 로고
    • T-cell activation by peptide antigen: Effect of peptide sequence and method of antigen presentation
    • Watts, T.H, Gariepy, J, Schoolnik, G.K, and McConnell, H.M. 1985. T-cell activation by peptide antigen: Effect of peptide sequence and method of antigen presentation. Proc. Natl. Acad. Sci. U.S.A. 82:5480-5484.
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 5480-5484
    • Watts, T.H.1    Gariepy, J.2    Schoolnik, G.K.3    McConnell, H.M.4
  • 59
    • 0022632478 scopus 로고
    • T-cell-mediated association of peptide antigen and major histocompatibility complex protein detected by energy transfer in an evanescent wave-field
    • Watts, T.H, Gaub, H.E, and McConnell, H.M. 1986. T-cell-mediated association of peptide antigen and major histocompatibility complex protein detected by energy transfer in an evanescent wave-field. Nature 320:179-181.
    • (1986) Nature , vol.320 , pp. 179-181
    • Watts, T.H.1    Gaub, H.E.2    McConnell, H.M.3
  • 60
    • 0025898515 scopus 로고
    • Expression of a class II major histocompatibility complex (MHC) heterodimer in a lipid-linked form with enhanced peptide/soluble MHC complex formation at low pH
    • Wettstein, D.A, Boniface, J.J, Reay, P.A, Schild, H, and Davis, M.M. 1991. Expression of a class II major histocompatibility complex (MHC) heterodimer in a lipid-linked form with enhanced peptide/soluble MHC complex formation at low pH. J. Exp. Med. 174:219-228.
    • (1991) J. Exp. Med. , vol.174 , pp. 219-228
    • Wettstein, D.A.1    Boniface, J.J.2    Reay, P.A.3    Schild, H.4    Davis, M.M.5
  • 61
    • 84863229197 scopus 로고    scopus 로고
    • Actin retrograde flow and actomyosin II arc contraction drive receptor cluster dynamics at the immunological synapse in Jurkat T cells
    • Yi, J, Wu, X.S, Crites, T, and Hammer, J.A. 2012. Actin retrograde flow and actomyosin II arc contraction drive receptor cluster dynamics at the immunological synapse in Jurkat T cells. Mol. Biol. Cell 23:834-852.
    • (2012) Mol. Biol. Cell , vol.23 , pp. 834-852
    • Yi, J.1    Wu, X.S.2    Crites, T.3    Hammer, J.A.4
  • 64
    • 84855500059 scopus 로고    scopus 로고
    • Early integrin binding to Arg-Gly-Asp peptide activates actin polymerization and contractile movement that stimulates outward translocation
    • Yu, C.H, Law, J.B, Suryana, M, Low, H.Y, and Sheetz, M.P. 2011. Early integrin binding to Arg-Gly-Asp peptide activates actin polymerization and contractile movement that stimulates outward translocation. Proc. Natl. Acad. Sci. U.S.A. 108:20585-20590.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 20585-20590
    • Yu, C.H.1    Law, J.B.2    Suryana, M.3    Low, H.Y.4    Sheetz, M.P.5
  • 65
    • 84864920732 scopus 로고    scopus 로고
    • Spatial-temporal reorganization of activated integrins
    • Yu, C.H, Luo, W, and Sheetz, M.P. 2012. Spatial-temporal reorganization of activated integrins. Cell Adh. Migr. 6:280-284.
    • (2012) Cell Adh. Migr. , vol.6 , pp. 280-284
    • Yu, C.H.1    Luo, W.2    Sheetz, M.P.3
  • 67
    • 84923553217 scopus 로고    scopus 로고
    • Super-resolution imaging of the natural killer cell immunological synapse on a glass-supported planar lipid bilayer
    • Zheng, P, Bertolet, G, Chen, Y, Huang, S, and Liu, D. 2015. Super-resolution imaging of the natural killer cell immunological synapse on a glass-supported planar lipid bilayer. J. Vis. Exp. 96. doi: 10.3791/52502.
    • (2015) J. Vis. Exp. , vol.96
    • Zheng, P.1    Bertolet, G.2    Chen, Y.3    Huang, S.4    Liu, D.5
  • 68
    • 85075755675 scopus 로고    scopus 로고
    • Dustin et al., 2007. Seeabove.
    • (2007)
    • Dustin1
  • 69
    • 85075730385 scopus 로고    scopus 로고
    • See above
    • Vardana and Dustin, 2008. See above
    • (2008)
    • Vardana1    Dustin2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.