메뉴 건너뛰기




Volumn 256, Issue 1, 2013, Pages 30-47

Cofilin: A redox sensitive mediator of actin dynamics during T-cell activation and migration

Author keywords

Actin cytoskeleton; Costimulation; Immune synapse; Microenvironment; Redox; T cell activation

Indexed keywords

ACTIN; ACTIN BINDING PROTEIN; ACTIN RELATED PROTEIN 2-3 COMPLEX; CD2 ANTIGEN; COFILIN; DEOXYRIBONUCLEASE I; F ACTIN; LYMPHOCYTE FUNCTION ASSOCIATED ANTIGEN 1; PHOSPHOLIPID; PROTEIN KINASE B; RNA POLYMERASE II; WISKOTT ALDRICH SYNDROME PROTEIN;

EID: 84885336118     PISSN: 01052896     EISSN: 1600065X     Source Type: Journal    
DOI: 10.1111/imr.12115     Document Type: Article
Times cited : (68)

References (174)
  • 1
    • 84873735847 scopus 로고    scopus 로고
    • Cell polarisation and the immunological synapse
    • Angus KL, Griffiths GM. Cell polarisation and the immunological synapse. Curr Opin Cell Biol 2013;25:85-91.
    • (2013) Curr Opin Cell Biol , vol.25 , pp. 85-91
    • Angus, K.L.1    Griffiths, G.M.2
  • 3
    • 84863992208 scopus 로고    scopus 로고
    • F-actin polymerization and retrograde flow drive sustained PLCgamma1 signaling during T cell activation
    • Babich A, Li S, O'Connor RS, Milone MC, Freedman BD, Burkhardt JK. F-actin polymerization and retrograde flow drive sustained PLCgamma1 signaling during T cell activation. J Cell Biol 2012;197:775-787.
    • (2012) J Cell Biol , vol.197 , pp. 775-787
    • Babich, A.1    Li, S.2    O'Connor, R.S.3    Milone, M.C.4    Freedman, B.D.5    Burkhardt, J.K.6
  • 4
    • 84876247534 scopus 로고    scopus 로고
    • Actin engine in immunological synapse
    • Piragyte I, Jun CD. Actin engine in immunological synapse. Immune Netw 2012;12:71-83.
    • (2012) Immune Netw , vol.12 , pp. 71-83
    • Piragyte, I.1    Jun, C.D.2
  • 5
    • 0037244777 scopus 로고    scopus 로고
    • Actin cytoskeletal dynamics in T lymphocyte activation and migration
    • Samstag Y, Eibert SM, Klemke M, Wabnitz GH. Actin cytoskeletal dynamics in T lymphocyte activation and migration. J Leukoc Biol 2003;73:30-48.
    • (2003) J Leukoc Biol , vol.73 , pp. 30-48
    • Samstag, Y.1    Eibert, S.M.2    Klemke, M.3    Wabnitz, G.H.4
  • 6
    • 0022453434 scopus 로고
    • Nucleotide exchange between cytosolic ATP and F-actin-bound ADP may be a major energy-utilizing process in unstimulated platelets
    • Daniel JL, Molish IR, Robkin L, Holmsen H. Nucleotide exchange between cytosolic ATP and F-actin-bound ADP may be a major energy-utilizing process in unstimulated platelets. Eur J Biochem 1986;156:677-684.
    • (1986) Eur J Biochem , vol.156 , pp. 677-684
    • Daniel, J.L.1    Molish, I.R.2    Robkin, L.3    Holmsen, H.4
  • 7
    • 0037220750 scopus 로고    scopus 로고
    • Actin-ATP hydrolysis is a major energy drain for neurons
    • Bernstein BW, Bamburg JR. Actin-ATP hydrolysis is a major energy drain for neurons. J Neurosci 2003;23:1-6.
    • (2003) J Neurosci , vol.23 , pp. 1-6
    • Bernstein, B.W.1    Bamburg, J.R.2
  • 8
    • 77649153819 scopus 로고    scopus 로고
    • WASP: a key immunological multitasker
    • Thrasher AJ, Burns SO. WASP: a key immunological multitasker. Nat Rev Immunol 2010;10:182-192.
    • (2010) Nat Rev Immunol , vol.10 , pp. 182-192
    • Thrasher, A.J.1    Burns, S.O.2
  • 9
    • 0035090317 scopus 로고    scopus 로고
    • Activation of Arp2/3 complex-mediated actin polymerization by cortactin
    • Uruno T, et al. Activation of Arp2/3 complex-mediated actin polymerization by cortactin. Nat Cell Biol 2001;3:259-266.
    • (2001) Nat Cell Biol , vol.3 , pp. 259-266
    • Uruno, T.1
  • 10
    • 33744981370 scopus 로고    scopus 로고
    • HS1 functions as an essential actin-regulatory adaptor protein at the immune synapse
    • Gomez TS, et al. HS1 functions as an essential actin-regulatory adaptor protein at the immune synapse. Immunity 2006;24:741-752.
    • (2006) Immunity , vol.24 , pp. 741-752
    • Gomez, T.S.1
  • 11
    • 73349137004 scopus 로고    scopus 로고
    • Hematopoietic lineage cell-specific protein 1 is recruited to the immunological synapse by IL-2-inducible T cell kinase and regulates phospholipase Cgamma1 Microcluster dynamics during T cell spreading
    • Carrizosa E, et al. Hematopoietic lineage cell-specific protein 1 is recruited to the immunological synapse by IL-2-inducible T cell kinase and regulates phospholipase Cgamma1 Microcluster dynamics during T cell spreading. J Immunol 2009;183:7352-7361.
    • (2009) J Immunol , vol.183 , pp. 7352-7361
    • Carrizosa, E.1
  • 12
    • 78650637719 scopus 로고    scopus 로고
    • The Wiskott-Aldrich syndrome: the actin cytoskeleton and immune cell function
    • Blundell MP, Worth A, Bouma G, Thrasher AJ. The Wiskott-Aldrich syndrome: the actin cytoskeleton and immune cell function. Dis Markers 2010;29:157-175.
    • (2010) Dis Markers , vol.29 , pp. 157-175
    • Blundell, M.P.1    Worth, A.2    Bouma, G.3    Thrasher, A.J.4
  • 13
    • 34548259213 scopus 로고    scopus 로고
    • WAVE2 regulates high-affinity integrin binding by recruiting vinculin and talin to the immunological synapse
    • Nolz JC, et al. WAVE2 regulates high-affinity integrin binding by recruiting vinculin and talin to the immunological synapse. Mol Cell Biol 2007;27:5986-6000.
    • (2007) Mol Cell Biol , vol.27 , pp. 5986-6000
    • Nolz, J.C.1
  • 14
    • 30044446991 scopus 로고    scopus 로고
    • The WAVE2 complex regulates actin cytoskeletal reorganization and CRAC-mediated calcium entry during T cell activation
    • Nolz JC, et al. The WAVE2 complex regulates actin cytoskeletal reorganization and CRAC-mediated calcium entry during T cell activation. Curr Biol 2006;16:24-34.
    • (2006) Curr Biol , vol.16 , pp. 24-34
    • Nolz, J.C.1
  • 15
    • 0030006284 scopus 로고    scopus 로고
    • Wiskott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization
    • Symons M, et al. Wiskott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization. Cell 1996;84:723-734.
    • (1996) Cell , vol.84 , pp. 723-734
    • Symons, M.1
  • 16
    • 0032118427 scopus 로고    scopus 로고
    • Wiskott-Aldrich syndrome protein-deficient mice reveal a role for WASP in T but not B cell activation
    • Snapper SB, et al. Wiskott-Aldrich syndrome protein-deficient mice reveal a role for WASP in T but not B cell activation. Immunity 1998;9:81-91.
    • (1998) Immunity , vol.9 , pp. 81-91
    • Snapper, S.B.1
  • 17
    • 33749533257 scopus 로고    scopus 로고
    • Regulation of cytoskeletal dynamics at the immune synapse: new stars join the actin troupe
    • Billadeau DD, Burkhardt JK. Regulation of cytoskeletal dynamics at the immune synapse: new stars join the actin troupe. Traffic 2006;7:1451-1460.
    • (2006) Traffic , vol.7 , pp. 1451-1460
    • Billadeau, D.D.1    Burkhardt, J.K.2
  • 18
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • Pollard TD, Borisy GG. Cellular motility driven by assembly and disassembly of actin filaments. Cell 2003;112:453-465.
    • (2003) Cell , vol.112 , pp. 453-465
    • Pollard, T.D.1    Borisy, G.G.2
  • 19
    • 34147144013 scopus 로고    scopus 로고
    • Costimulation induced phosphorylation of L-plastin facilitates surface transport of the T cell activation molecules CD69 and CD25
    • Wabnitz GH, et al. Costimulation induced phosphorylation of L-plastin facilitates surface transport of the T cell activation molecules CD69 and CD25. Eur J Immunol 2007;37:649-662.
    • (2007) Eur J Immunol , vol.37 , pp. 649-662
    • Wabnitz, G.H.1
  • 20
    • 77956486432 scopus 로고    scopus 로고
    • Sustained LFA-1 cluster formation in the immune synapse requires the combined activities of L-plastin and calmodulin
    • Wabnitz GH, et al. Sustained LFA-1 cluster formation in the immune synapse requires the combined activities of L-plastin and calmodulin. Eur J Immunol 2010;40:2437-2449.
    • (2010) Eur J Immunol , vol.40 , pp. 2437-2449
    • Wabnitz, G.H.1
  • 21
    • 80054956266 scopus 로고    scopus 로고
    • L-plastin phosphorylation: a novel target for the immunosuppressive drug dexamethasone in primary human T cells
    • Wabnitz GH, et al. L-plastin phosphorylation: a novel target for the immunosuppressive drug dexamethasone in primary human T cells. Eur J Immunol 2011;41:3157-3169.
    • (2011) Eur J Immunol , vol.41 , pp. 3157-3169
    • Wabnitz, G.H.1
  • 22
    • 0027309439 scopus 로고
    • Purification and further characterization of macrophage 70-kDa protein, a calcium-regulated, actin-binding protein identical to L-plastin
    • Pacaud M, Derancourt J. Purification and further characterization of macrophage 70-kDa protein, a calcium-regulated, actin-binding protein identical to L-plastin. Biochemistry 1993;32:3448-3455.
    • (1993) Biochemistry , vol.32 , pp. 3448-3455
    • Pacaud, M.1    Derancourt, J.2
  • 23
    • 0026468443 scopus 로고
    • Human T cell L-plastin bundles actin filaments in a calcium-dependent manner
    • Namba Y, Ito M, Zu Y, Shigesada K, Maruyama K. Human T cell L-plastin bundles actin filaments in a calcium-dependent manner. J Biochem 1992;112:503-507.
    • (1992) J Biochem , vol.112 , pp. 503-507
    • Namba, Y.1    Ito, M.2    Zu, Y.3    Shigesada, K.4    Maruyama, K.5
  • 24
    • 0023689934 scopus 로고
    • Molecular cloning and characterization of plastin, a human leukocyte protein expressed in transformed human fibroblasts
    • Lin CS, Aebersold RH, Kent SB, Varma M, Leavitt J. Molecular cloning and characterization of plastin, a human leukocyte protein expressed in transformed human fibroblasts. Mol Cell Biol 1988;8:4659-4668.
    • (1988) Mol Cell Biol , vol.8 , pp. 4659-4668
    • Lin, C.S.1    Aebersold, R.H.2    Kent, S.B.3    Varma, M.4    Leavitt, J.5
  • 25
    • 0027454485 scopus 로고
    • Mapping of the alpha-actinin binding site within the beta 1 integrin cytoplasmic domain
    • Otey CA, Vasquez GB, Burridge K, Erickson BW. Mapping of the alpha-actinin binding site within the beta 1 integrin cytoplasmic domain. J Biol Chem 1993;268:21193-21197.
    • (1993) J Biol Chem , vol.268 , pp. 21193-21197
    • Otey, C.A.1    Vasquez, G.B.2    Burridge, K.3    Erickson, B.W.4
  • 26
    • 84863632247 scopus 로고    scopus 로고
    • EWI-2 association with alpha-actinin regulates T cell immune synapses and HIV viral infection
    • Gordon-Alonso M, et al. EWI-2 association with alpha-actinin regulates T cell immune synapses and HIV viral infection. J Immunol 2012;189:689-700.
    • (2012) J Immunol , vol.189 , pp. 689-700
    • Gordon-Alonso, M.1
  • 27
    • 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. Intermediate-affinity LFA-1 binds alpha-actinin-1 to control migration at the leading edge of the T cell. EMBO J 2008;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
  • 28
    • 0033280237 scopus 로고    scopus 로고
    • Proteins of the ADF/cofilin family: essential regulators of actin dynamics
    • Bamburg JR. Proteins of the ADF/cofilin family: essential regulators of actin dynamics. Annu Rev Cell Dev Biol 1999;15:185-230.
    • (1999) Annu Rev Cell Dev Biol , vol.15 , pp. 185-230
    • Bamburg, J.R.1
  • 29
    • 0027494863 scopus 로고
    • Analysis of the interactions of actin depolymerizing factor with G- and F-actin
    • Hayden SM, Miller PS, Brauweiler A, Bamburg JR. Analysis of the interactions of actin depolymerizing factor with G- and F-actin. Biochemistry 1993;32:9994-10004.
    • (1993) Biochemistry , vol.32 , pp. 9994-10004
    • Hayden, S.M.1    Miller, P.S.2    Brauweiler, A.3    Bamburg, J.R.4
  • 30
    • 84876041581 scopus 로고    scopus 로고
    • Biophysics of actin filament severing by cofilin
    • Elam WA, Kang H, De La Cruz EM. Biophysics of actin filament severing by cofilin. FEBS Lett 2013;587:1215-1219.
    • (2013) FEBS Lett , vol.587 , pp. 1215-1219
    • Elam, W.A.1    Kang, H.2    De La Cruz, E.M.3
  • 31
    • 33746189734 scopus 로고    scopus 로고
    • Energetics and kinetics of cooperative cofilin-actin filament interactions
    • Cao W, Goodarzi JP, De La Cruz EM. Energetics and kinetics of cooperative cofilin-actin filament interactions. J Mol Biol 2006;361:257-267.
    • (2006) J Mol Biol , vol.361 , pp. 257-267
    • Cao, W.1    Goodarzi, J.P.2    De La Cruz, E.M.3
  • 32
    • 0022403777 scopus 로고
    • pH control of actin polymerization by cofilin
    • Yonezawa N, Nishida E, Sakai H. pH control of actin polymerization by cofilin. J Biol Chem 1985;260:14410-14412.
    • (1985) J Biol Chem , vol.260 , pp. 14410-14412
    • Yonezawa, N.1    Nishida, E.2    Sakai, H.3
  • 33
    • 0029149885 scopus 로고
    • Reactivation of phosphorylated actin depolymerizing factor and identification of the regulatory site
    • Agnew BJ, Minamide LS, Bamburg JR. Reactivation of phosphorylated actin depolymerizing factor and identification of the regulatory site. J Biol Chem 1995;270:17582-17587.
    • (1995) J Biol Chem , vol.270 , pp. 17582-17587
    • Agnew, B.J.1    Minamide, L.S.2    Bamburg, J.R.3
  • 34
    • 0029678546 scopus 로고    scopus 로고
    • Phosphorylation of Ser-3 of cofilin regulates its essential function on actin
    • Moriyama K, Iida K, Yahara I. Phosphorylation of Ser-3 of cofilin regulates its essential function on actin. Genes Cells 1996;1:73-86.
    • (1996) Genes Cells , vol.1 , pp. 73-86
    • Moriyama, K.1    Iida, K.2    Yahara, I.3
  • 35
    • 0029859963 scopus 로고    scopus 로고
    • Dephosphorylation of serine-3 regulates nuclear translocation of cofilin
    • Nebl G, Meuer SC, Samstag Y. Dephosphorylation of serine-3 regulates nuclear translocation of cofilin. J Biol Chem 1996;271:26276-26280.
    • (1996) J Biol Chem , vol.271 , pp. 26276-26280
    • Nebl, G.1    Meuer, S.C.2    Samstag, Y.3
  • 36
    • 0034645797 scopus 로고    scopus 로고
    • Phosphorylation of Acanthamoeba actophorin (ADF/cofilin) blocks interaction with actin without a change in atomic structure
    • Blanchoin L, Robinson RC, Choe S, Pollard TD. Phosphorylation of Acanthamoeba actophorin (ADF/cofilin) blocks interaction with actin without a change in atomic structure. J Mol Biol 2000;295:203-211.
    • (2000) J Mol Biol , vol.295 , pp. 203-211
    • Blanchoin, L.1    Robinson, R.C.2    Choe, S.3    Pollard, T.D.4
  • 38
    • 0035399959 scopus 로고    scopus 로고
    • How is actin polymerization nucleated in vivo?
    • Condeelis J. How is actin polymerization nucleated in vivo? Trends Cell Biol 2001;11:288-293.
    • (2001) Trends Cell Biol , vol.11 , pp. 288-293
    • Condeelis, J.1
  • 39
    • 79959729826 scopus 로고    scopus 로고
    • A temporal model of cofilin regulation and the early peak of actin barbed ends in invasive tumor cells
    • Tania N, Prosk E, Condeelis J, Edelstein-Keshet L. A temporal model of cofilin regulation and the early peak of actin barbed ends in invasive tumor cells. Biophys J 2011;100:1883-1892.
    • (2011) Biophys J , vol.100 , pp. 1883-1892
    • Tania, N.1    Prosk, E.2    Condeelis, J.3    Edelstein-Keshet, L.4
  • 40
    • 65249141705 scopus 로고    scopus 로고
    • A common cofilin activity cycle in invasive tumor cells and inflammatory cells
    • van Rheenen J, Condeelis J, Glogauer M. A common cofilin activity cycle in invasive tumor cells and inflammatory cells. J Cell Sci 2009;122:305-311.
    • (2009) J Cell Sci , vol.122 , pp. 305-311
    • van Rheenen, J.1    Condeelis, J.2    Glogauer, M.3
  • 41
    • 71749095987 scopus 로고    scopus 로고
    • The cofilin activity cycle in lamellipodia and invadopodia
    • Oser M, Condeelis J. The cofilin activity cycle in lamellipodia and invadopodia. J Cell Biochem 2009;108:1252-1262.
    • (2009) J Cell Biochem , vol.108 , pp. 1252-1262
    • Oser, M.1    Condeelis, J.2
  • 42
    • 11844276055 scopus 로고    scopus 로고
    • The actin depolymerizing factor n-cofilin is essential for neural tube morphogenesis and neural crest cell migration
    • Gurniak CB, Perlas E, Witke W. The actin depolymerizing factor n-cofilin is essential for neural tube morphogenesis and neural crest cell migration. Dev Biol 2005;278:231-241.
    • (2005) Dev Biol , vol.278 , pp. 231-241
    • Gurniak, C.B.1    Perlas, E.2    Witke, W.3
  • 43
    • 0027446345 scopus 로고
    • Cofilin is an essential component of the yeast cortical cytoskeleton
    • Moon AL, Janmey PA, Louie KA, Drubin DG. Cofilin is an essential component of the yeast cortical cytoskeleton. J Cell Biol 1993;120:421-435.
    • (1993) J Cell Biol , vol.120 , pp. 421-435
    • Moon, A.L.1    Janmey, P.A.2    Louie, K.A.3    Drubin, D.G.4
  • 44
    • 0025339511 scopus 로고
    • A cell culture model for T lymphocyte clonal anergy
    • Schwartz RH. A cell culture model for T lymphocyte clonal anergy. Eur J Immunol 1990;248:1349-1356.
    • (1990) Eur J Immunol , vol.248 , pp. 1349-1356
    • Schwartz, R.H.1
  • 45
    • 0024327899 scopus 로고
    • Clonal expansion versus functional clonal inactivation: a costimulatory signalling pathway determines the outcome of T cell antigen receptor occupancy
    • Mueller DL, Jenkins MK, Schwartz RH. Clonal expansion versus functional clonal inactivation: a costimulatory signalling pathway determines the outcome of T cell antigen receptor occupancy. Annu Rev Immunol 1989;7:445-480.
    • (1989) Annu Rev Immunol , vol.7 , pp. 445-480
    • Mueller, D.L.1    Jenkins, M.K.2    Schwartz, R.H.3
  • 46
  • 47
    • 0025823771 scopus 로고
    • A serine phosphatase is involved in CD2-mediated activation of human T lymphocytes and natural killer cells
    • Samstag Y, Bader A, Meuer SC. A serine phosphatase is involved in CD2-mediated activation of human T lymphocytes and natural killer cells. J Immunol 1991;147:788-794.
    • (1991) J Immunol , vol.147 , pp. 788-794
    • Samstag, Y.1    Bader, A.2    Meuer, S.C.3
  • 48
    • 0021140557 scopus 로고
    • Alternative pathway of T cell activation: a functional role for the 50kD T11 sheep erythrocyte receptor protein
    • Meuer SC, et al. Alternative pathway of T cell activation: a functional role for the 50kD T11 sheep erythrocyte receptor protein. Cell 1984;36:897-906.
    • (1984) Cell , vol.36 , pp. 897-906
    • Meuer, S.C.1
  • 49
    • 0023120574 scopus 로고
    • Meyer zum Büschenfelde K-H, Meuer SC. Alternative pathway activation of T cells by binding of CD2 to its cell-surface ligand
    • Hünig T, Tiefenthaler G. Meyer zum Büschenfelde K-H, Meuer SC. Alternative pathway activation of T cells by binding of CD2 to its cell-surface ligand. Nature 1987;326:298-301.
    • (1987) Nature , vol.326 , pp. 298-301
    • Hünig, T.1    Tiefenthaler, G.2
  • 50
    • 0034004460 scopus 로고    scopus 로고
    • Cofilin: a missing link between T cell costimulation and rearrangement of the actin cytoskeleton
    • Lee KH, Meuer SC, Samstag Y. Cofilin: a missing link between T cell costimulation and rearrangement of the actin cytoskeleton. Eur J Immunol 2000;30:892-899.
    • (2000) Eur J Immunol , vol.30 , pp. 892-899
    • Lee, K.H.1    Meuer, S.C.2    Samstag, Y.3
  • 51
    • 31144470414 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase functions as a Ras effector in the signaling cascade that regulates dephosphorylation of the actin-remodeling protein cofilin after costimulation of untransformed human T lymphocytes
    • Wabnitz GH, Nebl G, Klemke M, Schroder AJ, Samstag Y. Phosphatidylinositol 3-kinase functions as a Ras effector in the signaling cascade that regulates dephosphorylation of the actin-remodeling protein cofilin after costimulation of untransformed human T lymphocytes. J Immunol 2006;176:1668-1674.
    • (2006) J Immunol , vol.176 , pp. 1668-1674
    • Wabnitz, G.H.1    Nebl, G.2    Klemke, M.3    Schroder, A.J.4    Samstag, Y.5
  • 52
    • 35348917602 scopus 로고    scopus 로고
    • Ras/PI3kinase/cofilin-independent activation of human CD45RA+ and CD45RO+ T cells by superagonistic CD28 stimulation
    • Sester U, Wabnitz GH, Kirchgessner H, Samstag Y. Ras/PI3kinase/cofilin-independent activation of human CD45RA+ and CD45RO+ T cells by superagonistic CD28 stimulation. Eur J Immunol 2007;37:2881-2891.
    • (2007) Eur J Immunol , vol.37 , pp. 2881-2891
    • Sester, U.1    Wabnitz, G.H.2    Kirchgessner, H.3    Samstag, Y.4
  • 53
    • 1242341975 scopus 로고    scopus 로고
    • Cofilin peptide homologs interfere with immunological synapse formation and T cell activation
    • Eibert SM, et al. Cofilin peptide homologs interfere with immunological synapse formation and T cell activation. Proc Natl Acad Sci USA 2004;101:1957-1962.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 1957-1962
    • Eibert, S.M.1
  • 54
    • 0031034123 scopus 로고    scopus 로고
    • CD28-mediated induction of proliferation in resting T cells in vitro and in vivo without engagement of the T cell receptor: evidence for functionally distinct forms of CD28
    • Tacke M, Hanke G, Hanke T, Hunig T. CD28-mediated induction of proliferation in resting T cells in vitro and in vivo without engagement of the T cell receptor: evidence for functionally distinct forms of CD28. Eur J Immunol 1997;27:239-247.
    • (1997) Eur J Immunol , vol.27 , pp. 239-247
    • Tacke, M.1    Hanke, G.2    Hanke, T.3    Hunig, T.4
  • 55
    • 0028351807 scopus 로고
    • Serine phosphorylation of a 67 kDa protein in human T lymphocytes represents an accessory receptor mediated signalling event
    • Henning SW, Meuer SC, Samstag Y. Serine phosphorylation of a 67 kDa protein in human T lymphocytes represents an accessory receptor mediated signalling event. J Immunol 1994;152:4808-4815.
    • (1994) J Immunol , vol.152 , pp. 4808-4815
    • Henning, S.W.1    Meuer, S.C.2    Samstag, Y.3
  • 56
    • 0033538574 scopus 로고    scopus 로고
    • The immunological synapse: a molecular machine controlling T cell activation
    • Grakoui A, et al. The immunological synapse: a molecular machine controlling T cell activation. Science 1999;285:221-227.
    • (1999) Science , vol.285 , pp. 221-227
    • Grakoui, A.1
  • 57
    • 27544441784 scopus 로고    scopus 로고
    • Actin and agonist MHC-peptide complex-dependent T cell receptor microclusters as scaffolds for signaling
    • Campi G, Varma R, Dustin ML. Actin and agonist MHC-peptide complex-dependent T cell receptor microclusters as scaffolds for signaling. J Exp Med 2005;202:1031-1036.
    • (2005) J Exp Med , vol.202 , pp. 1031-1036
    • Campi, G.1    Varma, R.2    Dustin, M.L.3
  • 58
    • 30044441433 scopus 로고    scopus 로고
    • Newly generated T cell receptor microclusters initiate and sustain T cell activation by recruitment of Zap70 and SLP-76
    • Yokosuka T, et al. Newly generated T cell receptor microclusters initiate and sustain T cell activation by recruitment of Zap70 and SLP-76. Nat Immunol 2005;6:1253-1262.
    • (2005) Nat Immunol , vol.6 , pp. 1253-1262
    • Yokosuka, T.1
  • 59
    • 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 XS, Crites T, Hammer JA 3rd. Actin retrograde flow and actomyosin II arc contraction drive receptor cluster dynamics at the immunological synapse in Jurkat T cells. Mol Biol Cell 2012;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
  • 60
    • 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. Mechanisms for segregating T cell receptor and adhesion molecules during immunological synapse formation in Jurkat T cells. Proc Natl Acad Sci USA 2007;104:20296-20301.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 20296-20301
    • Kaizuka, Y.1    Douglass, A.D.2    Varma, R.3    Dustin, M.L.4    Vale, R.D.5
  • 61
    • 80053130680 scopus 로고    scopus 로고
    • New insights into the T cell synapse from single molecule techniques
    • Dustin ML, Depoil D. New insights into the T cell synapse from single molecule techniques. Nat Rev Immunol 2011;11:672-684.
    • (2011) Nat Rev Immunol , vol.11 , pp. 672-684
    • Dustin, M.L.1    Depoil, D.2
  • 62
    • 0032545218 scopus 로고    scopus 로고
    • A receptor/cytoskeletal movement triggered by costimulation during T cell activation
    • Wülfing C, Davis MM. A receptor/cytoskeletal movement triggered by costimulation during T cell activation. Science 1998;282:2266-2269.
    • (1998) Science , vol.282 , pp. 2266-2269
    • Wülfing, C.1    Davis, M.M.2
  • 63
    • 0042931251 scopus 로고    scopus 로고
    • Regulation of sustained actin dynamics by the TCR and costimulation as a mechanism of receptor localization
    • Tskvitaria-Fuller I, Rozelle AL, Yin HL, Wülfing C. Regulation of sustained actin dynamics by the TCR and costimulation as a mechanism of receptor localization. J Immunol 2003;171:2287-2295.
    • (2003) J Immunol , vol.171 , pp. 2287-2295
    • Tskvitaria-Fuller, I.1    Rozelle, A.L.2    Yin, H.L.3    Wülfing, C.4
  • 64
    • 0034232037 scopus 로고    scopus 로고
    • The immunological synapse and the actin cytoskeleton: molecular hardware for T cell signaling
    • Dustin ML, Cooper JA. The immunological synapse and the actin cytoskeleton: molecular hardware for T cell signaling. Nat Immunol 2000;1:23-29.
    • (2000) Nat Immunol , vol.1 , pp. 23-29
    • Dustin, M.L.1    Cooper, J.A.2
  • 65
    • 0033614036 scopus 로고    scopus 로고
    • Costimulation: building an immunological synapse
    • Dustin ML, Shaw AS. Costimulation: building an immunological synapse. Science 1999;283:649-650.
    • (1999) Science , vol.283 , pp. 649-650
    • Dustin, M.L.1    Shaw, A.S.2
  • 66
    • 34249013684 scopus 로고    scopus 로고
    • Opposing effects of PKCtheta and WASp on symmetry breaking and relocation of the immunological synapse
    • Sims TN, et al. Opposing effects of PKCtheta and WASp on symmetry breaking and relocation of the immunological synapse. Cell 2007;129:773-785.
    • (2007) Cell , vol.129 , pp. 773-785
    • Sims, T.N.1
  • 67
    • 0023387681 scopus 로고
    • Cofilin is a component of intranuclear and cytoplasmic actin rods induced in cultured cells
    • Nishida E, Iida K, Yonezawa N, Koyasu S, Yahara I, Sakai H. Cofilin is a component of intranuclear and cytoplasmic actin rods induced in cultured cells. Proc Natl Acad Sci USA 1987;84:5262-5266.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 5262-5266
    • Nishida, E.1    Iida, K.2    Yonezawa, N.3    Koyasu, S.4    Yahara, I.5    Sakai, H.6
  • 69
    • 0026550804 scopus 로고
    • The KKRKK sequence is involved in heat shock-induced nuclear translocation of the 18-kDa actin-binding protein, cofilin
    • Iida K, Matsumoto S, Yahara I. The KKRKK sequence is involved in heat shock-induced nuclear translocation of the 18-kDa actin-binding protein, cofilin. Cell Struct Funct 1992;17:39-46.
    • (1992) Cell Struct Funct , vol.17 , pp. 39-46
    • Iida, K.1    Matsumoto, S.2    Yahara, I.3
  • 70
    • 0037515668 scopus 로고    scopus 로고
    • Latrunculin B or ATP depletion induces cofilin-dependent translocation of actin into nuclei of mast cells
    • Pendleton A, Pope B, Weeds A, Koffer A. Latrunculin B or ATP depletion induces cofilin-dependent translocation of actin into nuclei of mast cells. J Biol Chem 2003;278:14394-14400.
    • (2003) J Biol Chem , vol.278 , pp. 14394-14400
    • Pendleton, A.1    Pope, B.2    Weeds, A.3    Koffer, A.4
  • 71
    • 0030004208 scopus 로고    scopus 로고
    • Inhibition of constitutive serine phosphatase activity in T lymphoma cells results in phosphorylation of pp 19/cofilin and induces apoptosis
    • Samstag Y, Dreizler EM, Ambach A, Sczakiel G, Meuer SC. Inhibition of constitutive serine phosphatase activity in T lymphoma cells results in phosphorylation of pp 19/cofilin and induces apoptosis. J Immunol 1996;156:4167-4173.
    • (1996) J Immunol , vol.156 , pp. 4167-4173
    • Samstag, Y.1    Dreizler, E.M.2    Ambach, A.3    Sczakiel, G.4    Meuer, S.C.5
  • 72
    • 0018038933 scopus 로고
    • Selective assay of monomeric and filamentous actin in cell extracts, using inhibition of desoxyribonuclease I
    • Blikstad I, Markey F, Carlsson L, Persson T, Lindberg U. Selective assay of monomeric and filamentous actin in cell extracts, using inhibition of desoxyribonuclease I. Cell 1978;15:935-943.
    • (1978) Cell , vol.15 , pp. 935-943
    • Blikstad, I.1    Markey, F.2    Carlsson, L.3    Persson, T.4    Lindberg, U.5
  • 73
    • 79954769472 scopus 로고    scopus 로고
    • Engineering a waste management enzyme to overcome cancer resistance to apoptosis: adding DNase1 to the anti-cancer toolbox
    • Rosner K, et al. Engineering a waste management enzyme to overcome cancer resistance to apoptosis: adding DNase1 to the anti-cancer toolbox. Cancer Gene Ther 2011;18:346-357.
    • (2011) Cancer Gene Ther , vol.18 , pp. 346-357
    • Rosner, K.1
  • 74
    • 0027458695 scopus 로고
    • Characterization of the endogenous deoxyribonuclease involved in nuclear DNA degradation during apoptosis (programmed cell death)
    • Peitsch MC, et al. Characterization of the endogenous deoxyribonuclease involved in nuclear DNA degradation during apoptosis (programmed cell death). EMBO J 1993;12:371-377.
    • (1993) EMBO J , vol.12 , pp. 371-377
    • Peitsch, M.C.1
  • 75
    • 0018595534 scopus 로고
    • Intranuclear injection of anti-actin antibodies into Xenopus oocytes blocks chromosome condensation
    • Rungger D, Rungger-Brandle E, Chaponnier C, Gabbiani G. Intranuclear injection of anti-actin antibodies into Xenopus oocytes blocks chromosome condensation. Nature 1979;282:320-321.
    • (1979) Nature , vol.282 , pp. 320-321
    • Rungger, D.1    Rungger-Brandle, E.2    Chaponnier, C.3    Gabbiani, G.4
  • 76
    • 0021677114 scopus 로고
    • Microinjection of actin-binding proteins and actin antibodies demonstrates involvement of nuclear actin in transcription of lampbrush chromosomes
    • Scheer U, Hinssen H, Franke WW, Jockusch B. Microinjection of actin-binding proteins and actin antibodies demonstrates involvement of nuclear actin in transcription of lampbrush chromosomes. Cell 1984;39:111-122.
    • (1984) Cell , vol.39 , pp. 111-122
    • Scheer, U.1    Hinssen, H.2    Franke, W.W.3    Jockusch, B.4
  • 78
    • 7944239067 scopus 로고    scopus 로고
    • Actin is part of pre-initiation complexes and is necessary for transcription by RNA polymerase II
    • Hofmann WA, et al. Actin is part of pre-initiation complexes and is necessary for transcription by RNA polymerase II. Nat Cell Biol 2004;6:1094-1101.
    • (2004) Nat Cell Biol , vol.6 , pp. 1094-1101
    • Hofmann, W.A.1
  • 79
    • 79952637148 scopus 로고    scopus 로고
    • The F-actin severing protein cofilin-1 is required for RNA polymerase II transcription elongation
    • Obrdlik A, Percipalle P. The F-actin severing protein cofilin-1 is required for RNA polymerase II transcription elongation. Nucleus 2011;2:72-79.
    • (2011) Nucleus , vol.2 , pp. 72-79
    • Obrdlik, A.1    Percipalle, P.2
  • 80
    • 0029777285 scopus 로고    scopus 로고
    • Multiple p21ras effector pathways regulate nuclear factor of activated T cells
    • Genot E, Cleverley S, Henning S, Cantrell DA. Multiple p21ras effector pathways regulate nuclear factor of activated T cells. EMBO J 1996;15:3923-3933.
    • (1996) EMBO J , vol.15 , pp. 3923-3933
    • Genot, E.1    Cleverley, S.2    Henning, S.3    Cantrell, D.A.4
  • 81
    • 0034536444 scopus 로고    scopus 로고
    • The serine phosphatases PP1 and PP2A associate with and activate the actin-binding protein cofilin in human T lymphocytes
    • Ambach A, Saunus J, Konstandin M, Wesselborg S, Meuer SC, Samstag Y. The serine phosphatases PP1 and PP2A associate with and activate the actin-binding protein cofilin in human T lymphocytes. Eur J Immunol 2000;30:3422-3431.
    • (2000) Eur J Immunol , vol.30 , pp. 3422-3431
    • Ambach, A.1    Saunus, J.2    Konstandin, M.3    Wesselborg, S.4    Meuer, S.C.5    Samstag, Y.6
  • 82
    • 0037169335 scopus 로고    scopus 로고
    • Control of actin reorganization by Slingshot, a family of phosphatases that dephosphorylate ADF/cofilin
    • Niwa R, Nagata-Ohashi K, Takeichi M, Mizuno K, Uemura T. Control of actin reorganization by Slingshot, a family of phosphatases that dephosphorylate ADF/cofilin. Cell 2002;108:233-246.
    • (2002) Cell , vol.108 , pp. 233-246
    • Niwa, R.1    Nagata-Ohashi, K.2    Takeichi, M.3    Mizuno, K.4    Uemura, T.5
  • 83
    • 12344250639 scopus 로고    scopus 로고
    • Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics
    • Gohla A, Birkenfeld J, Bokoch GM. Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics. Nat Cell Biol 2005;7:21-29.
    • (2005) Nat Cell Biol , vol.7 , pp. 21-29
    • Gohla, A.1    Birkenfeld, J.2    Bokoch, G.M.3
  • 84
    • 84870557707 scopus 로고    scopus 로고
    • Signaling mechanisms and functional roles of cofilin phosphorylation and dephosphorylation
    • Mizuno K. Signaling mechanisms and functional roles of cofilin phosphorylation and dephosphorylation. Cell Signal 2013;25:457-469.
    • (2013) Cell Signal , vol.25 , pp. 457-469
    • Mizuno, K.1
  • 85
    • 84885366083 scopus 로고    scopus 로고
    • A reducing milieu renders cofilin insensitive to phosphatidylinotisol 4,5-bisphosphate inhibition
    • in press
    • Schulte B, et al. A reducing milieu renders cofilin insensitive to phosphatidylinotisol 4, 5-bisphosphate inhibition. J Biol Chem; in press.
    • J Biol Chem
    • Schulte, B.1
  • 86
    • 0025872395 scopus 로고
    • Down-regulation of T cell receptors on self-reactive T cells as a novel mechanism for extrathymic tolerance induction
    • Schönrich G, et al. Down-regulation of T cell receptors on self-reactive T cells as a novel mechanism for extrathymic tolerance induction. Cell 1991;65:293-304.
    • (1991) Cell , vol.65 , pp. 293-304
    • Schönrich, G.1
  • 87
    • 0036862530 scopus 로고    scopus 로고
    • Changes in actin dynamics at the T-cell/APC interface: implications for T-cell anergy?
    • Sechi AS, Buer J, Wehland J, Probst-Kepper M. Changes in actin dynamics at the T-cell/APC interface: implications for T-cell anergy? Immunol Rev 2002;189:98-110.
    • (2002) Immunol Rev , vol.189 , pp. 98-110
    • Sechi, A.S.1    Buer, J.2    Wehland, J.3    Probst-Kepper, M.4
  • 88
    • 71749086535 scopus 로고    scopus 로고
    • Gene related to anergy in lymphocytes (GRAIL) expression in CD4+ T cells impairs actin cytoskeletal organization during T cell/antigen-presenting cell interactions
    • Schartner JM, Simonson WT, Wernimont SA, Nettenstrom LM, Huttenlocher A, Seroogy CM. Gene related to anergy in lymphocytes (GRAIL) expression in CD4+ T cells impairs actin cytoskeletal organization during T cell/antigen-presenting cell interactions. J Biol Chem 2009;284:34674-34681.
    • (2009) J Biol Chem , vol.284 , pp. 34674-34681
    • Schartner, J.M.1    Simonson, W.T.2    Wernimont, S.A.3    Nettenstrom, L.M.4    Huttenlocher, A.5    Seroogy, C.M.6
  • 89
    • 80052885892 scopus 로고    scopus 로고
    • Evidence implicating the Ras pathway in multiple CD28 costimulatory functions in CD4+ T cells
    • Janardhan SV, Praveen K, Marks R, Gajewski TF. Evidence implicating the Ras pathway in multiple CD28 costimulatory functions in CD4+ T cells. PLoS ONE 2011;6:e24931.
    • (2011) PLoS ONE , vol.6
    • Janardhan, S.V.1    Praveen, K.2    Marks, R.3    Gajewski, T.F.4
  • 90
    • 0029991920 scopus 로고    scopus 로고
    • Blocked Ras activation in anergic CD4+ T cells
    • Fields PE, Gajewski TF, Fitch FW. Blocked Ras activation in anergic CD4+ T cells. Science 1996;271:1276-1278.
    • (1996) Science , vol.271 , pp. 1276-1278
    • Fields, P.E.1    Gajewski, T.F.2    Fitch, F.W.3
  • 91
    • 33750093594 scopus 로고    scopus 로고
    • T cell anergy is reversed by active Ras and is regulated by diacylglycerol kinase-alpha
    • Zha Y, et al. T cell anergy is reversed by active Ras and is regulated by diacylglycerol kinase-alpha. Nat Immunol 2006;7:1166-1173.
    • (2006) Nat Immunol , vol.7 , pp. 1166-1173
    • Zha, Y.1
  • 92
    • 77957272682 scopus 로고    scopus 로고
    • Modular design of immunological synapses and kinapses
    • Dustin ML. Modular design of immunological synapses and kinapses. Cold Spring Harb Perspect Biol 2009;1:a002873.
    • (2009) Cold Spring Harb Perspect Biol , vol.1
    • Dustin, M.L.1
  • 93
    • 0034792774 scopus 로고    scopus 로고
    • Amoeboid leukocyte crawling through extracellular matrix: lessons from the Dictyostelium paradigm of cell movement
    • Friedl P, Borgmann S, Brocker EB. Amoeboid leukocyte crawling through extracellular matrix: lessons from the Dictyostelium paradigm of cell movement. J Leukoc Biol 2001;70:491-509.
    • (2001) J Leukoc Biol , vol.70 , pp. 491-509
    • Friedl, P.1    Borgmann, S.2    Brocker, E.B.3
  • 94
    • 0142245603 scopus 로고    scopus 로고
    • Amoeboid shape change and contact guidance: T-lymphocyte crawling through fibrillar collagen is independent of matrix remodeling by MMPs and other proteases
    • Wolf K, Muller R, Borgmann S, Brocker EB, Friedl P. Amoeboid shape change and contact guidance: T-lymphocyte crawling through fibrillar collagen is independent of matrix remodeling by MMPs and other proteases. Blood 2003;102:3262-3269.
    • (2003) Blood , vol.102 , pp. 3262-3269
    • Wolf, K.1    Muller, R.2    Borgmann, S.3    Brocker, E.B.4    Friedl, P.5
  • 95
    • 77957223013 scopus 로고    scopus 로고
    • Mechanisms of force generation and force transmission during interstitial leukocyte migration
    • Renkawitz J, Sixt M. Mechanisms of force generation and force transmission during interstitial leukocyte migration. EMBO Rep 2010;11:744-750.
    • (2010) EMBO Rep , vol.11 , pp. 744-750
    • Renkawitz, J.1    Sixt, M.2
  • 96
    • 0031903617 scopus 로고    scopus 로고
    • CD4+ T lymphocytes migrating in three-dimensional collagen lattices lack focal adhesions and utilize beta1 integrin-independent strategies for polarization, interaction with collagen fibers and locomotion
    • Friedl P, Entschladen F, Conrad C, Niggemann B, Zanker KS. CD4+ T lymphocytes migrating in three-dimensional collagen lattices lack focal adhesions and utilize beta1 integrin-independent strategies for polarization, interaction with collagen fibers and locomotion. Eur J Immunol 1998;28:2331-2343.
    • (1998) Eur J Immunol , vol.28 , pp. 2331-2343
    • Friedl, P.1    Entschladen, F.2    Conrad, C.3    Niggemann, B.4    Zanker, K.S.5
  • 97
    • 0032400495 scopus 로고    scopus 로고
    • Cell migration strategies in 3-D extracellular matrix: differences in morphology, cell matrix interactions, and integrin function
    • Friedl P, Zanker KS, Brocker EB. Cell migration strategies in 3-D extracellular matrix: differences in morphology, cell matrix interactions, and integrin function. Microsc Res Tech 1998;43:369-378.
    • (1998) Microsc Res Tech , vol.43 , pp. 369-378
    • Friedl, P.1    Zanker, K.S.2    Brocker, E.B.3
  • 98
    • 77951597881 scopus 로고    scopus 로고
    • Breaching multiple barriers: leukocyte motility through venular walls and the interstitium
    • Nourshargh S, Hordijk PL, Sixt M. Breaching multiple barriers: leukocyte motility through venular walls and the interstitium. Nat Rev Mol Cell Biol 2010;11:366-378.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 366-378
    • Nourshargh, S.1    Hordijk, P.L.2    Sixt, M.3
  • 99
    • 70349314647 scopus 로고    scopus 로고
    • Mechanical modes of 'amoeboid' cell migration
    • Lammermann T, Sixt M. Mechanical modes of 'amoeboid' cell migration. Curr Opin Cell Biol 2009;21:636-644.
    • (2009) Curr Opin Cell Biol , vol.21 , pp. 636-644
    • Lammermann, T.1    Sixt, M.2
  • 100
    • 79957725789 scopus 로고    scopus 로고
    • Interstitial locomotion of leukocytes
    • Sixt M. Interstitial locomotion of leukocytes. Immunol Lett 2011;138:32-34.
    • (2011) Immunol Lett , vol.138 , pp. 32-34
    • Sixt, M.1
  • 101
    • 77956388103 scopus 로고    scopus 로고
    • An MEK-cofilin signalling module controls migration of human T cells in 3D but not 2D environments
    • Klemke M, Kramer E, Konstandin MH, Wabnitz GH, Samstag Y. An MEK-cofilin signalling module controls migration of human T cells in 3D but not 2D environments. EMBO J 2010;29:2915-2929.
    • (2010) EMBO J , vol.29 , pp. 2915-2929
    • Klemke, M.1    Kramer, E.2    Konstandin, M.H.3    Wabnitz, G.H.4    Samstag, Y.5
  • 102
    • 27544502276 scopus 로고    scopus 로고
    • Spatial and temporal regulation of cofilin activity by LIM kinase and Slingshot is critical for directional cell migration
    • Nishita M, Tomizawa C, Yamamoto M, Horita Y, Ohashi K, Mizuno K. Spatial and temporal regulation of cofilin activity by LIM kinase and Slingshot is critical for directional cell migration. J Cell Biol 2005;171:349-359.
    • (2005) J Cell Biol , vol.171 , pp. 349-359
    • Nishita, M.1    Tomizawa, C.2    Yamamoto, M.3    Horita, Y.4    Ohashi, K.5    Mizuno, K.6
  • 103
    • 0033811659 scopus 로고    scopus 로고
    • Deficiency of PTEN in Jurkat T cells causes constitutive localization of Itk to the plasma membrane and hyperresponsiveness to CD3 stimulation
    • Shan X, et al. Deficiency of PTEN in Jurkat T cells causes constitutive localization of Itk to the plasma membrane and hyperresponsiveness to CD3 stimulation. Mol Cell Biol 2000;20:6945-6957.
    • (2000) Mol Cell Biol , vol.20 , pp. 6945-6957
    • Shan, X.1
  • 104
    • 0033662376 scopus 로고    scopus 로고
    • The CD28 and CTLA-4 receptors associate with the serine/threonine phosphatase PP2A
    • Chuang E, et al. The CD28 and CTLA-4 receptors associate with the serine/threonine phosphatase PP2A. Immunity 2000;13:313-322.
    • (2000) Immunity , vol.13 , pp. 313-322
    • Chuang, E.1
  • 105
    • 51349166966 scopus 로고    scopus 로고
    • Oxidation of cofilin mediates T cell hyporesponsiveness under oxidative stress conditions
    • Klemke M, Wabnitz GH, Funke F, Funk B, Kirchgessner H, Samstag Y. Oxidation of cofilin mediates T cell hyporesponsiveness under oxidative stress conditions. Immunity 2008;29:404-413.
    • (2008) Immunity , vol.29 , pp. 404-413
    • Klemke, M.1    Wabnitz, G.H.2    Funke, F.3    Funk, B.4    Kirchgessner, H.5    Samstag, Y.6
  • 106
    • 33750977562 scopus 로고    scopus 로고
    • Mapping the phosphoinositide-binding site on chick cofilin explains how PIP2 regulates the cofilin-actin interaction
    • Gorbatyuk VY, et al. Mapping the phosphoinositide-binding site on chick cofilin explains how PIP2 regulates the cofilin-actin interaction. Mol Cell 2006;24:511-522.
    • (2006) Mol Cell , vol.24 , pp. 511-522
    • Gorbatyuk, V.Y.1
  • 107
    • 0026044059 scopus 로고
    • A short sequence responsible for both phosphoinositide binding and actin binding activities of cofilin
    • Yonezawa N, Homma Y, Yahara I, Sakai H, Nishida E. A short sequence responsible for both phosphoinositide binding and actin binding activities of cofilin. J Biol Chem 1991;266:17218-17221.
    • (1991) J Biol Chem , vol.266 , pp. 17218-17221
    • Yonezawa, N.1    Homma, Y.2    Yahara, I.3    Sakai, H.4    Nishida, E.5
  • 108
    • 0025277362 scopus 로고
    • Inhibition of the interaction of cofilin, destrin, and deoxyribonuclease I with actin by phosphoinositides
    • Yonezawa N, Nishida E, Iida K, Yahara I, Sakai H. Inhibition of the interaction of cofilin, destrin, and deoxyribonuclease I with actin by phosphoinositides. J Biol Chem 1990;265:8382-8386.
    • (1990) J Biol Chem , vol.265 , pp. 8382-8386
    • Yonezawa, N.1    Nishida, E.2    Iida, K.3    Yahara, I.4    Sakai, H.5
  • 109
    • 0347505003 scopus 로고    scopus 로고
    • CD28-mediated co-stimulation: a quantitative support for TCR signalling
    • Acuto O, Michel F. CD28-mediated co-stimulation: a quantitative support for TCR signalling. Nat Rev Immunol 2003;3:939-951.
    • (2003) Nat Rev Immunol , vol.3 , pp. 939-951
    • Acuto, O.1    Michel, F.2
  • 110
    • 0037564560 scopus 로고    scopus 로고
    • Molecular modifiers of T cell antigen receptor triggering threshold: the mechanism of CD28 costimulatory receptor
    • Acuto O, Mise-Omata S, Mangino G, Michel F. Molecular modifiers of T cell antigen receptor triggering threshold: the mechanism of CD28 costimulatory receptor. Immunol Rev 2003;192:21-31.
    • (2003) Immunol Rev , vol.192 , pp. 21-31
    • Acuto, O.1    Mise-Omata, S.2    Mangino, G.3    Michel, F.4
  • 111
    • 0242322243 scopus 로고    scopus 로고
    • CD28 costimulation: a source of Vav-1 for TCR signaling with the help of SLP-76?
    • Michel F, Acuto O. CD28 costimulation: a source of Vav-1 for TCR signaling with the help of SLP-76? Sci STKE 2002;2002:pe35.
    • (2002) Sci STKE , vol.2002
    • Michel, F.1    Acuto, O.2
  • 112
    • 4444296491 scopus 로고    scopus 로고
    • Phospholipase C and cofilin are required for carcinoma cell directionality in response to EGF stimulation
    • Mouneimne G, et al. Phospholipase C and cofilin are required for carcinoma cell directionality in response to EGF stimulation. J Cell Biol 2004;166:697-708.
    • (2004) J Cell Biol , vol.166 , pp. 697-708
    • Mouneimne, G.1
  • 113
    • 73949099768 scopus 로고    scopus 로고
    • Unbalancing the phosphatidylinositol-4,5-bisphosphate-cofilin interaction impairs cell steering
    • Leyman S, et al. Unbalancing the phosphatidylinositol-4, 5-bisphosphate-cofilin interaction impairs cell steering. Mol Biol Cell 2009;20:4509-4523.
    • (2009) Mol Biol Cell , vol.20 , pp. 4509-4523
    • Leyman, S.1
  • 114
    • 37249000008 scopus 로고    scopus 로고
    • EGF-induced PIP2 hydrolysis releases and activates cofilin locally in carcinoma cells
    • van Rheenen J, et al. EGF-induced PIP2 hydrolysis releases and activates cofilin locally in carcinoma cells. J Cell Biol 2007;179:1247-1259.
    • (2007) J Cell Biol , vol.179 , pp. 1247-1259
    • van Rheenen, J.1
  • 115
    • 77950859278 scopus 로고    scopus 로고
    • ADF/cofilin: a functional node in cell biology
    • Bernstein BW, Bamburg JR. ADF/cofilin: a functional node in cell biology. Trends Cell Biol 2010;20:187-195.
    • (2010) Trends Cell Biol , vol.20 , pp. 187-195
    • Bernstein, B.W.1    Bamburg, J.R.2
  • 116
    • 34249281332 scopus 로고    scopus 로고
    • The cofilin pathway in breast cancer invasion and metastasis
    • Wang W, Eddy R, Condeelis J. The cofilin pathway in breast cancer invasion and metastasis. Nat Rev Cancer 2007;7:429-440.
    • (2007) Nat Rev Cancer , vol.7 , pp. 429-440
    • Wang, W.1    Eddy, R.2    Condeelis, J.3
  • 117
    • 79958725413 scopus 로고    scopus 로고
    • Mitochondrial translocation of oxidized cofilin induces caspase-independent necrotic-like programmed cell death of T cells
    • Wabnitz GH, et al. Mitochondrial translocation of oxidized cofilin induces caspase-independent necrotic-like programmed cell death of T cells. Cell Death Dis 2010;1:e58.
    • (2010) Cell Death Dis , vol.1
    • Wabnitz, G.H.1
  • 118
    • 0025027664 scopus 로고
    • Differential responsiveness to CD3-Ti vs. CD2-dependent activation of human intestinal T lymphocytes
    • Pirzer UC, Schurmann G, Post S, Betzler M, Meuer SC. Differential responsiveness to CD3-Ti vs. CD2-dependent activation of human intestinal T lymphocytes. Eur J Immunol 1990;20:2339-2342.
    • (1990) Eur J Immunol , vol.20 , pp. 2339-2342
    • Pirzer, U.C.1    Schurmann, G.2    Post, S.3    Betzler, M.4    Meuer, S.C.5
  • 119
    • 0029986731 scopus 로고    scopus 로고
    • Differential regulation of human T cell responsiveness by mucosal versus blood monocytes
    • Qiao L, et al. Differential regulation of human T cell responsiveness by mucosal versus blood monocytes. Eur J Immunol 1996;26:922-927.
    • (1996) Eur J Immunol , vol.26 , pp. 922-927
    • Qiao, L.1
  • 120
    • 0025931643 scopus 로고
    • Activation and signaling status of human lamina propria T lymphocytes
    • Qiao L, Schurmann G, Betzler M, Meuer SC. Activation and signaling status of human lamina propria T lymphocytes. Gastroenterology 1991;101:1529-1536.
    • (1991) Gastroenterology , vol.101 , pp. 1529-1536
    • Qiao, L.1    Schurmann, G.2    Betzler, M.3    Meuer, S.C.4
  • 121
    • 0033807770 scopus 로고    scopus 로고
    • Thiol-mediated redox regulation of intestinal lamina propria T lymphocytes
    • Sido B, Braunstein J, Breitkreutz R, Herfarth C, Meuer SC. Thiol-mediated redox regulation of intestinal lamina propria T lymphocytes. J Exp Med 2000;192:907-912.
    • (2000) J Exp Med , vol.192 , pp. 907-912
    • Sido, B.1    Braunstein, J.2    Breitkreutz, R.3    Herfarth, C.4    Meuer, S.C.5
  • 122
    • 0030048536 scopus 로고    scopus 로고
    • Hydrogen peroxide secreted by tumor-derived macrophages down-modulates signal-transducing zeta molecules and inhibits tumor-specific T cell-and natural killer cell-mediated cytotoxicity
    • Kono K, et al. Hydrogen peroxide secreted by tumor-derived macrophages down-modulates signal-transducing zeta molecules and inhibits tumor-specific T cell-and natural killer cell-mediated cytotoxicity. Eur J Immunol 1996;26:1308-1313.
    • (1996) Eur J Immunol , vol.26 , pp. 1308-1313
    • Kono, K.1
  • 123
    • 0029841427 scopus 로고    scopus 로고
    • Oxidative stress by tumor-derived macrophages suppresses the expression of CD3 zeta chain of T-cell receptor complex and antigen-specific T-cell responses
    • Otsuji M, Kimura Y, Aoe T, Okamoto Y, Saito T. Oxidative stress by tumor-derived macrophages suppresses the expression of CD3 zeta chain of T-cell receptor complex and antigen-specific T-cell responses. Proc Natl Acad Sci USA 1996;93:13119-13124.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 13119-13124
    • Otsuji, M.1    Kimura, Y.2    Aoe, T.3    Okamoto, Y.4    Saito, T.5
  • 124
    • 0035874990 scopus 로고    scopus 로고
    • Activated granulocytes and granulocyte-derived hydrogen peroxide are the underlying mechanism of suppression of t-cell function in advanced cancer patients
    • Schmielau J, Finn OJ. Activated granulocytes and granulocyte-derived hydrogen peroxide are the underlying mechanism of suppression of t-cell function in advanced cancer patients. Cancer Res 2001;61:4756-4760.
    • (2001) Cancer Res , vol.61 , pp. 4756-4760
    • Schmielau, J.1    Finn, O.J.2
  • 125
    • 70349651926 scopus 로고    scopus 로고
    • Oxidant-induced apoptosis is mediated by oxidation of the actin-regulatory protein cofilin
    • Klamt F, et al. Oxidant-induced apoptosis is mediated by oxidation of the actin-regulatory protein cofilin. Nat Cell Biol 2009;11:1241-1246.
    • (2009) Nat Cell Biol , vol.11 , pp. 1241-1246
    • Klamt, F.1
  • 126
    • 79960286223 scopus 로고    scopus 로고
    • Signal transduction by reactive oxygen species
    • Finkel T. Signal transduction by reactive oxygen species. J Cell Biol 2011;194:7-15.
    • (2011) J Cell Biol , vol.194 , pp. 7-15
    • Finkel, T.1
  • 127
    • 1042289739 scopus 로고    scopus 로고
    • Solution structure of human cofilin: actin binding, pH sensitivity, and relationship to actin-depolymerizing factor
    • Pope BJ, Zierler-Gould KM, Kuhne R, Weeds AG, Ball LJ. Solution structure of human cofilin: actin binding, pH sensitivity, and relationship to actin-depolymerizing factor. J Biol Chem 2004;279:4840-4848.
    • (2004) J Biol Chem , vol.279 , pp. 4840-4848
    • Pope, B.J.1    Zierler-Gould, K.M.2    Kuhne, R.3    Weeds, A.G.4    Ball, L.J.5
  • 128
    • 0035965994 scopus 로고    scopus 로고
    • Human cofilin forms oligomers exhibiting actin bundling activity
    • Pfannstiel J, et al. Human cofilin forms oligomers exhibiting actin bundling activity. J Biol Chem 2001;276:49476-49484.
    • (2001) J Biol Chem , vol.276 , pp. 49476-49484
    • Pfannstiel, J.1
  • 129
    • 84860657462 scopus 로고    scopus 로고
    • Incorporation of cofilin into rods depends on disulfide intermolecular bonds: implications for actin regulation and neurodegenerative disease
    • Bernstein BW, Shaw AE, Minamide LS, Pak CW, Bamburg JR. Incorporation of cofilin into rods depends on disulfide intermolecular bonds: implications for actin regulation and neurodegenerative disease. J Neurosci 2012;32:6670-6681.
    • (2012) J Neurosci , vol.32 , pp. 6670-6681
    • Bernstein, B.W.1    Shaw, A.E.2    Minamide, L.S.3    Pak, C.W.4    Bamburg, J.R.5
  • 130
    • 18644362802 scopus 로고    scopus 로고
    • Preferential cell death of CD8+ effector memory (CCR7-CD45RA-) T cells by hydrogen peroxide-induced oxidative stress
    • Takahashi A, et al. Preferential cell death of CD8+ effector memory (CCR7-CD45RA-) T cells by hydrogen peroxide-induced oxidative stress. J Immunol 2005;174:6080-6087.
    • (2005) J Immunol , vol.174 , pp. 6080-6087
    • Takahashi, A.1
  • 132
    • 0344668558 scopus 로고    scopus 로고
    • Mitochondrial translocation of cofilin is an early step in apoptosis induction
    • Chua BT, Volbracht C, Tan KO, Li R, Yu VC, Li P. Mitochondrial translocation of cofilin is an early step in apoptosis induction. Nat Cell Biol 2003;5:1083-1089.
    • (2003) Nat Cell Biol , vol.5 , pp. 1083-1089
    • Chua, B.T.1    Volbracht, C.2    Tan, K.O.3    Li, R.4    Yu, V.C.5    Li, P.6
  • 133
    • 0037067724 scopus 로고    scopus 로고
    • Binding to chaperones allows import of a purified mitochondrial precursor into mitochondria
    • Artigues A, Iriarte A, Martinez-Carrion M. Binding to chaperones allows import of a purified mitochondrial precursor into mitochondria. J Biol Chem 2002;277:25047-25055.
    • (2002) J Biol Chem , vol.277 , pp. 25047-25055
    • Artigues, A.1    Iriarte, A.2    Martinez-Carrion, M.3
  • 134
    • 0032509352 scopus 로고    scopus 로고
    • Divergent Hsc70 binding properties of mitochondrial and cytosolic aspartate aminotransferase. Implications for their segregation to different cellular compartments
    • Artigues A, Crawford DL, Iriarte A, Martinez-Carrion M. Divergent Hsc70 binding properties of mitochondrial and cytosolic aspartate aminotransferase. Implications for their segregation to different cellular compartments. J Biol Chem 1998;273:33130-33134.
    • (1998) J Biol Chem , vol.273 , pp. 33130-33134
    • Artigues, A.1    Crawford, D.L.2    Iriarte, A.3    Martinez-Carrion, M.4
  • 135
    • 0038731167 scopus 로고    scopus 로고
    • Caspase-independent cell death in T lymphocytes
    • Jaattela M, Tschopp J. Caspase-independent cell death in T lymphocytes. Nat Immunol 2003;4:416-423.
    • (2003) Nat Immunol , vol.4 , pp. 416-423
    • Jaattela, M.1    Tschopp, J.2
  • 136
    • 83755196121 scopus 로고    scopus 로고
    • Redox remodeling by dendritic cells protects antigen-specific T cells against oxidative stress
    • Martner A, Aurelius J, Rydstrom A, Hellstrand K, Thoren FB. Redox remodeling by dendritic cells protects antigen-specific T cells against oxidative stress. J Immunol 2011;187:6243-6248.
    • (2011) J Immunol , vol.187 , pp. 6243-6248
    • Martner, A.1    Aurelius, J.2    Rydstrom, A.3    Hellstrand, K.4    Thoren, F.B.5
  • 137
    • 0037022345 scopus 로고    scopus 로고
    • Antigen-presenting dendritic cells provide the reducing extracellular microenvironment required for T lymphocyte activation
    • Angelini G, et al. Antigen-presenting dendritic cells provide the reducing extracellular microenvironment required for T lymphocyte activation. Proc Natl Acad Sci USA 2002;99:1491-1496.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 1491-1496
    • Angelini, G.1
  • 138
    • 34250849588 scopus 로고    scopus 로고
    • Cutting edge: antioxidative properties of myeloid dendritic cells: protection of T cells and NK cells from oxygen radical-induced inactivation and apoptosis
    • Thoren FB, Betten A, Romero AI, Hellstrand K. Cutting edge: antioxidative properties of myeloid dendritic cells: protection of T cells and NK cells from oxygen radical-induced inactivation and apoptosis. J Immunol 2007;179:21-25.
    • (2007) J Immunol , vol.179 , pp. 21-25
    • Thoren, F.B.1    Betten, A.2    Romero, A.I.3    Hellstrand, K.4
  • 139
  • 140
    • 65249111020 scopus 로고    scopus 로고
    • Actin dynamics and functions in the interphase nucleus: moving toward an understanding of nuclear polymeric actin
    • Gieni RS, Hendzel MJ. Actin dynamics and functions in the interphase nucleus: moving toward an understanding of nuclear polymeric actin. Biochem Cell Biol 2009;87:283-306.
    • (2009) Biochem Cell Biol , vol.87 , pp. 283-306
    • Gieni, R.S.1    Hendzel, M.J.2
  • 141
    • 0027243449 scopus 로고
    • Cytoplasmic localization and nuclear transport of cofilin in cultured myotubes
    • Abe H, Nagaoka R, Obinata T. Cytoplasmic localization and nuclear transport of cofilin in cultured myotubes. Exp Cell Res 1993;206:1-10.
    • (1993) Exp Cell Res , vol.206 , pp. 1-10
    • Abe, H.1    Nagaoka, R.2    Obinata, T.3
  • 142
    • 33646844623 scopus 로고    scopus 로고
    • Listeria monocytogenes: a multifaceted model
    • Hamon M, Bierne H, Cossart P. Listeria monocytogenes: a multifaceted model. Nat Rev Microbiol 2006;4:423-434.
    • (2006) Nat Rev Microbiol , vol.4 , pp. 423-434
    • Hamon, M.1    Bierne, H.2    Cossart, P.3
  • 143
    • 80051553821 scopus 로고    scopus 로고
    • InlB-mediated Listeria monocytogenes internalization requires a balanced phospholipase D activity maintained through phospho-cofilin
    • Han X, et al. InlB-mediated Listeria monocytogenes internalization requires a balanced phospholipase D activity maintained through phospho-cofilin. Mol Microbiol 2011;81:860-880.
    • (2011) Mol Microbiol , vol.81 , pp. 860-880
    • Han, X.1
  • 144
    • 34948828127 scopus 로고    scopus 로고
    • Direct stimulation of receptor-controlled phospholipase D1 by phospho-cofilin
    • Han L, et al. Direct stimulation of receptor-controlled phospholipase D1 by phospho-cofilin. EMBO J 2007;26:4189-4202.
    • (2007) EMBO J , vol.26 , pp. 4189-4202
    • Han, L.1
  • 145
  • 146
    • 0033533789 scopus 로고    scopus 로고
    • Reconstitution of actin-based motility of Listeria and Shigella using pure proteins
    • Loisel TP, Boujemaa R, Pantaloni D, Carlier MF. Reconstitution of actin-based motility of Listeria and Shigella using pure proteins. Nature 1999;401:613-616.
    • (1999) Nature , vol.401 , pp. 613-616
    • Loisel, T.P.1    Boujemaa, R.2    Pantaloni, D.3    Carlier, M.F.4
  • 147
    • 0031731076 scopus 로고    scopus 로고
    • Identification of cofilin, coronin, Rac and capZ in actin tails using a Listeria affinity approach
    • David V, et al. Identification of cofilin, coronin, Rac and capZ in actin tails using a Listeria affinity approach. J Cell Sci 1998;111(Pt 19):2877-2884.
    • (1998) J Cell Sci , vol.111 , Issue.PART 19 , pp. 2877-2884
    • David, V.1
  • 148
    • 80051554560 scopus 로고    scopus 로고
    • Listeria monocytogenes cell invasion: a new role for cofilin in co-ordinating actin dynamics and membrane lipids
    • Bamburg JR. Listeria monocytogenes cell invasion: a new role for cofilin in co-ordinating actin dynamics and membrane lipids. Mol Microbiol 2011;81:851-854.
    • (2011) Mol Microbiol , vol.81 , pp. 851-854
    • Bamburg, J.R.1
  • 149
    • 50249107532 scopus 로고    scopus 로고
    • HIV envelope-CXCR4 signaling activates cofilin to overcome cortical actin restriction in resting CD4 T cells
    • Yoder A, et al. HIV envelope-CXCR4 signaling activates cofilin to overcome cortical actin restriction in resting CD4 T cells. Cell 2008;134:782-792.
    • (2008) Cell , vol.134 , pp. 782-792
    • Yoder, A.1
  • 150
    • 77950514618 scopus 로고    scopus 로고
    • Lentiviral Nef proteins utilize PAK2-mediated deregulation of cofilin as a general strategy to interfere with actin remodeling
    • Stolp B, Abraham L, Rudolph JM, Fackler OT. Lentiviral Nef proteins utilize PAK2-mediated deregulation of cofilin as a general strategy to interfere with actin remodeling. J Virol 2010;84:3935-3948.
    • (2010) J Virol , vol.84 , pp. 3935-3948
    • Stolp, B.1    Abraham, L.2    Rudolph, J.M.3    Fackler, O.T.4
  • 151
    • 68549123450 scopus 로고    scopus 로고
    • HIV-1 Nef interferes with host cell motility by deregulation of Cofilin
    • Stolp B, et al. HIV-1 Nef interferes with host cell motility by deregulation of Cofilin. Cell Host Microbe 2009;6:174-186.
    • (2009) Cell Host Microbe , vol.6 , pp. 174-186
    • Stolp, B.1
  • 152
    • 33646386905 scopus 로고    scopus 로고
    • The activity status of cofilin is directly related to invasion, intravasation, and metastasis of mammary tumors
    • Wang W, et al. The activity status of cofilin is directly related to invasion, intravasation, and metastasis of mammary tumors. J Cell Biol 2006;173:395-404.
    • (2006) J Cell Biol , vol.173 , pp. 395-404
    • Wang, W.1
  • 153
    • 36348968323 scopus 로고    scopus 로고
    • Cofilin determines the migration behavior and turning frequency of metastatic cancer cells
    • Sidani M, et al. Cofilin determines the migration behavior and turning frequency of metastatic cancer cells. J Cell Biol 2007;179:777-791.
    • (2007) J Cell Biol , vol.179 , pp. 777-791
    • Sidani, M.1
  • 154
    • 33750948427 scopus 로고    scopus 로고
    • Spatial and temporal control of cofilin activity is required for directional sensing during chemotaxis
    • Mouneimne G, et al. Spatial and temporal control of cofilin activity is required for directional sensing during chemotaxis. Curr Biol 2006;16:2193-2205.
    • (2006) Curr Biol , vol.16 , pp. 2193-2205
    • Mouneimne, G.1
  • 155
    • 79955425392 scopus 로고    scopus 로고
    • A novel spatiotemporal RhoC activation pathway locally regulates cofilin activity at invadopodia
    • Bravo-Cordero JJ, Oser M, Chen X, Eddy R, Hodgson L, Condeelis J. A novel spatiotemporal RhoC activation pathway locally regulates cofilin activity at invadopodia. Curr Biol 2011;21:635-644.
    • (2011) Curr Biol , vol.21 , pp. 635-644
    • Bravo-Cordero, J.J.1    Oser, M.2    Chen, X.3    Eddy, R.4    Hodgson, L.5    Condeelis, J.6
  • 156
    • 13444301091 scopus 로고    scopus 로고
    • Molecular mechanisms of invadopodium formation: the role of the N-WASP-Arp2/3 complex pathway and cofilin
    • Yamaguchi H, et al. Molecular mechanisms of invadopodium formation: the role of the N-WASP-Arp2/3 complex pathway and cofilin. J Cell Biol 2005;168:441-452.
    • (2005) J Cell Biol , vol.168 , pp. 441-452
    • Yamaguchi, H.1
  • 157
    • 20144362409 scopus 로고    scopus 로고
    • Arginase I is constitutively expressed in human granulocytes and participates in fungicidal activity
    • Munder M, et al. Arginase I is constitutively expressed in human granulocytes and participates in fungicidal activity. Blood 2005;105:2549-2556.
    • (2005) Blood , vol.105 , pp. 2549-2556
    • Munder, M.1
  • 158
    • 61349100687 scopus 로고    scopus 로고
    • Myeloid-derived suppressor cells as regulators of the immune system
    • Gabrilovich DI, Nagaraj S. Myeloid-derived suppressor cells as regulators of the immune system. Nat Rev Immunol 2009;9:162-174.
    • (2009) Nat Rev Immunol , vol.9 , pp. 162-174
    • Gabrilovich, D.I.1    Nagaraj, S.2
  • 159
    • 77953775808 scopus 로고    scopus 로고
    • Control of immune response by amino acid metabolism
    • Grohmann U, Bronte V. Control of immune response by amino acid metabolism. Immunol Rev 2010;236:243-264.
    • (2010) Immunol Rev , vol.236 , pp. 243-264
    • Grohmann, U.1    Bronte, V.2
  • 160
    • 77954022658 scopus 로고    scopus 로고
    • Arginase is overactive in psoriatic skin
    • Abeyakirthi S, et al. Arginase is overactive in psoriatic skin. Br J Dermatol 2010;163:193-196.
    • (2010) Br J Dermatol , vol.163 , pp. 193-196
    • Abeyakirthi, S.1
  • 161
    • 20244367914 scopus 로고    scopus 로고
    • Arginase-producing myeloid suppressor cells in renal cell carcinoma patients: a mechanism of tumor evasion
    • Zea AH, et al. Arginase-producing myeloid suppressor cells in renal cell carcinoma patients: a mechanism of tumor evasion. Cancer Res 2005;65:3044-3048.
    • (2005) Cancer Res , vol.65 , pp. 3044-3048
    • Zea, A.H.1
  • 162
    • 4143130091 scopus 로고    scopus 로고
    • Arginase I production in the tumor microenvironment by mature myeloid cells inhibits T-cell receptor expression and antigen-specific T-cell responses
    • Rodriguez PC, et al. Arginase I production in the tumor microenvironment by mature myeloid cells inhibits T-cell receptor expression and antigen-specific T-cell responses. Cancer Res 2004;64:5839-5849.
    • (2004) Cancer Res , vol.64 , pp. 5839-5849
    • Rodriguez, P.C.1
  • 163
    • 84860005763 scopus 로고    scopus 로고
    • Arginine deficiency leads to impaired cofilin dephosphorylation in activated human T lymphocytes
    • Feldmeyer N, et al. Arginine deficiency leads to impaired cofilin dephosphorylation in activated human T lymphocytes. Int Immunol 2012;24:303-313.
    • (2012) Int Immunol , vol.24 , pp. 303-313
    • Feldmeyer, N.1
  • 164
    • 84878124921 scopus 로고    scopus 로고
    • Cytotoxicity of tumor antigen specific human T cells is unimpaired by arginine depletion
    • Munder M, et al. Cytotoxicity of tumor antigen specific human T cells is unimpaired by arginine depletion. PLoS ONE 2013;8:e63521.
    • (2013) PLoS ONE , vol.8
    • Munder, M.1
  • 165
    • 77953578878 scopus 로고    scopus 로고
    • Proteomic surveillance of autoantigens in patients with Behcet's disease by a proteomic approach
    • Ooka S, et al. Proteomic surveillance of autoantigens in patients with Behcet's disease by a proteomic approach. Microbiol Immunol 2010;54:354-361.
    • (2010) Microbiol Immunol , vol.54 , pp. 354-361
    • Ooka, S.1
  • 167
    • 34948814168 scopus 로고    scopus 로고
    • Macrophages suppress T cell responses and arthritis development in mice by producing reactive oxygen species
    • Gelderman KA, et al. Macrophages suppress T cell responses and arthritis development in mice by producing reactive oxygen species. J Clin Invest 2007;117:3020-3028.
    • (2007) J Clin Invest , vol.117 , pp. 3020-3028
    • Gelderman, K.A.1
  • 168
    • 0025908328 scopus 로고
    • T-cell differentiation is influenced by thymic microenvironments
    • van Ewijk W. T-cell differentiation is influenced by thymic microenvironments. Annu Rev Immunol 1991;9:591-615.
    • (1991) Annu Rev Immunol , vol.9 , pp. 591-615
    • van Ewijk, W.1
  • 169
    • 0027284230 scopus 로고
    • Human T-cell clonal anergy is induced by antigen presentation in the absence of B7 costimulation
    • Gimmi CD, Freeman GJ, Gribben JG, Gray G, Nadler LM. Human T-cell clonal anergy is induced by antigen presentation in the absence of B7 costimulation. Proc Natl Acad Sci USA 1993;90:6586-6590.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 6586-6590
    • Gimmi, C.D.1    Freeman, G.J.2    Gribben, J.G.3    Gray, G.4    Nadler, L.M.5
  • 170
    • 77953541634 scopus 로고    scopus 로고
    • Inflammatory cytokines as a third signal for T cell activation
    • Curtsinger JM, Mescher MF. Inflammatory cytokines as a third signal for T cell activation. Curr Opin Immunol 2010;22:333-340.
    • (2010) Curr Opin Immunol , vol.22 , pp. 333-340
    • Curtsinger, J.M.1    Mescher, M.F.2
  • 171
    • 0034278725 scopus 로고    scopus 로고
    • Dendritic cell regulation of TH1-TH2 development
    • Moser M, Murphy KM. Dendritic cell regulation of TH1-TH2 development. Nat Immunol 2000;1:199-205.
    • (2000) Nat Immunol , vol.1 , pp. 199-205
    • Moser, M.1    Murphy, K.M.2
  • 172
    • 21844440052 scopus 로고    scopus 로고
    • Tuning immune responses: diversity and adaptation of the immunological synapse
    • Friedl P, den Boer AT, Gunzer M. Tuning immune responses: diversity and adaptation of the immunological synapse. Nat Rev Immunol 2005;5:532-545.
    • (2005) Nat Rev Immunol , vol.5 , pp. 532-545
    • Friedl, P.1    den Boer, A.T.2    Gunzer, M.3
  • 174
    • 77952310268 scopus 로고    scopus 로고
    • Functional anatomy of T cell activation and synapse formation
    • Fooksman DR, et al. Functional anatomy of T cell activation and synapse formation. Annu Rev Immunol 2010;28:79-105.
    • (2010) Annu Rev Immunol , vol.28 , pp. 79-105
    • Fooksman, D.R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.