메뉴 건너뛰기




Volumn 85, Issue 2, 2008, Pages 513-529

LC/MS identification of 12 intracellular cytoskeletal and inflammatory proteins from monocytes adherent on surface-adsorbed fibronectin-derived peptides

Author keywords

AG18; Host response; Inflammation; Phorbol myristate acetate; PHSRN; RGD; U937

Indexed keywords

INFLAMMATION; PHORBOL MYRISTATE ACETATE; PHOSPHOTYROSINE PROTEINS; PROMONOCYTIC CELLS;

EID: 42149093968     PISSN: 15493296     EISSN: 15524965     Source Type: Journal    
DOI: 10.1002/jbm.a.31306     Document Type: Article
Times cited : (6)

References (77)
  • 1
    • 0035168305 scopus 로고    scopus 로고
    • Biological responses to materials
    • Anderson JM. Biological responses to materials. Annu Rev Mater Res 2001;31:81-110.
    • (2001) Annu Rev Mater Res , vol.31 , pp. 81-110
    • Anderson, J.M.1
  • 2
    • 0037666212 scopus 로고    scopus 로고
    • Nondisposable materials, chronic inflammation, and adjuvant action
    • Hamilton JA. Nondisposable materials, chronic inflammation, and adjuvant action. J Leuk Bio 2003;73:702-712.
    • (2003) J Leuk Bio , vol.73 , pp. 702-712
    • Hamilton, J.A.1
  • 3
    • 43949164802 scopus 로고
    • Mechanisms of inflammation and infection with implanted devices
    • Anderson, JM. Mechanisms of inflammation and infection with implanted devices. Cardiovasc Pathol 1993;2:33S-41S.
    • (1993) Cardiovasc Pathol , vol.2
    • Anderson, J.M.1
  • 4
    • 0024000488 scopus 로고
    • Inflammatory response to implants
    • Anderson JM. Inflammatory response to implants. ASAIO. 1988;11:101-107.
    • (1988) ASAIO , vol.11 , pp. 101-107
    • Anderson, J.M.1
  • 5
    • 0036178447 scopus 로고    scopus 로고
    • Signal transduction by cell adhesion receptors and the cytoskeleton: Functions of integrins, Cadherins, selectins, and immunoglobulin-superfamily members
    • Juliano RL. Signal transduction by cell adhesion receptors and the cytoskeleton: Functions of integrins, Cadherins, selectins, and immunoglobulin-superfamily members. Annu Rev Phamacol Toxicol 2002;42:283-323.
    • (2002) Annu Rev Phamacol Toxicol , vol.42 , pp. 283-323
    • Juliano, R.L.1
  • 6
    • 0032901416 scopus 로고    scopus 로고
    • Adhesion of human monocytic THP-1 cells to endothelial cell adhesion molecules or extracellular matrix proteins via β1 integrins regulates heparin binding epidermal growth factor-like growth factor (HB-EGF) expression
    • Mograbi B, Rochet N, Emiliozzi C, Bernard R. Adhesion of human monocytic THP-1 cells to endothelial cell adhesion molecules or extracellular matrix proteins via β1 integrins regulates heparin binding epidermal growth factor-like growth factor (HB-EGF) expression. Euro Cytokine Network 1999;10:79-86.
    • (1999) Euro Cytokine Network , vol.10 , pp. 79-86
    • Mograbi, B.1    Rochet, N.2    Emiliozzi, C.3    Bernard, R.4
  • 7
    • 23744443917 scopus 로고    scopus 로고
    • Monocyte/lymphocyte interactions and the foreign body response: In vitro effects of biomaterial surface chemistry
    • Part A
    • MacEwan MR, Brodbeck WG, Matsuda T, Anderson JM. Monocyte/lymphocyte interactions and the foreign body response: In vitro effects of biomaterial surface chemistry. J Biomed Mater Res Part A 2005;74:285-293.
    • (2005) J Biomed Mater Res , vol.74 , pp. 285-293
    • MacEwan, M.R.1    Brodbeck, W.G.2    Matsuda, T.3    Anderson, J.M.4
  • 8
    • 0037024096 scopus 로고    scopus 로고
    • Protein and surface effects on monocyte and macrophage adhesion, maturation, and survival
    • Collier TO, Anderson JM. Protein and surface effects on monocyte and macrophage adhesion, maturation, and survival. J Biomed Mater Res 2002;60:487-496.
    • (2002) J Biomed Mater Res , vol.60 , pp. 487-496
    • Collier, T.O.1    Anderson, J.M.2
  • 9
    • 0032433053 scopus 로고    scopus 로고
    • Complementary roles for scavenger receptor A and CD36 of human monocyte-derived macro-phages in adhesion to surfaces coated with oxidized low-density lipoproteins and in secretion of H2O2
    • Maxeiner H, Husemann J, Thomas CA, Loike JD, El Khoury J, Silverstein SC. Complementary roles for scavenger receptor A and CD36 of human monocyte-derived macro-phages in adhesion to surfaces coated with oxidized low-density lipoproteins and in secretion of H2O2. J Exp Med 1998;188:2257-2265.
    • (1998) J Exp Med , vol.188 , pp. 2257-2265
    • Maxeiner, H.1    Husemann, J.2    Thomas, C.A.3    Loike, J.D.4    El Khoury, J.5    Silverstein, S.C.6
  • 10
    • 33750146181 scopus 로고    scopus 로고
    • The interrelated role of fibronectin and interleukin-1 in biomaterial-modulated macrophage function
    • Schmidt DR, Kao WJ. The interrelated role of fibronectin and interleukin-1 in biomaterial-modulated macrophage function. Biomaterials 2007;28:371-382.
    • (2007) Biomaterials , vol.28 , pp. 371-382
    • Schmidt, D.R.1    Kao, W.J.2
  • 11
    • 0029775681 scopus 로고    scopus 로고
    • Ruoslahti E. RGD and other recognition sequences for integrins. Annu Rev Cell Dev Biol 1996;12:697-715.
    • Ruoslahti E. RGD and other recognition sequences for integrins. Annu Rev Cell Dev Biol 1996;12:697-715.
  • 12
    • 33645972915 scopus 로고    scopus 로고
    • Effect of RGD secondary structure and the synergy site PHSRN on cell adhesion, spreading and specific integrin engagement
    • Ochsenhirt SE, Kokkoli E, McCarthy JB, Tirrell M. Effect of RGD secondary structure and the synergy site PHSRN on cell adhesion, spreading and specific integrin engagement. Biomaterials 2006;27:3863-3874.
    • (2006) Biomaterials , vol.27 , pp. 3863-3874
    • Ochsenhirt, S.E.1    Kokkoli, E.2    McCarthy, J.B.3    Tirrell, M.4
  • 13
    • 33745004875 scopus 로고    scopus 로고
    • The effect of RGD fluorosurfactant polymer modification of ePTFE on endothelial cell adhesion, growth and function
    • Larsen CC, Kligman F, Kottke-Marchant K, Marchant RE. The effect of RGD fluorosurfactant polymer modification of ePTFE on endothelial cell adhesion, growth and function. Biomaterials 2006;27:4846-4855.
    • (2006) Biomaterials , vol.27 , pp. 4846-4855
    • Larsen, C.C.1    Kligman, F.2    Kottke-Marchant, K.3    Marchant, R.E.4
  • 14
    • 0032877635 scopus 로고    scopus 로고
    • Cell signaling by protein tyrosine phosphorylation
    • Fischer E. Cell signaling by protein tyrosine phosphorylation. Adv Enzyme Regul 1999;39:359-369.
    • (1999) Adv Enzyme Regul , vol.39 , pp. 359-369
    • Fischer, E.1
  • 15
    • 0036595065 scopus 로고    scopus 로고
    • Tyrosine phosphorylation in signaling and disease
    • Hunter T. Tyrosine phosphorylation in signaling and disease. Keio J Med 2002;51:61-71.
    • (2002) Keio J Med , vol.51 , pp. 61-71
    • Hunter, T.1
  • 16
    • 0036605185 scopus 로고    scopus 로고
    • Analysis of protein phosphorylation using mass spectrometry: Deciphering the phosphoproteome
    • Mann M, Ong SE, Gronborg M, Steen H, Jensen ON, Pandey A. Analysis of protein phosphorylation using mass spectrometry: Deciphering the phosphoproteome. Trends Biotech 2002; 20:261-268.
    • (2002) Trends Biotech , vol.20 , pp. 261-268
    • Mann, M.1    Ong, S.E.2    Gronborg, M.3    Steen, H.4    Jensen, O.N.5    Pandey, A.6
  • 17
    • 4444306056 scopus 로고    scopus 로고
    • Intracellular protein phosphorylation in adherent U937 monocytes mediated by various culture conditions and fibronectin-derived surface ligands
    • Chen XX, Zuckerman ST, Kao WJ. Intracellular protein phosphorylation in adherent U937 monocytes mediated by various culture conditions and fibronectin-derived surface ligands. Biomaterials 2005;26:873-882.
    • (2005) Biomaterials , vol.26 , pp. 873-882
    • Chen, X.X.1    Zuckerman, S.T.2    Kao, W.J.3
  • 19
    • 26644437215 scopus 로고    scopus 로고
    • Identification of mammalian proteins cross-linked to DNA by ionizing radiation
    • Barker S, Weinfeld M, Zheng J, Li L, Murray D. Identification of mammalian proteins cross-linked to DNA by ionizing radiation. J Biol Chem 2005;280:33826-33838.
    • (2005) J Biol Chem , vol.280 , pp. 33826-33838
    • Barker, S.1    Weinfeld, M.2    Zheng, J.3    Li, L.4    Murray, D.5
  • 20
    • 1842430894 scopus 로고    scopus 로고
    • A combination of proteomics, principal component analysis and transcriptomics is a powerful tool for the identification of biomarkers for macrophage maturation in the U937 cell line
    • Verhoeckx KCM, Bijlsma S, de Groene EM, Witkamp RF, van der Greef J, Rodenburg RJT. A combination of proteomics, principal component analysis and transcriptomics is a powerful tool for the identification of biomarkers for macrophage maturation in the U937 cell line. Proteomics 2004;4:1014-1028.
    • (2004) Proteomics , vol.4 , pp. 1014-1028
    • Verhoeckx, K.C.M.1    Bijlsma, S.2    de Groene, E.M.3    Witkamp, R.F.4    van der Greef, J.5    Rodenburg, R.J.T.6
  • 21
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold R, Mann M. Mass spectrometry-based proteomics. Nature 2003;422:198-207.
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 22
    • 4444335470 scopus 로고    scopus 로고
    • The ABC's (and XYZ's) of peptide sequencing
    • Steen H, Mann M. The ABC's (and XYZ's) of peptide sequencing. Nat Rev 2004;5:699-711.
    • (2004) Nat Rev , vol.5 , pp. 699-711
    • Steen, H.1    Mann, M.2
  • 23
    • 0036470450 scopus 로고    scopus 로고
    • What does it mean to identify a protein in proteomics?
    • Rappsilber J, Mann M. What does it mean to identify a protein in proteomics? Trends Biochem Sci 2002;27:74-78.
    • (2002) Trends Biochem Sci , vol.27 , pp. 74-78
    • Rappsilber, J.1    Mann, M.2
  • 24
    • 0017155490 scopus 로고
    • Establishment and characterization of a human histiocytic lymphoma cell line (U-937)
    • Sundstrom C, Nilsson K. Establishment and characterization of a human histiocytic lymphoma cell line (U-937). Int J Cancer 1976;17:565-577.
    • (1976) Int J Cancer , vol.17 , pp. 565-577
    • Sundstrom, C.1    Nilsson, K.2
  • 25
    • 12944269065 scopus 로고
    • Rapid identification of proteins by peptide-mass fingerprinting
    • Pappin DJC, Hojrup P, Bleasby AJ. Rapid identification of proteins by peptide-mass fingerprinting. Curr Biol 1993;3:327-332.
    • (1993) Curr Biol , vol.3 , pp. 327-332
    • Pappin, D.J.C.1    Hojrup, P.2    Bleasby, A.J.3
  • 26
    • 10944257339 scopus 로고    scopus 로고
    • Profiling the global tyrosine phosphorylation state
    • Machida K, Mayer BJ, Nollau P. Profiling the global tyrosine phosphorylation state. Mol Cell Proteomics 2003;2:215-233.
    • (2003) Mol Cell Proteomics , vol.2 , pp. 215-233
    • Machida, K.1    Mayer, B.J.2    Nollau, P.3
  • 27
    • 33745271556 scopus 로고    scopus 로고
    • The N-terminal fragment of GRP94 is sufficient for peptide presentation via professional antigen-presenting cells
    • Biswas C, Sriram U, Ciric B, Ostrovsky O, Gallucci S, Argon Y. The N-terminal fragment of GRP94 is sufficient for peptide presentation via professional antigen-presenting cells. Int Immunol 2006;18:1147-1157.
    • (2006) Int Immunol , vol.18 , pp. 1147-1157
    • Biswas, C.1    Sriram, U.2    Ciric, B.3    Ostrovsky, O.4    Gallucci, S.5    Argon, Y.6
  • 30
    • 0032544543 scopus 로고    scopus 로고
    • Heat-shock protein 90 (hsp90) binds in vitro to tubulin dimmer and inhibits microtubule formation
    • Garnier C, Barbier P, Gilli R, Lopez C, Peyrot V, Briand C. Heat-shock protein 90 (hsp90) binds in vitro to tubulin dimmer and inhibits microtubule formation. Biochem Biophys Res Commun 1998;250:414-419.
    • (1998) Biochem Biophys Res Commun , vol.250 , pp. 414-419
    • Garnier, C.1    Barbier, P.2    Gilli, R.3    Lopez, C.4    Peyrot, V.5    Briand, C.6
  • 31
    • 0042839620 scopus 로고    scopus 로고
    • Titin: Properties and family relationships
    • Tskhovrebova L, Trinick J. Titin: Properties and family relationships. Mol Cell Biol 2003;4:679-689.
    • (2003) Mol Cell Biol , vol.4 , pp. 679-689
    • Tskhovrebova, L.1    Trinick, J.2
  • 32
    • 8744221697 scopus 로고    scopus 로고
    • Properties of titin immunoglobulin and Fibronectin-3 domains
    • Tskhovrebova L, Trinick J. Properties of titin immunoglobulin and Fibronectin-3 domains. J Biol Chem 2004;279:46351-46354.
    • (2004) J Biol Chem , vol.279 , pp. 46351-46354
    • Tskhovrebova, L.1    Trinick, J.2
  • 33
    • 33645960432 scopus 로고    scopus 로고
    • Effect of surface-adsorbed proteins and phosphorylation inhibitor AG18 on intracellular protein expression in adherent macrophages
    • Zuckerman ST, Kao WJ. Effect of surface-adsorbed proteins and phosphorylation inhibitor AG18 on intracellular protein expression in adherent macrophages. Biomaterials 2006;27: 3745-3757.
    • (2006) Biomaterials , vol.27 , pp. 3745-3757
    • Zuckerman, S.T.1    Kao, W.J.2
  • 34
    • 26944487335 scopus 로고    scopus 로고
    • Translation elongation factor 1A is essential for regulation of the actin cytoskeleton and cell morphology
    • Gross SR, Kinzy TG. Translation elongation factor 1A is essential for regulation of the actin cytoskeleton and cell morphology. Nat Struct Mol Biol 2005;12:772-778.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 772-778
    • Gross, S.R.1    Kinzy, T.G.2
  • 35
    • 0033105845 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein D0B is a sequence-specific DNA-binding protein
    • Tolnay M, Vereshchagina LA, Tsokos GC. Heterogeneous nuclear ribonucleoprotein D0B is a sequence-specific DNA-binding protein. Biochem J 1999;338:417-425.
    • (1999) Biochem J , vol.338 , pp. 417-425
    • Tolnay, M.1    Vereshchagina, L.A.2    Tsokos, G.C.3
  • 36
    • 0031688491 scopus 로고    scopus 로고
    • Complement receptor 2 in the regulation of the immune response
    • Tolnay M, Tsokos GC. Complement receptor 2 in the regulation of the immune response. Clin Immunol Immunopathol 1998;88:123-132.
    • (1998) Clin Immunol Immunopathol , vol.88 , pp. 123-132
    • Tolnay, M.1    Tsokos, G.C.2
  • 37
    • 0031296662 scopus 로고    scopus 로고
    • Transcriptional regulation of the complement receptor 2 gene: Role of a heterogeneous nuclear ribonucleoprotein
    • Tolnay M, Lambris JD, Tsokos GC. Transcriptional regulation of the complement receptor 2 gene: Role of a heterogeneous nuclear ribonucleoprotein. J Immunol 1997;159:5492-5501.
    • (1997) J Immunol , vol.159 , pp. 5492-5501
    • Tolnay, M.1    Lambris, J.D.2    Tsokos, G.C.3
  • 38
    • 0033841668 scopus 로고    scopus 로고
    • Serum regulates the expression of complement receptor 2 on human B cell lines
    • Tolnay M, Tsokos GC. Serum regulates the expression of complement receptor 2 on human B cell lines. Immunopharmacol Immunotoxicol 200C;22:205-219.
    • Immunopharmacol Immunotoxicol , vol.200 C , Issue.22 , pp. 205-219
    • Tolnay, M.1    Tsokos, G.C.2
  • 39
    • 0037115912 scopus 로고    scopus 로고
    • Enzymology of the repair of free radicals-induced DNA damage
    • Gros L, Saparbaev MK, Laval J. Enzymology of the repair of free radicals-induced DNA damage. Oncogene 2002;21:8905-8925.
    • (2002) Oncogene , vol.21 , pp. 8905-8925
    • Gros, L.1    Saparbaev, M.K.2    Laval, J.3
  • 40
    • 0032809592 scopus 로고    scopus 로고
    • Transcription and growth regulatory functions of the HIN-200 family of proteins
    • Johnstone RW, Trapani JA. Transcription and growth regulatory functions of the HIN-200 family of proteins. Mol Cell Biol 1999;19:5833-5838.
    • (1999) Mol Cell Biol , vol.19 , pp. 5833-5838
    • Johnstone, R.W.1    Trapani, J.A.2
  • 41
    • 22144490446 scopus 로고    scopus 로고
    • The HIN-200 family: More than interferon-inducible genes?
    • Ludlow LEA, Johnstone RW, Clarke CJP. The HIN-200 family: More than interferon-inducible genes? Exp Cell Res 2005;308:1-17.
    • (2005) Exp Cell Res , vol.308 , pp. 1-17
    • Ludlow, L.E.A.1    Johnstone, R.W.2    Clarke, C.J.P.3
  • 43
    • 33645455276 scopus 로고    scopus 로고
    • Molecular recognition of an RNA trafficking element by heterogeneous nuclear ribonucleoprotein A2
    • Landsberg MJ, Moran-Jones K, Smith R. Molecular recognition of an RNA trafficking element by heterogeneous nuclear ribonucleoprotein A2. Biochemistry 2006;45:3943-3951.
    • (2006) Biochemistry , vol.45 , pp. 3943-3951
    • Landsberg, M.J.1    Moran-Jones, K.2    Smith, R.3
  • 44
    • 33646930155 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein-A2/B1 modulate collagen prolyl 4-hydroxylase, α(I) mRNA stability
    • Fahling M, Mrowka R, Steege A, Martinka P, Persson PB, Thiele BJ. Heterogeneous nuclear ribonucleoprotein-A2/B1 modulate collagen prolyl 4-hydroxylase, α(I) mRNA stability. J Biol Chem 2006;281:9279-9286.
    • (2006) J Biol Chem , vol.281 , pp. 9279-9286
    • Fahling, M.1    Mrowka, R.2    Steege, A.3    Martinka, P.4    Persson, P.B.5    Thiele, B.J.6
  • 45
    • 30044446861 scopus 로고    scopus 로고
    • The hnRNPs F and H2 bind to similar sequences to influence gene expression
    • Alkan SA, Martincic K, Milcarek C The hnRNPs F and H2 bind to similar sequences to influence gene expression. Biochem J 2006;393:361-371.
    • (2006) Biochem J , vol.393 , pp. 361-371
    • Alkan, S.A.1    Martincic, K.2    Milcarek, C.3
  • 46
    • 0026091353 scopus 로고
    • Moesin: A member of the protein 4.1-Talin-Ezrin family of proteins
    • Lankes WT, Heinz F. Moesin: A member of the protein 4.1-Talin-Ezrin family of proteins. Proc Natl Acad Sci USA 1991; 88:8297-8301.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 8297-8301
    • Lankes, W.T.1    Heinz, F.2
  • 47
    • 0029795488 scopus 로고    scopus 로고
    • Regulations mechanism of ERM (Ezrin/Radixin/Moesin) protein/plasma membrane association: Possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway
    • Hirao M, Sato N, Kondo T, Yonemura S, Monden M, Sasaki T, Takai Y, Tsukita S, Tsukita S. Regulations mechanism of ERM (Ezrin/Radixin/Moesin) protein/plasma membrane association: Possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway. J Cell Biol 1996;135:37-51.
    • (1996) J Cell Biol , vol.135 , pp. 37-51
    • Hirao, M.1    Sato, N.2    Kondo, T.3    Yonemura, S.4    Monden, M.5    Sasaki, T.6    Takai, Y.7    Tsukita, S.8    Tsukita, S.9
  • 48
    • 0034724536 scopus 로고    scopus 로고
    • Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain
    • Pearson MA, Reczek D, Bretscher A, Karplus PA. Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain. Cell 2000;101:259-270.
    • (2000) Cell , vol.101 , pp. 259-270
    • Pearson, M.A.1    Reczek, D.2    Bretscher, A.3    Karplus, P.A.4
  • 49
    • 0036346708 scopus 로고    scopus 로고
    • ERM proteins and merlin: Integrators at the cell cortex
    • Bretscher A, Edwards K, Fehon RG. ERM proteins and merlin: Integrators at the cell cortex. Mol Cell Biol 2002;3:586-599.
    • (2002) Mol Cell Biol , vol.3 , pp. 586-599
    • Bretscher, A.1    Edwards, K.2    Fehon, R.G.3
  • 50
    • 22144437706 scopus 로고    scopus 로고
    • Stimulus-induced phosphorylation of PKC θ at the C-terminal hydrophobic motif in human T lymphocytes
    • Freeley M, Volkov Y, Kelleher D, Long A. Stimulus-induced phosphorylation of PKC θ at the C-terminal hydrophobic motif in human T lymphocytes. Biochem Biophys Res Commun 2005;334:619-630.
    • (2005) Biochem Biophys Res Commun , vol.334 , pp. 619-630
    • Freeley, M.1    Volkov, Y.2    Kelleher, D.3    Long, A.4
  • 51
    • 2542588542 scopus 로고    scopus 로고
    • Ezrin/radixin/moesin proteins and Rho GTPase signaling in leukocytes
    • Ivetic A, Ridley AJ. Ezrin/radixin/moesin proteins and Rho GTPase signaling in leukocytes. Immunology 2004;112:165-176.
    • (2004) Immunology , vol.112 , pp. 165-176
    • Ivetic, A.1    Ridley, A.J.2
  • 52
    • 0035652354 scopus 로고    scopus 로고
    • Exclusion of CD43 from the immunological synapse is mediated by phosphorylation-regulated relocation of the cytoskeletal adaptor moesin
    • Delon J, Kaibuchi K, Germain RN. Exclusion of CD43 from the immunological synapse is mediated by phosphorylation-regulated relocation of the cytoskeletal adaptor moesin. Immunity 2001;15:691-701.
    • (2001) Immunity , vol.15 , pp. 691-701
    • Delon, J.1    Kaibuchi, K.2    Germain, R.N.3
  • 53
    • 0030712860 scopus 로고    scopus 로고
    • ERM (Ezrin/Radixin/Moesin)-based molecular mechanism of microvillar breakdown at an early stage of apoptosis
    • Kondo T, Takeuchi K, Doi Y, Yonemura S, Nagata S, Tsukita S, Tsukita S. ERM (Ezrin/Radixin/Moesin)-based molecular mechanism of microvillar breakdown at an early stage of apoptosis. J Cell Biol 1997;139:749-758.
    • (1997) J Cell Biol , vol.139 , pp. 749-758
    • Kondo, T.1    Takeuchi, K.2    Doi, Y.3    Yonemura, S.4    Nagata, S.5    Tsukita, S.6    Tsukita, S.7
  • 55
    • 0344826472 scopus 로고    scopus 로고
    • Chemokine stimulation of human peripheral blood T lymphocytes induces rapid dephosphorylation of ERM proteins, which facilitates loss of microvilli and polarization
    • Brown MJ, Nijhara R, Hallam JA, Gignac M, Yamada KM, Erlandsen SL, Delon J, Kruhlak M, Shaw S. Chemokine stimulation of human peripheral blood T lymphocytes induces rapid dephosphorylation of ERM proteins, which facilitates loss of microvilli and polarization. Blood 2003;102:3890-3899.
    • (2003) Blood , vol.102 , pp. 3890-3899
    • Brown, M.J.1    Nijhara, R.2    Hallam, J.A.3    Gignac, M.4    Yamada, K.M.5    Erlandsen, S.L.6    Delon, J.7    Kruhlak, M.8    Shaw, S.9
  • 56
    • 0026760578 scopus 로고
    • Identification of the two major epidermal growth factor-induced tyrosine phosphorylation sites in the microvillar core protein ezrin
    • Krieg J, Hunter T. Identification of the two major epidermal growth factor-induced tyrosine phosphorylation sites in the microvillar core protein ezrin. J Biol Chem 1992;267:19258-19265.
    • (1992) J Biol Chem , vol.267 , pp. 19258-19265
    • Krieg, J.1    Hunter, T.2
  • 57
    • 29344471072 scopus 로고    scopus 로고
    • Understanding microtubule dynamics for improved cancer therapy
    • Honore S, Pasquier E, Braguer D. Understanding microtubule dynamics for improved cancer therapy. Cell Mol Life Sci 2005;62:3039-3056.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 3039-3056
    • Honore, S.1    Pasquier, E.2    Braguer, D.3
  • 58
    • 0034743675 scopus 로고    scopus 로고
    • Structural insights into microtubule function
    • Nogales E. Structural insights into microtubule function. Annu Rev Biophys Biomol Struct 2001;30:397-420.
    • (2001) Annu Rev Biophys Biomol Struct , vol.30 , pp. 397-420
    • Nogales, E.1
  • 60
    • 0033555527 scopus 로고    scopus 로고
    • Phosphorylation- and activation-independent association of the tyrosine kinase Syk and the tyrosine kinase substrates Cbl and Vav with tubulin in B-cells
    • Fernandez JA, Keshvara LM, Peters JD, Furlong MT, Harrison ML, Geahlen RL. Phosphorylation- and activation-independent association of the tyrosine kinase Syk and the tyrosine kinase substrates Cbl and Vav with tubulin in B-cells. J Biol Chem 1999;274:1401-1406.
    • (1999) J Biol Chem , vol.274 , pp. 1401-1406
    • Fernandez, J.A.1    Keshvara, L.M.2    Peters, J.D.3    Furlong, M.T.4    Harrison, M.L.5    Geahlen, R.L.6
  • 61
    • 0029867911 scopus 로고    scopus 로고
    • Syk, activated by cross-linking the B-cell antigen receptor, localizes to the cytosol where it interacts with and phosphorylates α-tubulin on tyrosine
    • Peters JD, Furlong MT, Asai DJ, Harrison ML, Geahlen RL. Syk, activated by cross-linking the B-cell antigen receptor, localizes to the cytosol where it interacts with and phosphorylates α-tubulin on tyrosine. J Biol Chem 1996;271:4755-4762.
    • (1996) J Biol Chem , vol.271 , pp. 4755-4762
    • Peters, J.D.1    Furlong, M.T.2    Asai, D.J.3    Harrison, M.L.4    Geahlen, R.L.5
  • 62
    • 2442610400 scopus 로고    scopus 로고
    • The spleen tyrosine kinase (Syk) in human disease, implications for design of tyrosine kinase inhibitor based therapy
    • Navara CS. The spleen tyrosine kinase (Syk) in human disease, implications for design of tyrosine kinase inhibitor based therapy. Curr Pharm Des 2004;10:1739-1744.
    • (2004) Curr Pharm Des , vol.10 , pp. 1739-1744
    • Navara, C.S.1
  • 63
    • 0028892669 scopus 로고
    • Phosphorylation of elongation factor 1 (EF-1) by protein kinase C stimulates DGP/GTP-exchange activity
    • Peters HI, Change YE, Traugh JA. Phosphorylation of elongation factor 1 (EF-1) by protein kinase C stimulates DGP/GTP-exchange activity. Eur J Biochem 1995;234:550-556.
    • (1995) Eur J Biochem , vol.234 , pp. 550-556
    • Peters, H.I.1    Change, Y.E.2    Traugh, J.A.3
  • 64
    • 0036175770 scopus 로고    scopus 로고
    • Interactions of elongation factor la with F-actin and β-actin mRNA: Implications for anchoring mRNA in cell protrusions
    • Liu G, Grant WM, Persky D, Latham VM, Singer RH, Condeelis J. Interactions of elongation factor la with F-actin and β-actin mRNA: Implications for anchoring mRNA in cell protrusions. Mol Biol Cell 2002;13:579-592.
    • (2002) Mol Biol Cell , vol.13 , pp. 579-592
    • Liu, G.1    Grant, W.M.2    Persky, D.3    Latham, V.M.4    Singer, R.H.5    Condeelis, J.6
  • 65
    • 0035838320 scopus 로고    scopus 로고
    • A Rho-dependent signaling pathway operating through myosin localizes β-actin mRNA in fibroblasts
    • Latham VM, Yu EHS, Tullio AN, Adelstein RS, Singer RH. A Rho-dependent signaling pathway operating through myosin localizes β-actin mRNA in fibroblasts. Curr Biol 2001;11:1010-1016.
    • (2001) Curr Biol , vol.11 , pp. 1010-1016
    • Latham, V.M.1    Yu, E.H.S.2    Tullio, A.N.3    Adelstein, R.S.4    Singer, R.H.5
  • 66
    • 0035912805 scopus 로고    scopus 로고
    • The physiological significance of β-actin mRNA localization in determining cell polarity and directional motility
    • Shestakova EA, Singer RH, Condeelis J. The physiological significance of β-actin mRNA localization in determining cell polarity and directional motility. Proc Natl Acad Sci USA 2001;98:7045-7050.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 7045-7050
    • Shestakova, E.A.1    Singer, R.H.2    Condeelis, J.3
  • 67
    • 33646235651 scopus 로고    scopus 로고
    • Identification of elongation factor 1α as a potential associated binding partner for Akt2
    • Lau J, Castelli LA, Lin ECK, Macaulay SL. Identification of elongation factor 1α as a potential associated binding partner for Akt2. Mol Cell Biochem 2006;286:17-22.
    • (2006) Mol Cell Biochem , vol.286 , pp. 17-22
    • Lau, J.1    Castelli, L.A.2    Lin, E.C.K.3    Macaulay, S.L.4
  • 68
    • 0026043769 scopus 로고
    • Phosphorylation of Valyl-tRNA synthetase and elongation factor 1 in response to phorbol esters is associated with stimulation of both activities
    • Venema RC, Peters HI, Traugh JA. Phosphorylation of Valyl-tRNA synthetase and elongation factor 1 in response to phorbol esters is associated with stimulation of both activities. J Biol Chem 1991;266:11993-11998.
    • (1991) J Biol Chem , vol.266 , pp. 11993-11998
    • Venema, R.C.1    Peters, H.I.2    Traugh, J.A.3
  • 69
    • 0025744934 scopus 로고
    • Phosphorylation of elongation factor 1 (EF-1) and Valyl-tRNA synthetase by Protein Kinase C and stimulation of EF-1 activity
    • Venema RC, Peters HI, Traugh JA. Phosphorylation of elongation factor 1 (EF-1) and Valyl-tRNA synthetase by Protein Kinase C and stimulation of EF-1 activity. J Biol Chem 1991;266:12574-12580.
    • (1991) J Biol Chem , vol.266 , pp. 12574-12580
    • Venema, R.C.1    Peters, H.I.2    Traugh, J.A.3
  • 71
    • 33745763276 scopus 로고    scopus 로고
    • Reciprocal upregulation of urokinase plasminogen activator and its inhibitor, PAI-2, by Borrelia burgdorferi affects bacterial penetration and host-inflammatory response
    • Haile WB, Coleman JL, Benach JL. Reciprocal upregulation of urokinase plasminogen activator and its inhibitor, PAI-2, by Borrelia burgdorferi affects bacterial penetration and host-inflammatory response. Cell Microbiol 2006;8:1349-1360.
    • (2006) Cell Microbiol , vol.8 , pp. 1349-1360
    • Haile, W.B.1    Coleman, J.L.2    Benach, J.L.3
  • 72
    • 1642380279 scopus 로고    scopus 로고
    • Helicobacter pylori induces plasminogen activator inhibitor 2 in gastric epithelial cells through Nuclear Factor κB and RhoA: Implications for invasion and apoptosis
    • Varro A, Noble PJM, Pritchard DM, Kennedy S, Hart CA, Dimaline R, Dockray GJ. Helicobacter pylori induces plasminogen activator inhibitor 2 in gastric epithelial cells through Nuclear Factor κB and RhoA: Implications for invasion and apoptosis. Cancer Res 2004;64:1695-1702.
    • (2004) Cancer Res , vol.64 , pp. 1695-1702
    • Varro, A.1    Noble, P.J.M.2    Pritchard, D.M.3    Kennedy, S.4    Hart, C.A.5    Dimaline, R.6    Dockray, G.J.7
  • 75
    • 1542380035 scopus 로고    scopus 로고
    • Involvement of Toll-like Receptors 2 and 4 in cellular activation by High Mobility Group Box 1 protein
    • Park JS, Svetkauskaite D, He Q, Kim JY, Strassheim D, Ishizaka A, Abraham E. Involvement of Toll-like Receptors 2 and 4 in cellular activation by High Mobility Group Box 1 protein. J Biol Chem 2004;279:7370-7377.
    • (2004) J Biol Chem , vol.279 , pp. 7370-7377
    • Park, J.S.1    Svetkauskaite, D.2    He, Q.3    Kim, J.Y.4    Strassheim, D.5    Ishizaka, A.6    Abraham, E.7
  • 77
    • 33645757512 scopus 로고    scopus 로고
    • ASC directs NF-κB activation by regulating receptor interacting protein-2 (RIP2) caspase-1 interactions
    • Sarkar A, Duncan M, Hart J, Hertlein E, Guttridge DC, Wewers MD. ASC directs NF-κB activation by regulating receptor interacting protein-2 (RIP2) caspase-1 interactions. J Immunol 2006;176:4979-4986.
    • (2006) J Immunol , vol.176 , pp. 4979-4986
    • Sarkar, A.1    Duncan, M.2    Hart, J.3    Hertlein, E.4    Guttridge, D.C.5    Wewers, M.D.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.