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Volumn 59, Issue 6, 1996, Pages 864-871

Paradoxical effects of colchicine on the activation of human neutrophils by chemotactic factors and inflammatory microcrystals

Author keywords

Microtubules; NADPH oxidase; Tyrosine phosphorylation

Indexed keywords

CHEMOTACTIC FACTOR; COLCHICINE; INDOMETACIN; LUMICOLCHICINE; NOCODAZOLE; PACLITAXEL; PHENYLBUTAZONE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; SUPEROXIDE; TRIMETHYLCOLCHICINIC ACID; VINBLASTINE;

EID: 0030011678     PISSN: 07415400     EISSN: None     Source Type: Journal    
DOI: 10.1002/jlb.59.6.864     Document Type: Article
Times cited : (26)

References (51)
  • 1
    • 0028174522 scopus 로고
    • The role of individual Fc gamma receptors in aggregated IgC-stimulated protein tyrosine phosphorylation in the human neutrophil
    • Richard, S., Shaw, A. S., Showell, H. J., Connelly, P. A. (1994) The role of individual Fc gamma receptors in aggregated IgC-stimulated protein tyrosine phosphorylation in the human neutrophil. Biochem. Biophys. Res. Commun. 199, 653-661.
    • (1994) Biochem. Biophys. Res. Commun. , vol.199 , pp. 653-661
    • Richard, S.1    Shaw, A.S.2    Showell, H.J.3    Connelly, P.A.4
  • 2
    • 0028263663 scopus 로고
    • Tyrosine phosphorylation in activated human neutrophils - comparison of the effects of different classes of agonists and identification of the signaling pathways involved
    • Rollet, E., Caon, A. C., Roberge, C. J., Liao, N. W., Malawista, S. E., McColl, S. R., Naccache, P. H. (1994) Tyrosine phosphorylation in activated human neutrophils - comparison of the effects of different classes of agonists and identification of the signaling pathways involved. J. Immunol. 153, 353-363.
    • (1994) J. Immunol. , vol.153 , pp. 353-363
    • Rollet, E.1    Caon, A.C.2    Roberge, C.J.3    Liao, N.W.4    Malawista, S.E.5    McColl, S.R.6    Naccache, P.H.7
  • 4
    • 0025201008 scopus 로고
    • Selective inhibition of human neutrophil functional responsiveness by erbstatin, an inhibitor of tyrosine protein kinase
    • Naccache, P. H., Gilbert, C., Caon, A. C., Caudry, M., Huang, C. K., Bonak, V. A., Umezawa, K., McColl, S. R. (1990) Selective inhibition of human neutrophil functional responsiveness by erbstatin, an inhibitor of tyrosine protein kinase. Blood 76, 2098-2104.
    • (1990) Blood , vol.76 , pp. 2098-2104
    • Naccache, P.H.1    Gilbert, C.2    Caon, A.C.3    Caudry, M.4    Huang, C.K.5    Bonak, V.A.6    Umezawa, K.7    McColl, S.R.8
  • 5
    • 0026541691 scopus 로고
    • Tyrosine phosphorylation is involved in receptor coupling to phospholipase-D but not phospholipase-C in the human neutrophil
    • Uings, I. J., Thompson, N. T., Randall, R. W., Spacey, C. D., Bonser, R. W., Hudson, A. T., Garland, L. G. (1992) Tyrosine phosphorylation is involved in receptor coupling to phospholipase-D but not phospholipase-C in the human neutrophil. Biochem. J. 281, 597-600.
    • (1992) Biochem. J. , vol.281 , pp. 597-600
    • Uings, I.J.1    Thompson, N.T.2    Randall, R.W.3    Spacey, C.D.4    Bonser, R.W.5    Hudson, A.T.6    Garland, L.G.7
  • 6
    • 0026710617 scopus 로고
    • Peroxides of vanadate induce activation of phospholipase D in HL-60 cells. Role of tyrosine phosphorylation
    • Bourgoin, S., Grinstein, S. (1992) Peroxides of vanadate induce activation of phospholipase D in HL-60 cells. Role of tyrosine phosphorylation. J. Biol. Chem. 267, 11908-11916.
    • (1992) J. Biol. Chem. , vol.267 , pp. 11908-11916
    • Bourgoin, S.1    Grinstein, S.2
  • 7
    • 0027155908 scopus 로고
    • Phospholipase-D activity in phagocytic leukocytes is synergistically regulated by C-protein-based and tyrosine kinase-based mechanisms
    • Dubyak, G. R., Schomisch, S. J., Kusner, D. J., Xie, M. S. (1993) Phospholipase-D activity in phagocytic leukocytes is synergistically regulated by C-protein-based and tyrosine kinase-based mechanisms. Biochem. J. 292, 121-128.
    • (1993) Biochem. J. , vol.292 , pp. 121-128
    • Dubyak, G.R.1    Schomisch, S.J.2    Kusner, D.J.3    Xie, M.S.4
  • 8
    • 0027223839 scopus 로고
    • Tyrosine kinase activation and signal transduction mediated by phospholipase-D
    • Hock, H. B. (1993) Tyrosine kinase activation and signal transduction mediated by phospholipase-D. Lab. Invest. 69, 1-4.
    • (1993) Lab. Invest. , vol.69 , pp. 1-4
    • Hock, H.B.1
  • 9
    • 0026688312 scopus 로고
    • Granulocyte-macrophage colony-stimulating factor primes phospholipase D activity in human neutrophils "in vitro". Role of calcium, G proteins and tyrosine kinases
    • Bourgoin, S., Poubelle, P. E., Liao, N. W., Umezawa, K., Borgeat, P., Naccache, P. H. (1992) Granulocyte-macrophage colony-stimulating factor primes phospholipase D activity in human neutrophils "in vitro". Role of calcium, G proteins and tyrosine kinases. Cell Signal. 4, 487-500.
    • (1992) Cell Signal. , vol.4 , pp. 487-500
    • Bourgoin, S.1    Poubelle, P.E.2    Liao, N.W.3    Umezawa, K.4    Borgeat, P.5    Naccache, P.H.6
  • 10
    • 0028362908 scopus 로고
    • Regulation of stimulated integrin surface expression in human neulrophils by tyrosine phosphorylation
    • Naccache, P. H., Jean, N., Liao, N. W., Bator, J. M., McColl, S. R., Kubes, P. (1994) Regulation of stimulated integrin surface expression in human neulrophils by tyrosine phosphorylation. Blood 84, 616-624.
    • (1994) Blood , vol.84 , pp. 616-624
    • Naccache, P.H.1    Jean, N.2    Liao, N.W.3    Bator, J.M.4    McColl, S.R.5    Kubes, P.6
  • 11
    • 0026704459 scopus 로고
    • Evidence for the involvement of tyrosine kinases in the locomotory responses of human neutrophils
    • Caudry, M., Caon, A. C., Gilbert, C., Lille, S., Naccache, P. H. (1991) Evidence for the involvement of tyrosine kinases in the locomotory responses of human neutrophils J. Leukoc. Biol. 51, 103-108.
    • (1991) J. Leukoc. Biol. , vol.51 , pp. 103-108
    • Caudry, M.1    Caon, A.C.2    Gilbert, C.3    Lille, S.4    Naccache, P.H.5
  • 12
    • 0028227906 scopus 로고
    • Signal transduction pathway in human polymorphonuclear leukocytes for chemotaxis induced by a chemotactic factor -distinct from the pathway for sSuperoxide anion production
    • Yasui, K., Yamazaki, M., Miyabayashi, M., Tsuno, T., Komiyama, A. (1994) Signal transduction pathway in human polymorphonuclear leukocytes for chemotaxis induced by a chemotactic factor -distinct from the pathway for sSuperoxide anion production. J. Immunol. 152, 5922-5929.
    • (1994) J. Immunol. , vol.152 , pp. 5922-5929
    • Yasui, K.1    Yamazaki, M.2    Miyabayashi, M.3    Tsuno, T.4    Komiyama, A.5
  • 13
    • 0027232096 scopus 로고
    • Crystal-induced neutrophil activation. III. Inflammatory microcrystals induce a distinct pattern of lyrosine phosphorylation in human neutrophils
    • Caudry, M., Roberge, C. J., de Médicis, R., Lussier, A., Poubelle, P. E., Naccache, P. H. (1993) Crystal-induced neutrophil activation. III. Inflammatory microcrystals induce a distinct pattern of lyrosine phosphorylation in human neutrophils. J. Clin. Invest. 91, 1649-1655.
    • (1993) J. Clin. Invest. , vol.91 , pp. 1649-1655
    • Caudry, M.1    Roberge, C.J.2    De Médicis, R.3    Lussier, A.4    Poubelle, P.E.5    Naccache, P.H.6
  • 14
    • 0027360268 scopus 로고
    • Crystal-induced neutrophil activation. 4. Specific inhibition of tyrosine phosphorylation by colchicine
    • Roberge, C. J., Caudry, M., De Médicis, R., Lussier, A., Poubelle, P. E., Naccache, P. H. (1993) Crystal-induced neutrophil activation. 4. Specific inhibition of tyrosine phosphorylation by colchicine. J. Clin. Invest. 92, 1722-1729.
    • (1993) J. Clin. Invest. , vol.92 , pp. 1722-1729
    • Roberge, C.J.1    Caudry, M.2    De Médicis, R.3    Lussier, A.4    Poubelle, P.E.5    Naccache, P.H.6
  • 15
    • 0022612342 scopus 로고
    • Stimulated cytokineplasts from human polymorphonuclear leukocytes mobilize calcium and polymerize actin. Cytoplasts made in cytochatasin B retain a defect in actin polymerization
    • Dye, D. E., Malawista, S. E., Naccache, P. H., Sha'afi, R. I. (1986) Stimulated cytokineplasts from human polymorphonuclear leukocytes mobilize calcium and polymerize actin. Cytoplasts made in cytochatasin B retain a defect in actin polymerization. J. Clin. Invest. 77, 34-37.
    • (1986) J. Clin. Invest. , vol.77 , pp. 34-37
    • Dye, D.E.1    Malawista, S.E.2    Naccache, P.H.3    Sha'afi, R.I.4
  • 16
    • 0022345949 scopus 로고
    • Functional integrity of cytokineplasts: Specific chemotactic and capping responses
    • Dyett, D. E., Malawista, S. E., van Blaricom G., Melnick, D. A., Malech, H. L. (1985) Functional integrity of cytokineplasts: specific chemotactic and capping responses. J. Immunol. 135, 2090-2094.
    • (1985) J. Immunol. , vol.135 , pp. 2090-2094
    • Dyett, D.E.1    Malawista, S.E.2    Van Blaricom, G.3    Melnick, D.A.4    Malech, H.L.5
  • 17
    • 0020449117 scopus 로고
    • The cytokineplasts: Purified, stable, and functional motile machinery from human blood polymorphonuclear leukocytes
    • Malawista, S. E., Boisfleury Chevance, A. (1982) The cytokineplasts: purified, stable, and functional motile machinery from human blood polymorphonuclear leukocytes. J. Cell Biol. 95, 960-973.
    • (1982) J. Cell Biol. , vol.95 , pp. 960-973
    • Malawista, S.E.1    Boisfleury Chevance, A.2
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Staehlin, T., Gordon, J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76, 4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehlin, T.2    Gordon, J.3
  • 22
    • 0007463081 scopus 로고
    • Taxol induces the assembly of free microtubules in living cells and blocks the organizing capacity of the centrosomes and kinetochores
    • De Brabander, M., Geuens, G., Nuydens, R., Willebrods, R., De Mey, J. (1981) Taxol induces the assembly of free microtubules in living cells and blocks the organizing capacity of the centrosomes and kinetochores. Proc. Natl. Acad. Sci. USA 78, 5608-5612.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 5608-5612
    • De Brabander, M.1    Geuens, G.2    Nuydens, R.3    Willebrods, R.4    De Mey, J.5
  • 24
    • 0023127177 scopus 로고
    • Cytoplasts made from human blood polymorphonuclear leukocytes with or without heat: Preservation of both motile function and respiratory burst oxidase activity
    • Malawista, S. E., van Blaricom, G. (1987) Cytoplasts made from human blood polymorphonuclear leukocytes with or without heat: preservation of both motile function and respiratory burst oxidase activity. Proc. Natl. Acad. Sci. USA 84, 454-458.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 454-458
    • Malawista, S.E.1    Van Blaricom, G.2
  • 25
    • 0021992617 scopus 로고
    • Cytokineplasts from human blood polymorphonuclear leukocytes. Lack of oxidase activity and extended functional longevity
    • Malawista, S. E., Van Blaricom, G., Cretella, S. B. (1985) Cytokineplasts from human blood polymorphonuclear leukocytes. Lack of oxidase activity and extended functional longevity. Inflammation [New York] 9, 99-106.
    • (1985) Inflammation [New York] , vol.9 , pp. 99-106
    • Malawista, S.E.1    Van Blaricom, G.2    Cretella, S.B.3
  • 26
    • 0027189961 scopus 로고
    • The biochemical basis of the NADPH oxidase of phagocytes
    • Segal, A. W., Abo, A. (1993) The biochemical basis of the NADPH oxidase of phagocytes. Trends Biochem. Sci. 18, 43-47.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 43-47
    • Segal, A.W.1    Abo, A.2
  • 27
    • 0025992764 scopus 로고
    • The superoxide-generating oxidase of phagocytic cells - physiological, molecular and pathological aspects
    • Morel, F., Doussiere, J., Vignais, P. V. (1991) The superoxide-generating oxidase of phagocytic cells - physiological, molecular and pathological aspects. Eur. J. Biochem. 201, 523-546.
    • (1991) Eur. J. Biochem. , vol.201 , pp. 523-546
    • Morel, F.1    Doussiere, J.2    Vignais, P.V.3
  • 28
    • 0025981739 scopus 로고
    • Crystal-induced neutrophil activation. I. Initiation and modulation of calcium mobilization and Superoxide production by microcrystals
    • Naccache, P. H., Grimard, M., Roberge, C. J., Gilbert, C., Lussier, A., de Médicis, R., Poubelle, P. E. (1991) Crystal-induced neutrophil activation. I. Initiation and modulation of calcium mobilization and Superoxide production by microcrystals. Arthritis Rheumatol. 33, 333-342.
    • (1991) Arthritis Rheumatol. , vol.33 , pp. 333-342
    • Naccache, P.H.1    Grimard, M.2    Roberge, C.J.3    Gilbert, C.4    Lussier, A.5    De Médicis, R.6    Poubelle, P.E.7
  • 29
    • 0020032997 scopus 로고
    • Stimulation of the respiratory burst in human neutrophils by crystals phagocytosis
    • Simchowitz, L., Atkinson, J. P., Spilberg, I. (1982) Stimulation of the respiratory burst in human neutrophils by crystals phagocytosis. Arthritis Rheumatol. 25, 181-188.
    • (1982) Arthritis Rheumatol. , vol.25 , pp. 181-188
    • Simchowitz, L.1    Atkinson, J.P.2    Spilberg, I.3
  • 30
    • 0023796777 scopus 로고
    • Colchicine in therapy. State of the art and new perspectives for an old drug
    • Famaey, J. P. (1988) Colchicine in therapy. State of the art and new perspectives for an old drug. Clin. Exp. Rheumatol. 6, 305-317.
    • (1988) Clin. Exp. Rheumatol. , vol.6 , pp. 305-317
    • Famaey, J.P.1
  • 31
    • 0027361085 scopus 로고
    • Colchicine, crystals, and neutrophil tyrosine phosphorylation
    • Smallwood, J. I., Malawista, S. E. (1993) Colchicine, crystals, and neutrophil tyrosine phosphorylation. J. Clin. Invest. 92, 1602-1603.
    • (1993) J. Clin. Invest. , vol.92 , pp. 1602-1603
    • Smallwood, J.I.1    Malawista, S.E.2
  • 32
    • 0014117442 scopus 로고
    • The mechanism of action of Colchicine
    • Borisy, G. G., Taylor, E. W. (1967) The mechanism of action of Colchicine. J. Cell Biol. 34, 525-534.
    • (1967) J. Cell Biol. , vol.34 , pp. 525-534
    • Borisy, G.G.1    Taylor, E.W.2
  • 33
    • 0026328348 scopus 로고
    • Interactions of Colchicine with tubulin
    • Hastie, S. B. (1991) Interactions of Colchicine with tubulin. Pharmacol. Ther. 51, 377-401.
    • (1991) Pharmacol. Ther. , vol.51 , pp. 377-401
    • Hastie, S.B.1
  • 34
    • 0026670898 scopus 로고
    • Taxol increases steady-state levels of lipopolysaccharide-inducible genes and protein-lyrosine phosphorylation in murine macrophages
    • Manthey, C. L., Brandes, M. E., Perera, P. Y., Vogel, S. N. (1992) Taxol increases steady-state levels of lipopolysaccharide-inducible genes and protein-lyrosine phosphorylation in murine macrophages. J. Immunol. 149, 2459-2465.
    • (1992) J. Immunol. , vol.149 , pp. 2459-2465
    • Manthey, C.L.1    Brandes, M.E.2    Perera, P.Y.3    Vogel, S.N.4
  • 35
    • 0027382375 scopus 로고
    • Taxol shares the ability of bacterial lipopolysaccharide to induce tyrosine phosphorylation of microtubule-associated protein kinase
    • Ding, A., Sanchez, E., Nathan, C. F. (1993) Taxol shares the ability of bacterial lipopolysaccharide to induce tyrosine phosphorylation of microtubule-associated protein kinase. J. Immunol. 151, 5596-5602.
    • (1993) J. Immunol. , vol.151 , pp. 5596-5602
    • Ding, A.1    Sanchez, E.2    Nathan, C.F.3
  • 36
    • 0029582940 scopus 로고
    • Interactions between the protein-tyrosine kinase ZAP-70, the proto-oncoprotein vav, and tubulin in jurkat t cells
    • Huby, R. D. J., Carlile, G. W., Ley, S. C. (1995) Interactions between the protein-tyrosine kinase ZAP-70, the proto-oncoprotein vav, and tubulin in jurkat t cells. J. Biol. Chem. 270, 30241-30244.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30241-30244
    • Huby, R.D.J.1    Carlile, G.W.2    Ley, S.C.3
  • 37
    • 0020368092 scopus 로고
    • Effect of microtubule-disrupting agents on Superoxide production in human polymorphonuclear leukocytes
    • Kitagawa, S., Takaku, F. (1982) Effect of microtubule-disrupting agents on Superoxide production in human polymorphonuclear leukocytes. Biochim. Biophys. Acta 719, 589-598.
    • (1982) Biochim. Biophys. Acta , vol.719 , pp. 589-598
    • Kitagawa, S.1    Takaku, F.2
  • 38
    • 0020573287 scopus 로고
    • Unsaturated fatty acids as second messengers of Superoxide generation by macrophages
    • Bromberg, Y., Pick, E. (1983) Unsaturated fatty acids as second messengers of Superoxide generation by macrophages. Cell. Immunol. 79, 240-252.
    • (1983) Cell. Immunol. , vol.79 , pp. 240-252
    • Bromberg, Y.1    Pick, E.2
  • 39
    • 0019504929 scopus 로고
    • Superoxide anion and hydrogen peroxide production by chemically elicited peritoneal macrophages. Induction by multiple nonphagocytic stimuli
    • Pick, E., Keisari, Y. (1981) Superoxide anion and hydrogen peroxide production by chemically elicited peritoneal macrophages. Induction by multiple nonphagocytic stimuli. Cell. Immunol. 59, 301-318.
    • (1981) Cell. Immunol. , vol.59 , pp. 301-318
    • Pick, E.1    Keisari, Y.2
  • 40
    • 0026705637 scopus 로고
    • Rapid priming of calcium mobilization and superoxide anion production in human neutrophils by substimulatory concentrations of phorbol esters: A novel role for protein kinase C and tyrosine phosphorylation in the up-modulation of signal transduction
    • Gilbert, C., Gaudry, M., Naccache, P. H. (1992) Rapid priming of calcium mobilization and superoxide anion production in human neutrophils by substimulatory concentrations of phorbol esters: a novel role for protein kinase C and tyrosine phosphorylation in the up-modulation of signal transduction. Cell. Signal. 4, 511-523.
    • (1992) Cell. Signal. , vol.4 , pp. 511-523
    • Gilbert, C.1    Gaudry, M.2    Naccache, P.H.3
  • 41
    • 0026795613 scopus 로고
    • Reconstitution of neutrophil NADPH oxidase activity in the cell-free system by 4 components - p67-phox, p47-phox, p21rac1, and cytochrome-6-245
    • Abo, A., Boyhan, A., West, I., Thrasher, A. J., Segal, A. W. (1992) Reconstitution of neutrophil NADPH oxidase activity in the cell-free system by 4 components - p67-phox, p47-phox, p21rac1, and cytochrome-6-245. J. Biol. Chem. 267, 16767-16770.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16767-16770
    • Abo, A.1    Boyhan, A.2    West, I.3    Thrasher, A.J.4    Segal, A.W.5
  • 42
    • 0026445719 scopus 로고
    • Tyrosine phosphorylation of paxillin and pp125(FAK) accompanies cell adhesion to extracellular matrix - a role in cytoskeletal assembly
    • Burridge, K., Turner, C. E., Romer, L. H. (1992) Tyrosine phosphorylation of paxillin and pp125(FAK) accompanies cell adhesion to extracellular matrix - a role in cytoskeletal assembly. J. Cell Biol. 119, 893-903.
    • (1992) J. Cell Biol. , vol.119 , pp. 893-903
    • Burridge, K.1    Turner, C.E.2    Romer, L.H.3
  • 43
    • 0027293670 scopus 로고
    • Detection of src homology 3-binding proteins, including paxillin, in normal and v-src-transformed balb/c 3t3 cells
    • Weng, Z. C., Taylor, J. A., Turner, C. E., Brugge, J.S., Seideldugan, C. (1993) Detection of src homology 3-binding proteins, including paxillin, in normal and v-src-transformed balb/c 3t3 cells. J. Biol. Chem. 268, 14956-14963.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14956-14963
    • Weng, Z.C.1    Taylor, J.A.2    Turner, C.E.3    Brugge, J.S.4    Seideldugan, C.5
  • 44
    • 0028049088 scopus 로고
    • Platelet-derived growth factor modulation of focal adhesion kinase (p125FAK) and paxillin tyrosine phosphorylation in swiss 3t3 cells - bell-shaped dose response and cross-talk with bombesin
    • Rankin, S., Rozengurt, E. (1994) Platelet-derived growth factor modulation of focal adhesion kinase (p125FAK) and paxillin tyrosine phosphorylation in swiss 3t3 cells - bell-shaped dose response and cross-talk with bombesin. J. Biol. Chem. 269, 704-710.
    • (1994) J. Biol. Chem. , vol.269 , pp. 704-710
    • Rankin, S.1    Rozengurt, E.2
  • 45
    • 0028145707 scopus 로고
    • Tyrosine phosphorylation of the gamma-subunit of Fc(gamma)-receplors, p72(syk), and paxillin during Fc-receptor-mediated phagocytosis in macrophages
    • Greenberg, S., Chang, P., Silverstein, S. C. (1994) Tyrosine phosphorylation of the gamma-subunit of Fc(gamma)-receplors, p72(syk), and paxillin during Fc-receptor-mediated phagocytosis in macrophages. J. Biol. Chem. 269, 3897-3902.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3897-3902
    • Greenberg, S.1    Chang, P.2    Silverstein, S.C.3
  • 46
    • 0027966390 scopus 로고
    • Paxillin - a cytoskeletal target for tyrosine kinases
    • Turner, C. E. (1994) Paxillin - a cytoskeletal target for tyrosine kinases. BioEssays 16, 47-52.
    • (1994) BioEssays , vol.16 , pp. 47-52
    • Turner, C.E.1
  • 47
    • 0027338195 scopus 로고
    • Involvement of p72(syk), a protein-tyrosine kinase, in Fc-gamma receptor signaling
    • Agarwal, A., Salem, P., Robbins, K. C. (1993) Involvement of p72(syk), a protein-tyrosine kinase, in Fc-gamma receptor signaling. J. Biol. Chem. 268, 15900-15905.
    • (1993) J. Biol. Chem. , vol.268 , pp. 15900-15905
    • Agarwal, A.1    Salem, P.2    Robbins, K.C.3
  • 48
    • 0027433056 scopus 로고
    • Activation of protein-tyrosine kinase p72(syk) with concanavalin A in polymorphonuclear neutrophils
    • Asahi, M., Taniguchi, T., Hashimoto, E., Inazu, T., Maeda, H., Yamamura, H. (1993) Activation of protein-tyrosine kinase p72(syk) with concanavalin A in polymorphonuclear neutrophils. J. Biol. Chem. 268, 23334-23338.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23334-23338
    • Asahi, M.1    Taniguchi, T.2    Hashimoto, E.3    Inazu, T.4    Maeda, H.5    Yamamura, H.6
  • 51
    • 0028998794 scopus 로고
    • Regulation of human leukocyte p21-activated kinases through G protein-coupled receptors
    • Knaus, U. G., Morris, S., Dong, H. J., Chernoff, J., Bokoch, G. M. (1995) Regulation of human leukocyte p21-activated kinases through G protein-coupled receptors. Science 269, 221-223.
    • (1995) Science , vol.269 , pp. 221-223
    • Knaus, U.G.1    Morris, S.2    Dong, H.J.3    Chernoff, J.4    Bokoch, G.M.5


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