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Volumn 29, Issue 4, 2008, Pages 551-564

Redox Regulation of Interleukin-4 Signaling

Author keywords

MOLIMMUNO

Indexed keywords

CYTOKINE RECEPTOR; ERYTHROPOIETIN; ERYTHROPOIETIN RECEPTOR; INSULIN RECEPTOR; INTERLEUKIN 3; INTERLEUKIN 3 RECEPTOR; INTERLEUKIN 4 RECEPTOR; NOX5L PROTEIN; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN TYROSINE PHOSPHATASE 1B; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE 1; TUMOR NECROSIS FACTOR ALPHA; TUMOR NECROSIS FACTOR ALPHA RECEPTOR; UNCLASSIFIED DRUG;

EID: 53349160071     PISSN: 10747613     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.immuni.2008.07.019     Document Type: Article
Times cited : (85)

References (57)
  • 3
    • 0036121371 scopus 로고    scopus 로고
    • Regulation of insulin-like growth factor type I (IGF-I) receptor kinase activity by protein tyrosine phosphatase 1B (PTP-1B) and enhanced IGF-I-mediated suppression of apoptosis and motility in PTP-1B-deficient fibroblasts
    • Buckley D.A., Cheng A., Kiely P.A., Tremblay M.L., and O'Connor R. Regulation of insulin-like growth factor type I (IGF-I) receptor kinase activity by protein tyrosine phosphatase 1B (PTP-1B) and enhanced IGF-I-mediated suppression of apoptosis and motility in PTP-1B-deficient fibroblasts. Mol. Cell. Biol. 22 (2002) 1998-2010
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 1998-2010
    • Buckley, D.A.1    Cheng, A.2    Kiely, P.A.3    Tremblay, M.L.4    O'Connor, R.5
  • 4
    • 33745815084 scopus 로고    scopus 로고
    • Nox1-dependent reactive oxygen generation is regulated by Rac1
    • Cheng G., Diebold B.A., Hughes Y., and Lambeth J.D. Nox1-dependent reactive oxygen generation is regulated by Rac1. J. Biol. Chem. 281 (2006) 17718-17726
    • (2006) J. Biol. Chem. , vol.281 , pp. 17718-17726
    • Cheng, G.1    Diebold, B.A.2    Hughes, Y.3    Lambeth, J.D.4
  • 6
    • 0032524583 scopus 로고    scopus 로고
    • Rac1, and not Rac2, is involved in the regulation of the intracellular hydrogen peroxide level in HepG2 cells
    • Cool R.H., Merten E., Theiss C., and Acker H. Rac1, and not Rac2, is involved in the regulation of the intracellular hydrogen peroxide level in HepG2 cells. Biochem. J. 332 (1998) 5-8
    • (1998) Biochem. J. , vol.332 , pp. 5-8
    • Cool, R.H.1    Merten, E.2    Theiss, C.3    Acker, H.4
  • 7
    • 0022503237 scopus 로고
    • The effect of the inhibitor diphenylene iodonium on the superoxide-generating system of neutrophils. Specific labelling of a component polypeptide of the oxidase
    • Cross A.R., and Jones O.T. The effect of the inhibitor diphenylene iodonium on the superoxide-generating system of neutrophils. Specific labelling of a component polypeptide of the oxidase. Biochem. J. 237 (1986) 111-116
    • (1986) Biochem. J. , vol.237 , pp. 111-116
    • Cross, A.R.1    Jones, O.T.2
  • 8
    • 0032080849 scopus 로고    scopus 로고
    • Inhibition of mitogen-activated protein kinase kinase blocks T cell proliferation but does not induce or prevent anergy
    • DeSilva D.R., Jones E.A., Favata M.F., Jaffee B.D., Magolda R.L., Trzaskos J.M., and Scherle P.A. Inhibition of mitogen-activated protein kinase kinase blocks T cell proliferation but does not induce or prevent anergy. J. Immunol. 160 (1998) 4175-4181
    • (1998) J. Immunol. , vol.160 , pp. 4175-4181
    • DeSilva, D.R.1    Jones, E.A.2    Favata, M.F.3    Jaffee, B.D.4    Magolda, R.L.5    Trzaskos, J.M.6    Scherle, P.A.7
  • 11
    • 0026324171 scopus 로고
    • Protein tyrosine phosphatases: A diverse family of intracellular and transmembrane enzymes
    • Fischer E.H., Charbonneau H., and Tonks N.K. Protein tyrosine phosphatases: A diverse family of intracellular and transmembrane enzymes. Science 253 (1991) 401-406
    • (1991) Science , vol.253 , pp. 401-406
    • Fischer, E.H.1    Charbonneau, H.2    Tonks, N.K.3
  • 12
    • 0031055324 scopus 로고    scopus 로고
    • Development of "substrate-trapping" mutants to identify physiological substrates of protein tyrosine phosphatases
    • Flint A.J., Tiganis T., Barford D., and Tonks N.K. Development of "substrate-trapping" mutants to identify physiological substrates of protein tyrosine phosphatases. Proc. Natl. Acad. Sci. USA 94 (1997) 1680-1685
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 1680-1685
    • Flint, A.J.1    Tiganis, T.2    Barford, D.3    Tonks, N.K.4
  • 13
    • 33744913842 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase gamma signaling through protein kinase Czeta induces NADPH oxidase-mediated oxidant generation and NF-kappaB activation in endothelial cells
    • Frey R.S., Gao X., Javaid K., Siddiqui S.S., Rahman A., and Malik A.B. Phosphatidylinositol 3-kinase gamma signaling through protein kinase Czeta induces NADPH oxidase-mediated oxidant generation and NF-kappaB activation in endothelial cells. J. Biol. Chem. 281 (2006) 16128-16138
    • (2006) J. Biol. Chem. , vol.281 , pp. 16128-16138
    • Frey, R.S.1    Gao, X.2    Javaid, K.3    Siddiqui, S.S.4    Rahman, A.5    Malik, A.B.6
  • 14
    • 33745978446 scopus 로고    scopus 로고
    • cAMP-response element-binding protein mediates acid-induced NADPH oxidase NOX5-S expression in Barrett esophageal adenocarcinoma cells
    • Fu X., Beer D.G., Behar J., Wands J., Lambeth D., and Cao W. cAMP-response element-binding protein mediates acid-induced NADPH oxidase NOX5-S expression in Barrett esophageal adenocarcinoma cells. J. Biol. Chem. 281 (2006) 20368-20382
    • (2006) J. Biol. Chem. , vol.281 , pp. 20368-20382
    • Fu, X.1    Beer, D.G.2    Behar, J.3    Wands, J.4    Lambeth, D.5    Cao, W.6
  • 15
    • 0034678730 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase inhibitors, Wortmannin or LY294002, inhibited accumulation of p21 protein after gamma-irradiation by stabilization of the protein
    • Fukuchi K., Watanabe H., Tomoyasu S., Ichimura S., Tatsumi K., and Gomi K. Phosphatidylinositol 3-kinase inhibitors, Wortmannin or LY294002, inhibited accumulation of p21 protein after gamma-irradiation by stabilization of the protein. Biochim. Biophys. Acta 1496 (2000) 207-220
    • (2000) Biochim. Biophys. Acta , vol.1496 , pp. 207-220
    • Fukuchi, K.1    Watanabe, H.2    Tomoyasu, S.3    Ichimura, S.4    Tatsumi, K.5    Gomi, K.6
  • 16
    • 0030603158 scopus 로고    scopus 로고
    • Inhibition of protein kinase C mu by various inhibitors. Differentiation from protein kinase c isoenzymes
    • Gschwendt M., Dieterich S., Rennecke J., Kittstein W., Mueller H.J., and Johannes F.J. Inhibition of protein kinase C mu by various inhibitors. Differentiation from protein kinase c isoenzymes. FEBS Lett. 392 (1996) 77-80
    • (1996) FEBS Lett. , vol.392 , pp. 77-80
    • Gschwendt, M.1    Dieterich, S.2    Rennecke, J.3    Kittstein, W.4    Mueller, H.J.5    Johannes, F.J.6
  • 17
    • 0032545279 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatase Shp-1 is a negative regulator of IL-4- and IL-13-dependent signal transduction
    • Haque S.J., Harbor P., Tabrizi M., Yi T., and Williams B.R. Protein-tyrosine phosphatase Shp-1 is a negative regulator of IL-4- and IL-13-dependent signal transduction. J. Biol. Chem. 273 (1998) 33893-33896
    • (1998) J. Biol. Chem. , vol.273 , pp. 33893-33896
    • Haque, S.J.1    Harbor, P.2    Tabrizi, M.3    Yi, T.4    Williams, B.R.5
  • 18
    • 0034714399 scopus 로고    scopus 로고
    • Identification of critical residues required for suppressor of cytokine signaling-specific regulation of interleukin-4 signaling
    • Haque S.J., Harbor P.C., and Williams B.R. Identification of critical residues required for suppressor of cytokine signaling-specific regulation of interleukin-4 signaling. J. Biol. Chem. 275 (2000) 26500-26506
    • (2000) J. Biol. Chem. , vol.275 , pp. 26500-26506
    • Haque, S.J.1    Harbor, P.C.2    Williams, B.R.3
  • 19
    • 33947714618 scopus 로고    scopus 로고
    • Interleukins and STAT signaling
    • Haque S.J., and Sharma P. Interleukins and STAT signaling. Vitam. Horm. 74 (2006) 165-206
    • (2006) Vitam. Horm. , vol.74 , pp. 165-206
    • Haque, S.J.1    Sharma, P.2
  • 21
    • 0027247814 scopus 로고
    • Resting myoplasmic free calcium in frog skeletal muscle fibers estimated with fluo-3
    • Harkins A.B., Kurebayashi N., and Baylor S.M. Resting myoplasmic free calcium in frog skeletal muscle fibers estimated with fluo-3. Biophys. J. 65 (1993) 865-881
    • (1993) Biophys. J. , vol.65 , pp. 865-881
    • Harkins, A.B.1    Kurebayashi, N.2    Baylor, S.M.3
  • 22
    • 0028838012 scopus 로고
    • Dimerization of cell surface receptors in signal transduction
    • Heldin C.H. Dimerization of cell surface receptors in signal transduction. Cell 80 (1995) 213-223
    • (1995) Cell , vol.80 , pp. 213-223
    • Heldin, C.H.1
  • 23
    • 0027938509 scopus 로고
    • Interleukin 4 receptor signaling in human monocytes and U937 cells involves the activation of a phosphatidylcholine-specific phospholipase C: A comparison with chemotactic peptide, FMLP, phospholipase D, and sphingomyelinase
    • Ho J.L., Zhu B., He S., Du B., and Rothman R. Interleukin 4 receptor signaling in human monocytes and U937 cells involves the activation of a phosphatidylcholine-specific phospholipase C: A comparison with chemotactic peptide, FMLP, phospholipase D, and sphingomyelinase. J. Exp. Med. 180 (1994) 1457-1469
    • (1994) J. Exp. Med. , vol.180 , pp. 1457-1469
    • Ho, J.L.1    Zhu, B.2    He, S.3    Du, B.4    Rothman, R.5
  • 24
    • 0028037158 scopus 로고
    • Possible role of tyrosine kinase activity in interleukin 4-induced expression of germ-line C epsilon transcripts in a human Burkitt lymphoma B-cell line, DND39
    • Ikizawa K., Kajiwara K., Koshio T., and Yanagihara Y. Possible role of tyrosine kinase activity in interleukin 4-induced expression of germ-line C epsilon transcripts in a human Burkitt lymphoma B-cell line, DND39. J. Allergy Clin. Immunol. 94 (1994) 620-624
    • (1994) J. Allergy Clin. Immunol. , vol.94 , pp. 620-624
    • Ikizawa, K.1    Kajiwara, K.2    Koshio, T.3    Yanagihara, Y.4
  • 25
    • 0034607083 scopus 로고    scopus 로고
    • Possible involvement of Shc in IL-4-induced germline epsilon transcription in a human B cell line
    • Ikizawa K., and Yanagihara Y. Possible involvement of Shc in IL-4-induced germline epsilon transcription in a human B cell line. Biochem. Biophys. Res. Commun. 268 (2000) 54-59
    • (2000) Biochem. Biophys. Res. Commun. , vol.268 , pp. 54-59
    • Ikizawa, K.1    Yanagihara, Y.2
  • 26
    • 33847697219 scopus 로고    scopus 로고
    • Novel mechanism of activation of NADPH oxidase 5. calcium sensitization via phosphorylation
    • Jagnandan D., Church J.E., Banfi B., Stuehr D.J., Marrero M.B., and Fulton D.J. Novel mechanism of activation of NADPH oxidase 5. calcium sensitization via phosphorylation. J. Biol. Chem. 282 (2007) 6494-6507
    • (2007) J. Biol. Chem. , vol.282 , pp. 6494-6507
    • Jagnandan, D.1    Church, J.E.2    Banfi, B.3    Stuehr, D.J.4    Marrero, M.B.5    Fulton, D.J.6
  • 27
    • 0028316195 scopus 로고
    • Induction of apoptotic DNA fragmentation and cell death in HL-60 human promyelocytic leukemia cells by pharmacological inhibitors of protein kinase C
    • Jarvis W.D., Turner A.J., Povirk L.F., Traylor R.S., and Grant S. Induction of apoptotic DNA fragmentation and cell death in HL-60 human promyelocytic leukemia cells by pharmacological inhibitors of protein kinase C. Cancer Res. 54 (1994) 1707-1714
    • (1994) Cancer Res. , vol.54 , pp. 1707-1714
    • Jarvis, W.D.1    Turner, A.J.2    Povirk, L.F.3    Traylor, R.S.4    Grant, S.5
  • 28
    • 24744468043 scopus 로고    scopus 로고
    • Point mutations in the proline-rich region of p22phox are dominant inhibitors of Nox1- and Nox2-dependent reactive oxygen generation
    • Kawahara T., Ritsick D., Cheng G., and Lambeth J.D. Point mutations in the proline-rich region of p22phox are dominant inhibitors of Nox1- and Nox2-dependent reactive oxygen generation. J. Biol. Chem. 280 (2005) 31859-31869
    • (2005) J. Biol. Chem. , vol.280 , pp. 31859-31869
    • Kawahara, T.1    Ritsick, D.2    Cheng, G.3    Lambeth, J.D.4
  • 29
    • 0025731835 scopus 로고
    • Nitric oxide: An endogenous modulator of leukocyte adhesion
    • Kubes P., Suzuki M., and Granger D.N. Nitric oxide: An endogenous modulator of leukocyte adhesion. Proc. Natl. Acad. Sci. USA 88 (1991) 4651-4655
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 4651-4655
    • Kubes, P.1    Suzuki, M.2    Granger, D.N.3
  • 30
    • 1542406446 scopus 로고    scopus 로고
    • NOX enzymes and the biology of reactive oxygen
    • Lambeth J.D. NOX enzymes and the biology of reactive oxygen. Nat. Rev. Immunol. 4 (2004) 181-189
    • (2004) Nat. Rev. Immunol. , vol.4 , pp. 181-189
    • Lambeth, J.D.1
  • 31
    • 34250888056 scopus 로고    scopus 로고
    • Regulation of Nox and Duox enzymatic activity and expression
    • Lambeth J.D., Kawahara T., and Diebold B. Regulation of Nox and Duox enzymatic activity and expression. Free Radic. Biol. Med. 43 (2007) 319-331
    • (2007) Free Radic. Biol. Med. , vol.43 , pp. 319-331
    • Lambeth, J.D.1    Kawahara, T.2    Diebold, B.3
  • 32
    • 0032546955 scopus 로고    scopus 로고
    • Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor
    • Lee S.R., Kwon K.S., Kim S.R., and Rhee S.G. Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor. J. Biol. Chem. 273 (1998) 15366-15372
    • (1998) J. Biol. Chem. , vol.273 , pp. 15366-15372
    • Lee, S.R.1    Kwon, K.S.2    Kim, S.R.3    Rhee, S.G.4
  • 33
    • 0035877633 scopus 로고    scopus 로고
    • Insulin-stimulated hydrogen peroxide reversibly inhibits protein-tyrosine phosphatase 1b in vivo and enhances the early insulin action cascade
    • Mahadev K., Zilbering A., Zhu L., and Goldstein B.J. Insulin-stimulated hydrogen peroxide reversibly inhibits protein-tyrosine phosphatase 1b in vivo and enhances the early insulin action cascade. J. Biol. Chem. 276 (2001) 21938-21942
    • (2001) J. Biol. Chem. , vol.276 , pp. 21938-21942
    • Mahadev, K.1    Zilbering, A.2    Zhu, L.3    Goldstein, B.J.4
  • 34
    • 25844490385 scopus 로고    scopus 로고
    • Serine phosphorylation of Stat6 negatively controls its DNA-binding function
    • Maiti N.R., Sharma P., Harbor P.C., and Haque S.J. Serine phosphorylation of Stat6 negatively controls its DNA-binding function. J. Interferon Cytokine Res. 25 (2005) 553-563
    • (2005) J. Interferon Cytokine Res. , vol.25 , pp. 553-563
    • Maiti, N.R.1    Sharma, P.2    Harbor, P.C.3    Haque, S.J.4
  • 35
    • 0036184190 scopus 로고    scopus 로고
    • Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo
    • Meng T.C., Fukada T., and Tonks N.K. Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo. Mol. Cell 9 (2002) 387-399
    • (2002) Mol. Cell , vol.9 , pp. 387-399
    • Meng, T.C.1    Fukada, T.2    Tonks, N.K.3
  • 37
    • 4444334342 scopus 로고    scopus 로고
    • Dexamethasone blocks hypoxia-induced endothelial dysfunction in organ-cultured pulmonary arteries
    • Murata T., Hori M., Sakamoto K., Karaki H., and Ozaki H. Dexamethasone blocks hypoxia-induced endothelial dysfunction in organ-cultured pulmonary arteries. Am. J. Respir. Crit. Care Med. 170 (2004) 647-655
    • (2004) Am. J. Respir. Crit. Care Med. , vol.170 , pp. 647-655
    • Murata, T.1    Hori, M.2    Sakamoto, K.3    Karaki, H.4    Ozaki, H.5
  • 40
    • 0037718255 scopus 로고    scopus 로고
    • Evaluation of the probes 2′,7′-dichlorofluorescin diacetate, luminol, and lucigenin as indicators of reactive species formation
    • Myhre O., Andersen J.M., Aarnes H., and Fonnum F. Evaluation of the probes 2′,7′-dichlorofluorescin diacetate, luminol, and lucigenin as indicators of reactive species formation. Biochem. Pharmacol. 65 (2003) 1575-1582
    • (2003) Biochem. Pharmacol. , vol.65 , pp. 1575-1582
    • Myhre, O.1    Andersen, J.M.2    Aarnes, H.3    Fonnum, F.4
  • 42
    • 0036233585 scopus 로고    scopus 로고
    • Cytokine signaling in 2002: New surprises in the Jak/Stat pathway
    • O'Shea J.J., Gadina M., and Schreiber R.D. Cytokine signaling in 2002: New surprises in the Jak/Stat pathway. Cell 109 Suppl (2002) S121-S131
    • (2002) Cell , vol.109 , Issue.SUPPL
    • O'Shea, J.J.1    Gadina, M.2    Schreiber, R.D.3
  • 43
    • 0023124410 scopus 로고
    • Receptors for B-cell stimulatory factor-1 expressed on cells of haematopoietic lineage
    • Ohara J., and Paul W.E. Receptors for B-cell stimulatory factor-1 expressed on cells of haematopoietic lineage. Nature 325 (1987) 537-540
    • (1987) Nature , vol.325 , pp. 537-540
    • Ohara, J.1    Paul, W.E.2
  • 44
    • 2942628119 scopus 로고    scopus 로고
    • Sequential activation of phosphatidylinositol 3-kinase, beta Pix, Rac1, and Nox1 in growth factor-induced production of H2O2
    • Park H.S., Lee S.H., Park D., Lee J.S., Ryu S.H., Lee W.J., Rhee S.G., and Bae Y.S. Sequential activation of phosphatidylinositol 3-kinase, beta Pix, Rac1, and Nox1 in growth factor-induced production of H2O2. Mol. Cell. Biol. 24 (2004) 4384-4394
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 4384-4394
    • Park, H.S.1    Lee, S.H.2    Park, D.3    Lee, J.S.4    Ryu, S.H.5    Lee, W.J.6    Rhee, S.G.7    Bae, Y.S.8
  • 45
    • 1242342002 scopus 로고    scopus 로고
    • Preferential oxidation of the second phosphatase domain of receptor-like PTP-alpha revealed by an antibody against oxidized protein tyrosine phosphatases
    • Persson C., Sjoblom T., Groen A., Kappert K., Engstrom U., Hellman U., Heldin C.H., den Hertog J., and Ostman A. Preferential oxidation of the second phosphatase domain of receptor-like PTP-alpha revealed by an antibody against oxidized protein tyrosine phosphatases. Proc. Natl. Acad. Sci. USA 101 (2004) 1886-1891
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 1886-1891
    • Persson, C.1    Sjoblom, T.2    Groen, A.3    Kappert, K.4    Engstrom, U.5    Hellman, U.6    Heldin, C.H.7    den Hertog, J.8    Ostman, A.9
  • 46
    • 33646343978 scopus 로고    scopus 로고
    • Illuminating insights into protein-protein interactions using bioluminescence resonance energy transfer (BRET)
    • Pfleger K.D., and Eidne K.A. Illuminating insights into protein-protein interactions using bioluminescence resonance energy transfer (BRET). Nat. Methods 3 (2006) 165-174
    • (2006) Nat. Methods , vol.3 , pp. 165-174
    • Pfleger, K.D.1    Eidne, K.A.2
  • 47
    • 0031459486 scopus 로고    scopus 로고
    • Nifedipine, an L-type calcium channel blocker, restores the hypnotic response in rats made tolerant to the alpha-2 adrenergic agonist dexmedetomidine
    • Reid K., Guo T.Z., Davies M.F., and Maze M. Nifedipine, an L-type calcium channel blocker, restores the hypnotic response in rats made tolerant to the alpha-2 adrenergic agonist dexmedetomidine. J. Pharmacol. Exp. Ther. 283 (1997) 993-999
    • (1997) J. Pharmacol. Exp. Ther. , vol.283 , pp. 993-999
    • Reid, K.1    Guo, T.Z.2    Davies, M.F.3    Maze, M.4
  • 48
    • 0034633602 scopus 로고    scopus 로고
    • Hydrogen peroxide: A key messenger that modulates protein phosphorylation through cysteine oxidation
    • Rhee S.G., Bae Y.S., Lee S.R., and Kwon J. Hydrogen peroxide: A key messenger that modulates protein phosphorylation through cysteine oxidation. Sci. STKE 2000 (2000) PE1
    • (2000) Sci. STKE , vol.2000
    • Rhee, S.G.1    Bae, Y.S.2    Lee, S.R.3    Kwon, J.4
  • 49
    • 0038411479 scopus 로고    scopus 로고
    • Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate
    • Salmeen A., Andersen J.N., Myers M.P., Meng T.C., Hinks J.A., Tonks N.K., and Barford D. Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate. Nature 423 (2003) 769-773
    • (2003) Nature , vol.423 , pp. 769-773
    • Salmeen, A.1    Andersen, J.N.2    Myers, M.P.3    Meng, T.C.4    Hinks, J.A.5    Tonks, N.K.6    Barford, D.7
  • 50
    • 0028925051 scopus 로고
    • Heparin-insensitive calcium release from intracellular stores triggered by the recombinant human parathyroid hormone receptor
    • Seuwen K., and Boddeke H.G. Heparin-insensitive calcium release from intracellular stores triggered by the recombinant human parathyroid hormone receptor. Br. J. Pharmacol. 114 (1995) 1613-1620
    • (1995) Br. J. Pharmacol. , vol.114 , pp. 1613-1620
    • Seuwen, K.1    Boddeke, H.G.2
  • 51
    • 0032527809 scopus 로고    scopus 로고
    • Invasion of T-lymphoma cells: Cooperation between Rho family GTPases and lysophospholipid receptor signaling
    • Stam J.C., Michiels F., van der Kammen R.A., Moolenaar W.H., and Collard J.G. Invasion of T-lymphoma cells: Cooperation between Rho family GTPases and lysophospholipid receptor signaling. EMBO J. 17 (1998) 4066-4074
    • (1998) EMBO J. , vol.17 , pp. 4066-4074
    • Stam, J.C.1    Michiels, F.2    van der Kammen, R.A.3    Moolenaar, W.H.4    Collard, J.G.5
  • 52
    • 0019333905 scopus 로고
    • New calcium indicators and buffers with high selectivity against magnesium and protons: Design, synthesis, and properties of prototype structures
    • Tsien R.Y. New calcium indicators and buffers with high selectivity against magnesium and protons: Design, synthesis, and properties of prototype structures. Biochemistry 19 (1980) 2396-2404
    • (1980) Biochemistry , vol.19 , pp. 2396-2404
    • Tsien, R.Y.1
  • 53
    • 0038749600 scopus 로고    scopus 로고
    • Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B
    • van Montfort R.L., Congreve M., Tisi D., Carr R., and Jhoti H. Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B. Nature 423 (2003) 773-777
    • (2003) Nature , vol.423 , pp. 773-777
    • van Montfort, R.L.1    Congreve, M.2    Tisi, D.3    Carr, R.4    Jhoti, H.5
  • 54
    • 0034673663 scopus 로고    scopus 로고
    • IL-4 regulation of IL-6 production involves Rac/Cdc42- and p38 MAPK-dependent pathways in keratinocytes
    • Wery-Zennaro S., Zugaza J.L., Letourneur M., Bertoglio J., and Pierre J. IL-4 regulation of IL-6 production involves Rac/Cdc42- and p38 MAPK-dependent pathways in keratinocytes. Oncogene 19 (2000) 1596-1604
    • (2000) Oncogene , vol.19 , pp. 1596-1604
    • Wery-Zennaro, S.1    Zugaza, J.L.2    Letourneur, M.3    Bertoglio, J.4    Pierre, J.5
  • 55
    • 0037047335 scopus 로고    scopus 로고
    • CD45 controls interleukin-4-mediated IgE class switch recombination in human B cells through its function as a Janus kinase phosphatase
    • Yamada T., Zhu D., Saxon A., and Zhang K. CD45 controls interleukin-4-mediated IgE class switch recombination in human B cells through its function as a Janus kinase phosphatase. J. Biol. Chem. 277 (2002) 28830-28835
    • (2002) J. Biol. Chem. , vol.277 , pp. 28830-28835
    • Yamada, T.1    Zhu, D.2    Saxon, A.3    Zhang, K.4
  • 56
    • 0032534060 scopus 로고    scopus 로고
    • Generation of a novel stem cell factor-dependent mast cell progenitor
    • Yuan Q., Gurish M.F., Friend D.S., Austen K.F., and Boyce J.A. Generation of a novel stem cell factor-dependent mast cell progenitor. J. Immunol. 161 (1998) 5143-5146
    • (1998) J. Immunol. , vol.161 , pp. 5143-5146
    • Yuan, Q.1    Gurish, M.F.2    Friend, D.S.3    Austen, K.F.4    Boyce, J.A.5
  • 57
    • 0141992862 scopus 로고    scopus 로고
    • Phosphatidylcholine-specific phospholipase C activity is necessary for the activation of STAT6
    • Zamorano J., Rivas M.D., Garcia-Trinidad A., Qu C.K., and Keegan A.D. Phosphatidylcholine-specific phospholipase C activity is necessary for the activation of STAT6. J. Immunol. 171 (2003) 4203-4209
    • (2003) J. Immunol. , vol.171 , pp. 4203-4209
    • Zamorano, J.1    Rivas, M.D.2    Garcia-Trinidad, A.3    Qu, C.K.4    Keegan, A.D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.