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Volumn 243, Issue 1, 1998, Pages 161-172

Endocytosed epidermal growth factor (EGF) receptors contribute to the EGF-mediated growth arrest in A431 cells by inducing a sustained increase in p21/CIP1

Author keywords

Bafilomycin A1; Endocytosed EGF receptor; Growth suppression; Monensin; P21 CIP1; Signal transduction

Indexed keywords

ADENOSINE TRIPHOSPHATASE; BAFILOMYCIN A1; EPIDERMAL GROWTH FACTOR; EPIDERMAL GROWTH FACTOR RECEPTOR; MONENSIN; TRANSFORMING GROWTH FACTOR ALPHA;

EID: 0032566271     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1006/excr.1998.4127     Document Type: Article
Times cited : (43)

References (50)
  • 1
    • 0025343230 scopus 로고
    • Signal transduction by receptors with tyrosine kinase activity
    • Ullrich, A., and Schlessinger, J. (1990). Signal transduction by receptors with tyrosine kinase activity. Cell 61, 203-212.
    • (1990) Cell , vol.61 , pp. 203-212
    • Ullrich, A.1    Schlessinger, J.2
  • 2
    • 0025321157 scopus 로고
    • Epidermal growth factor
    • Carpenter, G., and Cohen, S. (1990). Epidermal growth factor. J. Biol. Chem. 265, 7709-7712.
    • (1990) J. Biol. Chem. , vol.265 , pp. 7709-7712
    • Carpenter, G.1    Cohen, S.2
  • 3
    • 0028175091 scopus 로고
    • Raf meets Raf: Completing the framework of a signal transduction pathway
    • Avruch, J., Zhang, X.-F., and Kyriakis, J. M. (1994). Raf meets Raf: Completing the framework of a signal transduction pathway. Trends Biochem. Sci. 19, 279-283.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 279-283
    • Avruch, J.1    Zhang, X.-F.2    Kyriakis, J.M.3
  • 4
    • 0027279176 scopus 로고
    • How receptor tyrosine kinases activate Ras
    • Schlessinger, J. (1993). How receptor tyrosine kinases activate Ras. Trends Biochem. Sci. 18, 273-275.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 273-275
    • Schlessinger, J.1
  • 5
    • 0020039865 scopus 로고
    • Epidermal growth factor inhibits growth of A431 human epidermoid carcinoma in serum free culture
    • Barnes, D. W. (1982). Epidermal growth factor inhibits growth of A431 human epidermoid carcinoma in serum free culture. J. Cell Biol. 93, 1-4.
    • (1982) J. Cell Biol. , vol.93 , pp. 1-4
    • Barnes, D.W.1
  • 6
    • 0021256312 scopus 로고
    • Epidermal growth factor inhibits the synthesis of the nuclear protein cyclin in A431 human carcinoma cells
    • Bravo, R. (1984). Epidermal growth factor inhibits the synthesis of the nuclear protein cyclin in A431 human carcinoma cells. Proc. Natl. Acad. Sci. USA 81, 4848-4850.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 4848-4850
    • Bravo, R.1
  • 7
    • 0019861187 scopus 로고
    • Increased phosphotyrosine content and inhibition of proliferation in EGF-treated A431 cells
    • Gill, G. N., and Lazar, C. S. (1981). Increased phosphotyrosine content and inhibition of proliferation in EGF-treated A431 cells. Nature 293, 305-307.
    • (1981) Nature , vol.293 , pp. 305-307
    • Gill, G.N.1    Lazar, C.S.2
  • 9
    • 0028980376 scopus 로고
    • Cip1/WAF1/CDK2/PCNA complex by epidermal growth factor receptor activation mediate ligand-induced A431 cell growth inhibition
    • Cip1/WAF1/CDK2/PCNA complex by epidermal growth factor receptor activation mediate ligand-induced A431 cell growth inhibition. J. Cell Biol. 131, 235-242.
    • (1995) J. Cell Biol. , vol.131 , pp. 235-242
    • Fan, Z.1    Lu, Y.2    Wu, X.3    DeBlasio, A.4    Koff, A.5    Mendelsohn, J.6
  • 10
    • 0030013561 scopus 로고    scopus 로고
    • Growth inhibitory concentrations of EGF induce p21 (WAF1/Cip1) and alter cell cycle control in squamous carcinoma cells
    • Jakus, J., and Yeudall, W. A. (1996). Growth inhibitory concentrations of EGF induce p21 (WAF1/Cip1) and alter cell cycle control in squamous carcinoma cells. Oncogene 12, 2369-2376.
    • (1996) Oncogene , vol.12 , pp. 2369-2376
    • Jakus, J.1    Yeudall, W.A.2
  • 11
    • 0027385186 scopus 로고
    • Induction by EGF and interferon-γ of tyrosine phosphorylated DNA binding proteins in mouse liver nuclei
    • Ruff-Jamison, S., Chen, K., and Cohen, S. (1993). Induction by EGF and interferon-γ of tyrosine phosphorylated DNA binding proteins in mouse liver nuclei. Science 261, 1733-1736.
    • (1993) Science , vol.261 , pp. 1733-1736
    • Ruff-Jamison, S.1    Chen, K.2    Cohen, S.3
  • 12
    • 0028085525 scopus 로고
    • Epidermal growth factor and lipopolysaccharide activate Stat3 transcription factor in mouse liver
    • Ruff-Jamison, S., Zhong, Z., Wen, Z., Chen, K., Darnell, J. E., Jr., and Cohen, S. (1994). Epidermal growth factor and lipopolysaccharide activate Stat3 transcription factor in mouse liver. J. Biol. Chem. 269, 21933-21935.
    • (1994) J. Biol. Chem. , vol.269 , pp. 21933-21935
    • Ruff-Jamison, S.1    Zhong, Z.2    Wen, Z.3    Chen, K.4    Darnell J.E., Jr.5    Cohen, S.6
  • 13
    • 0027408634 scopus 로고
    • Cell-free activation of a DNA-binding protein by epidermal growth factor
    • Sadowski, H. B., and Gilman, M. Z. (1993). Cell-free activation of a DNA-binding protein by epidermal growth factor. Nature 362, 79-83.
    • (1993) Nature , vol.362 , pp. 79-83
    • Sadowski, H.B.1    Gilman, M.Z.2
  • 14
    • 0028349735 scopus 로고
    • Stat3: A STAT family member activated by tyrosine phosphorylation in response to epidermal growth factor and interleukin-6
    • Zhong, Z., Wen, Z., and Darnell, J. E., Jr. (1994). Stat3: A STAT family member activated by tyrosine phosphorylation in response to epidermal growth factor and interleukin-6. Science 264, 95-98.
    • (1994) Science , vol.264 , pp. 95-98
    • Zhong, Z.1    Wen, Z.2    Darnell J.E., Jr.3
  • 15
    • 0028950805 scopus 로고
    • Recruitment of epidermal growth factor receptors into coated pits requires their activated tyrosine kinase
    • Lamaze, C., and Schmid, S. L. (1995). Recruitment of epidermal growth factor receptors into coated pits requires their activated tyrosine kinase. J. Cell Biol. 129, 47-54.
    • (1995) J. Cell Biol. , vol.129 , pp. 47-54
    • Lamaze, C.1    Schmid, S.L.2
  • 16
    • 0025359062 scopus 로고
    • Kinase activity controls the sorting of the epidermal growth factor receptor within the multivesicular body
    • Felder, S., Miller, K., Moehren, G., Ullrich, A., Schlessinger, J., and Hopkins, C. R. (1990). Kinase activity controls the sorting of the epidermal growth factor receptor within the multivesicular body. Cell 61, 623-634.
    • (1990) Cell , vol.61 , pp. 623-634
    • Felder, S.1    Miller, K.2    Moehren, G.3    Ullrich, A.4    Schlessinger, J.5    Hopkins, C.R.6
  • 17
    • 0025370578 scopus 로고
    • Separate endocytotic pathways of kinase-defective and active EGF receptor mutants expressed in same cell
    • Honegger, A. M., Schmidt, A., Ullrich, A., and Schlessinger, J. (1990). Separate endocytotic pathways of kinase-defective and active EGF receptor mutants expressed in same cell. J. Cell Biol. 110, 1541-1548.
    • (1990) J. Cell Biol. , vol.110 , pp. 1541-1548
    • Honegger, A.M.1    Schmidt, A.2    Ullrich, A.3    Schlessinger, J.4
  • 18
    • 0028021551 scopus 로고
    • Phosphorylation of the epidermal growth factor receptor during internalization in A-431 cells
    • Nesterov, A., Lysan, S., Vdovina, I., Nikolsky, N., and Fujita, D. J. (1994). Phosphorylation of the epidermal growth factor receptor during internalization in A-431 cells. Arch. Biochem. Biophys. 313, 351-359.
    • (1994) Arch. Biochem. Biophys. , vol.313 , pp. 351-359
    • Nesterov, A.1    Lysan, S.2    Vdovina, I.3    Nikolsky, N.4    Fujita, D.J.5
  • 19
    • 0029554655 scopus 로고
    • Endosomes, receptor tyrosine kinase internalization and signal transduction
    • Bergeron, J. J., DiGuglielmo, G. M., Baass, P. C., Authier, F., and Posner, B. I. (1995). Endosomes, receptor tyrosine kinase internalization and signal transduction. Biosci. Rep. 15, 411-418.
    • (1995) Biosci. Rep. , vol.15 , pp. 411-418
    • Bergeron, J.J.1    DiGuglielmo, G.M.2    Baass, P.C.3    Authier, F.4    Posner, B.I.5
  • 20
    • 0027965262 scopus 로고
    • Compartmentalization of SHC, GRB2 and mSOS, and hyperphosphorylation of Raf-1 by EGF but not insulin in liver parenchyma
    • DiGuglielmo, G. M., Baass, P. C., Ou, W.-J., Posner, B. I., and Bergeron, J. J. M. (1994). Compartmentalization of SHC, GRB2 and mSOS, and hyperphosphorylation of Raf-1 by EGF but not insulin in liver parenchyma. EMBO J. 13, 4269-4277.
    • (1994) EMBO J. , vol.13 , pp. 4269-4277
    • DiGuglielmo, G.M.1    Baass, P.C.2    Ou, W.-J.3    Posner, B.I.4    Bergeron, J.J.M.5
  • 21
    • 0030461226 scopus 로고    scopus 로고
    • Control of EGF receptor signaling by clathrin-mediated endocytosis
    • Vieira, A. V., Lamaze, C., and Schmid, S. L. (1996). Control of EGF receptor signaling by clathrin-mediated endocytosis. Science 274, 2086-2089.
    • (1996) Science , vol.274 , pp. 2086-2089
    • Vieira, A.V.1    Lamaze, C.2    Schmid, S.L.3
  • 22
    • 0025070201 scopus 로고
    • Epidermal growth factor and transforming growth factor-alpha induce differential processing of the epidermal growth factor receptor
    • Decker, S. J. (1990). Epidermal growth factor and transforming growth factor-alpha induce differential processing of the epidermal growth factor receptor. Biochem. Biophys. Res. Commun. 166, 615-621.
    • (1990) Biochem. Biophys. Res. Commun. , vol.166 , pp. 615-621
    • Decker, S.J.1
  • 23
    • 14844349947 scopus 로고
    • Epidermal growth factor and transforming growth factor-α: Differential intracellular routing and processing of ligand-receptor complexes
    • Ebner, R., and Derynck, R. (1991). Epidermal growth factor and transforming growth factor-α: Differential intracellular routing and processing of ligand-receptor complexes. Cell Regul. 2, 599-612.
    • (1991) Cell Regul. , vol.2 , pp. 599-612
    • Ebner, R.1    Derynck, R.2
  • 24
    • 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
  • 25
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Staehelin, T., and 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    Staehelin, T.2    Gordon, J.3
  • 26
    • 0023924799 scopus 로고
    • The endocytosis of epidermal growth factor in A431 cells: A pH of microenvironment and the dynamics of receptor complex dissociation
    • Sorkin, A. D., Teslenko, L. V., and Nikolsky, N. N. (1988). The endocytosis of epidermal growth factor in A431 cells: A pH of microenvironment and the dynamics of receptor complex dissociation. Exp. Cell Res. 175, 192-205.
    • (1988) Exp. Cell Res. , vol.175 , pp. 192-205
    • Sorkin, A.D.1    Teslenko, L.V.2    Nikolsky, N.N.3
  • 27
    • 0025895762 scopus 로고
    • Activation of mitogen-activated protein kinase in BC3H1 myocytes by fluoroaluminate
    • Anderson, N. G., Kilgour, E., and Sturgill, T. W. (1991). Activation of mitogen-activated protein kinase in BC3H1 myocytes by fluoroaluminate. J. Biol. Chem. 266, 10131-10135.
    • (1991) J. Biol. Chem. , vol.266 , pp. 10131-10135
    • Anderson, N.G.1    Kilgour, E.2    Sturgill, T.W.3
  • 28
    • 0025830053 scopus 로고
    • Recent progress in characterization of protein kinase cascades for phosphorylation of ribosomal protein S6
    • Sturgill, T. W., and Wu, J. (1991). Recent progress in characterization of protein kinase cascades for phosphorylation of ribosomal protein S6. Biochim. Biophys. Acta 1092, 350-357.
    • (1991) Biochim. Biophys. Acta , vol.1092 , pp. 350-357
    • Sturgill, T.W.1    Wu, J.2
  • 29
    • 0022555867 scopus 로고
    • Acidification of the endocytotic and exocytotic pathways
    • Mellman, I., Fuchs, R., and Helenius, A. (1986). Acidification of the endocytotic and exocytotic pathways. Annu. Rev. Biochem. 55, 663-700.
    • (1986) Annu. Rev. Biochem. , vol.55 , pp. 663-700
    • Mellman, I.1    Fuchs, R.2    Helenius, A.3
  • 30
    • 0021331201 scopus 로고
    • Metabolic products of microorganisms. 224.Bafilomycins, a new group of macrolide antibiotics. Production, isolation, chemical structure and biological activity
    • Werner, G., Hagenmaier, H., Drautz, H., Baumgartner, A., and Zahner, H. (1984). Metabolic products of microorganisms. 224.Bafilomycins, a new group of macrolide antibiotics. Production, isolation, chemical structure and biological activity. J. Antibiot. 37, 110-117.
    • (1984) J. Antibiot. , vol.37 , pp. 110-117
    • Werner, G.1    Hagenmaier, H.2    Drautz, H.3    Baumgartner, A.4    Zahner, H.5
  • 32
    • 0024230493 scopus 로고
    • Rapid constitutive internalization and externalization of epidermal growth factor receptors in isolated rat hepatocytes
    • Gladhaug, I. P., and Christoffersen, T. (1988). Rapid constitutive internalization and externalization of epidermal growth factor receptors in isolated rat hepatocytes. J. Biol. Chem. 263, 12199-12203.
    • (1988) J. Biol. Chem. , vol.263 , pp. 12199-12203
    • Gladhaug, I.P.1    Christoffersen, T.2
  • 33
    • 0025359062 scopus 로고
    • Kinase activity controls the sorting of the epidermal growth factor receptor within the multivesicular body
    • Felder, S., Miller, K., Moehren, G., Ullrich, A., Schlessinger, J., and Hopkins, C. R. (1990). Kinase activity controls the sorting of the epidermal growth factor receptor within the multivesicular body. Cell 61, 623-634.
    • (1990) Cell , vol.61 , pp. 623-634
    • Felder, S.1    Miller, K.2    Moehren, G.3    Ullrich, A.4    Schlessinger, J.5    Hopkins, C.R.6
  • 34
    • 0028110831 scopus 로고
    • Relationship between the MAP kinase activity and the dual effect of EGF on A431 cell proliferation
    • Chajry, N., Martin, P.-M., Pages, G., Cochet, C., Afdel, K., and Berthois, Y. (1994). Relationship between the MAP kinase activity and the dual effect of EGF on A431 cell proliferation. Biochem. Biophys. Res. Commun. 203, 984-990.
    • (1994) Biochem. Biophys. Res. Commun. , vol.203 , pp. 984-990
    • Chajry, N.1    Martin, P.-M.2    Pages, G.3    Cochet, C.4    Afdel, K.5    Berthois, Y.6
  • 35
    • 0030024480 scopus 로고    scopus 로고
    • Regulation of p42 mitogen-activated protein kinase activity by protein phosphatase 2A under conditions of growth inhibition by epidermal growth factor in A431 cells
    • Chajry, N., Martin, P.-M., Cochet, C., and Berthois, Y. (1996). Regulation of p42 mitogen-activated protein kinase activity by protein phosphatase 2A under conditions of growth inhibition by epidermal growth factor in A431 cells. Eur. J. Biochem. 235, 97-102.
    • (1996) Eur. J. Biochem. , vol.235 , pp. 97-102
    • Chajry, N.1    Martin, P.-M.2    Cochet, C.3    Berthois, Y.4
  • 36
    • 0026540969 scopus 로고
    • Association of the tyrosine phosphorylated epidermal growth factor receptor with a 55-kD tyrosine phosphorylated protein at the cell surface and in endosomes
    • Wada, I., Lai, W. H., Posner, B. I., and Bergeron, J. J. (1992). Association of the tyrosine phosphorylated epidermal growth factor receptor with a 55-kD tyrosine phosphorylated protein at the cell surface and in endosomes. J. Cell Biol. 116, 321-330.
    • (1992) J. Cell Biol. , vol.116 , pp. 321-330
    • Wada, I.1    Lai, W.H.2    Posner, B.I.3    Bergeron, J.J.4
  • 37
    • 0027401986 scopus 로고
    • Epidermal growth factor stimulates the tyrosine phosphorylation of SHC in the mouse
    • Ruff-Jamison, S., Mc-Glade, J., Pawson, T., Chen, K., and Cohen, S. (1993). Epidermal growth factor stimulates the tyrosine phosphorylation of SHC in the mouse. J. Biol. Chem. 268, 7610-7612.
    • (1993) J. Biol. Chem. , vol.268 , pp. 7610-7612
    • Ruff-Jamison, S.1    Mc-Glade, J.2    Pawson, T.3    Chen, K.4    Cohen, S.5
  • 38
    • 0028872649 scopus 로고
    • Specificity of receptor tyrosine kinase signaling: Transient versus sustained extracellular signal-regulated kinase activation
    • Marshall, C. J. (1995). Specificity of receptor tyrosine kinase signaling: Transient versus sustained extracellular signal-regulated kinase activation. Cell 80, 179-185.
    • (1995) Cell , vol.80 , pp. 179-185
    • Marshall, C.J.1
  • 39
    • 0013599467 scopus 로고
    • Nerve growth factor receptors on human melanoma cells in culture
    • Fabricant, R. N., DeLarco, J. E., and Todaro, G. J. (1977). Nerve growth factor receptors on human melanoma cells in culture. Proc. Natl. Acad. Sci. USA 74, 565-569.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 565-569
    • Fabricant, R.N.1    DeLarco, J.E.2    Todaro, G.J.3
  • 40
    • 0342965191 scopus 로고
    • Visualization by fluorescence of the binding and internalization of epidermal growth factor in human carcinoma cells A-431
    • Haigler, H., Ash, J. F., Singer, S. J., and Cohen, S. (1978). Visualization by fluorescence of the binding and internalization of epidermal growth factor in human carcinoma cells A-431. Proc. Natl. Acad. Sci. USA 75, 3317-3321.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 3317-3321
    • Haigler, H.1    Ash, J.F.2    Singer, S.J.3    Cohen, S.4
  • 41
    • 0023677140 scopus 로고
    • Anomalous binding of epidermal growth factor to A431 cells is due to the effect of high receptor densities and a saturable endocytotic system
    • Wiley, H. S. (1988). Anomalous binding of epidermal growth factor to A431 cells is due to the effect of high receptor densities and a saturable endocytotic system. J. Cell Biol. 107, 801-810.
    • (1988) J. Cell Biol. , vol.107 , pp. 801-810
    • Wiley, H.S.1
  • 42
    • 0018774018 scopus 로고
    • Direct visualization of the binding and internalization of a ferritin conjugate of epidermal growth factor in human carcinoma cells A-431
    • Haigler, H. T., McKanna, J. A., and Cohen, S. (1979). Direct visualization of the binding and internalization of a ferritin conjugate of epidermal growth factor in human carcinoma cells A-431. J. Cell Biol. 81, 382-395.
    • (1979) J. Cell Biol. , vol.81 , pp. 382-395
    • Haigler, H.T.1    McKanna, J.A.2    Cohen, S.3
  • 43
    • 0018569173 scopus 로고
    • Hormone receptor topology and dynamics: Morphological analysis using ferritin-labeled epidermal growth factor
    • McKanna, J. A., Haigler, H. T., and Cohen, S. (1979). Hormone receptor topology and dynamics: Morphological analysis using ferritin-labeled epidermal growth factor. Proc. Natl. Acad. Sci. USA 76, 5689-5693.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 5689-5693
    • McKanna, J.A.1    Haigler, H.T.2    Cohen, S.3
  • 44
    • 0019826025 scopus 로고
    • Rotational diffusion of epidermal growth factor complexed to cell surface receptors reflects rapid microaggregation and endocytosis of occupied receptors
    • Zidovetzki, R., Yarden, Y., Schlessinger, J., and Jovin, T. M. (1981). Rotational diffusion of epidermal growth factor complexed to cell surface receptors reflects rapid microaggregation and endocytosis of occupied receptors. Proc. Natl. Acad. Sci. USA 78, 6981-6985.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 6981-6985
    • Zidovetzki, R.1    Yarden, Y.2    Schlessinger, J.3    Jovin, T.M.4
  • 45
    • 0020771261 scopus 로고
    • The morphologic pathway of binding and internalization of epidermal growth factor in cultured cells. Studies on A431, KB, and 3T3 cells, using multiple methods of labeling
    • Willingham, M. C., Haigler, H. T., Fitzgerald, D. J., Gallo, M. G., Rutherford, A. V., and Pastan, I. H. (1983). The morphologic pathway of binding and internalization of epidermal growth factor in cultured cells. Studies on A431, KB, and 3T3 cells, using multiple methods of labeling. Exp. Cell Res. 146, 163-175.
    • (1983) Exp. Cell Res. , vol.146 , pp. 163-175
    • Willingham, M.C.1    Haigler, H.T.2    Fitzgerald, D.J.3    Gallo, M.G.4    Rutherford, A.V.5    Pastan, I.H.6
  • 46
    • 0020335070 scopus 로고
    • 125I-epidermal growth factor and ferritin-low density lipoprotein in coated pits: A quantitative electron microscopic study in normal and mutant fibroblasts
    • 125I-epidermal growth factor and ferritin-low density lipoprotein in coated pits: A quantitative electron microscopic study in normal and mutant fibroblasts. J. Cell Biol. 95, 73-77.
    • (1982) J. Cell Biol. , vol.95 , pp. 73-77
    • Carpentier, J.L.1    Gorden, P.2    Anderson, R.G.3    Goldstein, J.L.4    Brown, M.S.5    Cohen, S.6    Orci, L.7
  • 47
    • 0019945866 scopus 로고
    • The endocytotic rate constant. A cellular parameter for quantitating receptor-mediated endocytosis
    • Wiley, H. S., and Cunningham, D. D. (1982). The endocytotic rate constant. A cellular parameter for quantitating receptor-mediated endocytosis. J. Biol. Chem. 257, 4222-4229.
    • (1982) J. Biol. Chem. , vol.257 , pp. 4222-4229
    • Wiley, H.S.1    Cunningham, D.D.2
  • 48
    • 0029928671 scopus 로고    scopus 로고
    • Tumor necrosis factor a: Posttranscriptional stabilization of WAF1 mRNA in p53-deficient human leukemic cells
    • Shiohara, M., Akashi, M., Gombart, A. F., Yang, R., and Koeffler, H. P. (1996). Tumor necrosis factor a: Posttranscriptional stabilization of WAF1 mRNA in p53-deficient human leukemic cells. J. Cell. Physiol. 166, 568-576.
    • (1996) J. Cell. Physiol. , vol.166 , pp. 568-576
    • Shiohara, M.1    Akashi, M.2    Gombart, A.F.3    Yang, R.4    Koeffler, H.P.5
  • 49
    • 0028874866 scopus 로고
    • IL-1 induces expression of WAF1 mRNA in human fibroblasts: Mechanisms of accumulation
    • Osawa, Y., Hachiya, M., Koeffler, H. P., Suzuki, G., and Akashi, M. (1995). IL-1 induces expression of WAF1 mRNA in human fibroblasts: Mechanisms of accumulation. Biochem. Biophys. Res. Commun. 13, 429-437.
    • (1995) Biochem. Biophys. Res. Commun. , vol.13 , pp. 429-437
    • Osawa, Y.1    Hachiya, M.2    Koeffler, H.P.3    Suzuki, G.4    Akashi, M.5
  • 50
    • 0029976068 scopus 로고    scopus 로고
    • CCAAT/enhancer-binding protein alpha (C/EBP alpha) inhibits cell proliferation through the p21 (WAF-1/CIP-1/SDI-1) protein
    • Timchenko, N. A., Wilde, M., Nakanishi, M., Smith, J. R., and Darlington, G. J. (1996). CCAAT/enhancer-binding protein alpha (C/EBP alpha) inhibits cell proliferation through the p21 (WAF-1/CIP-1/SDI-1) protein. Genes Dev. 10, 804-815.
    • (1996) Genes Dev. , vol.10 , pp. 804-815
    • Timchenko, N.A.1    Wilde, M.2    Nakanishi, M.3    Smith, J.R.4    Darlington, G.J.5


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