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Volumn 177, Issue 3, 2006, Pages 1492-1499

Phosphorylation of nonmuscle myosin heavy chain IIA on Ser1917 is mediated by protein kinase CβII and coincides with the onset of stimulated degranulation of RBL-2H3 mast cells

Author keywords

[No Author keywords available]

Indexed keywords

12 (2 CYANOETHYL) 6,7,12,13 TETRAHYDRO 13 METHYL 5 OXOINDOLO[2,3 A]PYRROLO[3,4 C]CARBAZOLE; CALCIMYCIN; MYOSIN IIA; PHORBOL 13 ACETATE 12 MYRISTATE; PHOSPHOPROTEIN PHOSPHATASE 2A; PROTEIN KINASE C ALPHA; PROTEIN KINASE C BETA; PROTEIN KINASE C BETAI; PROTEIN KINASE C BETAII; SERINE; UNCLASSIFIED DRUG;

EID: 33746215280     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: 10.4049/jimmunol.177.3.1492     Document Type: Article
Times cited : (42)

References (53)
  • 2
    • 10344222887 scopus 로고    scopus 로고
    • The ins and outs of IgE-dependent mast-cell exocytosis
    • Blank, U., and J. Rivera. 2004. The ins and outs of IgE-dependent mast-cell exocytosis. Trends Immunol. 25: 266-273.
    • (2004) Trends Immunol. , vol.25 , pp. 266-273
    • Blank, U.1    Rivera, J.2
  • 3
    • 0022371565 scopus 로고
    • Membrane and cytoskeletal changes associated with IgE-mediated serotonin release from rat basophilic leukemia cells
    • Pfeiffer, J. R., S. C. Seagrave, B. H. Davis, G. G. Deanin, and J. M. Oliver. 1985. Membrane and cytoskeletal changes associated with IgE-mediated serotonin release from rat basophilic leukemia cells. J. Cell Biol. 101: 2145-2155.
    • (1985) J. Cell Biol. , vol.101 , pp. 2145-2155
    • Pfeiffer, J.R.1    Seagrave, S.C.2    Davis, B.H.3    Deanin, G.G.4    Oliver, J.M.5
  • 4
    • 0023550959 scopus 로고
    • Rat basophilic leukemia cells stiffen when they secrete
    • Liu, Z. Y., J. I. Young, and E. L. Elson. 1987. Rat basophilic leukemia cells stiffen when they secrete. J. Cell Biol. 105: 2933-2943.
    • (1987) J. Cell Biol. , vol.105 , pp. 2933-2943
    • Liu, Z.Y.1    Young, J.I.2    Elson, E.L.3
  • 5
    • 0026090189 scopus 로고
    • Regulation of the antigen-induced F-actin response in rat basophilic leukemia cells by protein kinase C
    • Apgar, J. R. 1991. Regulation of the antigen-induced F-actin response in rat basophilic leukemia cells by protein kinase C. J. Cell Biol. 112: 1157-1163.
    • (1991) J. Cell Biol. , vol.112 , pp. 1157-1163
    • Apgar, J.R.1
  • 6
    • 0028153071 scopus 로고
    • PMA and calcium ionophore induce myosin and F-actin rearrangement during histamine secretion from RBL-2H3 cells
    • Ludowyke, R. I., K. Kawasugi, and P. W. French. 1994. PMA and calcium ionophore induce myosin and F-actin rearrangement during histamine secretion from RBL-2H3 cells. Cell Motil. Cytoskeleton 29: 354-365.
    • (1994) Cell Motil. Cytoskeleton , vol.29 , pp. 354-365
    • Ludowyke, R.I.1    Kawasugi, K.2    French, P.W.3
  • 7
    • 0036198540 scopus 로고    scopus 로고
    • Protein phosphatases 1 and 2A transiently associate with myosin during the peak rate of secretion from mast cells
    • Holst, J., A. T. Sim, and R. I. Ludowyke. 2002. Protein phosphatases 1 and 2A transiently associate with myosin during the peak rate of secretion from mast cells. Mol. Biol. Cell 13: 1083-1098.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1083-1098
    • Holst, J.1    Sim, A.T.2    Ludowyke, R.I.3
  • 8
    • 0029731663 scopus 로고    scopus 로고
    • Structure-function analysis of the motor domain of myosin
    • Ruppel, K. M., and J. A. Spudich. 1996. Structure-function analysis of the motor domain of myosin. Annu. Rev. Cell. Dev. Biol. 12: 543-573.
    • (1996) Annu. Rev. Cell. Dev. Biol. , vol.12 , pp. 543-573
    • Ruppel, K.M.1    Spudich, J.A.2
  • 9
    • 0034677906 scopus 로고    scopus 로고
    • Myosins: A diverse superfamily
    • Sellers, J. R. 2000. Myosins: a diverse superfamily. Biochim. Biophys. Acta 1496: 3-22.
    • (2000) Biochim. Biophys. Acta , vol.1496 , pp. 3-22
    • Sellers, J.R.1
  • 10
    • 0030054719 scopus 로고    scopus 로고
    • Regulation of class 1 and class II myosins by heavy chain phosphorylation
    • Brzeska, H., and E. D. Korn. 1996. Regulation of class 1 and class II myosins by heavy chain phosphorylation. J. Biol. Chem. 271: 16983-16986.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16983-16986
    • Brzeska, H.1    Korn, E.D.2
  • 11
    • 0033005168 scopus 로고    scopus 로고
    • Molecular mechanisms of nonmuscle myosin-II regulation
    • Bresnick, A. R. 1999. Molecular mechanisms of nonmuscle myosin-II regulation. Curr. Opin. Cell Biol. 11: 26-33.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 26-33
    • Bresnick, A.R.1
  • 14
    • 0029891947 scopus 로고    scopus 로고
    • Cloning of the cDNA encoding rat myosin heavy chain-A and evidence for the absence of myosin heavy chain-B in cultured rat mast (RBL-2H3) cells
    • Choi, O. H., C. S. Park, K. Itoh, R. S. Adelstein, and M. A. Beaven. 1996. Cloning of the cDNA encoding rat myosin heavy chain-A and evidence for the absence of myosin heavy chain-B in cultured rat mast (RBL-2H3) cells. J. Muscle Res. Cell Motil. 17: 69-77.
    • (1996) J. Muscle Res. Cell Motil. , vol.17 , pp. 69-77
    • Choi, O.H.1    Park, C.S.2    Itoh, K.3    Adelstein, R.S.4    Beaven, M.A.5
  • 15
    • 0026093527 scopus 로고
    • Identification of the serine residue phosphorylated by protein kinase C in vertebrate nonmuscle myosin heavy chains
    • Conti, M. A., J. R. Sellers, R. S. Adelstein, and M. Elzinga. 1991. Identification of the serine residue phosphorylated by protein kinase C in vertebrate nonmuscle myosin heavy chains. Biochemistry 30: 966-970.
    • (1991) Biochemistry , vol.30 , pp. 966-970
    • Conti, M.A.1    Sellers, J.R.2    Adelstein, R.S.3    Elzinga, M.4
  • 16
    • 0027769523 scopus 로고
    • Phosphorylation of vertebrate nonmuscle and smooth muscle myosin heavy chains and light chains
    • Moussavi, R. S., C. A. Kelley, and R. S. Adelstein. 1993. Phosphorylation of vertebrate nonmuscle and smooth muscle myosin heavy chains and light chains. Mol. Cell. Biochem. 127-128: 219-227.
    • (1993) Mol. Cell. Biochem. , vol.127-128 , pp. 219-227
    • Moussavi, R.S.1    Kelley, C.A.2    Adelstein, R.S.3
  • 17
    • 0028825025 scopus 로고
    • Phospholipid binding, phosphorylation by protein kinase C, and filament assembly of the COOH terminal heavy chain fragments of nonmuscle myosin II isoforms MIIA and MIIB
    • Murakami, N., S. S. Singh, V. P. Chauhan, and M. Elzinga. 1995. Phospholipid binding, phosphorylation by protein kinase C, and filament assembly of the COOH terminal heavy chain fragments of nonmuscle myosin II isoforms MIIA and MIIB. Biochemistry 34: 16046-16055.
    • (1995) Biochemistry , vol.34 , pp. 16046-16055
    • Murakami, N.1    Singh, S.S.2    Chauhan, V.P.3    Elzinga, M.4
  • 18
    • 0347986633 scopus 로고    scopus 로고
    • Emerging and diverse roles of protein kinase C in immune cell signalling
    • Tan, S. L., and P. J. Parker. 2003. Emerging and diverse roles of protein kinase C in immune cell signalling. Biochem. J. 376: 545-552.
    • (2003) Biochem. J. , vol.376 , pp. 545-552
    • Tan, S.L.1    Parker, P.J.2
  • 20
    • 0031571712 scopus 로고    scopus 로고
    • Functional effects of overexpression of protein kinase C-α, -β, -δ, -ε, and -η in the mast cell line RBL-2H3
    • Chang, E. Y., Z. Szallasi, P. Acs, V. Raizada, P. C. Wolfe, C. Fewtrell, P. M. Blumberg, and J. Rivera. 1997. Functional effects of overexpression of protein kinase C-α, -β, -δ, -ε, and -η in the mast cell line RBL-2H3. J. Immunol. 159: 2624-2632.
    • (1997) J. Immunol. , vol.159 , pp. 2624-2632
    • Chang, E.Y.1    Szallasi, Z.2    Acs, P.3    Raizada, V.4    Wolfe, P.C.5    Fewtrell, C.6    Blumberg, P.M.7    Rivera, J.8
  • 21
    • 0035016243 scopus 로고    scopus 로고
    • Protein kinase C θ is expressed in mast cells and is functionally involved in Fceεeceptor 1 signaling
    • Liu, Y., C. Graham, V. Parravicini, M. J. Brown, J. Rivera, and S. Shaw. 2001. Protein kinase C θ is expressed in mast cells and is functionally involved in Fceεeceptor 1 signaling. J. Leukocyte. Biol. 69: 831-840.
    • (2001) J. Leukocyte. Biol. , vol.69 , pp. 831-840
    • Liu, Y.1    Graham, C.2    Parravicini, V.3    Brown, M.J.4    Rivera, J.5    Shaw, S.6
  • 22
    • 0035044915 scopus 로고    scopus 로고
    • Studies of different aspects of the role of protein kinase C in mast cells
    • Nechushtan, H., and E. Razin. 2001. Studies of different aspects of the role of protein kinase C in mast cells. Int. Arch. Allergy Immunol. 124: 130-132.
    • (2001) Int. Arch. Allergy Immunol. , vol.124 , pp. 130-132
    • Nechushtan, H.1    Razin, E.2
  • 23
    • 0034161386 scopus 로고    scopus 로고
    • Inhibition of degranulalion and interleukin-6 production in mast cells derived from mice deficient in protein kinase Cβ
    • Nechushtan, H., M. Leitges, C. Cohen, G. Kay, and E. Razin. 2000. Inhibition of degranulalion and interleukin-6 production in mast cells derived from mice deficient in protein kinase Cβ. Blood 95: 1752-1757.
    • (2000) Blood , vol.95 , pp. 1752-1757
    • Nechushtan, H.1    Leitges, M.2    Cohen, C.3    Kay, G.4    Razin, E.5
  • 24
    • 0029119988 scopus 로고
    • Focal adhesion formation is associated with secretion of allergic mediators
    • Kawasugi, K., P. W. French, R. Penny, and R. I. Ludowyke. 1995. Focal adhesion formation is associated with secretion of allergic mediators. Cell Motil. Cytoskeleton 31: 215-224.
    • (1995) Cell Motil. Cytoskeleton , vol.31 , pp. 215-224
    • Kawasugi, K.1    French, P.W.2    Penny, R.3    Ludowyke, R.I.4
  • 25
    • 0025281303 scopus 로고
    • Establishment of a pancreatic β cell line that retains glucose-inducible insulin secretion: Special reference to expression of glucose transporter isoforms
    • Miyazaki, J., K. Araki, E. Yamato, H. Ikegami, T. Asano, Y. Shibasaki, Y. Oka, and K. Yamamura. 1990. Establishment of a pancreatic β cell line that retains glucose-inducible insulin secretion: special reference to expression of glucose transporter isoforms. Endocrinology 127: 126-132.
    • (1990) Endocrinology , vol.127 , pp. 126-132
    • Miyazaki, J.1    Araki, K.2    Yamato, E.3    Ikegami, H.4    Asano, T.5    Shibasaki, Y.6    Oka, Y.7    Yamamura, K.8
  • 26
    • 0036230225 scopus 로고    scopus 로고
    • Expression profiling of palmitate- and oleate-regulated genes provides novel insights into the effects of chronic lipid exposure on pancreatic β cell function
    • Busch, A. K., D. Cordery, G. S. Denyer, and T. J. Biden. 2002. Expression profiling of palmitate- and oleate-regulated genes provides novel insights into the effects of chronic lipid exposure on pancreatic β cell function. Diabetes 51: 977-987.
    • (2002) Diabetes , vol.51 , pp. 977-987
    • Busch, A.K.1    Cordery, D.2    Denyer, G.S.3    Biden, T.J.4
  • 27
    • 0035895998 scopus 로고    scopus 로고
    • Protein kinase Cδ activation by interleukin-1β stabilizes inducible nitric-oxide synthase mRNA in pancreatic β cells
    • Carpenter, L., D. Cordery, and T. J. Biden. 2001. Protein kinase Cδ activation by interleukin-1β stabilizes inducible nitric-oxide synthase mRNA in pancreatic β cells. J. Biol. Chem. 276: 5368-5374.
    • (2001) J. Biol. Chem. , vol.276 , pp. 5368-5374
    • Carpenter, L.1    Cordery, D.2    Biden, T.J.3
  • 28
    • 3042546955 scopus 로고    scopus 로고
    • Phospholipase D1 regulates secretagogue-stimulated insulin release in pancreatic β cells
    • Hughes, W. E., Z. Elgundi, P. Huang, M. A. Frohman, and T. J. Biden. 2004. Phospholipase D1 regulates secretagogue-stimulated insulin release in pancreatic β cells. J. Biol. Chem. 279: 27534-27541.
    • (2004) J. Biol. Chem. , vol.279 , pp. 27534-27541
    • Hughes, W.E.1    Elgundi, Z.2    Huang, P.3    Frohman, M.A.4    Biden, T.J.5
  • 29
    • 0029073925 scopus 로고
    • Synergistic interaction of Y1-neuropeptide Y and α1b-adrenergic receptors in the regulation of phospholipase C, protein kinase C, and arachidonic acid production
    • Selbie, L. A., K. Darby, C. Schmitz-Peiffer, C. L. Browne, H. Herzog, J. Shine, and T. J. Biden. 1995. Synergistic interaction of Y1-neuropeptide Y and α1b-adrenergic receptors in the regulation of phospholipase C, protein kinase C, and arachidonic acid production. J. Biol. Chem. 270: 11789-11796.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11789-11796
    • Selbie, L.A.1    Darby, K.2    Schmitz-Peiffer, C.3    Browne, C.L.4    Herzog, H.5    Shine, J.6    Biden, T.J.7
  • 31
    • 0000714961 scopus 로고    scopus 로고
    • Regulation of protein kinase cascades by protein phosphatase 2A
    • Millward, T. A., S. Zolnierowicz, and B. A. Hemmings. 1999. Regulation of protein kinase cascades by protein phosphatase 2A. Trends Biochem. Sci. 24: 186-191.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 186-191
    • Millward, T.A.1    Zolnierowicz, S.2    Hemmings, B.A.3
  • 34
    • 0027394147 scopus 로고
    • Different isozymes of protein kinase C mediate feedback inhibition of phospholipase C and stimulatory signals for exocytosis in rat RBL-2H3 cells
    • Ozawa, K., K. Yamada, M. G. Kazanietz, P. M. Blumberg, and M. A. Beaven. 1993. Different isozymes of protein kinase C mediate feedback inhibition of phospholipase C and stimulatory signals for exocytosis in rat RBL-2H3 cells. J. Biol. Chem. 268: 2280-2283.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2280-2283
    • Ozawa, K.1    Yamada, K.2    Kazanietz, M.G.3    Blumberg, P.M.4    Beaven, M.A.5
  • 35
    • 0346729966 scopus 로고    scopus 로고
    • PKCα is activated but not required during glucose-induced insulin secretion from rat pancreatic islets
    • Carpenter, L., C. J. Mitchell, Z. Z. Xu, P. Poronnik, G. W. Both, and T. J. Biden. 2004. PKCα is activated but not required during glucose-induced insulin secretion from rat pancreatic islets. Diabetes 53: 53-60.
    • (2004) Diabetes , vol.53 , pp. 53-60
    • Carpenter, L.1    Mitchell, C.J.2    Xu, Z.Z.3    Poronnik, P.4    Both, G.W.5    Biden, T.J.6
  • 36
    • 0030001021 scopus 로고    scopus 로고
    • Protein kinase C βII specifically binds to and is activated by F-actin
    • Blobe, G. C., D. S. Stribling, D. Fabbro, S. Stabel, and Y. A. Hannun. 1996. Protein kinase C βII specifically binds to and is activated by F-actin. J. Biol. Chem. 271: 15823-15830.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15823-15830
    • Blobe, G.C.1    Stribling, D.S.2    Fabbro, D.3    Stabel, S.4    Hannun, Y.A.5
  • 37
    • 0001093453 scopus 로고
    • Secretion from rat basophilic RBL-2H3 cells is associated with diphosphorylation of myosin light chains by myosin light chain kinase as well as phosphorylation by protein kinase C
    • Choi, O. H., R. S. Adelstein, and M. A. Beaven. 1994. Secretion from rat basophilic RBL-2H3 cells is associated with diphosphorylation of myosin light chains by myosin light chain kinase as well as phosphorylation by protein kinase C. J. Biol. Chem. 269: 536-541.
    • (1994) J. Biol. Chem. , vol.269 , pp. 536-541
    • Choi, O.H.1    Adelstein, R.S.2    Beaven, M.A.3
  • 38
    • 0025240003 scopus 로고
    • The 1989 Upjohn Award lecture: Cellular and molecular mechanisms in hormone and neurotransmitter secretion
    • Trifaro, J. M. 1990. The 1989 Upjohn Award lecture: cellular and molecular mechanisms in hormone and neurotransmitter secretion. Can. J. Physiol. Pharmacol. 68: 1-16.
    • (1990) Can. J. Physiol. Pharmacol. , vol.68 , pp. 1-16
    • Trifaro, J.M.1
  • 39
    • 0033174147 scopus 로고    scopus 로고
    • Rac regulates phosphorylation of the myosin-11 heavy chain, actinomyosin disassembly and cell spreading
    • van Leeuwen, F. N., S. van Delft, H. E. Kain, R. A. van der Kammen, and J. G. Collard. 1999. Rac regulates phosphorylation of the myosin-11 heavy chain, actinomyosin disassembly and cell spreading. Nat. Cell Biol. 1: 242-248.
    • (1999) Nat. Cell Biol. , vol.1 , pp. 242-248
    • Van Leeuwen, F.N.1    Van Delft, S.2    Kain, H.E.3    Van Der Kammen, R.A.4    Collard, J.G.5
  • 41
    • 0034687146 scopus 로고    scopus 로고
    • Two distinct mechanisms for regulation of nonmuscle myosin assembly via the heavy chain: Phosphorylation for MIIB and mts 1 binding for MIIA
    • Murakami, N., L. Kotula, and Y. W. Hwang. 2000. Two distinct mechanisms for regulation of nonmuscle myosin assembly via the heavy chain: phosphorylation for MIIB and mts 1 binding for MIIA. Biochemistry 39: 11441-11451.
    • (2000) Biochemistry , vol.39 , pp. 11441-11451
    • Murakami, N.1    Kotula, L.2    Hwang, Y.W.3
  • 42
    • 0032575599 scopus 로고    scopus 로고
    • 2+-dependent threonine phosphorylation of myosin heavy chain in rat pancreatic islets and RINm5F cells
    • 2+-dependent threonine phosphorylation of myosin heavy chain in rat pancreatic islets and RINm5F cells. J. Biol. Chem. 273: 22729-22737.
    • (1998) J. Biol. Chem. , vol.273 , pp. 22729-22737
    • Wilson, J.R.1    Ludowyke, R.I.2    Biden, T.J.3
  • 44
    • 0033499353 scopus 로고    scopus 로고
    • Increases in phosphorylation of the myosin II heavy chain, but not regulatory light chains, correlate with insulin secretion in rat pancreatic islets and RINm5F cells
    • Wilson, J. R., T. J. Biden, and R. I. Ludowyke. 1999. Increases in phosphorylation of the myosin II heavy chain, but not regulatory light chains, correlate with insulin secretion in rat pancreatic islets and RINm5F cells. Diabetes 48: 2383-2389.
    • (1999) Diabetes , vol.48 , pp. 2383-2389
    • Wilson, J.R.1    Biden, T.J.2    Ludowyke, R.I.3
  • 45
    • 0034602323 scopus 로고    scopus 로고
    • Calcium-dependent threonine phosphorylation of nonmuscle myosin in stimulated RBL-2H3 mast cells
    • Buxton, D. B., and R. S. Adelstein. 2000. Calcium-dependent threonine phosphorylation of nonmuscle myosin in stimulated RBL-2H3 mast cells. J. Biol. Chem. 275: 34772-34779.
    • (2000) J. Biol. Chem. , vol.275 , pp. 34772-34779
    • Buxton, D.B.1    Adelstein, R.S.2
  • 46
    • 0025095403 scopus 로고
    • Amino acid sequence around the serine phosphorylated by casein kinase II in brain myosin heavy chain
    • Murakami, N., G. Healy-Louie, and M. Elzinga. 1990. Amino acid sequence around the serine phosphorylated by casein kinase II in brain myosin heavy chain. J. Biol. Chem. 265: 1041-1047.
    • (1990) J. Biol. Chem. , vol.265 , pp. 1041-1047
    • Murakami, N.1    Healy-Louie, G.2    Elzinga, M.3
  • 47
    • 0024362253 scopus 로고
    • Antigen-induced secretion of histamine and the phosphorylation of myosin by protein kinase C in rat basophilic leukemia cells
    • Ludowyke, R. I., I. Peleg, M. A. Beaven, and R. S. Adelstein. 1989. Antigen-induced secretion of histamine and the phosphorylation of myosin by protein kinase C in rat basophilic leukemia cells. J. Biol. Chem. 264: 12492-12501.
    • (1989) J. Biol. Chem. , vol.264 , pp. 12492-12501
    • Ludowyke, R.I.1    Peleg, I.2    Beaven, M.A.3    Adelstein, R.S.4
  • 48
  • 49
    • 0034845686 scopus 로고    scopus 로고
    • Myosin II heavy chain isoforms are phosphorylated in an EGF-dependent manner: Involvement of protein kinase C
    • Straussman, R., L. Even, and S. Ravid. 2001. Myosin II heavy chain isoforms are phosphorylated in an EGF-dependent manner: involvement of protein kinase C. J. Cell Sci. 114: 3047-3057.
    • (2001) J. Cell Sci. , vol.114 , pp. 3047-3057
    • Straussman, R.1    Even, L.2    Ravid, S.3
  • 50
    • 0036854481 scopus 로고    scopus 로고
    • Protein kinase Cβ (PKCβ): Normal functions and diseases
    • Kawakami, T., Y. Kawakami, and J. Kitaura. 2002. Protein kinase Cβ (PKCβ): normal functions and diseases. J. Biochem. 132: 677-682.
    • (2002) J. Biochem. , vol.132 , pp. 677-682
    • Kawakami, T.1    Kawakami, Y.2    Kitaura, J.3
  • 52
    • 0035669720 scopus 로고    scopus 로고
    • Protein kinase C and the development of diabetic vascular complications
    • Way, K. J., N. Katai, and G. L. King. 2001. Protein kinase C and the development of diabetic vascular complications. Diabet. Med. 18: 945-959.
    • (2001) Diabet. Med. , vol.18 , pp. 945-959
    • Way, K.J.1    Katai, N.2    King, G.L.3
  • 53
    • 0035866371 scopus 로고    scopus 로고
    • Elevated protein kinase C 311 is an early promotive event in colon carcinogenesis
    • Gokmen-Polar, Y., N. R. Murray, M. A. Velasco, Z. Gatalica, and A. P. Fields. 2001. Elevated protein kinase C (311 is an early promotive event in colon carcinogenesis. Cancer Res. 61: 1375-1381.
    • (2001) Cancer Res. , vol.61 , pp. 1375-1381
    • Gokmen-Polar, Y.1    Murray, N.R.2    Velasco, M.A.3    Gatalica, Z.4    Fields, A.P.5


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