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Volumn 32, Issue 3, 2006, Pages 314-320

Calcineurin-dependent and calcineurin-independent signal transduction pathways activated as part of pancreatic growth

Author keywords

Camostat; Cholecystokinin; FK506; MAPKs; Pancreatic growth

Indexed keywords

CALCINEURIN; CALPAIN; CAMOSTAT; CHOLECYSTOKININ; GASTROINTESTINAL HORMONE; INITIATION FACTOR 1; MAMMALIAN TARGET OF RAPAMYCIN; MITOGEN ACTIVATED PROTEIN KINASE; PROTEIN KINASE; PROTEIN S6; RIBOSOME PROTEIN; STRESS ACTIVATED PROTEIN KINASE; TACROLIMUS; CAMOSTAT MESILATE; DRUG DERIVATIVE; GABEXATE; INITIATION FACTOR 4E;

EID: 33646694284     PISSN: 08853177     EISSN: None     Source Type: Journal    
DOI: 10.1097/01.mpa.0000218316.12577.c0     Document Type: Article
Times cited : (16)

References (51)
  • 1
    • 0022509410 scopus 로고
    • Plasma cholecystokinin and pancreatic growth during adaptation to dietary protein
    • Green GM, Levan VH, Liddle RA. Plasma cholecystokinin and pancreatic growth during adaptation to dietary protein. Am J Physiol. 1986;251:G70-G74.
    • (1986) Am J Physiol , vol.251
    • Green, G.M.1    Levan, V.H.2    Liddle, R.A.3
  • 2
    • 0019207223 scopus 로고
    • Trophic effects of gestation and lactation on rat pancreas
    • Jolicoeur L. Trophic effects of gestation and lactation on rat pancreas. Biomed Res. 1980;1:482-488.
    • (1980) Biomed Res , vol.1 , pp. 482-488
    • Jolicoeur, L.1
  • 3
    • 0017327664 scopus 로고
    • Effects of partial surgical pancreatectomy in rats. I. Pancreatic regeneration
    • Pearson KW, Scott D, Torrance B. Effects of partial surgical pancreatectomy in rats. I. Pancreatic regeneration. Gastroenterology. 1977;72:469-473.
    • (1977) Gastroenterology , vol.72 , pp. 469-473
    • Pearson, K.W.1    Scott, D.2    Torrance, B.3
  • 4
    • 0041561143 scopus 로고    scopus 로고
    • Pancreatic regeneration after ethionine-induced acute pancreatitis in rats lacking pancreatic CCK-A receptor gene expression
    • Sato T, Niikawa J, Usui I, et al. Pancreatic regeneration after ethionine-induced acute pancreatitis in rats lacking pancreatic CCK-A receptor gene expression. J Gastroenterol. 2003;38:672-680.
    • (2003) J Gastroenterol , vol.38 , pp. 672-680
    • Sato, T.1    Niikawa, J.2    Usui, I.3
  • 5
    • 19044373371 scopus 로고    scopus 로고
    • Aging is associated with decreased pancreatic acinar cell regeneration and phosphatidylinositol 3-kinase/Akt activation
    • Watanabe H, Saito H, Rychahou PG, et al. Aging is associated with decreased pancreatic acinar cell regeneration and phosphatidylinositol 3-kinase/Akt activation. Gastroenterology. 2005;128:1391-1404.
    • (2005) Gastroenterology , vol.128 , pp. 1391-1404
    • Watanabe, H.1    Saito, H.2    Rychahou, P.G.3
  • 6
    • 0006941942 scopus 로고    scopus 로고
    • Role of cholecystokinin in physiologic and pathophysiologic growth of the pancreas
    • Greeley GH Jr ed. Totowa, NJ: Humana Press
    • Logsdon CD. Role of cholecystokinin in physiologic and pathophysiologic growth of the pancreas. In: Greeley GH Jr ed. Gastrointestinal Endocrinology. Totowa, NJ: Humana Press, 1999:393-422.
    • (1999) Gastrointestinal Endocrinology , pp. 393-422
    • Logsdon, C.D.1
  • 7
    • 0018917726 scopus 로고
    • Stimulation of pancreatic growth by secretin, caerulein, and pentagastrin
    • Dembinski AB, Johnson LR. Stimulation of pancreatic growth by secretin, caerulein, and pentagastrin. Endocrinology. 1980;106:323-328.
    • (1980) Endocrinology , vol.106 , pp. 323-328
    • Dembinski, A.B.1    Johnson, L.R.2
  • 8
    • 0025176946 scopus 로고
    • Comparison of the effect of lorglumide on pancreatic growth stimulated by camostate in rat and hamster
    • Douglas BR, Woutersen RA, Jansen JB, et al. Comparison of the effect of lorglumide on pancreatic growth stimulated by camostate in rat and hamster. Life Sci. 1990;46:281-286.
    • (1990) Life Sci , vol.46 , pp. 281-286
    • Douglas, B.R.1    Woutersen, R.A.2    Jansen, J.B.3
  • 9
    • 0023504725 scopus 로고
    • Pancreatic growth: Interaction of exogenous cholecystokinin, a protease inhibitor, and a cholecystokinin receptor antagonist in mice
    • Niederau C, Liddle RA, Williams JA, et al. Pancreatic growth: interaction of exogenous cholecystokinin, a protease inhibitor, and a cholecystokinin receptor antagonist in mice. Gut. 1987;28:63-69.
    • (1987) Gut , vol.28 , pp. 63-69
    • Niederau, C.1    Liddle, R.A.2    Williams, J.A.3
  • 10
    • 2842527448 scopus 로고
    • Amylase secretion by isolated pancreatic acini after chronic cholecystokinin treatment in vivo
    • Otsuki M, Williams JA. Amylase secretion by isolated pancreatic acini after chronic cholecystokinin treatment in vivo. Am J Physiol. 1983;244:G683-G688.
    • (1983) Am J Physiol , vol.244
    • Otsuki, M.1    Williams, J.A.2
  • 11
    • 0018113471 scopus 로고
    • Interaction of caerulein and secretin on pancreatic size and composition in rat
    • Solomon TE, Petersen H, Elashoff J, et al. Interaction of caerulein and secretin on pancreatic size and composition in rat. Am J Physiol. 1978;235:E714-E719.
    • (1978) Am J Physiol , vol.235
    • Solomon, T.E.1    Petersen, H.2    Elashoff, J.3
  • 12
    • 0023032122 scopus 로고
    • Stimulation of pancreatic acinar cell growth by CCK, epidermal growth factor, and insulin in vitro
    • Logsdon CD. Stimulation of pancreatic acinar cell growth by CCK, epidermal growth factor, and insulin in vitro. Am J Physiol. 1986;251:G487-G494.
    • (1986) Am J Physiol , vol.251
    • Logsdon, C.D.1
  • 13
    • 0020591172 scopus 로고
    • Secretory responses of hypertrophied rat pancreas induced by repeated oral administrations of a synthetic protease inhibitor
    • Yonezawa H. Secretory responses of hypertrophied rat pancreas induced by repeated oral administrations of a synthetic protease inhibitor. Jpn J Physiol. 1983;33:183-195.
    • (1983) Jpn J Physiol , vol.33 , pp. 183-195
    • Yonezawa, H.1
  • 15
    • 0023137235 scopus 로고
    • Time course and cellular site of mitotic activity in the exocrine pancreas of the rat during sustained hormone stimulation
    • Lutcke H, Scheele GA, Kern HF. Time course and cellular site of mitotic activity in the exocrine pancreas of the rat during sustained hormone stimulation. Cell Tissue Res. 1987;247:385-391.
    • (1987) Cell Tissue Res , vol.247 , pp. 385-391
    • Lutcke, H.1    Scheele, G.A.2    Kern, H.F.3
  • 16
    • 0020794768 scopus 로고
    • Cell site and time course of DNA synthesis in pancreas after caerulein and secretin
    • Solomon TE, Vanier M, Morisset J. Cell site and time course of DNA synthesis in pancreas after caerulein and secretin. Am J Physiol. 1983;245:G99-G105.
    • (1983) Am J Physiol , vol.245
    • Solomon, T.E.1    Vanier, M.2    Morisset, J.3
  • 17
    • 0022952385 scopus 로고
    • Endogenous CCK release and pancreatic growth in rats after feeding a proteinase inhibitor (camostate)
    • Goke B, Printz H, Koop I, et al. Endogenous CCK release and pancreatic growth in rats after feeding a proteinase inhibitor (camostate). Pancreas. 1986;1:509-515.
    • (1986) Pancreas , vol.1 , pp. 509-515
    • Goke, B.1    Printz, H.2    Koop, I.3
  • 18
    • 0023894361 scopus 로고
    • Effects of camostat, a synthetic protease inhibitor, on endocrine and exocrine pancreas of the rat
    • Muller MK, Goebell H, Alfen R, et al. Effects of camostat, a synthetic protease inhibitor, on endocrine and exocrine pancreas of the rat. J Nutr. 1988;118:645-650.
    • (1988) J Nutr , vol.118 , pp. 645-650
    • Muller, M.K.1    Goebell, H.2    Alfen, R.3
  • 19
    • 0020957621 scopus 로고
    • Effects on the monkey, pig and rat pancreas of soy products with varying levels of trypsin inhibitor and comparison with the administration of cholecystokinin
    • Struthers BJ, MacDonald JR, Dahlgren RR, et al. Effects on the monkey, pig and rat pancreas of soy products with varying levels of trypsin inhibitor and comparison with the administration of cholecystokinin. J Nutr. 1983;113:86-97.
    • (1983) J Nutr , vol.113 , pp. 86-97
    • Struthers, B.J.1    MacDonald, J.R.2    Dahlgren, R.R.3
  • 20
    • 0023867136 scopus 로고
    • Effects of L-364,718, a new cholecystokinin receptor antagonist, on camostate-induced growth of the rat pancreas
    • Wisner JR Jr, McLaughlin RE, Rich KA, et al. Effects of L-364,718, a new cholecystokinin receptor antagonist, on camostate-induced growth of the rat pancreas. Gastroenterology. 1988;94:109-113.
    • (1988) Gastroenterology , vol.94 , pp. 109-113
    • Wisner Jr., J.R.1    McLaughlin, R.E.2    Rich, K.A.3
  • 21
    • 0036023893 scopus 로고    scopus 로고
    • Different effects of oral administration of synthetic trypsin inhibitor on the pancreas between cholecystokinin-A receptor gene knockout mice and wild type mice
    • Sato N, Suzuki S, Kanai S, et al. Different effects of oral administration of synthetic trypsin inhibitor on the pancreas between cholecystokinin-A receptor gene knockout mice and wild type mice. Jpn J Pharmacol. 2002;89:290-295.
    • (2002) Jpn J Pharmacol , vol.89 , pp. 290-295
    • Sato, N.1    Suzuki, S.2    Kanai, S.3
  • 22
    • 0035043954 scopus 로고    scopus 로고
    • Intracellular signaling mechanisms activated by cholecystokinin- regulating synthesis and secretion of digestive enzymes in pancreatic acinar cells
    • Williams JA. Intracellular signaling mechanisms activated by cholecystokinin-regulating synthesis and secretion of digestive enzymes in pancreatic acinar cells. Annu Rev Physiol. 2001;63:77-97.
    • (2001) Annu Rev Physiol , vol.63 , pp. 77-97
    • Williams, J.A.1
  • 23
    • 0027340184 scopus 로고
    • Effects of the immunosuppressants cyclosporin A and FK 506 on exocytosis in the rat exocrine pancreas in vitro
    • Waschulewski IH, Hall DV, Kern HF, et al. Effects of the immunosuppressants cyclosporin A and FK 506 on exocytosis in the rat exocrine pancreas in vitro. Br J Pharmacol. 1993;108:892-900.
    • (1993) Br J Pharmacol , vol.108 , pp. 892-900
    • Waschulewski, I.H.1    Hall, D.V.2    Kern, H.F.3
  • 24
    • 0028175820 scopus 로고
    • Cyclosporin a inhibits Ca2+/calmodulin-dependent protein phosphatase and secretion in pancreatic acinar cells
    • Groblewski GE, Wagner AC, Williams JA. Cyclosporin A inhibits Ca2+/calmodulin-dependent protein phosphatase and secretion in pancreatic acinar cells. J Biol Chem. 1994;269:15111-15117.
    • (1994) J Biol Chem , vol.269 , pp. 15111-15117
    • Groblewski, G.E.1    Wagner, A.C.2    Williams, J.A.3
  • 25
    • 2442647038 scopus 로고    scopus 로고
    • Calcineurin is required for translational control of protein synthesis in rat pancreatic acini
    • Sans MD, Williams JA. Calcineurin is required for translational control of protein synthesis in rat pancreatic acini. Am J Physiol. 2004;287: C310-C319.
    • (2004) Am J Physiol , vol.287
    • Sans, M.D.1    Williams, J.A.2
  • 26
    • 4344571051 scopus 로고    scopus 로고
    • Receptor biology and signal transduction in pancreatic acinar cells
    • Bi Y, Williams JA. Receptor biology and signal transduction in pancreatic acinar cells. Curr Opin Gastroenterol. 2004;20:427-434.
    • (2004) Curr Opin Gastroenterol , vol.20 , pp. 427-434
    • Bi, Y.1    Williams, J.A.2
  • 27
    • 0036968193 scopus 로고    scopus 로고
    • Cholecystokinin activates a variety of intracellular signal transduction mechanisms in rodent pancreatic acinar cells
    • Williams JA, Sans MD, Tashiro M, et al. Cholecystokinin activates a variety of intracellular signal transduction mechanisms in rodent pancreatic acinar cells. Pharmacol Toxicol. 2002;91:297-303.
    • (2002) Pharmacol Toxicol , vol.91 , pp. 297-303
    • Williams, J.A.1    Sans, M.D.2    Tashiro, M.3
  • 28
    • 0030720786 scopus 로고    scopus 로고
    • Cholecystokinin and EGF activate a MAPK cascade by different mechanisms in rat pancreatic acinar cells
    • Dabrowski A, Groblewski GE, Schafer C, et al. Cholecystokinin and EGF activate a MAPK cascade by different mechanisms in rat pancreatic acinar cells. Am J Physiol. 1997;273:C1472-C1479.
    • (1997) Am J Physiol , vol.273
    • Dabrowski, A.1    Groblewski, G.E.2    Schafer, C.3
  • 29
    • 0029864407 scopus 로고    scopus 로고
    • Jun kinases are rapidly activated by cholecystokinin in rat pancreas both in vitro and in vivo
    • Dabrowski A, Grady T, Logsdon CD, et al. Jun kinases are rapidly activated by cholecystokinin in rat pancreas both in vitro and in vivo. J Biol Chem. 1996;271:5686-5690.
    • (1996) J Biol Chem , vol.271 , pp. 5686-5690
    • Dabrowski, A.1    Grady, T.2    Logsdon, C.D.3
  • 30
    • 0032508660 scopus 로고    scopus 로고
    • A role for the p38 mitogen-activated protein kinase/Hsp 27 pathway in cholecystokinin-induced changes in the actin cytoskeleton in rat pancreatic acini
    • Schafer C, Ross SE, Bragado MJ, et al. A role for the p38 mitogen-activated protein kinase/Hsp 27 pathway in cholecystokinin-induced changes in the actin cytoskeleton in rat pancreatic acini. J Biol Chem. 1998;273:24173-24180.
    • (1998) J Biol Chem , vol.273 , pp. 24173-24180
    • Schafer, C.1    Ross, S.E.2    Bragado, M.J.3
  • 32
    • 0031708618 scopus 로고    scopus 로고
    • Regulation of protein synthesis by cholecystokinin in rat pancreatic acini involves PHAS-I and the p70 S6 kinase pathway
    • Bragado MJ, Groblewski GE, Williams JA. Regulation of protein synthesis by cholecystokinin in rat pancreatic acini involves PHAS-I and the p70 S6 kinase pathway. Gastroenterology. 1998;115:733-742.
    • (1998) Gastroenterology , vol.115 , pp. 733-742
    • Bragado, M.J.1    Groblewski, G.E.2    Williams, J.A.3
  • 33
    • 0036941633 scopus 로고    scopus 로고
    • Translational control of protein synthesis in pancreatic acinar cells
    • Sans MD, Williams JA. Translational control of protein synthesis in pancreatic acinar cells. Int J Gastrointest Cancer. 2002;31:107-115.
    • (2002) Int J Gastrointest Cancer , vol.31 , pp. 107-115
    • Sans, M.D.1    Williams, J.A.2
  • 34
    • 0030967687 scopus 로고    scopus 로고
    • Cholecystokinin stimulates heat shock protein 27 phosphorylation in rat pancreas both in vivo and in vitro
    • Groblewski GE, Grady T, Mehta N, et al. Cholecystokinin stimulates heat shock protein 27 phosphorylation in rat pancreas both in vivo and in vitro. Gastroenterology. 1997;112:1354-1361.
    • (1997) Gastroenterology , vol.112 , pp. 1354-1361
    • Groblewski, G.E.1    Grady, T.2    Mehta, N.3
  • 35
    • 0033006919 scopus 로고    scopus 로고
    • eIF4E activity is regulated at multiple levels
    • Raught B, Gingras AC. eIF4E activity is regulated at multiple levels. Int J Biochem Cell Biol. 1999;31:43-57.
    • (1999) Int J Biochem Cell Biol , vol.31 , pp. 43-57
    • Raught, B.1    Gingras, A.C.2
  • 36
    • 0027969060 scopus 로고
    • Chromatographic resolution of in vivo phosphorylated and nonphosphorylated eukaryotic translation initiation factor eIF-4E: Increased cap affinity of the phosphorylated form
    • Minich WB, Balasta ML, Goss DJ, et al. Chromatographic resolution of in vivo phosphorylated and nonphosphorylated eukaryotic translation initiation factor eIF-4E: increased cap affinity of the phosphorylated form. Proc Natl Acad Sci U S A. 1994;91:7668-7672.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 7668-7672
    • Minich, W.B.1    Balasta, M.L.2    Goss, D.J.3
  • 37
    • 0036098552 scopus 로고    scopus 로고
    • AP-1 as a regulator of cell life and death
    • Shaulian E, Karin M. AP-1 as a regulator of cell life and death. Nat Cell Biol. 2002;4:E131-E136.
    • (2002) Nat Cell Biol , vol.4
    • Shaulian, E.1    Karin, M.2
  • 38
    • 3242772151 scopus 로고    scopus 로고
    • Calcineurin-NFAT signaling regulates the cardiac hypertrophic response in coordination with the MAPKs
    • Molkentin JD. Calcineurin-NFAT signaling regulates the cardiac hypertrophic response in coordination with the MAPKs. Cardiovasc Res. 2004;63:467-475.
    • (2004) Cardiovasc Res , vol.63 , pp. 467-475
    • Molkentin, J.D.1
  • 39
    • 9644303358 scopus 로고    scopus 로고
    • Estrogen-induced proliferation of normal endometrial glandular cells is initiated by transcriptional activation of cyclin D1 via binding of c-Jun to an AP-1 sequence
    • Shiozawa T, Miyamoto T, Kashima H, et al. Estrogen-induced proliferation of normal endometrial glandular cells is initiated by transcriptional activation of cyclin D1 via binding of c-Jun to an AP-1 sequence. Oncogene. 2004;23:8603-8610.
    • (2004) Oncogene , vol.23 , pp. 8603-8610
    • Shiozawa, T.1    Miyamoto, T.2    Kashima, H.3
  • 40
    • 4143126573 scopus 로고    scopus 로고
    • Feeding activates protein synthesis in mouse pancreas at the translational level without increase in mRNA
    • Sans MD, Lee SH, D'Alecy LG, et al. Feeding activates protein synthesis in mouse pancreas at the translational level without increase in mRNA. Am J Physiol Gastrointest Liver Physiol. 2004;287:G667-G675.
    • (2004) Am J Physiol Gastrointest Liver Physiol , vol.287
    • Sans, M.D.1    Lee, S.H.2    D'Alecy, L.G.3
  • 41
    • 0032054816 scopus 로고    scopus 로고
    • The mRNA 5 cap-binding protein eIF4E and control of cell growth
    • Sonenberg N, Gingras AC. The mRNA 5 cap-binding protein eIF4E and control of cell growth. Curr Opin Cell Biol. 1998;10:268-275.
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 268-275
    • Sonenberg, N.1    Gingras, A.C.2
  • 42
    • 0033761629 scopus 로고    scopus 로고
    • Synthesis of the translational apparatus is regulated at the translational level
    • Meyuhas O. Synthesis of the translational apparatus is regulated at the translational level. Eur J Biochem. 2000;267:6321-6330.
    • (2000) Eur J Biochem , vol.267 , pp. 6321-6330
    • Meyuhas, O.1
  • 43
    • 0035736260 scopus 로고    scopus 로고
    • Akt/mTOR pathway is a crucial regulator of skeletal muscle hypertrophy and can prevent muscle atrophy in vivo
    • Bodine SC, Stitt TN, Gonzalez M, et al. Akt/mTOR pathway is a crucial regulator of skeletal muscle hypertrophy and can prevent muscle atrophy in vivo. Nat Cell Biol. 2001;3:1014-1019.
    • (2001) Nat Cell Biol , vol.3 , pp. 1014-1019
    • Bodine, S.C.1    Stitt, T.N.2    Gonzalez, M.3
  • 44
    • 22844436088 scopus 로고    scopus 로고
    • Adaptive changes in translation initiation activities for rat pancreatic protein synthesis with feeding of a high-protein diet
    • Hashi M, Yoshizawa F, Onozuka E, et al. Adaptive changes in translation initiation activities for rat pancreatic protein synthesis with feeding of a high-protein diet. J Nutr Biochem. 2005;16:507-512.
    • (2005) J Nutr Biochem , vol.16 , pp. 507-512
    • Hashi, M.1    Yoshizawa, F.2    Onozuka, E.3
  • 45
    • 0027934809 scopus 로고
    • Regulation of calcineurin phosphatase activity and interaction with the FK-506·FK-506 binding protein complex
    • Parsons JN, Wiederrecht GJ, Salowe S, et al. Regulation of calcineurin phosphatase activity and interaction with the FK-506·FK-506 binding protein complex. J Biol Chem. 1994;269:19610-19616.
    • (1994) J Biol Chem , vol.269 , pp. 19610-19616
    • Parsons, J.N.1    Wiederrecht, G.J.2    Salowe, S.3
  • 46
    • 0037123871 scopus 로고    scopus 로고
    • Cyclosporin a inhibits angiotensin II-induced c-Jun NH(2)-terminal kinase activation but not protein synthesis in vascular smooth muscle cells
    • Saito S, Frank GD, Motley ED, et al. Cyclosporin A inhibits angiotensin II-induced c-Jun NH(2)-terminal kinase activation but not protein synthesis in vascular smooth muscle cells. Eur J Pharmacol. 2002; 443:47-50.
    • (2002) Eur J Pharmacol , vol.443 , pp. 47-50
    • Saito, S.1    Frank, G.D.2    Motley, E.D.3
  • 47
    • 0034607990 scopus 로고    scopus 로고
    • Calcineurin promotes protein kinase C and c-Jun NH2-terminal kinase activation in the heart. Cross-talk between cardiac hypertrophic signaling pathways
    • De Windt LJ, Lim FTW, Haq S, et al. Calcineurin promotes protein kinase C and c-Jun NH2-terminal kinase activation in the heart. Cross-talk between cardiac hypertrophic signaling pathways. J Biol Chem. 2000;275:13571-13579.
    • (2000) J Biol Chem , vol.275 , pp. 13571-13579
    • De Windt, L.J.1    Lim, F.T.W.2    Haq, S.3
  • 48
    • 0141484390 scopus 로고    scopus 로고
    • Regulation of MAPK signaling pathways through immunophilin-ligand complex
    • Matsuda S, Koyasu S. Regulation of MAPK signaling pathways through immunophilin-ligand complex. Curr Top Med Chem. 2003;3: 1358-1367.
    • (2003) Curr Top Med Chem , vol.3 , pp. 1358-1367
    • Matsuda, S.1    Koyasu, S.2
  • 49
    • 0028027041 scopus 로고
    • Cross-linking CD28 leads to activation of 70-kDa S6 kinase
    • Pai SY, Calvo V, Wood M, et al. Cross-linking CD28 leads to activation of 70-kDa S6 kinase. Eur J Immunol. 1994;24:2364-2368.
    • (1994) Eur J Immunol , vol.24 , pp. 2364-2368
    • Pai, S.Y.1    Calvo, V.2    Wood, M.3
  • 50
    • 0030977269 scopus 로고    scopus 로고
    • Mitogen-activated protein kinases activate the serine/threonine kinases Mnk1 and Mnk2
    • Waskiewicz AJ, Flynn A, Proud CG, et al. Mitogen-activated protein kinases activate the serine/threonine kinases Mnk1 and Mnk2. Embo J. 1997;16:1909-1920.
    • (1997) Embo J , vol.16 , pp. 1909-1920
    • Waskiewicz, A.J.1    Flynn, A.2    Proud, C.G.3
  • 51
    • 5044232017 scopus 로고    scopus 로고
    • Liver regeneration: From myth to mechanism
    • Taub R. Liver regeneration: from myth to mechanism. Nat Rev Mol Cell Biol. 2004;5:836-847.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 836-847
    • Taub, R.1


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