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Volumn 130, Issue 1, 2006, Pages 104-119

Sustained phosphorylation of Bid is a marker for resistance to fas-induced apoptosis during chronic liver diseases

Author keywords

[No Author keywords available]

Indexed keywords

APOPTOTIC PROTEASE ACTIVATING FACTOR 1; BAG 1 PROTEIN; BIM PROTEIN; CASPASE 3; CASPASE 6; CASPASE 7; CASPASE 8; CASPASE 9; CYTOCHROME C; FAS ANTIBODY; FAS ASSOCIATED DEATH DOMAIN PROTEIN; FLICE INHIBITORY PROTEIN; INHIBITOR OF APOPTOSIS PROTEIN 1; INHIBITOR OF APOPTOSIS PROTEIN 2; MONOCLONAL ANTIBODY; PROTEIN BAD; PROTEIN BAK; PROTEIN BAX; PROTEIN BCL 2; PROTEIN BCL W; PROTEIN BCL XL; PROTEIN BID; PROTEIN FAS RECEPTOR; PROTEIN MCL 1; RECEPTOR; SECOND MITOCHONDRIAL ACTIVATOR OF CASPASE; SURVIVIN; TUMOR NECROSIS FACTOR RECEPTOR; UNCLASSIFIED DRUG; UNINDEXED DRUG; X LINKED INHIBITOR OF APOPTOSIS;

EID: 30044442328     PISSN: 00165085     EISSN: None     Source Type: Journal    
DOI: 10.1053/j.gastro.2005.10.012     Document Type: Article
Times cited : (28)

References (67)
  • 1
    • 0031950395 scopus 로고    scopus 로고
    • CD95-induced apoptosis in human liver disease
    • P.R. Galle, P.H. Krammer CD95-induced apoptosis in human liver disease Semin Liver Dis 18 1998 141 151
    • (1998) Semin Liver Dis , vol.18 , pp. 141-151
    • Galle, P.R.1    Krammer, P.H.2
  • 4
    • 0035052938 scopus 로고    scopus 로고
    • Hepatocellular carcinoma in primary biliary cirrhosis: Similar incidence to that in hepatitis C virus-related cirrhosis
    • L. Caballeria, A. Pares, A. Castells, A. Gines, C. Bru, J. Rodes Hepatocellular carcinoma in primary biliary cirrhosis similar incidence to that in hepatitis C virus-related cirrhosis Am J Gastroenterol 96 2001 1160 1163
    • (2001) Am J Gastroenterol , vol.96 , pp. 1160-1163
    • Caballeria, L.1    Pares, A.2    Castells, A.3    Gines, A.4    Bru, C.5    Rodes, J.6
  • 6
    • 0037698899 scopus 로고    scopus 로고
    • Cholangiocarcinoma: Current concepts and insights
    • G.J. Gores Cholangiocarcinoma current concepts and insights Hepatology 37 2003 961 969
    • (2003) Hepatology , vol.37 , pp. 961-969
    • Gores, G.J.1
  • 8
    • 0035129976 scopus 로고    scopus 로고
    • Bile acid-induced rat hepatocyte apoptosis is inhibited by antioxidants and blockers of the mitochondrial permeability transition
    • B. Yerushalmi, R. Dahl, M.W. Devereaux, E. Gumpricht, R.J. Sokol Bile acid-induced rat hepatocyte apoptosis is inhibited by antioxidants and blockers of the mitochondrial permeability transition Hepatology 33 2001 616 626
    • (2001) Hepatology , vol.33 , pp. 616-626
    • Yerushalmi, B.1    Dahl, R.2    Devereaux, M.W.3    Gumpricht, E.4    Sokol, R.J.5
  • 11
    • 4644238904 scopus 로고    scopus 로고
    • Reduced oncotic necrosis in Fas receptor-deficient C57BL/6J-lpr mice after bile duct ligation
    • J.S. Gujral, J. Liu, A. Farhood, H. Jaeschke Reduced oncotic necrosis in Fas receptor-deficient C57BL/6J-lpr mice after bile duct ligation Hepatology 40 2004 998 1007
    • (2004) Hepatology , vol.40 , pp. 998-1007
    • Gujral, J.S.1    Liu, J.2    Farhood, A.3    Jaeschke, H.4
  • 12
    • 0027137419 scopus 로고
    • Loss of fumarylacetoacetate hydrolase is responsible for the neonatal hepatic dysfunction phenotype of lethal albino mice
    • M. Grompe, M. Al-Dhalimy, M. Finegold, C.N. Ou, T. Burlingame, N.G. Kennaway, P. Soriano Loss of fumarylacetoacetate hydrolase is responsible for the neonatal hepatic dysfunction phenotype of lethal albino mice Genes Dev 7 1993 2298 2307
    • (1993) Genes Dev , vol.7 , pp. 2298-2307
    • Grompe, M.1    Al-Dhalimy, M.2    Finegold, M.3    Ou, C.N.4    Burlingame, T.5    Kennaway, N.G.6    Soriano, P.7
  • 15
    • 0036646943 scopus 로고    scopus 로고
    • Activation of caspases and cleavage of Bid are required for tyrosine and phenylalanine deficiency-induced apoptosis of human A375 melanoma cells
    • X. Ge, Y.M. Fu, Y.Q. Li, G.G. Meadows Activation of caspases and cleavage of Bid are required for tyrosine and phenylalanine deficiency-induced apoptosis of human A375 melanoma cells Arch Biochem Biophys 403 2002 50 58
    • (2002) Arch Biochem Biophys , vol.403 , pp. 50-58
    • Ge, X.1    Fu, Y.M.2    Li, Y.Q.3    Meadows, G.G.4
  • 16
    • 0141892617 scopus 로고    scopus 로고
    • NFkappaB inhibition decreases hepatocyte proliferation but does not alter apoptosis in obstructive jaundice
    • M.A. Bird, D. Black, P.A. Lange, C.M. Samson, M. Hayden, K.E. Behrns NFkappaB inhibition decreases hepatocyte proliferation but does not alter apoptosis in obstructive jaundice J Surg Res 114 2003 110 117
    • (2003) J Surg Res , vol.114 , pp. 110-117
    • Bird, M.A.1    Black, D.2    Lange, P.A.3    Samson, C.M.4    Hayden, M.5    Behrns, K.E.6
  • 18
    • 0033621839 scopus 로고    scopus 로고
    • NFkappaB mediates apoptosis through transcriptional activation of Fas (CD95) in adenoviral hepatitis
    • F. Kuhnel, L. Zender, Y. Paul, M.K. Tietze, C. Trautwein, M. Manns, S. Kubicka NFkappaB mediates apoptosis through transcriptional activation of Fas (CD95) in adenoviral hepatitis J Biol Chem 275 2000 6421 6427
    • (2000) J Biol Chem , vol.275 , pp. 6421-6427
    • Kuhnel, F.1    Zender, L.2    Paul, Y.3    Tietze, M.K.4    Trautwein, C.5    Manns, M.6    Kubicka, S.7
  • 20
    • 0034745222 scopus 로고    scopus 로고
    • NF-kappaB stimulates inducible nitric oxide synthase to protect mouse hepatocytes from TNF-alpha- and Fas-mediated apoptosis
    • E. Hatano, B.L. Bennett, A.M. Manning, T. Qian, J.J. Lemasters, D.A. Brenner NF-kappaB stimulates inducible nitric oxide synthase to protect mouse hepatocytes from TNF-alpha- and Fas-mediated apoptosis Gastroenterology 120 2001 1251 1262
    • (2001) Gastroenterology , vol.120 , pp. 1251-1262
    • Hatano, E.1    Bennett, B.L.2    Manning, A.M.3    Qian, T.4    Lemasters, J.J.5    Brenner, D.A.6
  • 21
    • 4944259394 scopus 로고    scopus 로고
    • Regulation of alpha-fetoprotein by nuclear factor-kappaB protects hepatocytes from tumor necrosis factor-alpha cytotoxicity during fetal liver development and hepatic oncogenesis
    • L.G. Cavin, M. Venkatraman, V.M. Factor, S. Kaur, I. Schroeder, F. Mercurio, A.A. Beg, S.S. Thorgeirsson, M. Arsura Regulation of alpha-fetoprotein by nuclear factor-kappaB protects hepatocytes from tumor necrosis factor-alpha cytotoxicity during fetal liver development and hepatic oncogenesis Cancer Res 64 2004 7030 7038
    • (2004) Cancer Res , vol.64 , pp. 7030-7038
    • Cavin, L.G.1    Venkatraman, M.2    Factor, V.M.3    Kaur, S.4    Schroeder, I.5    Mercurio, F.6    Beg, A.A.7    Thorgeirsson, S.S.8    Arsura, M.9
  • 23
    • 20444457553 scopus 로고    scopus 로고
    • Suppression of calcium release from inositol 1,4,5-trisphosphate- sensitive stores mediates the anti-apoptotic function of nuclear factor-{kappa}B
    • S. Camandola, R.G. Cutler, D.S. Gary, O. Milhavet, M.P. Mattson Suppression of calcium release from inositol 1,4,5-trisphosphate-sensitive stores mediates the anti-apoptotic function of nuclear factor-{kappa}B J Biol Chem 280 2005 22287 22296
    • (2005) J Biol Chem , vol.280 , pp. 22287-22296
    • Camandola, S.1    Cutler, R.G.2    Gary, D.S.3    Milhavet, O.4    Mattson, M.P.5
  • 24
    • 0033652765 scopus 로고    scopus 로고
    • Tumor necrosis factor alpha prevents tumor necrosis factor receptor-mediated mouse hepatocyte apoptosis, but not fas-mediated apoptosis: Role of nuclear factor-kappaB
    • M. Nagaki, T. Naiki, D.A. Brenner, Y. Osawa, M. Imose, H. Hayashi, Y. Banno, S. Nakashima, H. Moriwaki Tumor necrosis factor alpha prevents tumor necrosis factor receptor-mediated mouse hepatocyte apoptosis, but not fas-mediated apoptosis role of nuclear factor-kappaB Hepatology 32 2000 1272 1279
    • (2000) Hepatology , vol.32 , pp. 1272-1279
    • Nagaki, M.1    Naiki, T.2    Brenner, D.A.3    Osawa, Y.4    Imose, M.5    Hayashi, H.6    Banno, Y.7    Nakashima, S.8    Moriwaki, H.9
  • 25
    • 0035081675 scopus 로고    scopus 로고
    • Normal liver regeneration in p50/nuclear factor kappaB1 knockout mice
    • R.A. DeAngelis, K. Kovalovich, D.E. Cressman, R. Taub Normal liver regeneration in p50/nuclear factor kappaB1 knockout mice Hepatology 33 2001 915 924
    • (2001) Hepatology , vol.33 , pp. 915-924
    • Deangelis, R.A.1    Kovalovich, K.2    Cressman, D.E.3    Taub, R.4
  • 30
    • 0033613143 scopus 로고    scopus 로고
    • Caspase activation: The induced-proximity model
    • G.S. Salvesen, V.M. Dixit Caspase activation the induced-proximity model Proc Natl Acad Sci USA 96 1999 10964 10967
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 10964-10967
    • Salvesen, G.S.1    Dixit, V.M.2
  • 32
    • 0032555697 scopus 로고    scopus 로고
    • Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis
    • H. Li, H. Zhu, C.J. Xu, J. Yuan Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis Cell 94 1998 491 501
    • (1998) Cell , vol.94 , pp. 491-501
    • Li, H.1    Zhu, H.2    Xu, C.J.3    Yuan, J.4
  • 33
    • 0032555716 scopus 로고    scopus 로고
    • Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors
    • X. Luo, I. Budihardjo, H. Zou, C. Slaughter, X. Wang Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors Cell 94 1998 481 490
    • (1998) Cell , vol.94 , pp. 481-490
    • Luo, X.1    Budihardjo, I.2    Zou, H.3    Slaughter, C.4    Wang, X.5
  • 34
    • 0037151030 scopus 로고    scopus 로고
    • Bcl-2 family member Bfl-1/A1 sequesters truncated bid to inhibit in collaboration with pro-apoptotic Bak or Bax
    • A.B. Werner, E. de Vries, S.W. Tait, I. Bontjer, J. Borst Bcl-2 family member Bfl-1/A1 sequesters truncated bid to inhibit in collaboration with pro-apoptotic Bak or Bax J Biol Chem 277 2002 22781 22788
    • (2002) J Biol Chem , vol.277 , pp. 22781-22788
    • Werner, A.B.1    De Vries, E.2    Tait, S.W.3    Bontjer, I.4    Borst, J.5
  • 36
    • 0033981577 scopus 로고    scopus 로고
    • Bid induces the oligomerization and insertion of Bax into the outer mitochondrial membrane
    • R. Eskes, S. Desagher, B. Antonsson, J.C. Martinou Bid induces the oligomerization and insertion of Bax into the outer mitochondrial membrane Mol Cell Biol 20 2000 929 935
    • (2000) Mol Cell Biol , vol.20 , pp. 929-935
    • Eskes, R.1    Desagher, S.2    Antonsson, B.3    Martinou, J.C.4
  • 38
    • 0033519705 scopus 로고    scopus 로고
    • Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC
    • S. Shimizu, M. Narita, Y. Tsujimoto Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC Nature 399 1999 483 487
    • (1999) Nature , vol.399 , pp. 483-487
    • Shimizu, S.1    Narita, M.2    Tsujimoto, Y.3
  • 39
    • 0036187036 scopus 로고    scopus 로고
    • Three-dimensional structure of the apoptosome: Implications for assembly, procaspase-9 binding, and activation
    • D. Acehan, X. Jiang, D.G. Morgan, J.E. Heuser, X. Wang, C.W. Akey Three-dimensional structure of the apoptosome implications for assembly, procaspase-9 binding, and activation Mol Cell 9 2002 423 432
    • (2002) Mol Cell , vol.9 , pp. 423-432
    • Acehan, D.1    Jiang, X.2    Morgan, D.G.3    Heuser, J.E.4    Wang, X.5    Akey, C.W.6
  • 40
    • 0035827569 scopus 로고    scopus 로고
    • Cellular FLICE-inhibitory protein splice variants inhibit different steps of caspase-8 activation at the CD95 death-inducing signaling complex
    • A. Krueger, I. Schmitz, S. Baumann, P.H. Krammer, S. Kirchhoff Cellular FLICE-inhibitory protein splice variants inhibit different steps of caspase-8 activation at the CD95 death-inducing signaling complex J Biol Chem 276 2001 20633 20640
    • (2001) J Biol Chem , vol.276 , pp. 20633-20640
    • Krueger, A.1    Schmitz, I.2    Baumann, S.3    Krammer, P.H.4    Kirchhoff, S.5
  • 41
    • 0035890085 scopus 로고    scopus 로고
    • The expanding role of mitochondria in apoptosis
    • X. Wang The expanding role of mitochondria in apoptosis Genes Dev 15 2001 2922 2933
    • (2001) Genes Dev , vol.15 , pp. 2922-2933
    • Wang, X.1
  • 42
    • 0142117313 scopus 로고    scopus 로고
    • The Bcl-2 family: Roles in cell survival and oncogenesis
    • S. Cory, D.C. Huang, J.M. Adams The Bcl-2 family roles in cell survival and oncogenesis Oncogene 22 2003 8590 8607
    • (2003) Oncogene , vol.22 , pp. 8590-8607
    • Cory, S.1    Huang, D.C.2    Adams, J.M.3
  • 43
    • 0033179760 scopus 로고    scopus 로고
    • BCL-2 family members and the mitochondria in apoptosis
    • A. Gross, J.M. McDonnell, S.J. Korsmeyer BCL-2 family members and the mitochondria in apoptosis Genes Dev 13 1999 1899 1911
    • (1999) Genes Dev , vol.13 , pp. 1899-1911
    • Gross, A.1    McDonnell, J.M.2    Korsmeyer, S.J.3
  • 44
    • 0030963602 scopus 로고    scopus 로고
    • Cytosol-to-membrane redistribution of Bax and Bcl-X(L) during apoptosis
    • Y.T. Hsu, K.G. Wolter, R.J. Youle Cytosol-to-membrane redistribution of Bax and Bcl-X(L) during apoptosis Proc Natl Acad Sci U S A 94 1997 3668 3672
    • (1997) Proc Natl Acad Sci U S a , vol.94 , pp. 3668-3672
    • Hsu, Y.T.1    Wolter, K.G.2    Youle, R.J.3
  • 46
    • 0038182531 scopus 로고    scopus 로고
    • Post-translational modification of Bid has differential effects on its susceptibility to cleavage by caspase 8 or caspase 3
    • M. Degli Esposti, G. Ferry, P. Masdehors, J.A. Boutin, J.A. Hickman, C. Dive Post-translational modification of Bid has differential effects on its susceptibility to cleavage by caspase 8 or caspase 3 J Biol Chem 278 2003 15749 15757
    • (2003) J Biol Chem , vol.278 , pp. 15749-15757
    • Degli Esposti, M.1    Ferry, G.2    Masdehors, P.3    Boutin, J.A.4    Hickman, J.A.5    Dive, C.6
  • 48
    • 0030670332 scopus 로고    scopus 로고
    • P53 is phosphorylated in vitro and in vivo by the delta and epsilon isoforms of casein kinase 1 and enhances the level of casein kinase 1 delta in response to topoisomerase-directed drugs
    • U. Knippschild, D.M. Milne, L.E. Campbell, A.J. DeMaggio, E. Christenson, M.F. Hoekstra, D.W. Meek p53 is phosphorylated in vitro and in vivo by the delta and epsilon isoforms of casein kinase 1 and enhances the level of casein kinase 1 delta in response to topoisomerase-directed drugs Oncogene 15 1997 1727 1736
    • (1997) Oncogene , vol.15 , pp. 1727-1736
    • Knippschild, U.1    Milne, D.M.2    Campbell, L.E.3    Demaggio, A.J.4    Christenson, E.5    Hoekstra, M.F.6    Meek, D.W.7
  • 49
    • 0034737438 scopus 로고    scopus 로고
    • Damage-mediated phosphorylation of human p53 threonine 18 through a cascade mediated by a casein 1-like kinase. Effect on Mdm2 binding
    • K. Sakaguchi, S. Saito, Y. Higashimoto, S. Roy, C.W. Anderson, E. Appella Damage-mediated phosphorylation of human p53 threonine 18 through a cascade mediated by a casein 1-like kinase. Effect on Mdm2 binding J Biol Chem 275 2000 9278 9283
    • (2000) J Biol Chem , vol.275 , pp. 9278-9283
    • Sakaguchi, K.1    Saito, S.2    Higashimoto, Y.3    Roy, S.4    Anderson, C.W.5    Appella, E.6
  • 50
    • 4344562126 scopus 로고    scopus 로고
    • Mechanism of phosphorylation-dependent binding of APC to beta-catenin and its role in beta-catenin degradation
    • N.C. Ha, T. Tonozuka, J.L. Stamos, H.J. Choi, W.I. Weis Mechanism of phosphorylation-dependent binding of APC to beta-catenin and its role in beta-catenin degradation Mol Cell 15 2004 511 521
    • (2004) Mol Cell , vol.15 , pp. 511-521
    • Ha, N.C.1    Tonozuka, T.2    Stamos, J.L.3    Choi, H.J.4    Weis, W.I.5
  • 51
    • 0033835065 scopus 로고    scopus 로고
    • Fas engagement accelerates liver regeneration after partial hepatectomy
    • J. Desbarats, M.K. Newell Fas engagement accelerates liver regeneration after partial hepatectomy Nat Med 6 2000 920 923
    • (2000) Nat Med , vol.6 , pp. 920-923
    • Desbarats, J.1    Newell, M.K.2
  • 53
    • 0017831729 scopus 로고
    • With special reference to onchocerciasis
    • Suramin Hawking F with special reference to onchocerciasis Adv Pharmacol Chemother 15 1978 289 322
    • (1978) Adv Pharmacol Chemother , vol.15 , pp. 289-322
    • Hawking, F.1    Suramin2
  • 54
    • 0027066878 scopus 로고
    • Suramin rapidly alters cellular tyrosine phosphorylation in prostate cancer cell lines
    • O. Sator, C.A. McLellan, C.E. Myers, M.M. Bonner Suramin rapidly alters cellular tyrosine phosphorylation in prostate cancer cell lines J Clin Invest 90 1992 2166 2174
    • (1992) J Clin Invest , vol.90 , pp. 2166-2174
    • Sator, O.1    McLellan, C.A.2    Myers, C.E.3    Bonner, M.M.4
  • 55
    • 0032524855 scopus 로고    scopus 로고
    • Suramin is an active site-directed, reversible, and tight-binding inhibitor of protein-tyrosine phosphatases
    • O. Zhang, Y.F. Keng, Y. Zhao, L. Wu, Z.Y. Zhang Suramin is an active site-directed, reversible, and tight-binding inhibitor of protein-tyrosine phosphatases J Biol Chem 273 1998 12281 12287
    • (1998) J Biol Chem , vol.273 , pp. 12281-12287
    • Zhang, O.1    Keng, Y.F.2    Zhao, Y.3    Wu, L.4    Zhang, Z.Y.5
  • 56
    • 0042622251 scopus 로고    scopus 로고
    • Scansite 2.0: Proteome-wide prediction of cell signaling interactions using short sequence motifs
    • J.C. Obenauer, L.C. Cantley, M.B. Yaffe Scansite 2.0 Proteome-wide prediction of cell signaling interactions using short sequence motifs Nucleic Acids Res 31 2003 3635 3641
    • (2003) Nucleic Acids Res , vol.31 , pp. 3635-3641
    • Obenauer, J.C.1    Cantley, L.C.2    Yaffe, M.B.3
  • 58
    • 0035449355 scopus 로고    scopus 로고
    • Cell cycle checkpoint signaling through the ATM and ATR kinases
    • R.T. Abraham Cell cycle checkpoint signaling through the ATM and ATR kinases Genes Dev 15 2001 2177 2196
    • (2001) Genes Dev , vol.15 , pp. 2177-2196
    • Abraham, R.T.1
  • 59
    • 0032797275 scopus 로고    scopus 로고
    • Cyclin B-dependent kinase and caspase-1 activation precedes mitochondrial dysfunction in fumarylacetoacetate-induced apoptosis
    • R. Jorquera, R.M. Tanguay Cyclin B-dependent kinase and caspase-1 activation precedes mitochondrial dysfunction in fumarylacetoacetate-induced apoptosis FASEB J 13 1999 2284 2298
    • (1999) FASEB J , vol.13 , pp. 2284-2298
    • Jorquera, R.1    Tanguay, R.M.2
  • 62
    • 0033534446 scopus 로고    scopus 로고
    • Caspase cleaved BID targets mitochondria and is required for cytochrome c release, while BCL-XL prevents this release but not tumor necrosis factor-R1/Fas death
    • A. Gross, X.M. Yin, K. Wang, M.C. Wei, J. Jockel, C. Milliman, H. Erdjument-Bromage, P. Tempst, S.J. Korsmeyer Caspase cleaved BID targets mitochondria and is required for cytochrome c release, while BCL-XL prevents this release but not tumor necrosis factor-R1/Fas death J Biol Chem 274 1999 1156 1163
    • (1999) J Biol Chem , vol.274 , pp. 1156-1163
    • Gross, A.1    Yin, X.M.2    Wang, K.3    Wei, M.C.4    Jockel, J.5    Milliman, C.6    Erdjument-Bromage, H.7    Tempst, P.8    Korsmeyer, S.J.9
  • 63
    • 0034534795 scopus 로고    scopus 로고
    • Posttranslational N-myristoylation of BID as a molecular switch for targeting mitochondria and apoptosis
    • J. Zha, S. Weiler, K.J. Oh, M.C. Wei, S.J. Korsmeyer Posttranslational N-myristoylation of BID as a molecular switch for targeting mitochondria and apoptosis Science 290 2000 1761 1765
    • (2000) Science , vol.290 , pp. 1761-1765
    • Zha, J.1    Weiler, S.2    Oh, K.J.3    Wei, M.C.4    Korsmeyer, S.J.5
  • 65
    • 2942591023 scopus 로고    scopus 로고
    • Nuclear export of phosphorylated galectin-3 regulates its antiapoptotic activity in response to chemotherapeutic drugs
    • Y. Takenaka, T. Fukumori, T. Yoshii, N. Oka, H. Inohara, H.R. Kim, R.S. Bresalier, A. Raz Nuclear export of phosphorylated galectin-3 regulates its antiapoptotic activity in response to chemotherapeutic drugs Mol Cell Biol 24 2004 4395 4406
    • (2004) Mol Cell Biol , vol.24 , pp. 4395-4406
    • Takenaka, Y.1    Fukumori, T.2    Yoshii, T.3    Oka, N.4    Inohara, H.5    Kim, H.R.6    Bresalier, R.S.7    Raz, A.8
  • 66
    • 0028871365 scopus 로고
    • Casein kinase-1 phosphorylates the p75 tumor necrosis factor receptor and negatively regulates tumor necrosis factor signaling for apoptosis
    • R. Beyaert, B. Vanhaesebroeck, W. Declercq, J. Van Lint, P. Vandenabele, P. Agostinis, J.R. Vandenheede, W. Fiers Casein kinase-1 phosphorylates the p75 tumor necrosis factor receptor and negatively regulates tumor necrosis factor signaling for apoptosis J Biol Chem 270 1995 23293 23299
    • (1995) J Biol Chem , vol.270 , pp. 23293-23299
    • Beyaert, R.1    Vanhaesebroeck, B.2    Declercq, W.3    Van Lint, J.4    Vandenabele, P.5    Agostinis, P.6    Vandenheede, J.R.7    Fiers, W.8


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