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Volumn 193, Issue 5, 2011, Pages 867-884

PKCζ mediates disturbed flow-induced endothelial apoptosis via p53 SUMOylation

Author keywords

[No Author keywords available]

Indexed keywords

3 NITROTYROSINE; PROTEIN BCL 2; PROTEIN KINASE C ZETA; PROTEIN P53;

EID: 79959442340     PISSN: 00219525     EISSN: 00219525     Source Type: Journal    
DOI: 10.1083/jcb.201010051     Document Type: Article
Times cited : (93)

References (59)
  • 1
    • 4544318079 scopus 로고    scopus 로고
    • The hinge-helix 1 region of peroxisome proliferator-activated receptor gamma1 (PPARgamma1) mediates interaction with extracellular signal-regulated kinase 5 and PPARgamma1 transcriptional activation: involvement in flow-induced PPARgamma activation in endothelial cells
    • Akaike, M., W. Che, N.L. Marmarosh, S. Ohta, M. Osawa, B. Ding, B.C. Berk, C. Yan, and J. Abe. 2004. The hinge-helix 1 region of peroxisome proliferator-activated receptor gamma1 (PPARgamma1) mediates interaction with extracellular signal-regulated kinase 5 and PPARgamma1 transcriptional activation: involvement in flow-induced PPARgamma activation in endothelial cells. Mol. Cell. Biol. 24:8691-8704.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 8691-8704
    • Akaike, M.1    Che, W.2    Marmarosh, N.L.3    Ohta, S.4    Osawa, M.5    Ding, B.6    Berk, B.C.7    Yan, C.8    Abe, J.9
  • 4
    • 7944223078 scopus 로고    scopus 로고
    • Structure and regulation of Src family kinases
    • Boggon, T.J., and M.J. Eck. 2004. Structure and regulation of Src family kinases. Oncogene. 23:7918-7927.
    • (2004) Oncogene , vol.23 , pp. 7918-7927
    • Boggon, T.J.1    Eck, M.J.2
  • 5
    • 34047103990 scopus 로고    scopus 로고
    • C-terminal modifications regulate MDM2 dissociation and nuclear export of p53
    • Carter, S., O. Bischof, A. Dejean, and K.H. Vousden. 2007. C-terminal modifications regulate MDM2 dissociation and nuclear export of p53. Nat. Cell Biol. 9:428-435.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 428-435
    • Carter, S.1    Bischof, O.2    Dejean, A.3    Vousden, K.H.4
  • 6
    • 2942735131 scopus 로고    scopus 로고
    • SENP1 enhances androgen receptor-dependent transcription through desumoylation of histone deacetylase 1
    • Cheng, J., D. Wang, Z. Wang, and E.T. Yeh. 2004. SENP1 enhances androgen receptor-dependent transcription through desumoylation of histone deacetylase 1. Mol. Cell. Biol. 24:6021-6028.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 6021-6028
    • Cheng, J.1    Wang, D.2    Wang, Z.3    Yeh, E.T.4
  • 11
    • 34447648183 scopus 로고    scopus 로고
    • Flow antagonizes TNF-alpha signaling in endothelial cells by inhibiting caspase-dependent PKC zeta processing
    • Garin, G., J.I. Abe, A. Mohan, W. Lu, C. Yan, A.C. Newby, A. Rhaman, and B.C. Berk. 2007. Flow antagonizes TNF-alpha signaling in endothelial cells by inhibiting caspase-dependent PKC zeta processing. Circ. Res. 101:97-105.
    • (2007) Circ. Res. , vol.101 , pp. 97-105
    • Garin, G.1    Abe, J.I.2    Mohan, A.3    Lu, W.4    Yan, C.5    Newby, A.C.6    Rhaman, A.7    Berk, B.C.8
  • 12
    • 40549111934 scopus 로고    scopus 로고
    • Protective mechanisms of p53-p21-pRb proteins against DNA damage-induced cell death
    • Garner, E., and K. Raj. 2008. Protective mechanisms of p53-p21-pRb proteins against DNA damage-induced cell death. Cell Cycle. 7:277-282.
    • (2008) Cell Cycle , vol.7 , pp. 277-282
    • Garner, E.1    Raj, K.2
  • 13
    • 34548036682 scopus 로고    scopus 로고
    • Cells with defective p53-p21-pRb pathway are susceptible to apoptosis induced by p84N5 via caspase-6
    • Garner, E., F. Martinon, J. Tschopp, P. Beard, and K. Raj. 2007. Cells with defective p53-p21-pRb pathway are susceptible to apoptosis induced by p84N5 via caspase-6. Cancer Res. 67:7631-7637.
    • (2007) Cancer Res , vol.67 , pp. 7631-7637
    • Garner, E.1    Martinon, F.2    Tschopp, J.3    Beard, P.4    Raj, K.5
  • 14
    • 4444351219 scopus 로고    scopus 로고
    • Regulation of human p53 activity and cell localization by alternative splicing
    • Ghosh, A., D. Stewart, and G. Matlashewski. 2004. Regulation of human p53 activity and cell localization by alternative splicing. Mol. Cell. Biol. 24:7987-7997.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 7987-7997
    • Ghosh, A.1    Stewart, D.2    Matlashewski, G.3
  • 15
    • 0034847978 scopus 로고    scopus 로고
    • Induction of p53-independent apoptosis by simian virus 40 small t antigen
    • Gjoerup, O., D. Zaveri, and T.M. Roberts. 2001. Induction of p53-independent apoptosis by simian virus 40 small t antigen. J. Virol. 75:9142-9155.
    • (2001) J. Virol. , vol.75 , pp. 9142-9155
    • Gjoerup, O.1    Zaveri, D.2    Roberts, T.M.3
  • 16
    • 0034255365 scopus 로고    scopus 로고
    • The NF-kappa B signal transduction pathway in aortic endothelial cells is primed for activation in regions predisposed to atherosclerotic lesion formation
    • Hajra, L., A.I. Evans, M. Chen, S.J. Hyduk, T. Collins, and M.I. Cybulsky. 2000. The NF-kappa B signal transduction pathway in aortic endothelial cells is primed for activation in regions predisposed to atherosclerotic lesion formation. Proc. Natl. Acad. Sci. USA. 97:9052-9057.
    • (2000) Proc. Natl. Acad. Sci. USA. , vol.97 , pp. 9052-9057
    • Hajra, L.1    Evans, A.I.2    Chen, M.3    Hyduk, S.J.4    Collins, T.5    Cybulsky, M.I.6
  • 19
    • 0032716312 scopus 로고    scopus 로고
    • Sustained JNK activation induces endothelial apoptosis: studies with colchicine and shear stress
    • Hu, Y.L., S. Li, J.Y. Shyy, and S. Chien. 1999. Sustained JNK activation induces endothelial apoptosis: studies with colchicine and shear stress. Am. J. Physiol. 277:H1593-H1599.
    • (1999) Am. J. Physiol. , vol.277
    • Hu, Y.L.1    Li, S.2    Shyy, J.Y.3    Chien, S.4
  • 20
    • 0033597952 scopus 로고    scopus 로고
    • Patterns of vascular cell adhesion molecule-1 and intercellular adhesion molecule-1 expression in rabbit and mouse atherosclerotic lesions and at sites predisposed to lesion formation
    • Iiyama, K., L. Hajra, M. Iiyama, H. Li, M. DiChiara, B.D. Medoff, and M.I. Cybulsky. 1999. Patterns of vascular cell adhesion molecule-1 and intercellular adhesion molecule-1 expression in rabbit and mouse atherosclerotic lesions and at sites predisposed to lesion formation. Circ. Res. 85:199-207.
    • (1999) Circ. Res. , vol.85 , pp. 199-207
    • Iiyama, K.1    Hajra, L.2    Iiyama, M.3    Li, H.4    DiChiara, M.5    Medoff, B.D.6    Cybulsky, M.I.7
  • 21
    • 0026453418 scopus 로고
    • Peroxynitrite formation from macrophage-derived nitric oxide
    • Ischiropoulos, H., L. Zhu, and J.S. Beckman. 1992. Peroxynitrite formation from macrophage-derived nitric oxide. Arch. Biochem. Biophys. 298:446-451.
    • (1992) Arch. Biochem. Biophys. , vol.298 , pp. 446-451
    • Ischiropoulos, H.1    Zhu, L.2    Beckman, J.S.3
  • 22
    • 33748469407 scopus 로고    scopus 로고
    • Low-grade chronic inflammation in regions of the normal mouse arterial intima predisposed to atherosclerosis
    • Jongstra-Bilen, J., M. Haidari, S.N. Zhu, M. Chen, D. Guha, and M.I. Cybulsky. 2006. Low-grade chronic inflammation in regions of the normal mouse arterial intima predisposed to atherosclerosis. J. Exp. Med. 203:2073-2083.
    • (2006) J. Exp. Med. , vol.203 , pp. 2073-2083
    • Jongstra-Bilen, J.1    Haidari, M.2    Zhu, S.N.3    Chen, M.4    Guha, D.5    Cybulsky, M.I.6
  • 24
    • 0034668930 scopus 로고    scopus 로고
    • Peroxynitrite activates the phosphoinositide 3-kinase/Akt pathway in human skin primary fibroblasts
    • Klotz, L.O., S.M. Schieke, H. Sies, and N.J. Holbrook. 2000. Peroxynitrite activates the phosphoinositide 3-kinase/Akt pathway in human skin primary fibroblasts. Biochem. J. 352:219-225.
    • (2000) Biochem. J. , vol.352 , pp. 219-225
    • Klotz, L.O.1    Schieke, S.M.2    Sies, H.3    Holbrook, N.J.4
  • 25
    • 0035799530 scopus 로고    scopus 로고
    • Functional analysis and intracellular localization of p53 modified by SUMO-1
    • Kwek, S.S., J. Derry, A.L. Tyner, Z. Shen, and A.V. Gudkov. 2001. Functional analysis and intracellular localization of p53 modified by SUMO-1. Oncogene. 20:2587-2599.
    • (2001) Oncogene , vol.20 , pp. 2587-2599
    • Kwek, S.S.1    Derry, J.2    Tyner, A.L.3    Shen, Z.4    Gudkov, A.V.5
  • 26
    • 27144547642 scopus 로고    scopus 로고
    • Peroxynitrite is a potent inhibitor of NF-kappaB activation triggered by inflammatory stimuli in cardiac and endothelial cell lines
    • Levrand, S., B. Pesse, F. Feihl, B. Waeber, P. Pacher, J. Rolli, M.D. Schaller, and L. Liaudet. 2005. Peroxynitrite is a potent inhibitor of NF-kappaB activation triggered by inflammatory stimuli in cardiac and endothelial cell lines. J. Biol. Chem. 280:34878-34887.
    • (2005) J. Biol. Chem. , vol.280 , pp. 34878-34887
    • Levrand, S.1    Pesse, B.2    Feihl, F.3    Waeber, B.4    Pacher, P.5    Rolli, J.6    Schaller, M.D.7    Liaudet, L.8
  • 27
    • 4444306896 scopus 로고    scopus 로고
    • Role of protein kinase Czeta in thrombin-induced endothelial permeability changes: inhibition by angiopoietin-1
    • Li, X., C.N. Hahn, M. Parsons, J. Drew, M.A. Vadas, and J.R. Gamble. 2004. Role of protein kinase Czeta in thrombin-induced endothelial permeability changes: inhibition by angiopoietin-1. Blood. 104:1716-1724.
    • (2004) Blood , vol.104 , pp. 1716-1724
    • Li, X.1    Hahn, C.N.2    Parsons, M.3    Drew, J.4    Vadas, M.A.5    Gamble, J.R.6
  • 28
    • 63849103058 scopus 로고    scopus 로고
    • Role of peroxynitrite in the redox regulation of cell signal transduction pathways
    • Liaudet, L., G. Vassalli, and P. Pacher. 2009. Role of peroxynitrite in the redox regulation of cell signal transduction pathways. Front. Biosci. 14:4809-4814.
    • (2009) Front. Biosci. , vol.14 , pp. 4809-4814
    • Liaudet, L.1    Vassalli, G.2    Pacher, P.3
  • 30
    • 24744449131 scopus 로고    scopus 로고
    • Endothelial protein kinase C isoform identity and differential activity of PKCzeta in an athero-susceptible region of porcine aorta
    • Magid, R., and P.F. Davies. 2005. Endothelial protein kinase C isoform identity and differential activity of PKCzeta in an athero-susceptible region of porcine aorta. Circ. Res. 97:443-449.
    • (2005) Circ. Res. , vol.97 , pp. 443-449
    • Magid, R.1    Davies, P.F.2
  • 31
    • 22144482659 scopus 로고    scopus 로고
    • PIAS proteins are involved in the SUMO-1 modification, intracellular translocation and transcriptional repressive activity of RET finger protein
    • Matsuura, T., Y. Shimono, K. Kawai, H. Murakami, T. Urano, Y. Niwa, H. Goto, and M. Takahashi. 2005. PIAS proteins are involved in the SUMO-1 modification, intracellular translocation and transcriptional repressive activity of RET finger protein. Exp. Cell Res. 308:65-77.
    • (2005) Exp. Cell Res. , vol.308 , pp. 65-77
    • Matsuura, T.1    Shimono, Y.2    Kawai, K.3    Murakami, H.4    Urano, T.5    Niwa, Y.6    Goto, H.7    Takahashi, M.8
  • 32
    • 16444370187 scopus 로고    scopus 로고
    • Endogenous p53 protects vascular smooth muscle cells from apoptosis and reduces atherosclerosis in ApoE knockout mice
    • Mercer, J., N. Figg, V. Stoneman, D. Braganza, and M.R. Bennett. 2005. Endogenous p53 protects vascular smooth muscle cells from apoptosis and reduces atherosclerosis in ApoE knockout mice. Circ. Res. 96:667-674.
    • (2005) Circ. Res. , vol.96 , pp. 667-674
    • Mercer, J.1    Figg, N.2    Stoneman, V.3    Braganza, D.4    Bennett, M.R.5
  • 34
    • 50149097809 scopus 로고    scopus 로고
    • A complex barcode underlies the heterogeneous response of p53 to stress
    • Murray-Zmijewski, F., E.A. Slee, and X. Lu. 2008. A complex barcode underlies the heterogeneous response of p53 to stress. Nat. Rev. Mol. Cell Biol. 9:702-712.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 702-712
    • Murray-Zmijewski, F.1    Slee, E.A.2    Lu, X.3
  • 35
    • 0035413601 scopus 로고    scopus 로고
    • Protein kinase C: structural and spatial regulation by phosphorylation, cofactors, and macromolecular interactions
    • Newton, A.C. 2001. Protein kinase C: structural and spatial regulation by phosphorylation, cofactors, and macromolecular interactions. Chem. Rev. 101:2353-2364.
    • (2001) Chem. Rev. , vol.101 , pp. 2353-2364
    • Newton, A.C.1
  • 36
    • 0042692785 scopus 로고    scopus 로고
    • Nucleocytoplasmic shuttling of p53 is essential for MDM2-mediated cytoplasmic degradation but not ubiquitination
    • O'Keefe, K., H. Li, and Y. Zhang. 2003. Nucleocytoplasmic shuttling of p53 is essential for MDM2-mediated cytoplasmic degradation but not ubiquitination. Mol. Cell. Biol. 23:6396-6405.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 6396-6405
    • O'Keefe, K.1    Li, H.2    Zhang, Y.3
  • 37
  • 38
    • 52049123045 scopus 로고    scopus 로고
    • Physiologic stressmediated signaling in the endothelium
    • Reinhart-King, C.A., K. Fujiwara, and B.C. Berk. 2008. Physiologic stressmediated signaling in the endothelium. Methods Enzymol. 443:25-44.
    • (2008) Methods Enzymol , vol.443 , pp. 25-44
    • Reinhart-King, C.A.1    Fujiwara, K.2    Berk, B.C.3
  • 39
    • 17444374230 scopus 로고    scopus 로고
    • Src kinase regulation by phosphorylation and dephosphorylation
    • Roskoski, R. Jr. 2005. Src kinase regulation by phosphorylation and dephosphorylation. Biochem. Biophys. Res. Commun. 331:1-14.
    • (2005) Biochem. Biophys. Res. Commun. , vol.331 , pp. 1-14
    • Roskoski Jr., R.1
  • 40
    • 0035576878 scopus 로고    scopus 로고
    • PIASy, a nuclear matrix-associated SUMO E3 ligase, represses LEF1 activity by sequestration into nuclear bodies
    • Sachdev, S., L. Bruhn, H. Sieber, A. Pichler, F. Melchior, and R. Grosschedl. 2001. PIASy, a nuclear matrix-associated SUMO E3 ligase, represses LEF1 activity by sequestration into nuclear bodies. Genes Dev. 15:3088-3103.
    • (2001) Genes Dev , vol.15 , pp. 3088-3103
    • Sachdev, S.1    Bruhn, L.2    Sieber, H.3    Pichler, A.4    Melchior, F.5    Grosschedl, R.6
  • 42
    • 0242721318 scopus 로고    scopus 로고
    • Caspase processing activates atypical protein kinase C zeta by relieving autoinhibition and destabilizes the protein
    • Smith, L., Z. Wang, and J.B. Smith. 2003. Caspase processing activates atypical protein kinase C zeta by relieving autoinhibition and destabilizes the protein. Biochem. J. 375:663-671.
    • (2003) Biochem. J. , vol.375 , pp. 663-671
    • Smith, L.1    Wang, Z.2    Smith, J.B.3
  • 43
    • 0345129995 scopus 로고    scopus 로고
    • Novel roles of specific isoforms of protein kinase C in activation of the c-fos serum response element
    • Soh, J.W., E.H. Lee, R. Prywes, and I.B. Weinstein. 1999. Novel roles of specific isoforms of protein kinase C in activation of the c-fos serum response element. Mol. Cell. Biol. 19:1313-1324.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1313-1324
    • Soh, J.W.1    Lee, E.H.2    Prywes, R.3    Weinstein, I.B.4
  • 44
    • 45549094869 scopus 로고    scopus 로고
    • Protein kinase Czeta-dependent LKB1 serine 428 phosphorylation increases LKB1 nucleus export and apoptosis in endothelial cells
    • Song, P., Z. Xie, Y. Wu, J. Xu, Y. Dong, and M.H. Zou. 2008. Protein kinase Czeta-dependent LKB1 serine 428 phosphorylation increases LKB1 nucleus export and apoptosis in endothelial cells. J. Biol. Chem. 283:12446-12455.
    • (2008) J. Biol. Chem. , vol.283 , pp. 12446-12455
    • Song, P.1    Xie, Z.2    Wu, Y.3    Xu, J.4    Dong, Y.5    Zou, M.H.6
  • 45
    • 34547673497 scopus 로고    scopus 로고
    • Peroxynitrite: biochemistry, pathophysiology and development of therapeutics
    • Szabó, C., H. Ischiropoulos, and R. Radi. 2007. Peroxynitrite: biochemistry, pathophysiology and development of therapeutics. Nat. Rev. Drug Discov. 6:662-680.
    • (2007) Nat. Rev. Drug Discov. , vol.6 , pp. 662-680
    • Szabó, C.1    Ischiropoulos, H.2    Radi, R.3
  • 46
    • 0029827580 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase (ERK1/2) activation by shear stress and adhesion in endothelial cells. Essential role for a herbimycin-sensitive kinase
    • Takahashi, M., and B.C. Berk. 1996. Mitogen-activated protein kinase (ERK1/2) activation by shear stress and adhesion in endothelial cells. Essential role for a herbimycin-sensitive kinase. J. Clin. Invest. 98:2623-2631.
    • (1996) J. Clin. Invest. , vol.98 , pp. 2623-2631
    • Takahashi, M.1    Berk, B.C.2
  • 47
    • 0033568723 scopus 로고    scopus 로고
    • Rapid and irreversible inactivation of protein tyrosine phosphatases PTP1B, CD45, and LAR by peroxynitrite
    • Takakura, K., J.S. Beckman, L.A. MacMillan-Crow, and J.P. Crow. 1999. Rapid and irreversible inactivation of protein tyrosine phosphatases PTP1B, CD45, and LAR by peroxynitrite. Arch. Biochem. Biophys. 369:197-207.
    • (1999) Arch. Biochem. Biophys. , vol.369 , pp. 197-207
    • Takakura, K.1    Beckman, J.S.2    MacMillan-Crow, L.A.3    Crow, J.P.4
  • 49
    • 0033621560 scopus 로고    scopus 로고
    • p21WAF1/CIP1 antisense therapy radiosensitizes human colon cancer by converting growth arrest to apoptosis
    • Tian, H., E.K. Wittmack, and T.J. Jorgensen. 2000. p21WAF1/CIP1 antisense therapy radiosensitizes human colon cancer by converting growth arrest to apoptosis. Cancer Res. 60:679-684.
    • (2000) Cancer Res , vol.60 , pp. 679-684
    • Tian, H.1    Wittmack, E.K.2    Jorgensen, T.J.3
  • 50
    • 0031833126 scopus 로고    scopus 로고
    • Laminar shear stress: mechanisms by which endothelial cells transduce an atheroprotective force
    • Traub, O., and B.C. Berk. 1998. Laminar shear stress: mechanisms by which endothelial cells transduce an atheroprotective force. Arterioscler. Thromb. Vasc. Biol. 18:677-685.
    • (1998) Arterioscler. Thromb. Vasc. Biol. , vol.18 , pp. 677-685
    • Traub, O.1    Berk, B.C.2
  • 53
    • 77952570613 scopus 로고    scopus 로고
    • SENP1 participates in the dynamic regulation of Elk-1 SUMOylation
    • Witty, J., E. Aguilar-Martinez, and A.D. Sharrocks. 2010. SENP1 participates in the dynamic regulation of Elk-1 SUMOylation. Biochem. J. 428:247-254.
    • (2010) Biochem. J. , vol.428 , pp. 247-254
    • Witty, J.1    Aguilar-Martinez, E.2    Sharrocks, A.D.3
  • 54
    • 36348979264 scopus 로고    scopus 로고
    • Relative reduction of endothelial nitric-oxide synthase expression and transcription in atherosclerosis-prone regions of the mouse aorta and in an in vitro model of disturbed flow
    • Won, D., S.N. Zhu, M. Chen, A.M. Teichert, J.E. Fish, C.C. Matouk, M. Bonert, M. Ojha, P.A. Marsden, and M.I. Cybulsky. 2007. Relative reduction of endothelial nitric-oxide synthase expression and transcription in atherosclerosis-prone regions of the mouse aorta and in an in vitro model of disturbed flow. Am. J. Pathol. 171:1691-1704.
    • (2007) Am. J. Pathol. , vol.171 , pp. 1691-1704
    • Won, D.1    Zhu, S.N.2    Chen, M.3    Teichert, A.M.4    Fish, J.E.5    Matouk, C.C.6    Bonert, M.7    Ojha, M.8    Marsden, P.A.9    Cybulsky, M.I.10
  • 55
    • 33845956237 scopus 로고    scopus 로고
    • ERK5 activation inhibits inflammatory responses via peroxisome proliferator-activated receptor delta (PPARdelta) stimulation
    • Woo, C.H., M.P. Massett, T. Shishido, S. Itoh, B. Ding, C. McClain, W. Che, S.R. Vulapalli, C. Yan, and J. Abe. 2006. ERK5 activation inhibits inflammatory responses via peroxisome proliferator-activated receptor delta (PPARdelta) stimulation. J. Biol. Chem. 281:32164-32174.
    • (2006) J. Biol. Chem. , vol.281 , pp. 32164-32174
    • Woo, C.H.1    Massett, M.P.2    Shishido, T.3    Itoh, S.4    Ding, B.5    McClain, C.6    Che, W.7    Vulapalli, S.R.8    Yan, C.9    Abe, J.10
  • 56
    • 40949145324 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinase 5 SUMOylation antagonizes shear stress-induced antiinflammatory response and endothelial nitric oxide synthase expression in endothelial cells
    • Woo, C.H., T. Shishido, C. McClain, J.H. Lim, J.D. Li, J. Yang, C. Yan, and J.I. Abe. 2008. Extracellular signal-regulated kinase 5 SUMOylation antagonizes shear stress-induced antiinflammatory response and endothelial nitric oxide synthase expression in endothelial cells. Circ. Res. 102:538-545.
    • (2008) Circ. Res. , vol.102 , pp. 538-545
    • Woo, C.H.1    Shishido, T.2    McClain, C.3    Lim, J.H.4    Li, J.D.5    Yang, J.6    Yan, C.7    Abe, J.I.8
  • 57
    • 63549129144 scopus 로고    scopus 로고
    • SUMOylation and De-SUMOylation: wrestling with life's processes
    • Yeh, E.T. 2009. SUMOylation and De-SUMOylation: wrestling with life's processes. J. Biol. Chem. 284:8223-8227.
    • (2009) J. Biol. Chem. , vol.284 , pp. 8223-8227
    • Yeh, E.T.1
  • 58
    • 0034698082 scopus 로고    scopus 로고
    • Peroxynitrite targets the epidermal growth factor receptor, Raf-1, and MEK independently to activate MAPK
    • Zhang, P., Y.Z. Wang, E. Kagan, and J.C. Bonner. 2000. Peroxynitrite targets the epidermal growth factor receptor, Raf-1, and MEK independently to activate MAPK. J. Biol. Chem. 275:22479-22486.
    • (2000) J. Biol. Chem. , vol.275 , pp. 22479-22486
    • Zhang, P.1    Wang, Y.Z.2    Kagan, E.3    Bonner, J.C.4


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