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Volumn 287, Issue 51, 2012, Pages 43071-43082

Identification of novel interaction between ADAM17 (a disintegrin and metalloprotease 17) and thioredoxin-1

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVITY REGULATION; CATALYTIC DOMAINS; CELL MODEL; CONVERTING ENZYME; CROSS-LINKED COMPLEX; CYTOPLASMIC DOMAINS; ECTODOMAIN SHEDDING; EXTRACELLULAR; HEK293 CELLS; HEPARIN BINDING; IMMUNOBLOTTING; IMMUNOLOCALIZATION; IMMUNOPRECIPITATIONS; IN-VITRO; LYSINE RESIDUES; METALLO-PROTEASE; OVER-EXPRESSION; PHORBOL 12 MYRISTATE 13 ACETATES; RECEPTOR LIGANDS; SHEDDASE; SOLID-PHASE BINDING ASSAY; SURFACE PROTEINS;

EID: 84871105065     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.364513     Document Type: Article
Times cited : (33)

References (50)
  • 1
    • 56749133149 scopus 로고    scopus 로고
    • The ADAMs. Signaling scissors in the tumour microenvironment
    • Murphy, G. (2008) The ADAMs. Signaling scissors in the tumour microenvironment. Nat. Rev. Cancer 8, 929-941
    • (2008) Nat. Rev. Cancer , vol.8 , pp. 929-941
    • Murphy, G.1
  • 2
    • 76849107016 scopus 로고    scopus 로고
    • Direct activation of TACE-mediated ectodomain shedding by p38 MAP kinase regulates EGF receptor-depent cell proliferation
    • Xu, P., and Derynck, R. (2010) Direct activation of TACE-mediated ectodomain shedding by p38 MAP kinase regulates EGF receptor-depent cell proliferation. Mol. Cell 37, 551-566
    • (2010) Mol. Cell , vol.37 , pp. 551-566
    • Xu, P.1    Derynck, R.2
  • 5
    • 0033573049 scopus 로고    scopus 로고
    • Ectodomain shedding of TGF-α and other transmembrane proteins is induced by receptor tyrosine kinase activation and MAP kinase signaling cascades
    • Fan, H., and Derynck, R. (1999) Ectodomain shedding of TGF-α and other transmembrane proteins is induced by receptor tyrosine kinase activation and MAP kinase signaling cascades. EMBO J. 18, 6962-6972 (Pubitemid 30000449)
    • (1999) EMBO Journal , vol.18 , Issue.24 , pp. 6962-6972
    • Fan, H.1    Derynck, R.2
  • 6
    • 0035985185 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinase phosphorylates tumor necrosis factor α-converting enzyme at threonine 735: A potential role in regulated shedding
    • DOI 10.1091/mbc.01-11-0561
    • Díaz-Rodríguez, E., Montero, J. C., Esparís-Ogando, A., Yuste, L., and Pandiella, A. (2002) Extracellular signal-regulated kinase phosphorylates tumor necrosis factor α-converting enzyme at threonine 735. A potentialrole in regulated shedding. Mol. Biol. Cell 13, 2031-2044 (Pubitemid 34651490)
    • (2002) Molecular Biology of the Cell , vol.13 , Issue.6 , pp. 2031-2044
    • Diaz-Rodriguez, E.1    Montero, J.C.2    Esparis-Ogando, A.3    Yuste, L.4    Pandiella, A.5
  • 8
    • 0035260351 scopus 로고    scopus 로고
    • Reactive oxygen species mediate tumor necrosis factor α-converting, enzyme-dependent ectodomainshedding induced by phorbol myristate acetate
    • Zhang, Z., Oliver, P., Lancaster, J. R., Jr., Schwarzenberger, P. O., Joshi, M. S., Cork, J., and Kolls, J. K. (2001) Reactive oxygen species mediate tumor necrosis factor α-converting, enzyme-dependent ectodomainshedding induced by phorbol myristate acetate. FASEB J. 15, 303-305
    • (2001) FASEB J. , vol.15 , pp. 303-305
    • Zhang, Z.1    Oliver, P.2    Lancaster Jr., J.R.3    Schwarzenberger, P.O.4    Joshi, M.S.5    Cork, J.6    Kolls, J.K.7
  • 9
    • 80053030745 scopus 로고    scopus 로고
    • Shedding of the Mer tyrosine kinase receptor is mediated by ADAM17 protein through a pathway involving reactive oxygen species, protein kinase Cδ, and p38 mitogen-activated protein kinase (MAPK)
    • Thorp, E., Vaisar, T., Subramanian, M., Mautner, L., Blobel, C., and Tabas, I. (2011) Shedding of the Mer tyrosine kinase receptor is mediated by ADAM17 protein through a pathway involving reactive oxygen species, protein kinase Cδ, and p38 mitogen-activated protein kinase (MAPK). J. Biol. Chem. 286, 33335-33344
    • (2011) J. Biol. Chem. , vol.286 , pp. 33335-33344
    • Thorp, E.1    Vaisar, T.2    Subramanian, M.3    Mautner, L.4    Blobel, C.5    Tabas, I.6
  • 10
    • 80053927932 scopus 로고    scopus 로고
    • Reactive oxygen species and p38 mitogen-activated protein kinase mediate tumor necrosis factorα-converting enzyme (TACE/ADAM-17) activation in primary human monocytes
    • Scott, A. J., O'Dea, K. P., O'Callaghan, D., Williams, L., Dokpesi, J. O., Tatton, L., Handy, J. M., Hogg, P. J., and Takata. (2011) Reactive oxygen species and p38 mitogen-activated protein kinase mediate tumor necrosis factorα-converting enzyme (TACE/ADAM-17) activation in primary human monocytes. J. Biol. Chem. 286, 35466-35476
    • (2011) J. Biol. Chem. , vol.286 , pp. 35466-35476
    • Scott, A.J.1    O'Dea, K.P.2    O'Callaghan, D.3    Williams, L.4    Dokpesi, J.O.5    Tatton, L.6    Handy, J.M.7    Hogg, P.J.8    Takata9
  • 11
    • 2442732615 scopus 로고    scopus 로고
    • Evidence for an interaction of the metalloprotease-disintegrin tumour necrosis factor α convertase (TACE) with mitotic arrest deficient 2 (MAD2), and of the metalloprotease-disintegrin MDC9 with a novel MAD2-related protein, MAD2β
    • DOI 10.1042/0264-6021:3430673
    • Nelson, K. K., Schlöndorff, J., and Blobel, C. P. (1999) Evidence for an interaction of the metalloprotease-disintegrin tumour necrosis factor α-convertase (TACE) with mitotic arrest deficient 2 (MAD2), and of themetalloprotease-disintegrin MDC9 with a novel MAD2-related protein, MAD2β. Biochem. J. 343, 673-680 (Pubitemid 29537381)
    • (1999) Biochemical Journal , vol.343 , Issue.3 , pp. 673-680
    • Nelson, K.K.1    Schlondorff, J.2    Blobel, C.P.3
  • 12
    • 0037044786 scopus 로고    scopus 로고
    • Evidence for regulation of the tumor necrosis factor α-convertase (TACE) by protein-tyrosine phosphatase PTPH1
    • DOI 10.1074/jbc.M207459200
    • Zheng, Y., Schlondorff, J., and Blobel, C. P. (2002) Evidence for regulation of the tumor necrosis factor α-convertase (TACE) by protein-tyrosinephosphatase PTPH1. J. Biol. Chem. 277, 42463-42470 (Pubitemid 35285612)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.45 , pp. 42463-42470
    • Zheng, Y.1    Schlondorff, J.2    Blobel, C.P.3
  • 14
    • 0034672264 scopus 로고    scopus 로고
    • Metalloprotease-disintegrin ADAM 12 binds to the SH3 domain of Src and activates Src tyrosine kinase in C2C12 cells
    • DOI 10.1042/0264-6021:3520883
    • Kang, Q., Cao, Y., and Zolkiewska, A. (2000) Metalloprotease-disintegrin ADAM 12 binds to the SH3 domain of Src and activates Src tyrosine kinase in C2C12 cells. Biochem. J. 352, 883-892 (Pubitemid 32015046)
    • (2000) Biochemical Journal , vol.352 , Issue.3 , pp. 883-892
    • Kang, Q.1    Cao, Y.2    Zolkiewska, A.3
  • 15
    • 0034735912 scopus 로고    scopus 로고
    • Meltrin α cytoplasmic domain interacts with SH3 domains of Src and Grb2 and is phosphorylated by v-Src
    • DOI 10.1038/sj.onc.1203986
    • Suzuki, A., Kadota, N., Hara, T., Nakagami, Y., Izumi, T., Takenawa, T., Sabe, H., and Endo, T. (2000) Meltrin α cytoplasmic domain interacts with SH3 domains of Src and Grb2 and is phosphorylated by v-Src. Oncogene. 19, 5842-5850 (Pubitemid 32005364)
    • (2000) Oncogene , vol.19 , Issue.51 , pp. 5842-5850
    • Suzuki, A.1    Kadota, N.2    Hara, T.3    Nakagami, Y.4    Izumi, T.5    Takenawa, T.6    Sabe, H.7    Endo, T.8
  • 16
    • 0035816683 scopus 로고    scopus 로고
    • Direct interaction between the cytoplasmic tail of ADAM 12 and the Src homology 3 domain of p85αactivates phosphatidylinositol 3-kinase in C2C12 cells
    • Kang, Q., Cao, Y., and Zolkiewska, A. (2001) Direct interaction between the cytoplasmic tail of ADAM 12 and the Src homology 3 domain of p85αactivates phosphatidylinositol 3-kinase in C2C12 cells. J. Biol. Chem. 276, 24466-24472
    • (2001) J. Biol. Chem. , vol.276 , pp. 24466-24472
    • Kang, Q.1    Cao, Y.2    Zolkiewska, A.3
  • 17
    • 0035878794 scopus 로고    scopus 로고
    • Metalloprotease-disintegrin ADAM 12 interacts with α-actinin-1
    • Cao, Y., Kang, Q., and Zolkiewska, A. (2001) Metalloprotease-disintegrin ADAM 12 interacts with α-actinin-1. Biochem. J. 357, 353-361
    • (2001) Biochem. J. , vol.357 , pp. 353-361
    • Cao, Y.1    Kang, Q.2    Zolkiewska, A.3
  • 18
    • 0037930878 scopus 로고    scopus 로고
    • The adaptor protein fish associates with members of the ADAMs family and localizes to podosomes of Src-transformed cells
    • DOI 10.1074/jbc.M300267200
    • Abram, C. L., Seals, D. F., Pass, I., Salinsky, D., Maurer, L., Roth, T. M., and Courtneidge, S. A. (2003) The adaptor protein fish associates with members of the ADAMs family and localizes to podosomes of Src-transformed cells. J. Biol. Chem. 278, 16844-16851 (Pubitemid 36799554)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.19 , pp. 16844-16851
    • Abram, C.L.1    Seals, D.F.2    Pass, I.3    Salinsky, D.4    Maurer, L.5    Roth, T.M.6    Courtneidge, S.A.7
  • 19
    • 0242580234 scopus 로고    scopus 로고
    • PACSIN3 Binds ADAM12/Meltrin α and Up-regulates Ectodomain Shedding of Heparin-binding Epidermal Growth Factor-like Growth Factor
    • DOI 10.1074/jbc.M306393200
    • Mori, S., Tanaka, M., Nanba, D., Nishiwaki, E., Ishiguro, H., Higashiyama, S., and Matsuura, N. (2003) PACSIN3 binds ADAM12/meltrin α and up-regulates ectodomain shedding of heparin-binding epidermal growth factor-like growth factor. J. Biol. Chem. 278, 46029-46034 (Pubitemid 37432752)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.46 , pp. 46029-46034
    • Mori, S.1    Tanaka, M.2    Nanba, D.3    Nishiwaki, E.4    Ishiguro, H.5    Higashiyama, S.6    Matsuura, N.7
  • 20
    • 4744355650 scopus 로고    scopus 로고
    • ADAM binding protein Eve-1 is required for ectodomain shedding of epidermal growth factor receptor ligands
    • DOI 10.1074/jbc.M400086200
    • Tanaka, M., Nanba, D., Mori, S., Shiba, F., Ishiguro, H., Yoshino, K., Matsuura, N., and Higashiyama, S. (2004) ADAM binding protein Eve-1 is required for ectodomain shedding of epidermal growth factor receptor ligands. J. Biol. Chem. 279, 41950-41959 (Pubitemid 39313645)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.40 , pp. 41950-41959
    • Tanaka, M.1    Nanba, D.2    Mori, S.3    Shiba, F.4    Ishiguro, H.5    Yoshino, K.6    Matsuura, N.7    Higashiyama, S.8
  • 23
    • 0038581051 scopus 로고    scopus 로고
    • TACE cleavage of proamphiregulin regulates GPCR-induced proliferation and motility of cancer cells
    • DOI 10.1093/emboj/cdg231
    • Gschwind, A., Hart, S., Fischer, O. M., and Ullrich, A. (2003) TACE cleavage of proamphiregulin regulates GPCR-induced proliferation and motility of cancer cells. EMBO J. 22, 2411-2421 (Pubitemid 36604980)
    • (2003) EMBO Journal , vol.22 , Issue.10 , pp. 2411-2421
    • Gschwind, A.1    Hart, S.2    Fischer, O.M.3    Ullrich, A.4
  • 24
    • 0029117425 scopus 로고
    • Induction of heparin-binding EGF-like growth factor expression during myogenesis. Activation of the gene by MyoD and localization of the transmembrane form of the protein on the myotube surface
    • Chen, X., Raab, G., Deutsch, U., Zhang, J., Ezzell, R. M., and Klagsbrun, M. (1995) Induction of heparin-binding EGF-like growth factor expression during myogenesis. Activation of the gene by MyoD and localization of the transmembrane form of the protein on the myotube surface. J. Biol. Chem. 270, 18285-18294
    • (1995) J. Biol. Chem. , vol.270 , pp. 18285-18294
    • Chen, X.1    Raab, G.2    Deutsch, U.3    Zhang, J.4    Ezzell, R.M.5    Klagsbrun, M.6
  • 25
    • 0032079871 scopus 로고    scopus 로고
    • Extracellular calcium influx stimulates metalloproteinase cleavage and secretion of heparin-binding EGF-like growth factor independently of protein kinase C
    • DOI 10.1002/(SICI)1097-4644(19980501)69:2<143::AID-JCB5>3.0.CO;2-S
    • Dethlefsen, S. M., Raab, G., Moses, M. A., Adam, R. M., Klagsbrun, M., and Freeman, M. R. (1998) Extracellular calcium influx stimulates metalloproteinase cleavage and secretion of heparin-binding EGF-like growth factor independently of protein kinase C. J. Cell. Biochem. 69, 143-153 (Pubitemid 28152947)
    • (1998) Journal of Cellular Biochemistry , vol.69 , Issue.2 , pp. 143-153
    • Dethlefsen, S.M.1    Raab, G.2    Moses, M.A.3    Adam, R.M.4    Klagsbrun, M.5    Freeman, M.R.6
  • 26
    • 21644432821 scopus 로고    scopus 로고
    • An oxidative stress mechanism mediates chelerythrine-induced heparin-binding EGF-like growth factor ectodomain shedding
    • DOI 10.1002/jcb.20276
    • Kim, J., Lin, J., Adam, R. M., Lamb, C., Shively, S. B., and Freeman, M. R. (2005) An oxidative stress mechanism mediates chelerythrine-induced heparin-binding EGF-like growth factor ectodomain shedding. J. Cell. Biochem. 94, 39-49 (Pubitemid 41420322)
    • (2005) Journal of Cellular Biochemistry , vol.94 , Issue.1 , pp. 39-49
    • Kim, J.1    Lin, J.2    Adam, R.M.3    Lamb, C.4    Shively, S.B.5    Freeman, M.R.6
  • 27
    • 62449310986 scopus 로고    scopus 로고
    • Membrane protease degradomics. Proteomic identification and quantification of cell surface protease substrates
    • Butler, G. S., Dean, R. A., Smith, D., and Overall, C. M. (2009) Membrane protease degradomics. Proteomic identification and quantification of cell surface protease substrates. Methods Mol. Biol. 528, 159-176
    • (2009) Methods Mol. Biol. , vol.528 , pp. 159-176
    • Butler, G.S.1    Dean, R.A.2    Smith, D.3    Overall, C.M.4
  • 28
    • 0036369512 scopus 로고    scopus 로고
    • Structure determination by NMR. Isotope labeling
    • Li, M. X., Corson, D. C., and Sykes, B. D. (2002) Structure determination by NMR. Isotope labeling. Methods Mol. Biol. 173, 255-265
    • (2002) Methods Mol. Biol. , vol.173 , pp. 255-265
    • Li, M.X.1    Corson, D.C.2    Sykes, B.D.3
  • 29
    • 77956624674 scopus 로고    scopus 로고
    • New insights into the structural elements involved in the skin haemorrhage induced by snake venom metalloproteinases
    • Oliveira, A. K., Paes Leme, A. F., Asega, A. F., Camargo, A. C., Fox, J. W., and Serrano, S. M. (2010) New insights into the structural elements involved in the skin haemorrhage induced by snake venom metalloproteinases. Thromb. Haemost. 104, 485-497
    • (2010) Thromb. Haemost. , vol.104 , pp. 485-497
    • Oliveira, A.K.1    Paes Leme, A.F.2    Asega, A.F.3    Camargo, A.C.4    Fox, J.W.5    Serrano, S.M.6
  • 30
    • 0037039335 scopus 로고    scopus 로고
    • Mapping protein-protein interactions in solution by NMR spectroscopy
    • Zuiderweg, E. R. (2002) Mapping protein-protein interactions in solution by NMR spectroscopy. Biochemistry 41, 1-7
    • (2002) Biochemistry , vol.41 , pp. 1-7
    • Zuiderweg, E.R.1
  • 31
    • 34249765651 scopus 로고
    • NMRView. A computer program for the visualization and analysis of NMR data
    • Johnson, B. A., and Blevins, R. A. (1994) NMRView. A computer program for the visualization and analysis of NMR data. J. Biomol. NMR 4, 603-614
    • (1994) J. Biomol. NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 32
    • 0347722841 scopus 로고    scopus 로고
    • Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients
    • PII S0079656598000259
    • Sattler, M., Schleucher, J., and Griesinger, C. (1999) Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients. Prog. NMR Spectrosc. 34, 93-158 (Pubitemid 129595216)
    • (1999) Progress in Nuclear Magnetic Resonance Spectroscopy , vol.34 , Issue.2 , pp. 93-158
    • Sattler, M.1    Schleucher, J.2    Griesinger, C.3
  • 33
    • 0000195671 scopus 로고
    • Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy
    • Bodenhausen, G., and Ruben, D. J. (1980) Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy. Chem. Phys. Lett. 69, 185-189
    • (1980) Chem. Phys. Lett. , vol.69 , pp. 185-189
    • Bodenhausen, G.1    Ruben, D.J.2
  • 34
    • 34249094851 scopus 로고    scopus 로고
    • A mass accuracy sensitive probability based scoring algorithm for database searching of tandem mass spectrometry data
    • Xu, H., and Freitas, M. A. (2007) A mass accuracy sensitive probability based scoring algorithm for database searching of tandem mass spectrometry data. BMC Bioinformatics 8, 133
    • (2007) BMC Bioinformatics , vol.8 , pp. 133
    • Xu, H.1    Freitas, M.A.2
  • 35
    • 0036007815 scopus 로고    scopus 로고
    • Intramolecular cross-linking experiments on cytochrome c and ribonuclease A using an isotope multiplet method
    • DOI 10.1002/rcm.554
    • Pearson, K. M., Pannell, L. K., and Fales, H. M. (2002) Intramolecular cross-linking experiments on cytochrome c and ribonuclease A using an isotope multiplet method. Rapid Commun. Mass Spectrom. 16, 149-159 (Pubitemid 34117996)
    • (2002) Rapid Communications in Mass Spectrometry , vol.16 , Issue.3 , pp. 149-159
    • Pearson, K.M.1    Pannell, L.K.2    Fales, H.M.3
  • 36
    • 0041846956 scopus 로고    scopus 로고
    • MS2Assign, automated assignment and nomenclature of tandem mass spectra of chemically crosslinked peptides
    • DOI 10.1016/S1044-0305(03)00327-1
    • Schilling, B., Row, R. H., Gibson, B. W., Guo, X., and Young, M. M. (2003) MS2Assign, automated assignment and nomenclature of tandem mass spectra of chemically crosslinked peptides. J. Am. Soc. Mass Spectrom. 14, 834-850 (Pubitemid 36904256)
    • (2003) Journal of the American Society for Mass Spectrometry , vol.14 , Issue.8 , pp. 834-850
    • Schilling, B.1    Row, R.H.2    Gibson, B.W.3    Guo, X.4    Young, M.M.5
  • 37
    • 74249090260 scopus 로고    scopus 로고
    • Improving physical realism, stereochemistry, and side-chain accuracy in homology modeling. Four approaches that performed well in CASP8
    • Krieger, E., Joo, K., Lee, J., Lee, J., Raman, S., Thompson, J., Tyka, M., Baker, D., and Karplus, K. (2009) Improving physical realism, stereochemistry, and side-chain accuracy in homology modeling. Four approaches that performed well in CASP8. Proteins. 77, 114-122
    • (2009) Proteins , vol.77 , pp. 114-122
    • Krieger, E.1    Joo, K.2    Lee, J.3    Lee, J.4    Raman, S.5    Thompson, J.6    Tyka, M.7    Baker, D.8    Karplus, K.9
  • 38
    • 77954065271 scopus 로고    scopus 로고
    • I-TASSER. A unified platform for automated protein structure and function prediction
    • Roy, A., Kucukural, A., and Zhang, Y. (2010) I-TASSER. A unified platform for automated protein structure and function prediction. Nat. Protoc. 5, 725-738
    • (2010) Nat. Protoc. , vol.5 , pp. 725-738
    • Roy, A.1    Kucukural, A.2    Zhang, Y.3
  • 39
    • 10344232638 scopus 로고    scopus 로고
    • Scoring function for automated assessment of protein structure template quality
    • DOI 10.1002/prot.20264
    • Zhang, Y., and Skolnick, J. (2004) Scoring function for automated assessment of protein structure template quality. Proteins 57, 702-710 (Pubitemid 39626992)
    • (2004) Proteins: Structure, Function and Genetics , vol.57 , Issue.4 , pp. 702-710
    • Zhang, Y.1    Skolnick, J.2
  • 40
    • 77949617607 scopus 로고    scopus 로고
    • PyRosetta. A script-based interface for implementing molecular modeling algorithms using Rosetta
    • Chaudhury, S., Lyskov, S., and Gray, J. J. (2010) PyRosetta. A script-based interface for implementing molecular modeling algorithms using Rosetta. Bioinformatics 26, 689-691
    • (2010) Bioinformatics , vol.26 , pp. 689-691
    • Chaudhury, S.1    Lyskov, S.2    Gray, J.J.3
  • 41
    • 34547902170 scopus 로고    scopus 로고
    • Cell-surface thioredoxin-1: Possible involvement in thiol-mediated leukocyte-endothelial cell interaction through lipid rafts
    • DOI 10.1089/ars.2007.1661
    • Hara, T., Kondo, N., Nakamura, H., Okuyama, H., Mitsui, A., Hoshino, Y., and Yodoi, J. (2007) Cell-surface thioredoxin-1. Possible involvement in thiol-mediated leukocyte-endothelial cell interaction through lipid rafts. Antioxid. Redox Signal. 9, 1427-1437 (Pubitemid 47255023)
    • (2007) Antioxidants and Redox Signaling , vol.9 , Issue.9 , pp. 1427-1437
    • Hara, T.1    Kondo, N.2    Nakamura, H.3    Okuyama, H.4    Mitsui, A.5    Hoshino, Y.6    Yodoi, J.7
  • 42
    • 0038719741 scopus 로고    scopus 로고
    • Characterization of growth factor-induced serine phosphorylation of tumor necrosis factor-α converting enzyme and of an alternatively translated polypeptide
    • DOI 10.1074/jbc.M300331200
    • Fan, H., Turck, C. W., and Derynck, R. (2003) Characterization of growth factor-induced serine phosphorylation of tumor necrosis factor-α converting enzyme and of an alternatively translated polypeptide. J. Biol. Chem. 278, 18617-18627 (Pubitemid 36799489)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.20 , pp. 18617-18627
    • Fan, H.1    Turck, C.W.2    Derynck, R.3
  • 43
    • 77954214884 scopus 로고    scopus 로고
    • Anti-oxidative, anti-cancer and anti-inflammatory actions by thioredoxin 1 and thioredoxin-binding protein-2
    • Watanabe, R., Nakamura, H., Masutani, H., and Yodoi. (2010) Anti-oxidative, anti-cancer and anti-inflammatory actions by thioredoxin 1 and thioredoxin-binding protein-2. Pharmacol. Ther. 127, 261-270
    • (2010) Pharmacol. Ther. , vol.127 , pp. 261-270
    • Watanabe, R.1    Nakamura, H.2    Masutani, H.3    Yodoi4
  • 44
    • 77956312086 scopus 로고    scopus 로고
    • Structure, function, and mechanism of thioredoxin proteins
    • Collet, J. F., and Messens, J. (2010) Structure, function, and mechanism of thioredoxin proteins. Antioxid. Redox Signal. 13, 1205-1216
    • (2010) Antioxid. Redox Signal. , vol.13 , pp. 1205-1216
    • Collet, J.F.1    Messens, J.2
  • 45
    • 2942569101 scopus 로고    scopus 로고
    • Oxidative and osmotic stress signaling in tumor cells is mediated by ADAM proteases and heparin-binding epidermal growth factor
    • DOI 10.1128/MCB.24.12.5172-5183.2004
    • Fischer, O. M., Hart, S., Gschwind, A., Prenzel, N., and Ullrich, A. (2004) Oxidative and osmotic stress signaling in tumor cells is mediated by ADAM proteases and heparin-binding epidermal growth factor. Mol. Cell Biol. 24, 5172-5183 (Pubitemid 38738154)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.12 , pp. 5172-5183
    • Fischer, O.M.1    Hart, S.2    Gschwind, A.3    Prenzel, N.4    Ullrich, A.5
  • 46
    • 4544225647 scopus 로고    scopus 로고
    • Mitochondrial function is required for hydrogen peroxide-induced growth factor receptor transactivation and downstream signaling
    • DOI 10.1074/jbc.M404859200
    • Chen, K., Thomas, S. R., Albano, A., Murphy, M. P., and Keaney, J. F., Jr. (2004) Mitochondrial function is required for hydrogen peroxide-induced growth factor receptor transactivation and downstream signaling. J. Biol. Chem. 279, 35079-35086 (Pubitemid 39318144)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.33 , pp. 35079-35086
    • Chen, K.1    Thomas, S.R.2    Albano, A.3    Murphy, M.P.4    Keaney Jr., J.F.5
  • 47
    • 73849141240 scopus 로고    scopus 로고
    • Mitochondrial reactive oxygen species mediate GPCR-induced TACE/ADAM17-dependent transforming growth factor-α shedding
    • Myers, T. J., Brennaman, L. H., Stevenson, M., Higashiyama, S., Russell, W. E., Lee, D. C., and Sunnarborg, S. W. (2009) Mitochondrial reactive oxygen species mediate GPCR-induced TACE/ADAM17-dependent transforming growth factor-α shedding. Mol. Biol. Cell 20, 5236-5249
    • (2009) Mol. Biol. Cell , vol.20 , pp. 5236-5249
    • Myers, T.J.1    Brennaman, L.H.2    Stevenson, M.3    Higashiyama, S.4    Russell, W.E.5    Lee, D.C.6    Sunnarborg, S.W.7
  • 48
    • 61449229249 scopus 로고    scopus 로고
    • Regulation of mature ADAM17 by redox agents for L-selectin shedding
    • Wang, Y., Herrera, A. H., Li, Y., Belani, K. K., and Walcheck, B. (2009) Regulation of mature ADAM17 by redox agents for L-selectin shedding. J. Immunol. 182, 2449-2457
    • (2009) J. Immunol. , vol.182 , pp. 2449-2457
    • Wang, Y.1    Herrera, A.H.2    Li, Y.3    Belani, K.K.4    Walcheck, B.5
  • 49
    • 77954896191 scopus 로고    scopus 로고
    • ADAMs and protein disulfide isomerase. The key to regulated cell-surface protein ectodomain shedding?
    • Bass, R., and Edwards, D. R. (2010) ADAMs and protein disulfide isomerase. The key to regulated cell-surface protein ectodomain shedding? Biochem. J. 428, e3-e5
    • (2010) Biochem. J. , vol.428
    • Bass, R.1    Edwards, D.R.2


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