메뉴 건너뛰기




Volumn 287, Issue 35, 2012, Pages 29290-29300

Protein disulfide isomerase is required for platelet-derived growth factor-induced vascular smooth muscle cell migration, Nox1 NADPH oxidase expression, and RhoGTPase activation

Author keywords

[No Author keywords available]

Indexed keywords

ADHESION STRUCTURES; BASE LINE; CELL TYPES; COLOCALIZATION; CYTOSKELETAL; ENDOPLASMIC RETICULUM; FOCAL ADHESIONS; GROWTH FACTOR; GTPASES; NADPH OXIDASE; NEOINTIMA; OVER-EXPRESSION; PLATELET-DERIVED GROWTH FACTORS; PROTEIN DISULFIDE ISOMERASES; PROTEIN-PROTEIN INTERACTION NETWORKS; REACTIVE OXYGEN SPECIES; RESTENOSIS; RHOGTPASE; STRESS FIBERS; SUB-CELLULAR; SYSTEMS BIOLOGY; THERAPEUTIC TARGETS; VASCULAR SMOOTH MUSCLE CELLS;

EID: 84865463143     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.394551     Document Type: Article
Times cited : (71)

References (70)
  • 1
    • 0030925749 scopus 로고    scopus 로고
    • Perspectives series. Cell adhesion in vascular biology: Smooth muscle migration in atherosclerosis and restenosis
    • Schwartz, S. M. (1997) Perspectives series. Cell adhesion in vascular biology: smooth muscle migration in atherosclerosis and restenosis. J. Clin. Invest. 99, 2814-2816
    • (1997) J. Clin. Invest. , vol.99 , pp. 2814-2816
    • Schwartz, S.M.1
  • 3
    • 2442666453 scopus 로고    scopus 로고
    • Phosphoinositide-dependent kinase 1 and p21-activated protein kinase mediate reactive oxygen species-dependent regulation of platelet-derived growth factor-induced smooth muscle cell migration
    • Weber, D. S., Taniyama, Y., Rocic, P., Seshiah, P. N., Dechert, M. A., Gerthoffer, W. T., and Griendling, K. K. (2004) Phosphoinositide-dependent kinase 1 and p21-activated protein kinase mediate reactive oxygen species-dependent regulation of platelet-derived growth factor-induced smooth muscle cell migration. Circ. Res. 94, 1219-1226
    • (2004) Circ. Res. , vol.94 , pp. 1219-1226
    • Weber, D.S.1    Taniyama, Y.2    Rocic, P.3    Seshiah, P.N.4    Dechert, M.A.5    Gerthoffer, W.T.6    Griendling, K.K.7
  • 8
    • 64749111284 scopus 로고    scopus 로고
    • Protein disulfide isomerase overexpression in vascular smooth muscle cells induces spontaneous preemptive NADPH oxidase activation and Nox1 mRNA expression: Effects of nitrosothiol exposure
    • Fernandes, D. C., Manoel, A. H., Wosniak, J., Jr., and Laurindo, F. R. (2009) Protein disulfide isomerase overexpression in vascular smooth muscle cells induces spontaneous preemptive NADPH oxidase activation and Nox1 mRNA expression: effects of nitrosothiol exposure. Arch. Biochem. Biophys. 484, 197-204
    • (2009) Arch. Biochem. Biophys. , vol.484 , pp. 197-204
    • Fernandes, D.C.1    Manoel, A.H.2    Wosniak Jr., J.3    Laurindo, F.R.4
  • 9
    • 70349643912 scopus 로고    scopus 로고
    • Protein disulfide isomerase (PDI) associates with NADPH oxidase and is required for phagocytosis of Leishmania chagasi promastigotes by macrophages
    • Santos, C. X., Stolf, B. S., Takemoto, P. V., Amanso, A. M., Lopes, L. R., Souza, E. B., Goto, H., and Laurindo, F. R. (2009) Protein disulfide isomerase (PDI) associates with NADPH oxidase and is required for phagocytosis of Leishmania chagasi promastigotes by macrophages. J. Leukoc. Biol. 86, 989-998
    • (2009) J. Leukoc. Biol. , vol.86 , pp. 989-998
    • Santos, C.X.1    Stolf, B.S.2    Takemoto, P.V.3    Amanso, A.M.4    Lopes, L.R.5    Souza, E.B.6    Goto, H.7    Laurindo, F.R.8
  • 10
    • 28844477782 scopus 로고    scopus 로고
    • Regulation of NAD(P)H oxidase by associated protein disulfide isomerase in vascular smooth muscle cells
    • Janiszewski, M., Lopes, L. R., Carmo, A. O., Pedro, M. A., Brandes, R. P., Santos, C. X., and Laurindo, F. R. (2005) Regulation of NAD(P)H oxidase by associated protein disulfide isomerase in vascular smooth muscle cells. J. Biol. Chem. 280, 40813-40819
    • (2005) J. Biol. Chem. , vol.280 , pp. 40813-40819
    • Janiszewski, M.1    Lopes, L.R.2    Carmo, A.O.3    Pedro, M.A.4    Brandes, R.P.5    Santos, C.X.6    Laurindo, F.R.7
  • 11
    • 0038457818 scopus 로고    scopus 로고
    • The thioredoxin-like fold: Hidden domains in protein disulfide isomerases and other chaperone proteins
    • Clissold, P. M., and Bicknell, R. (2003) The thioredoxin-like fold: hidden domains in protein disulfide isomerases and other chaperone proteins. Bioessays 25, 603-611
    • (2003) Bioessays , vol.25 , pp. 603-611
    • Clissold, P.M.1    Bicknell, R.2
  • 12
    • 14044271131 scopus 로고    scopus 로고
    • The human protein disulphide isomerase family: Substrate interactions and functional properties
    • Ellgaard, L., and Ruddock, L. W. (2005) The human protein disulphide isomerase family: substrate interactions and functional properties. EMBO Rep. 6, 28-32
    • (2005) EMBO Rep. , vol.6 , pp. 28-32
    • Ellgaard, L.1    Ruddock, L.W.2
  • 13
    • 0033210414 scopus 로고    scopus 로고
    • Protein disulfide isomerase: The multifunctional redox chaperone of the endoplasmic reticulum
    • Noiva, R. (1999) Protein disulfide isomerase: the multifunctional redox chaperone of the endoplasmic reticulum. Semin. Cell Dev. Biol. 10, 481-493
    • (1999) Semin. Cell Dev. Biol. , vol.10 , pp. 481-493
    • Noiva, R.1
  • 16
    • 39749084641 scopus 로고    scopus 로고
    • Active caspase-1 is a regulator of unconventional protein secretion
    • Keller, M., Rüegg, A., Werner, S., and Beer, H. D. (2008) Active caspase-1 is a regulator of unconventional protein secretion. Cell 132, 818-831
    • (2008) Cell , vol.132 , pp. 818-831
    • Keller, M.1    Rüegg, A.2    Werner, S.3    Beer, H.D.4
  • 17
    • 79957989772 scopus 로고    scopus 로고
    • Protein disulfide isomerase blocks CEBPA translation and is up-regulated during the unfolded protein response in AML
    • Haefliger, S., Klebig, C., Schaubitzer, K., Schardt, J., Timchenko, N., Mueller, B. U., and Pabst, T. (2011) Protein disulfide isomerase blocks CEBPA translation and is up-regulated during the unfolded protein response in AML. Blood 117, 5931-5940
    • (2011) Blood , vol.117 , pp. 5931-5940
    • Haefliger, S.1    Klebig, C.2    Schaubitzer, K.3    Schardt, J.4    Timchenko, N.5    Mueller, B.U.6    Pabst, T.7
  • 18
    • 33750002010 scopus 로고    scopus 로고
    • Redox regulation facilitates optimal peptide selection by MHC class I during antigen processing
    • Park, B., Lee, S., Kim, E., Cho, K., Riddell, S. R., Cho, S., and Ahn, K. (2006) Redox regulation facilitates optimal peptide selection by MHC class I during antigen processing. Cell 127, 369-382
    • (2006) Cell , vol.127 , pp. 369-382
    • Park, B.1    Lee, S.2    Kim, E.3    Cho, K.4    Riddell, S.R.5    Cho, S.6    Ahn, K.7
  • 19
    • 50549089349 scopus 로고    scopus 로고
    • PDIA3, HSPA5 and vimentin, proteins identified by 2-DE in the valvular tissue, are the target antigens of peripheral and heart infiltrating T cells from chronic rheumatic heart disease patients
    • Faé, K. C., Diefenbach da Silva, D., Bilate, A. M., Tanaka, A. C., Pomerantzeff, P. M., Kiss, M. H., Silva, C. A., Cunha-Neto, E., Kalil, J., and Guilherme, L. (2008) PDIA3, HSPA5 and vimentin, proteins identified by 2-DE in the valvular tissue, are the target antigens of peripheral and heart infiltrating T cells from chronic rheumatic heart disease patients. J. Autoimmun. 31, 136-141
    • (2008) J. Autoimmun. , vol.31 , pp. 136-141
    • Faé, K.C.1    Diefenbach Da Silva, D.2    Bilate, A.M.3    Tanaka, A.C.4    Pomerantzeff, P.M.5    Kiss, M.H.6    Silva, C.A.7    Cunha-Neto, E.8    Kalil, J.9    Guilherme, L.10
  • 20
    • 0029163450 scopus 로고
    • Secretion, surface localization, turnover, and steady state expression of protein disulfide isomerase in rat hepatocytes
    • Terada, K., Manchikalapudi, P., Noiva, R., Jauregui, H. O., Stockert, R. J., and Schilsky, M. L. (1995) Secretion, surface localization, turnover, and steady state expression of protein disulfide isomerase in rat hepatocytes. J. Biol. Chem. 270, 20410-20416
    • (1995) J. Biol. Chem. , vol.270 , pp. 20410-20416
    • Terada, K.1    Manchikalapudi, P.2    Noiva, R.3    Jauregui, H.O.4    Stockert, R.J.5    Schilsky, M.L.6
  • 21
    • 0035918587 scopus 로고    scopus 로고
    • Protein disulfide isomerase and sulfhydryl-dependent pathways in platelet activation
    • Essex, D. W., Li, M., Miller, A., and Feinman, R. D. (2001) Protein disulfide isomerase and sulfhydryl-dependent pathways in platelet activation. Biochemistry 40, 6070-6075
    • (2001) Biochemistry , vol.40 , pp. 6070-6075
    • Essex, D.W.1    Li, M.2    Miller, A.3    Feinman, R.D.4
  • 26
    • 65349088460 scopus 로고    scopus 로고
    • Cross-talk between mitochondria and NADPH oxidase: Effects of mild mitochondrial dysfunction on angiotensin II-mediated increase in Nox isoform expression and activity in vascular smooth muscle cells
    • Wosniak, J., Jr., Santos, C. X., Kowaltowski, A. J., and Laurindo, F. R. (2009) Cross-talk between mitochondria and NADPH oxidase: effects of mild mitochondrial dysfunction on angiotensin II-mediated increase in Nox isoform expression and activity in vascular smooth muscle cells. Antioxid. Redox Signal. 11, 1265-1278
    • (2009) Antioxid. Redox Signal. , vol.11 , pp. 1265-1278
    • Wosniak Jr., J.1    Santos, C.X.2    Kowaltowski, A.J.3    Laurindo, F.R.4
  • 27
    • 0033081753 scopus 로고    scopus 로고
    • Regulation of the small GTP-binding protein Rho by cell adhesion and the cytoskeleton
    • Ren, X. D., Kiosses, W. B., and Schwartz, M. A. (1999) Regulation of the small GTP-binding protein Rho by cell adhesion and the cytoskeleton. EMBO J. 18, 578-585
    • (1999) EMBO J. , vol.18 , pp. 578-585
    • Ren, X.D.1    Kiosses, W.B.2    Schwartz, M.A.3
  • 29
    • 2942552459 scopus 로고    scopus 로고
    • An automated method for finding molecular complexes in large protein interaction networks
    • Bader, G. D., and Hogue, C. W. (2003) An automated method for finding molecular complexes in large protein interaction networks. BMC Bioinformatics 4, 2
    • (2003) BMC Bioinformatics , vol.4 , pp. 2
    • Bader, G.D.1    Hogue, C.W.2
  • 30
    • 48449102450 scopus 로고    scopus 로고
    • Hubba: Hub objects analyzer, a framework of interactome hubs identification for network biology
    • Lin, C. Y., Chin, C. H., Wu, H. H., Chen, S. H., Ho, C. W., and Ko, M. T. (2008) Hubba: hub objects analyzer, a framework of interactome hubs identification for network biology. Nucleic Acids Res. 36, W438-443
    • (2008) Nucleic Acids Res. , vol.36
    • Lin, C.Y.1    Chin, C.H.2    Wu, H.H.3    Chen, S.H.4    Ho, C.W.5    Ko, M.T.6
  • 31
    • 24044440971 scopus 로고    scopus 로고
    • BiNGO: A Cytoscape plugin to assess overrepresentation of gene ontology categories in biological networks
    • Maere, S., Heymans, K., and Kuiper, M. (2005) BiNGO: a Cytoscape plugin to assess overrepresentation of gene ontology categories in biological networks. Bioinformatics 21, 3448-3449
    • (2005) Bioinformatics , vol.21 , pp. 3448-3449
    • Maere, S.1    Heymans, K.2    Kuiper, M.3
  • 32
    • 33847264343 scopus 로고    scopus 로고
    • Enrichment or depletion of a GO category within a class of genes: Which test?
    • Rivals, I., Personnaz, L., Taing, L., and Potier, M. C. (2007) Enrichment or depletion of a GO category within a class of genes: which test? Bioinformatics 23, 401-407
    • (2007) Bioinformatics , vol.23 , pp. 401-407
    • Rivals, I.1    Personnaz, L.2    Taing, L.3    Potier, M.C.4
  • 33
    • 0001677717 scopus 로고
    • Controlling the false discovery rate: A practical and powerful approach to multiple testing
    • Benjamini, Y., and Hochberg, Y. (1995) Controlling the false discovery rate: a practical and powerful approach to multiple testing. J. Royal Statistical Society Series B-Methodological 57, 289-300
    • (1995) J. Royal Statistical Society Series B-Methodological , vol.57 , pp. 289-300
    • Benjamini, Y.1    Hochberg, Y.2
  • 34
    • 79952674000 scopus 로고    scopus 로고
    • Interactome networks and human disease
    • Vidal, M., Cusick, M. E., and Barabási, A. L. (2011) Interactome networks and human disease. Cell 144, 986-998
    • (2011) Cell , vol.144 , pp. 986-998
    • Vidal, M.1    Cusick, M.E.2    Barabási, A.L.3
  • 35
    • 71549132149 scopus 로고    scopus 로고
    • Protein disulfide isomerase: A critical evaluation of its function in disulfide bond formation
    • Hatahet, F., and Ruddock, L. W. (2009) Protein disulfide isomerase: a critical evaluation of its function in disulfide bond formation. Antioxid. Redox Signal. 11, 2807-2850
    • (2009) Antioxid. Redox Signal. , vol.11 , pp. 2807-2850
    • Hatahet, F.1    Ruddock, L.W.2
  • 36
    • 13944249973 scopus 로고    scopus 로고
    • Centrality and network flow
    • Borgatti, S. P. (2005) Centrality and network flow. Social Networks 27, 55-71
    • (2005) Social Networks , vol.27 , pp. 55-71
    • Borgatti, S.P.1
  • 38
    • 33645285957 scopus 로고    scopus 로고
    • Regulation of NADPH oxidases: The role of Rac proteins
    • Hordijk, P. L. (2006) Regulation of NADPH oxidases: the role of Rac proteins. Circ. Res. 98, 453-462
    • (2006) Circ. Res. , vol.98 , pp. 453-462
    • Hordijk, P.L.1
  • 39
  • 40
    • 0038433238 scopus 로고    scopus 로고
    • Podosomes: Adhesion hot-spots of invasive cells
    • Linder, S., and Aepfelbacher, M. (2003) Podosomes: adhesion hot-spots of invasive cells. Trends Cell Biol. 13, 376-385
    • (2003) Trends Cell Biol. , vol.13 , pp. 376-385
    • Linder, S.1    Aepfelbacher, M.2
  • 41
    • 70349352744 scopus 로고    scopus 로고
    • Mechanisms and implications of reactive oxygen species generation during the unfolded protein response: Roles of endoplasmic reticulum oxidoreductases, mitochondrial electron transport, and NADPH oxidase
    • Santos, C. X., Tanaka, L. Y., Wosniak, J., and Laurindo, F. R. (2009) Mechanisms and implications of reactive oxygen species generation during the unfolded protein response: roles of endoplasmic reticulum oxidoreductases, mitochondrial electron transport, and NADPH oxidase. Antioxid. Redox Signal. 11, 2409-2427
    • (2009) Antioxid. Redox Signal. , vol.11 , pp. 2409-2427
    • Santos, C.X.1    Tanaka, L.Y.2    Wosniak, J.3    Laurindo, F.R.4
  • 42
    • 79551585674 scopus 로고    scopus 로고
    • Protein disulfide isomerase knockdown-induced cell death is cell line-dependent and involves apoptosis in MCF-7 cells
    • Hashida, T., Kotake, Y., and Ohta, S. (2011) Protein disulfide isomerase knockdown-induced cell death is cell line-dependent and involves apoptosis in MCF-7 cells. J. Toxicol. Sci. 36, 1-7
    • (2011) J. Toxicol. Sci. , vol.36 , pp. 1-7
    • Hashida, T.1    Kotake, Y.2    Ohta, S.3
  • 43
    • 43949107171 scopus 로고    scopus 로고
    • Endoplasmic reticulum chaperones are involved in the morphogenesis of rotavirus infectious particles
    • Maruri-Avidal, L., López, S., and Arias, C. F. (2008) Endoplasmic reticulum chaperones are involved in the morphogenesis of rotavirus infectious particles. J. Virol. 82, 5368-5380
    • (2008) J. Virol. , vol.82 , pp. 5368-5380
    • Maruri-Avidal, L.1    López, S.2    Arias, C.F.3
  • 44
    • 50149086087 scopus 로고    scopus 로고
    • Down-regulation of protein disulfide isomerase in sepsis and its role in tumor necrosis factor-α release
    • Zhou, M., Jacob, A., Ho, N., Miksa, M., Wu, R., Maitra, S. R., and Wang, P. (2008) Down-regulation of protein disulfide isomerase in sepsis and its role in tumor necrosis factor-α release. Crit. Care 12, R100
    • (2008) Crit. Care , vol.12
    • Zhou, M.1    Jacob, A.2    Ho, N.3    Miksa, M.4    Wu, R.5    Maitra, S.R.6    Wang, P.7
  • 45
    • 51749114237 scopus 로고    scopus 로고
    • Protein folding includes oligomerization: Examples from the endoplasmic reticulum and cytosol
    • Christis, C., Lubsen, N. H., and Braakman, I. (2008) Protein folding includes oligomerization: examples from the endoplasmic reticulum and cytosol. FEBS J. 275, 4700-4727
    • (2008) FEBS J. , vol.275 , pp. 4700-4727
    • Christis, C.1    Lubsen, N.H.2    Braakman, I.3
  • 46
    • 0035877651 scopus 로고    scopus 로고
    • Role of extracellular molecular chaperones in the folding of oxidized proteins: Refolding of colloidal thyroglobulin by protein disulfide isomerase and immunoglobulin heavy chain-binding protein
    • Delom, F., Mallet, B., Carayon, P., and Lejeune, P. J. (2001) Role of extracellular molecular chaperones in the folding of oxidized proteins: refolding of colloidal thyroglobulin by protein disulfide isomerase and immunoglobulin heavy chain-binding protein. J. Biol. Chem. 276, 21337-21342
    • (2001) J. Biol. Chem. , vol.276 , pp. 21337-21342
    • Delom, F.1    Mallet, B.2    Carayon, P.3    Lejeune, P.J.4
  • 47
    • 0036786353 scopus 로고    scopus 로고
    • Sustained integrin ligation involves extracellular free sulfhydryls and enzymatically catalyzed disulfide exchange
    • Lahav, J., Jurk, K., Hess, O., Barnes, M. J., Farndale, R. W., Luboshitz, J., and Kehrel, B. E. (2002) Sustained integrin ligation involves extracellular free sulfhydryls and enzymatically catalyzed disulfide exchange. Blood 100, 2472-2478
    • (2002) Blood , vol.100 , pp. 2472-2478
    • Lahav, J.1    Jurk, K.2    Hess, O.3    Barnes, M.J.4    Farndale, R.W.5    Luboshitz, J.6    Kehrel, B.E.7
  • 48
    • 0034674762 scopus 로고    scopus 로고
    • Protein disulfide isomerase mediates integrin-dependent adhesion
    • Lahav, J., Gofer-Dadosh, N., Luboshitz, J., Hess, O., and Shaklai, M. (2000) Protein disulfide isomerase mediates integrin-dependent adhesion. FEBS Lett. 475, 89-92
    • (2000) FEBS Lett. , vol.475 , pp. 89-92
    • Lahav, J.1    Gofer-Dadosh, N.2    Luboshitz, J.3    Hess, O.4    Shaklai, M.5
  • 49
    • 0029144477 scopus 로고
    • Localization of protein disulfide isomerase to the external surface of the platelet plasma membrane
    • Essex, D. W., Chen, K., and Swiatkowska, M. (1995) Localization of protein disulfide isomerase to the external surface of the platelet plasma membrane. Blood 86, 2168-2173
    • (1995) Blood , vol.86 , pp. 2168-2173
    • Essex, D.W.1    Chen, K.2    Swiatkowska, M.3
  • 50
    • 0345772126 scopus 로고    scopus 로고
    • Inhibitors of protein-disulfide isomerase prevent cleavage of disulfide bonds in receptor-bound glycoprotein 120 and prevent HIV-1 entry
    • Gallina, A., Hanley, T. M., Mandel, R., Trahey, M., Broder, C. C., Viglianti, G. A., and Ryser, H. J. (2002) Inhibitors of protein-disulfide isomerase prevent cleavage of disulfide bonds in receptor-bound glycoprotein 120 and prevent HIV-1 entry. J. Biol. Chem. 277, 50579-50588
    • (2002) J. Biol. Chem. , vol.277 , pp. 50579-50588
    • Gallina, A.1    Hanley, T.M.2    Mandel, R.3    Trahey, M.4    Broder, C.C.5    Viglianti, G.A.6    Ryser, H.J.7
  • 51
    • 79960601577 scopus 로고    scopus 로고
    • Galectin-9 binding to cell surface protein disulfide isomerase regulates the redox environment to enhance T-cell migration and HIV entry
    • Bi, S., Hong, P. W., Lee, B., and Baum, L. G. (2011) Galectin-9 binding to cell surface protein disulfide isomerase regulates the redox environment to enhance T-cell migration and HIV entry. Proc. Natl. Acad. Sci. U.S.A. 108, 10650-10655
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 10650-10655
    • Bi, S.1    Hong, P.W.2    Lee, B.3    Baum, L.G.4
  • 53
    • 0034683079 scopus 로고    scopus 로고
    • Oxidative stress as a signaling mechanism of the vascular response to injury: The redox hypothesis of restenosis
    • Azevedo, L. C., Pedro, M. A., Souza, L. C., de Souza, H. P., Janiszewski, M., da Luz, P. L., and Laurindo, F. R. (2000) Oxidative stress as a signaling mechanism of the vascular response to injury: the redox hypothesis of restenosis. Cardiovasc. Res. 47, 436-445
    • (2000) Cardiovasc. Res. , vol.47 , pp. 436-445
    • Azevedo, L.C.1    Pedro, M.A.2    Souza, L.C.3    De Souza, H.P.4    Janiszewski, M.5    Da Luz, P.L.6    Laurindo, F.R.7
  • 56
    • 78649918283 scopus 로고    scopus 로고
    • Oxidative protein folding by an endoplasmic reticulum-localized peroxiredoxin
    • Zito, E., Melo, E. P., Yang, Y., Wahlander, Å., Neubert, T. A., and Ron, D. (2010) Oxidative protein folding by an endoplasmic reticulum-localized peroxiredoxin. Mol. Cell 40, 787-797
    • (2010) Mol. Cell , vol.40 , pp. 787-797
    • Zito, E.1    Melo, E.P.2    Yang, Y.3    Wahlander, Å.4    Neubert, T.A.5    Ron, D.6
  • 57
    • 70849101711 scopus 로고    scopus 로고
    • Protein disulphide isomerase family members show distinct substrate specificity: P5 is targeted to BiP client proteins
    • Jessop, C. E., Watkins, R. H., Simmons, J. J., Tasab, M., and Bulleid, N. J. (2009) Protein disulphide isomerase family members show distinct substrate specificity: P5 is targeted to BiP client proteins. J. Cell Sci. 122, 4287-4295
    • (2009) J. Cell Sci. , vol.122 , pp. 4287-4295
    • Jessop, C.E.1    Watkins, R.H.2    Simmons, J.J.3    Tasab, M.4    Bulleid, N.J.5
  • 58
  • 59
  • 60
    • 33745183117 scopus 로고    scopus 로고
    • Association of RhoGDIα with Rac1 GTPase mediates free radical production during myocardial hypertrophy
    • Custodis, F., Eberl, M., Kilter, H., Böhm, M., and Laufs, U. (2006) Association of RhoGDIα with Rac1 GTPase mediates free radical production during myocardial hypertrophy. Cardiovasc. Res. 71, 342-351
    • (2006) Cardiovasc. Res. , vol.71 , pp. 342-351
    • Custodis, F.1    Eberl, M.2    Kilter, H.3    Böhm, M.4    Laufs, U.5
  • 61
    • 66149117890 scopus 로고    scopus 로고
    • RhoGDP dissociation inhibitor 2 suppresses metastasis via unconventional regulation of RhoGTPases
    • Moissoglu, K., McRoberts, K. S., Meier, J. A., Theodorescu, D., and Schwartz, M. A. (2009) RhoGDP dissociation inhibitor 2 suppresses metastasis via unconventional regulation of RhoGTPases. Cancer Res. 69, 2838-2844
    • (2009) Cancer Res. , vol.69 , pp. 2838-2844
    • Moissoglu, K.1    McRoberts, K.S.2    Meier, J.A.3    Theodorescu, D.4    Schwartz, M.A.5
  • 62
    • 33749563294 scopus 로고    scopus 로고
    • Induction of the unfolded protein response in familial amyotrophic lateral sclerosis and association of protein-disulfide isomerase with superoxide dismutase 1
    • Atkin, J. D., Farg, M. A., Turner, B. J., Tomas, D., Lysaght, J. A., Nunan, J., Rembach, A., Nagley, P., Beart, P. M., Cheema, S. S., and Horne, M. K. (2006) Induction of the unfolded protein response in familial amyotrophic lateral sclerosis and association of protein-disulfide isomerase with superoxide dismutase 1. J. Biol. Chem. 281, 30152-30165
    • (2006) J. Biol. Chem. , vol.281 , pp. 30152-30165
    • Atkin, J.D.1    Farg, M.A.2    Turner, B.J.3    Tomas, D.4    Lysaght, J.A.5    Nunan, J.6    Rembach, A.7    Nagley, P.8    Beart, P.M.9    Cheema, S.S.10    Horne, M.K.11
  • 64
    • 79953307234 scopus 로고    scopus 로고
    • Rac1 regulates the activity of mTORC1 and mTORC2 and controls cellular size
    • Saci, A., Cantley, L. C., and Carpenter, C. L. (2011) Rac1 regulates the activity of mTORC1 and mTORC2 and controls cellular size. Mol. Cell 42, 50-61
    • (2011) Mol. Cell , vol.42 , pp. 50-61
    • Saci, A.1    Cantley, L.C.2    Carpenter, C.L.3
  • 66
    • 67949124784 scopus 로고    scopus 로고
    • On vesicle formation and tethering in the ER-Golgi shuttle
    • Spang, A. (2009) On vesicle formation and tethering in the ER-Golgi shuttle. Curr. Opin. Cell Biol. 21, 531-536
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 531-536
    • Spang, A.1
  • 67
    • 71649099053 scopus 로고    scopus 로고
    • Dual modes of cdc42 recycling fine-tune polarized morphogenesis
    • Slaughter, B. D., Das, A., Schwartz, J. W., Rubinstein, B., and Li, R. (2009) Dual modes of cdc42 recycling fine-tune polarized morphogenesis. Dev. Cell 17, 823-835
    • (2009) Dev. Cell , vol.17 , pp. 823-835
    • Slaughter, B.D.1    Das, A.2    Schwartz, J.W.3    Rubinstein, B.4    Li, R.5
  • 70
    • 39949084140 scopus 로고    scopus 로고
    • Spatial control of Rho (Rac-Rop) signaling in tip-growing plant cells
    • Kost, B. (2008) Spatial control of Rho (Rac-Rop) signaling in tip-growing plant cells. Trends Cell Biol. 18, 119-127
    • (2008) Trends Cell Biol. , vol.18 , pp. 119-127
    • Kost, B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.