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Volumn 41, Issue 2, 2009, Pages 274-285

Proinflammatory cytokines provoke oxidative damage to actin in neuronal cells mediated by Rac1 and NADPH oxidase

Author keywords

Actin; Cytokines; Lamellipodia; NADPH oxidase; Oxygen radicals; Rac1

Indexed keywords

ACTIN; INTERLEUKIN 1BETA; RAC1 PROTEIN; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; TUMOR NECROSIS FACTOR ALPHA;

EID: 67349164761     PISSN: 10447431     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mcn.2009.03.007     Document Type: Article
Times cited : (47)

References (65)
  • 2
    • 0035487313 scopus 로고    scopus 로고
    • Cytokines and acute neurodegeneration
    • Allan S., and Rothwell N. Cytokines and acute neurodegeneration. Nat. Rev. Neurosci. 2 (2001) 734-744
    • (2001) Nat. Rev. Neurosci. , vol.2 , pp. 734-744
    • Allan, S.1    Rothwell, N.2
  • 3
    • 0036570159 scopus 로고    scopus 로고
    • Oxidatively modified proteins in aging and disease
    • Beal M.F. Oxidatively modified proteins in aging and disease. Free Radic. Biol. Med. 32 (2002) 797-803
    • (2002) Free Radic. Biol. Med. , vol.32 , pp. 797-803
    • Beal, M.F.1
  • 4
    • 33846794822 scopus 로고    scopus 로고
    • The NOX family of ROS-generating NADPH oxidases: physiology and pathophysiology
    • Bedard K., and Krause K.H. The NOX family of ROS-generating NADPH oxidases: physiology and pathophysiology. Physiol. Rev. 87 (2007) 245-313
    • (2007) Physiol. Rev. , vol.87 , pp. 245-313
    • Bedard, K.1    Krause, K.H.2
  • 5
    • 0033053617 scopus 로고    scopus 로고
    • Reactive oxygen intermediate-dependent NF-kB activation by interleukin-1beta requires 5-lipoxygenase or NADPH oxidase activity
    • Bonizzi G., Piette J., Schoonbroodt S., Greimers R., Havard L., Merville M.-P., and Bours V. Reactive oxygen intermediate-dependent NF-kB activation by interleukin-1beta requires 5-lipoxygenase or NADPH oxidase activity. Mol. Cell. Biol. 19 (1999) 1950-1960
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1950-1960
    • Bonizzi, G.1    Piette, J.2    Schoonbroodt, S.3    Greimers, R.4    Havard, L.5    Merville, M.-P.6    Bours, V.7
  • 6
    • 0037101889 scopus 로고    scopus 로고
    • Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part I: creatine kinase BB, glutamine synthase, and ubiquitin carboxy-terminal hydrolase L-1
    • Castegna A., Aksenov M., Aksenova M., Thongboonkerd V., Klein J.B., Pierce W.M., Booze R., Markesbery W.R., and Butterfield D.A. Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part I: creatine kinase BB, glutamine synthase, and ubiquitin carboxy-terminal hydrolase L-1. Free Radic. Biol. Med. 33 (2002) 562-571
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 562-571
    • Castegna, A.1    Aksenov, M.2    Aksenova, M.3    Thongboonkerd, V.4    Klein, J.B.5    Pierce, W.M.6    Booze, R.7    Markesbery, W.R.8    Butterfield, D.A.9
  • 7
    • 0035900676 scopus 로고    scopus 로고
    • Reactive oxygen species are downstream products of TRAF-mediated signal transduction
    • Chandel N.S., Schumacker P.T., and Arch R.H. Reactive oxygen species are downstream products of TRAF-mediated signal transduction. J. Biol. Chem. 276 (2001) 42728-42736
    • (2001) J. Biol. Chem. , vol.276 , pp. 42728-42736
    • Chandel, N.S.1    Schumacker, P.T.2    Arch, R.H.3
  • 11
    • 0033813282 scopus 로고    scopus 로고
    • Rac1 inhibits TNF-alpha-induced endothelial cell apoptosis: dual regulation by reactive oxygen species
    • Deshpande S., Angkeow P., Huang J., Ozaki M., and Irani K. Rac1 inhibits TNF-alpha-induced endothelial cell apoptosis: dual regulation by reactive oxygen species. FASEB 14 (2000) 1705-1714
    • (2000) FASEB , vol.14 , pp. 1705-1714
    • Deshpande, S.1    Angkeow, P.2    Huang, J.3    Ozaki, M.4    Irani, K.5
  • 12
    • 0036086130 scopus 로고    scopus 로고
    • Free radicals in the physiological control of cell function
    • Droge W. Free radicals in the physiological control of cell function. Physiol. Rev. 82 (2002) 47-95
    • (2002) Physiol. Rev. , vol.82 , pp. 47-95
    • Droge, W.1
  • 14
    • 0036751954 scopus 로고    scopus 로고
    • Oxidative stress in brain aging. Implications for therapeutics of neurodegenerative diseases
    • Floyd R.A., and Hensley K. Oxidative stress in brain aging. Implications for therapeutics of neurodegenerative diseases. Neurobiol. Aging. 23 (2002) 795-807
    • (2002) Neurobiol. Aging. , vol.23 , pp. 795-807
    • Floyd, R.A.1    Hensley, K.2
  • 15
    • 0029814413 scopus 로고    scopus 로고
    • Rac "insert region" is a novel effector region that is implicated in the activation of NADPH oxidase, but not PAK65
    • Freeman J., Abo A., and Lambeth J. Rac "insert region" is a novel effector region that is implicated in the activation of NADPH oxidase, but not PAK65. J. Biol. Chem. 271 (1996) 19794-19801
    • (1996) J. Biol. Chem. , vol.271 , pp. 19794-19801
    • Freeman, J.1    Abo, A.2    Lambeth, J.3
  • 17
    • 21744445111 scopus 로고    scopus 로고
    • The actin cytoskeleton: a key regulator of apoptosis and ageing?
    • Gourlay C.W., and Ayscough K.R. The actin cytoskeleton: a key regulator of apoptosis and ageing?. Nat. Rev. Mol. Cell Biol. 6 (2005) 583-589
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 583-589
    • Gourlay, C.W.1    Ayscough, K.R.2
  • 18
    • 15944372262 scopus 로고    scopus 로고
    • Activation and assembly of the NADPH oxidase: a structural perspective
    • Groemping Y., and Rittinger K. Activation and assembly of the NADPH oxidase: a structural perspective. Biochem. J. 386 (2005) 401-416
    • (2005) Biochem. J. , vol.386 , pp. 401-416
    • Groemping, Y.1    Rittinger, K.2
  • 19
    • 0034729916 scopus 로고    scopus 로고
    • Rho GTPases: molecular switches that control the organization and dynamics of the actin cytoskeleton
    • Hall A., and Nobes C. Rho GTPases: molecular switches that control the organization and dynamics of the actin cytoskeleton. Philosoph. Trans. Royal Soc. London B 355 (2000) 965-970
    • (2000) Philosoph. Trans. Royal Soc. London B , vol.355 , pp. 965-970
    • Hall, A.1    Nobes, C.2
  • 20
    • 0034729916 scopus 로고    scopus 로고
    • Rho GTPases: molecular switches that control the organization and dynamics of the actin cytoskeleton
    • Hall A., and Nobes C.D. Rho GTPases: molecular switches that control the organization and dynamics of the actin cytoskeleton. Philosoph. Trans. Royal Soc. London Biol. Sci. 355 (2000) 965-970
    • (2000) Philosoph. Trans. Royal Soc. London Biol. Sci. , vol.355 , pp. 965-970
    • Hall, A.1    Nobes, C.D.2
  • 21
    • 0035192726 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha induces stress fiber formation through ceramide production: role of sphingosine kinase
    • Hanna A.N., Berthiaume L.G., Kikuchi Y., Begg D., Bourgoin S., and Brindley D.N. Tumor necrosis factor-alpha induces stress fiber formation through ceramide production: role of sphingosine kinase. Mol. Biol. Cell 12 (2001) 3618-3630
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3618-3630
    • Hanna, A.N.1    Berthiaume, L.G.2    Kikuchi, Y.3    Begg, D.4    Bourgoin, S.5    Brindley, D.N.6
  • 22
    • 33645285957 scopus 로고    scopus 로고
    • Regulation of NADPH oxidases: the role of Rac proteins
    • Hordijk P.L. Regulation of NADPH oxidases: the role of Rac proteins. Circ. Res. 98 (2006) 453-462
    • (2006) Circ. Res. , vol.98 , pp. 453-462
    • Hordijk, P.L.1
  • 23
    • 0035076234 scopus 로고    scopus 로고
    • The insert region of rac1 is essential for membrane ruffling but not cellular transformation
    • Karnoub A., Der C., and Campbell S. The insert region of rac1 is essential for membrane ruffling but not cellular transformation. Mol. Cell. Biol. 21 (2001) 2847-2857
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 2847-2857
    • Karnoub, A.1    Der, C.2    Campbell, S.3
  • 24
    • 0032496326 scopus 로고    scopus 로고
    • Role of rac1 and oxygen radicals in collagenase-1 expression induced by cell shape change
    • Kheradmand F., Werner E., Tremble P., Symons M., and Werb Z. Role of rac1 and oxygen radicals in collagenase-1 expression induced by cell shape change. Science 280 (1998) 898-902
    • (1998) Science , vol.280 , pp. 898-902
    • Kheradmand, F.1    Werner, E.2    Tremble, P.3    Symons, M.4    Werb, Z.5
  • 25
    • 0031857290 scopus 로고    scopus 로고
    • Interaction of reactive oxygen species with ion transport mechanisms
    • Kourie J.I. Interaction of reactive oxygen species with ion transport mechanisms. Am. J. Physiol. 275 (1998) C1-24
    • (1998) Am. J. Physiol. , vol.275
    • Kourie, J.I.1
  • 26
    • 0028987684 scopus 로고
    • The stimulus-sensitive H2O2-generating system present in human fat-cell plasma membranes is multireceptor-linked and under antagonistic control by hormones and cytokines
    • Krieger-Brauer H.I., and Kather H. The stimulus-sensitive H2O2-generating system present in human fat-cell plasma membranes is multireceptor-linked and under antagonistic control by hormones and cytokines. Biochem. J. 307 (1995) 543-548
    • (1995) Biochem. J. , vol.307 , pp. 543-548
    • Krieger-Brauer, H.I.1    Kather, H.2
  • 27
    • 0036134932 scopus 로고    scopus 로고
    • Nox/Duox family of nicotinamide adenine dinucleotide (phosphate) oxidases
    • Lambeth J.D. Nox/Duox family of nicotinamide adenine dinucleotide (phosphate) oxidases. Curr. Opin. Hematol. 9 (2002) 11-17
    • (2002) Curr. Opin. Hematol. , vol.9 , pp. 11-17
    • Lambeth, J.D.1
  • 28
    • 1542406446 scopus 로고    scopus 로고
    • NOX enzymes and the biology of reactive oxygen
    • Lambeth J.D. NOX enzymes and the biology of reactive oxygen. Nat. Rev. Immunol. 4 (2004) 181-189
    • (2004) Nat. Rev. Immunol. , vol.4 , pp. 181-189
    • Lambeth, J.D.1
  • 29
    • 34347257042 scopus 로고    scopus 로고
    • Nox enzymes, ROS, and chronic disease: an example of antagonistic pleiotropy
    • Lambeth J.D. Nox enzymes, ROS, and chronic disease: an example of antagonistic pleiotropy. Free Radic. Biol. Med. 43 (2007) 332-347
    • (2007) Free Radic. Biol. Med. , vol.43 , pp. 332-347
    • Lambeth, J.D.1
  • 31
    • 0035868484 scopus 로고    scopus 로고
    • Protein and DNA oxidation in spinal injury: neurofilaments-an oxidation target
    • Leski M.L., Bao F., Wu L., Qian H., Sun D., and Liu D. Protein and DNA oxidation in spinal injury: neurofilaments-an oxidation target. Free Radic. Biol. Med. 30 (2001) 613-624
    • (2001) Free Radic. Biol. Med. , vol.30 , pp. 613-624
    • Leski, M.L.1    Bao, F.2    Wu, L.3    Qian, H.4    Sun, D.5    Liu, D.6
  • 32
    • 0028291974 scopus 로고
    • Carbonyl assays for determination of oxidatively modified proteins
    • Levine R.L., Williams J.A., Stadtman E.R., and Shacter E. Carbonyl assays for determination of oxidatively modified proteins. Meth. Enzymol. 233 (1994) 346-357
    • (1994) Meth. Enzymol. , vol.233 , pp. 346-357
    • Levine, R.L.1    Williams, J.A.2    Stadtman, E.R.3    Shacter, E.4
  • 33
    • 0037205457 scopus 로고    scopus 로고
    • Intracellular localization and preassembly of the NADPH oxidase complex in cultured endothelial cells
    • Li J.M., and Shah A.M. Intracellular localization and preassembly of the NADPH oxidase complex in cultured endothelial cells. J. Biol. Chem. 277 (2002) 19952-19960
    • (2002) J. Biol. Chem. , vol.277 , pp. 19952-19960
    • Li, J.M.1    Shah, A.M.2
  • 37
    • 0034574572 scopus 로고    scopus 로고
    • Rho GTPases in neuronal morphogenesis
    • Luo L. Rho GTPases in neuronal morphogenesis. Nat. Rev. Neurosci. 1 (2000) 173-180
    • (2000) Nat. Rev. Neurosci. , vol.1 , pp. 173-180
    • Luo, L.1
  • 38
    • 0036441201 scopus 로고    scopus 로고
    • Actin cytoskeleton regulation in neuronal morphogenesis and structural plasticity
    • Luo L. Actin cytoskeleton regulation in neuronal morphogenesis and structural plasticity. Annu. Rev. Cell Dev. Biol. 18 (2002) 601-635
    • (2002) Annu. Rev. Cell Dev. Biol. , vol.18 , pp. 601-635
    • Luo, L.1
  • 39
    • 0034960315 scopus 로고    scopus 로고
    • Superoxide generation of phagocytes and nonphagocytic cells
    • Meier B. Superoxide generation of phagocytes and nonphagocytic cells. Protoplasma. 217 (2001) 117-124
    • (2001) Protoplasma. , vol.217 , pp. 117-124
    • Meier, B.1
  • 40
    • 0030889534 scopus 로고    scopus 로고
    • Paraquat induces actin assembly in depolymerizing conditions
    • Milzani A., Dalledonne I., Vailati G., and Colombo R. Paraquat induces actin assembly in depolymerizing conditions. FASEB 11 (1997) 261-270
    • (1997) FASEB , vol.11 , pp. 261-270
    • Milzani, A.1    Dalledonne, I.2    Vailati, G.3    Colombo, R.4
  • 43
    • 11444256801 scopus 로고    scopus 로고
    • Glia and their cytokines in progression of neurodegeneration
    • Mrak R.E., and Griffin W.S. Glia and their cytokines in progression of neurodegeneration. Neurobiol Aging 26 (2005) 349-354
    • (2005) Neurobiol Aging , vol.26 , pp. 349-354
    • Mrak, R.E.1    Griffin, W.S.2
  • 45
    • 0036469263 scopus 로고    scopus 로고
    • Tumor necrosis factor inhibits neurite outgrowth and branching of hippocampal neurons by a rho-dependent mechanism
    • Neumann H., Schweigreiter R., Yamashita T., Rosenkranz K., Wekerle H., and Barde Y.A. Tumor necrosis factor inhibits neurite outgrowth and branching of hippocampal neurons by a rho-dependent mechanism. J. Neurosci. 22 (2002) 854-862
    • (2002) J. Neurosci. , vol.22 , pp. 854-862
    • Neumann, H.1    Schweigreiter, R.2    Yamashita, T.3    Rosenkranz, K.4    Wekerle, H.5    Barde, Y.A.6
  • 46
    • 29744431971 scopus 로고    scopus 로고
    • Rac1-NADPH oxidase-regulated generation of reactive oxygen species mediates glutamate-induced apoptosis in SH-SY5Y human neuroblastoma cells
    • Nikolova S., Lee Y.S., Lee Y.S., and Kim J.A. Rac1-NADPH oxidase-regulated generation of reactive oxygen species mediates glutamate-induced apoptosis in SH-SY5Y human neuroblastoma cells. Free Radic. Res. 39 (2005) 1295-1304
    • (2005) Free Radic. Res. , vol.39 , pp. 1295-1304
    • Nikolova, S.1    Lee, Y.S.2    Lee, Y.S.3    Kim, J.A.4
  • 47
  • 48
    • 0028961293 scopus 로고
    • Rho, rac and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia and filopodia
    • Nobes C., and Hall A. Rho, rac and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia and filopodia. Cell. 81 (1995) 53-62
    • (1995) Cell. , vol.81 , pp. 53-62
    • Nobes, C.1    Hall, A.2
  • 49
    • 0002081257 scopus 로고    scopus 로고
    • Induction and activation by zinc of NADPH oxidase in cultured cortical neurons and astrocytes
    • Noh K.-M., and Koh J.-Y. Induction and activation by zinc of NADPH oxidase in cultured cortical neurons and astrocytes. J. Neurosci. 20 (2000) 1-5
    • (2000) J. Neurosci. , vol.20 , pp. 1-5
    • Noh, K.-M.1    Koh, J.-Y.2
  • 50
    • 0033556172 scopus 로고    scopus 로고
    • Multiple signal transduction pathways regulate TNF-induced actin reorganization in macrophages: inhibition of Cdc42-mediated filopodium formation by TNF
    • Peppelenbosch M., Boone E., Jones G.E., van Deventer S.J., Haegeman G., Fiers W., Grooten J., and Ridley A.J. Multiple signal transduction pathways regulate TNF-induced actin reorganization in macrophages: inhibition of Cdc42-mediated filopodium formation by TNF. J. Immunol. 162 (1999) 837-845
    • (1999) J. Immunol. , vol.162 , pp. 837-845
    • Peppelenbosch, M.1    Boone, E.2    Jones, G.E.3    van Deventer, S.J.4    Haegeman, G.5    Fiers, W.6    Grooten, J.7    Ridley, A.J.8
  • 51
    • 33645285000 scopus 로고    scopus 로고
    • Molecular functions of nuclear actin in transcription
    • Percipalle P., and Visa N. Molecular functions of nuclear actin in transcription. J. Cell Biol. 172 (2006) 967-971
    • (2006) J. Cell Biol. , vol.172 , pp. 967-971
    • Percipalle, P.1    Visa, N.2
  • 52
    • 0032841725 scopus 로고    scopus 로고
    • Activation of the small GTPase cdc42 by the inflammatory cytokines TNF and IL-1, and by the Eppstein-Barr virus transforming protein LMP1
    • Puls A., Eliopoulos A., Nobes C., Bridges T., Young L., and Hall A. Activation of the small GTPase cdc42 by the inflammatory cytokines TNF and IL-1, and by the Eppstein-Barr virus transforming protein LMP1. J. Cell Sci. 112 (1999) 2983-2992
    • (1999) J. Cell Sci. , vol.112 , pp. 2983-2992
    • Puls, A.1    Eliopoulos, A.2    Nobes, C.3    Bridges, T.4    Young, L.5    Hall, A.6
  • 53
    • 0025218905 scopus 로고
    • Flow cytometric analysis of respiratory burst activity in phagocytes with hydroethidine and 2′,7′-dichlorofluorescin
    • Rothe G., and Valet G. Flow cytometric analysis of respiratory burst activity in phagocytes with hydroethidine and 2′,7′-dichlorofluorescin. J. Leukoc. Biol. 47 (1990) 440-448
    • (1990) J. Leukoc. Biol. , vol.47 , pp. 440-448
    • Rothe, G.1    Valet, G.2
  • 54
    • 0034534995 scopus 로고    scopus 로고
    • Interleukin 1 in the brain: biology, pathology and therapeutic target
    • Rothwell N.J., and Luheshi G.N. Interleukin 1 in the brain: biology, pathology and therapeutic target. Trends Neurosci. 23 (2000) 618-625
    • (2000) Trends Neurosci. , vol.23 , pp. 618-625
    • Rothwell, N.J.1    Luheshi, G.N.2
  • 55
    • 0029912652 scopus 로고    scopus 로고
    • Rac1 regulates a cytokine-stimulated, redox-dependent pathway necessary for NF-kB activation
    • Sulciner D., Irani K., Yu Z., Ferrans V., Goldschmidt-Clermont P., and Finkel T. Rac1 regulates a cytokine-stimulated, redox-dependent pathway necessary for NF-kB activation. Mol. Cell. Biol. 16 (1996) 7115-7121
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 7115-7121
    • Sulciner, D.1    Irani, K.2    Yu, Z.3    Ferrans, V.4    Goldschmidt-Clermont, P.5    Finkel, T.6
  • 57
    • 0034607872 scopus 로고    scopus 로고
    • Nerve growth factor-induced neuronal differentiation requires generation of rac1-regulated reactive oxygen species
    • Suzukawa K., Miura K., Mitsushita J., Resau J., Hirose K., Crystal R., and Kamata T. Nerve growth factor-induced neuronal differentiation requires generation of rac1-regulated reactive oxygen species. J. Biol. Chem. 275 (2000) 13175-13178
    • (2000) J. Biol. Chem. , vol.275 , pp. 13175-13178
    • Suzukawa, K.1    Miura, K.2    Mitsushita, J.3    Resau, J.4    Hirose, K.5    Crystal, R.6    Kamata, T.7
  • 58
    • 0025785552 scopus 로고
    • Control of actin polymerization in live and permeabilized fibroblasts
    • Symons M., and Mitchison T. Control of actin polymerization in live and permeabilized fibroblasts. J. Cell Biol. 114 (1991) 503-513
    • (1991) J. Cell Biol. , vol.114 , pp. 503-513
    • Symons, M.1    Mitchison, T.2
  • 59
    • 17744417909 scopus 로고    scopus 로고
    • NADPH oxidase contributes directly to oxidative stress and apoptosis in nerve growth factor-deprived sympathetic neurons
    • Tammariello S., Quinn M., and Estus S. NADPH oxidase contributes directly to oxidative stress and apoptosis in nerve growth factor-deprived sympathetic neurons. J. Neurosci. 20 (2000) 1-5
    • (2000) J. Neurosci. , vol.20 , pp. 1-5
    • Tammariello, S.1    Quinn, M.2    Estus, S.3
  • 60
    • 0035800889 scopus 로고    scopus 로고
    • Methods of detection of vascular reactive species: nitric oxide, superoxide, hydrogen peroxide, and peroxynitrite
    • Tarpey M.M., and Fridovich I. Methods of detection of vascular reactive species: nitric oxide, superoxide, hydrogen peroxide, and peroxynitrite. Circ. Res. 89 (2001) 224-236
    • (2001) Circ. Res. , vol.89 , pp. 224-236
    • Tarpey, M.M.1    Fridovich, I.2
  • 62
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications
    • Towbin H., Staehelin T., and Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. U. S. A. 76 (1979) 4350-4354
    • (1979) Proc. Natl. Acad. Sci. U. S. A. , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 63
    • 0021355340 scopus 로고
    • A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids
    • Wessel D., and Flugge U.I. A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids. Anal. Biochem. 138 (1984) 141-143
    • (1984) Anal. Biochem. , vol.138 , pp. 141-143
    • Wessel, D.1    Flugge, U.I.2
  • 64
    • 2642615752 scopus 로고    scopus 로고
    • Regulation of TNF alpha-induced reorganization of the actin cytoskeleton and cell-cell junctions by rho, rac, and cdc42 in human endothelial cells
    • Wojciak-Stothard B., Entwistle A., Garg R., and Ridley A. Regulation of TNF alpha-induced reorganization of the actin cytoskeleton and cell-cell junctions by rho, rac, and cdc42 in human endothelial cells. J. Cell Physiol. 176 (1998) 150-165
    • (1998) J. Cell Physiol. , vol.176 , pp. 150-165
    • Wojciak-Stothard, B.1    Entwistle, A.2    Garg, R.3    Ridley, A.4
  • 65
    • 15544387084 scopus 로고    scopus 로고
    • Rac and Rho play opposing roles in the regulation of hypoxia/reoxygenation-induced permeability changes in pulmonary artery endothelial cells
    • Wojciak-Stothard B., Tsang L.Y., and Haworth S.G. Rac and Rho play opposing roles in the regulation of hypoxia/reoxygenation-induced permeability changes in pulmonary artery endothelial cells. Am. J. Physiol. Lung Cell. Mol. Physiol. 288 (2005) L749-L760
    • (2005) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.288
    • Wojciak-Stothard, B.1    Tsang, L.Y.2    Haworth, S.G.3


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