메뉴 건너뛰기




Volumn 295, Issue 2, 2004, Pages 300-314

Rho localization in cells and tissues

Author keywords

Cleavage furrow; Localization; Microvilli; Rho GTPase; TCA fixation; Translocation

Indexed keywords

ANTIBODY; RHO GUANINE NUCLEOTIDE BINDING PROTEIN;

EID: 1842839923     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yexcr.2004.01.005     Document Type: Article
Times cited : (118)

References (56)
  • 1
    • 0025720725 scopus 로고
    • Microfilament structure and function in the cortical cytoskeleton
    • Bretscher A. Microfilament structure and function in the cortical cytoskeleton. Annu. Rev. Cell Biol. 7:1991;337-374.
    • (1991) Annu. Rev. Cell Biol. , vol.7 , pp. 337-374
    • Bretscher, A.1
  • 2
    • 0027333420 scopus 로고
    • Life at the leading edge: The formation of cell protrusions
    • Condeelis J. Life at the leading edge: the formation of cell protrusions. Annu. Rev. Cell Biol. 9:1993;411-444.
    • (1993) Annu. Rev. Cell Biol. , vol.9 , pp. 411-444
    • Condeelis, J.1
  • 3
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • Hall A. Rho GTPases and the actin cytoskeleton. Science. 279:1998;509-514.
    • (1998) Science , vol.279 , pp. 509-514
    • Hall, A.1
  • 4
    • 0026778133 scopus 로고
    • The small GTP-binding protein Rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
    • Ridley A.J., Hall A. The small GTP-binding protein Rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell. 70:1992;389-399.
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 5
  • 6
    • 0029789678 scopus 로고    scopus 로고
    • The p160 RhoA-binding kinase ROK alpha is a member of a kinase family and is involved in the organization of the cytoskeleton
    • Leung T., Chen X.Q., Manser E., Lim L. The p160 RhoA-binding kinase ROK alpha is a member of a kinase family and is involved in the organization of the cytoskeleton. Mol. Cell. Biol. 16:1996;5313-5327.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5313-5327
    • Leung, T.1    Chen, X.Q.2    Manser, E.3    Lim, L.4
  • 10
    • 0028986034 scopus 로고
    • The Ras-related protein Cdc42Hs and bradykinin promote formation of peripheral actin microspikes and filopodia in Swiss 3T3 fibroblasts
    • Kozma R., Ahmed S., Best A., Lim L. The Ras-related protein Cdc42Hs and bradykinin promote formation of peripheral actin microspikes and filopodia in Swiss 3T3 fibroblasts. Mol. Cell. Biol. 15:1995;1942-1952.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1942-1952
    • Kozma, R.1    Ahmed, S.2    Best, A.3    Lim, L.4
  • 11
    • 0032585538 scopus 로고    scopus 로고
    • Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex
    • Machesky L.M., Insall R.H. Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex. Curr. Biol. 8:1998;1347-1356.
    • (1998) Curr. Biol. , vol.8 , pp. 1347-1356
    • MacHesky, L.M.1    Insall, R.H.2
  • 12
    • 0033574722 scopus 로고    scopus 로고
    • The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly
    • Rohatgi R., Ma L., Miki H., Lopez M., Kirchhausen T., Takenawa T., Kirschner M.W. The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly. Cell. 97:1999;221-231.
    • (1999) Cell , vol.97 , pp. 221-231
    • Rohatgi, R.1    Ma, L.2    Miki, H.3    Lopez, M.4    Kirchhausen, T.5    Takenawa, T.6    Kirschner, M.W.7
  • 13
    • 0026654125 scopus 로고
    • The small GTP-binding protein Rac regulates growth factor-induced membrane ruffling
    • Ridley A.J., Paterson H.F., Johnston C.L., Diekmann D., Hall A. The small GTP-binding protein Rac regulates growth factor-induced membrane ruffling. Cell. 70:1992;401-410.
    • (1992) Cell , vol.70 , pp. 401-410
    • Ridley, A.J.1    Paterson, H.F.2    Johnston, C.L.3    Diekmann, D.4    Hall, A.5
  • 14
    • 0034619847 scopus 로고    scopus 로고
    • IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling
    • Miki H., Yamaguchi H., Suetsugu S., Takenawa T. IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling. Nature. 408:2000;732-735.
    • (2000) Nature , vol.408 , pp. 732-735
    • Miki, H.1    Yamaguchi, H.2    Suetsugu, S.3    Takenawa, T.4
  • 15
    • 0031907484 scopus 로고    scopus 로고
    • RhoA-dependent phosphorylation and relocalization of ERM proteins into apical membrane/actin protrusions in fibroblasts
    • Shaw R.J., Henry M., Solomon F., Jacks T. RhoA-dependent phosphorylation and relocalization of ERM proteins into apical membrane/actin protrusions in fibroblasts. Mol. Biol. Cell. 9:1998;403-419.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 403-419
    • Shaw, R.J.1    Henry, M.2    Solomon, F.3    Jacks, T.4
  • 16
    • 0033612533 scopus 로고    scopus 로고
    • Direct involvement of ezrin/radixin/moeisn (ERM)-binding membrane proteins in the organization of microvilli in collaboration with activated ERM proteins
    • Yonemura S., Tsukita Sa., Tsukita Sh. Direct involvement of ezrin/radixin/moeisn (ERM)-binding membrane proteins in the organization of microvilli in collaboration with activated ERM proteins. J. Cell Biol. 145:1999;1497-1509.
    • (1999) J. Cell Biol. , vol.145 , pp. 1497-1509
    • Yonemura, S.1    Tsukita, Sa.2    Tsukita, Sh.3
  • 17
    • 0037096169 scopus 로고    scopus 로고
    • Rho-dependent and -independent activation mechanisms of ezrin/radixin/moesin proteins: An essential role for polyphosphoinositides in vivo
    • Yonemura S., Matsui T., Tsukita Sh., Tsukita Sa. Rho-dependent and -independent activation mechanisms of ezrin/radixin/moesin proteins: an essential role for polyphosphoinositides in vivo. J. Cell. Sci. 115:2002;2569-2580.
    • (2002) J. Cell. Sci. , vol.115 , pp. 2569-2580
    • Yonemura, S.1    Matsui, T.2    Tsukita, Sh.3    Tsukita, Sa.4
  • 18
    • 0033000016 scopus 로고    scopus 로고
    • Participation of small GTPases in dorsal closure of the Drosophila embryo: Distinct roles for Rho subfamily proteins in epithelial morphogenesis
    • Harden N., Ricos M., Ong Y.M., Chia W., Lim L. Participation of small GTPases in dorsal closure of the Drosophila embryo: distinct roles for Rho subfamily proteins in epithelial morphogenesis. J. Cell. Sci. 112:1999;273-284.
    • (1999) J. Cell. Sci. , vol.112 , pp. 273-284
    • Harden, N.1    Ricos, M.2    Ong, Y.M.3    Chia, W.4    Lim, L.5
  • 19
    • 0033398527 scopus 로고    scopus 로고
    • Mutations in the Rho1 small GTPase disrupt morphogenesis and segmentation during early Drosophila development
    • Magie C.R., Meyer M.R., Gorsuch M.S., Parkhurst S.M. Mutations in the Rho1 small GTPase disrupt morphogenesis and segmentation during early Drosophila development. Development. 126:1999;5353-5364.
    • (1999) Development , vol.126 , pp. 5353-5364
    • Magie, C.R.1    Meyer, M.R.2    Gorsuch, M.S.3    Parkhurst, S.M.4
  • 21
    • 0034601487 scopus 로고    scopus 로고
    • Genomic analysis of metastasis reveals an essential role for RhoC
    • Clark E.A., Golub T.R., Lander E.S., Hynes R.O. Genomic analysis of metastasis reveals an essential role for RhoC. Nature. 406:2000;532-535.
    • (2000) Nature , vol.406 , pp. 532-535
    • Clark, E.A.1    Golub, T.R.2    Lander, E.S.3    Hynes, R.O.4
  • 22
    • 0035003212 scopus 로고    scopus 로고
    • Regulation of the cytoskeleton by Rho-family GTPases: Implications for tumor cell invasion
    • Price L.S., Collard J.G. Regulation of the cytoskeleton by Rho-family GTPases: implications for tumor cell invasion. Semin. Cancer Biol. 11:2001;167-173.
    • (2001) Semin. Cancer Biol. , vol.11 , pp. 167-173
    • Price, L.S.1    Collard, J.G.2
  • 23
    • 0035575585 scopus 로고    scopus 로고
    • Rho family proteins: Coordinating cell responses
    • Ridley A.J. Rho family proteins: coordinating cell responses. Trends Cell Biol. 11:2001;471-477.
    • (2001) Trends Cell Biol. , vol.11 , pp. 471-477
    • Ridley, A.J.1
  • 25
    • 0034603198 scopus 로고    scopus 로고
    • Structure of the Rho family GTP-binding protein Cdc42 in complex with the multifunctional regulator RhoGDI
    • Hoffman G.R., Nassar N., Cerione R.A. Structure of the Rho family GTP-binding protein Cdc42 in complex with the multifunctional regulator RhoGDI. Cell. 100:2000;345-356.
    • (2000) Cell , vol.100 , pp. 345-356
    • Hoffman, G.R.1    Nassar, N.2    Cerione, R.A.3
  • 26
    • 0025906597 scopus 로고
    • Post translational modification of the C-terminal region of the Rho protein are important for its interaction with the membranes and inhibitory GDP/GTP exchange proteins
    • Hori Y., Kikuchi A., Isomura M., Katayama M., Miura Y., Fujioka H., Kaibuchi K., Takai Y. Post translational modification of the C-terminal region of the Rho protein are important for its interaction with the membranes and inhibitory GDP/GTP exchange proteins. Oncogene. 6:1991;515-522.
    • (1991) Oncogene , vol.6 , pp. 515-522
    • Hori, Y.1    Kikuchi, A.2    Isomura, M.3    Katayama, M.4    Miura, Y.5    Fujioka, H.6    Kaibuchi, K.7    Takai, Y.8
  • 27
    • 12644264656 scopus 로고    scopus 로고
    • Differential translocation of Rho family GTPases by lysophosphatidic acid, endothelin-1, and platelet-derived growth factor
    • Fleming I.N., Elliott C.M., Exton J.H. Differential translocation of Rho family GTPases by lysophosphatidic acid, endothelin-1, and platelet-derived growth factor. J. Biol. Chem. 271:1996;33067-33073.
    • (1996) J. Biol. Chem. , vol.271 , pp. 33067-33073
    • Fleming, I.N.1    Elliott, C.M.2    Exton, J.H.3
  • 28
    • 0026612457 scopus 로고
    • Intracellular localization of the p21rho proteins
    • Adamson P., Paterson H.F., Hall A. Intracellular localization of the p21rho proteins. J. Cell Biol. 119:1992;617-627.
    • (1992) J. Cell Biol. , vol.119 , pp. 617-627
    • Adamson, P.1    Paterson, H.F.2    Hall, A.3
  • 29
    • 0029131982 scopus 로고
    • Translocation of activated Rho from the cytoplasm to membrane ruffling area, cell-cell adhesion sites and cleavage furrows
    • Takaishi K., Sasaki T., Kameyama T., Tsukita Sa., Tsukita Sh., Takai Y. Translocation of activated Rho from the cytoplasm to membrane ruffling area, cell-cell adhesion sites and cleavage furrows. Oncogene. 11:1995;39-48.
    • (1995) Oncogene , vol.11 , pp. 39-48
    • Takaishi, K.1    Sasaki, T.2    Kameyama, T.3    Tsukita, Sa.4    Tsukita, Sh.5    Takai, Y.6
  • 30
    • 0000315614 scopus 로고    scopus 로고
    • Dissociation of LPA-induced cytoskeletal contraction from stress fiber formation by differential localization of RhoA
    • Kranenburg O., Poland M., Gebbink M., Oomen L., Moolenar W.H. Dissociation of LPA-induced cytoskeletal contraction from stress fiber formation by differential localization of RhoA. J. Cell. Sci. 110:1997;2417-2427.
    • (1997) J. Cell. Sci. , vol.110 , pp. 2417-2427
    • Kranenburg, O.1    Poland, M.2    Gebbink, M.3    Oomen, L.4    Moolenar, W.H.5
  • 31
    • 0035825193 scopus 로고    scopus 로고
    • Differential localization of Rho GTPases in live cells: Regulation by hypervariable regions and RhoGDI binding
    • Michaelson D., Silletti J., Murphy G., D'Eustachio P., Rush M., Philips M.R. Differential localization of Rho GTPases in live cells: regulation by hypervariable regions and RhoGDI binding. J. Cell Biol. 152:2001;111-126.
    • (2001) J. Cell Biol. , vol.152 , pp. 111-126
    • Michaelson, D.1    Silletti, J.2    Murphy, G.3    D'Eustachio, P.4    Rush, M.5    Philips, M.R.6
  • 32
    • 0026802046 scopus 로고
    • A gene family consisting of ezrin, radixin and moesin. Its specific localization at actin filament/plasma membrane association sites
    • Sato N., Funayama N., Nagafuchi A., Yonemura S., Tsukita Sa., Tsukita Sh. A gene family consisting of ezrin, radixin and moesin. Its specific localization at actin filament/plasma membrane association sites. J. Cell. Sci. 103:1992;131-143.
    • (1992) J. Cell. Sci. , vol.103 , pp. 131-143
    • Sato, N.1    Funayama, N.2    Nagafuchi, A.3    Yonemura, S.4    Tsukita, Sa.5    Tsukita, Sh.6
  • 33
    • 0030712860 scopus 로고    scopus 로고
    • ERM (ezrin/radixin/moesin)-based molecular mechanism of microvillar breakdown at an early stage of apoptosis
    • Kondo T., Takeuchi K., Doi Y., Yonemura S., Nagata S., Tsukita Sh., Tsukita Sa. ERM (ezrin/radixin/moesin)-based molecular mechanism of microvillar breakdown at an early stage of apoptosis. J. Cell Biol. 139:1997;749-758.
    • (1997) J. Cell Biol. , vol.139 , pp. 749-758
    • Kondo, T.1    Takeuchi, K.2    Doi, Y.3    Yonemura, S.4    Nagata, S.5    Tsukita, Sh.6    Tsukita, Sa.7
  • 34
    • 0029164777 scopus 로고
    • Purification and properties of recombinant Rho-GDP dissociation inhibitor
    • Tanaka K., Sasaki T., Takai Y. Purification and properties of recombinant Rho-GDP dissociation inhibitor. Methods Enzymol. 256:1995;41-49.
    • (1995) Methods Enzymol. , vol.256 , pp. 41-49
    • Tanaka, K.1    Sasaki, T.2    Takai, Y.3
  • 35
    • 0032950502 scopus 로고    scopus 로고
    • Immunofluorescence detection of ezrin/radixin/moesin (ERM) proteins with their carboxyl-terminal threonine phosphorylated in cultured cells and tissues: Application of a novel fixation protocol using trichloroacetic acid (TCA) as a fixative
    • Hayashi K., Yonemura S., Matsui T., Tsukita Sa., Tsukita Sh. Immunofluorescence detection of ezrin/radixin/moesin (ERM) proteins with their carboxyl-terminal threonine phosphorylated in cultured cells and tissues: application of a novel fixation protocol using trichloroacetic acid (TCA) as a fixative. J. Cell. Sci. 112:1999;1149-1158.
    • (1999) J. Cell. Sci. , vol.112 , pp. 1149-1158
    • Hayashi, K.1    Yonemura, S.2    Matsui, T.3    Tsukita, Sa.4    Tsukita, Sh.5
  • 36
    • 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., Schwartz M.A. Regulation of the small GTP-binding protein Rho by cell adhesion and the cytoskeleton. EMBO J. 18:1999;578-585.
    • (1999) EMBO J. , vol.18 , pp. 578-585
    • Ren, X.-D.1    Kiosses, W.B.2    Schwartz, M.A.3
  • 38
    • 0034619765 scopus 로고    scopus 로고
    • Rho-kinase/ROCK is involved in cytokinesis through the phosphorylation of myosin light chain and not ezrin/radixin/moesin proteins at the cleavage furrow
    • Kosako H., Yoshida T., Matsumura F., Ishizaki T., Narumiya S., Inagaki M. Rho-kinase/ROCK is involved in cytokinesis through the phosphorylation of myosin light chain and not ezrin/radixin/moesin proteins at the cleavage furrow. Oncogene. 19:2000;6059-6064.
    • (2000) Oncogene , vol.19 , pp. 6059-6064
    • Kosako, H.1    Yoshida, T.2    Matsumura, F.3    Ishizaki, T.4    Narumiya, S.5    Inagaki, M.6
  • 39
    • 0034655981 scopus 로고    scopus 로고
    • Neutrophil polarity and locomotion are associated with surface redistribution of leukosialin (CD43), an antiadhesive molecule
    • Seveau S., Keller H., Maxfield F.R., Piller F., Halbwachs-Mecarelli L. Neutrophil polarity and locomotion are associated with surface redistribution of leukosialin (CD43), an antiadhesive molecule. Blood. 95:2000;2462-2470.
    • (2000) Blood , vol.95 , pp. 2462-2470
    • Seveau, S.1    Keller, H.2    Maxfield, F.R.3    Piller, F.4    Halbwachs-Mecarelli, L.5
  • 40
    • 0018607228 scopus 로고
    • Rapid induction of morphological changes in human carcinoma cells A-431 by epidermal growth factor
    • Chinkers M., McKanna J.A., Cohen S. Rapid induction of morphological changes in human carcinoma cells A-431 by epidermal growth factor. J. Cell Biol. 83:1979;260-265.
    • (1979) J. Cell Biol. , vol.83 , pp. 260-265
    • Chinkers, M.1    McKanna, J.A.2    Cohen, S.3
  • 41
    • 1242266253 scopus 로고
    • Binding of trichloroacetic acid by protein
    • Grimbleby F.H., Ntailianas H.A. Binding of trichloroacetic acid by protein. Nature. 189:1961;835-836.
    • (1961) Nature , vol.189 , pp. 835-836
    • Grimbleby, F.H.1    Ntailianas, H.A.2
  • 42
    • 0036667233 scopus 로고    scopus 로고
    • Rho1 interacts with p120ctn and α-catenin, and regulates cadherin-based adherens junction components in Drosophila
    • Magie C.R., Pinto-Santini D., Parkhurst S.M. Rho1 interacts with p120ctn and α-catenin, and regulates cadherin-based adherens junction components in Drosophila. Development. 129:2002;3771-3782.
    • (2002) Development , vol.129 , pp. 3771-3782
    • Magie, C.R.1    Pinto-Santini, D.2    Parkhurst, S.M.3
  • 43
    • 0030968177 scopus 로고    scopus 로고
    • The small GTPasses Rho and Rac are required for the establishment of cadherin-dependent cell-cell contacts
    • Braga V.M.M., Machesky L.M., Hall A., Hotchin N.A. The small GTPasses Rho and Rac are required for the establishment of cadherin-dependent cell-cell contacts. J. Cell Biol. 137:1997;1421-1431.
    • (1997) J. Cell Biol. , vol.137 , pp. 1421-1431
    • Braga, V.M.M.1    MacHesky, L.M.2    Hall, A.3    Hotchin, N.A.4
  • 44
    • 0030718609 scopus 로고    scopus 로고
    • Regulation of cell-cell adhesion by Rac and Rho small G proteins in MDCK cells
    • Takaishi K., Sasaki T., Kotani H., Nishioka H., Takai Y. Regulation of cell-cell adhesion by Rac and Rho small G proteins in MDCK cells. J. Cell Biol. 139:1997;1047-1059.
    • (1997) J. Cell Biol. , vol.139 , pp. 1047-1059
    • Takaishi, K.1    Sasaki, T.2    Kotani, H.3    Nishioka, H.4    Takai, Y.5
  • 45
    • 0036570588 scopus 로고    scopus 로고
    • Role of Rho family GTPases in epithelial morphogenesis
    • Van Aelst L., Symons M. Role of Rho family GTPases in epithelial morphogenesis. Genes Dev. 16:2002;1032-1054.
    • (2002) Genes Dev. , vol.16 , pp. 1032-1054
    • Van Aelst, L.1    Symons, M.2
  • 46
    • 0028821093 scopus 로고
    • Cell-to-cell adherens junction formation and actin filament organization: Similarities and differences between non-polarized fibroblasts and polarized epithelial cells
    • Yonemura S., Itoh M., Nagafuchi A., Tsukita Sh. Cell-to-cell adherens junction formation and actin filament organization: similarities and differences between non-polarized fibroblasts and polarized epithelial cells. J. Cell. Sci. 108:1995;127-142.
    • (1995) J. Cell. Sci. , vol.108 , pp. 127-142
    • Yonemura, S.1    Itoh, M.2    Nagafuchi, A.3    Tsukita, Sh.4
  • 47
    • 0027509362 scopus 로고
    • Regulation of cytoplasmic division of Xenopus embryo by Rho p21 and its inhibitory GDP/GTP exchange protein (Rho GDI)
    • Kishi K., Sasaki T., Kuroda S., Itoh T., Takai Y. Regulation of cytoplasmic division of Xenopus embryo by Rho p21 and its inhibitory GDP/GTP exchange protein (Rho GDI). J. Cell Biol. 120:1993;1187-1195.
    • (1993) J. Cell Biol. , vol.120 , pp. 1187-1195
    • Kishi, K.1    Sasaki, T.2    Kuroda, S.3    Itoh, T.4    Takai, Y.5
  • 48
    • 0027691240 scopus 로고
    • A Rho-like protein is involved in the organization of the contractile ring in dividing sand dollar eggs
    • Mabuchi I., Hamaguchi Y., Fujimoto H., Morii N., Mishima M., Narumiya S. A Rho-like protein is involved in the organization of the contractile ring in dividing sand dollar eggs. Zygote. 1:1993;325-331.
    • (1993) Zygote , vol.1 , pp. 325-331
    • Mabuchi, I.1    Hamaguchi, Y.2    Fujimoto, H.3    Morii, N.4    Mishima, M.5    Narumiya, S.6
  • 49
    • 0032423641 scopus 로고    scopus 로고
    • Localization of Rho GTPase in sea urchin eggs
    • Nishimura Y., Nakano K., Mabuchi I. Localization of Rho GTPase in sea urchin eggs. FEBS Lett. 441:1998;121-126.
    • (1998) FEBS Lett. , vol.441 , pp. 121-126
    • Nishimura, Y.1    Nakano, K.2    Mabuchi, I.3
  • 50
    • 0035157971 scopus 로고    scopus 로고
    • Activation of RhoA and ROCK are essential for detachment of migrating leukocytes
    • Alblas J., Ulfman L., Hordijk P., Koenderman L. Activation of RhoA and ROCK are essential for detachment of migrating leukocytes. Mol. Biol. Cell. 12:2001;2137-2145.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2137-2145
    • Alblas, J.1    Ulfman, L.2    Hordijk, P.3    Koenderman, L.4
  • 51
    • 0027183643 scopus 로고
    • Ezrin is concentrated in the apical microvilli of a wide variety of epithelial cells whereas moesin is found primarily in endothelial cells
    • Berryman M., Franck Z., Bretscher A. Ezrin is concentrated in the apical microvilli of a wide variety of epithelial cells whereas moesin is found primarily in endothelial cells. J. Cell. Sci. 105:1993;1025-1043.
    • (1993) J. Cell. Sci. , vol.105 , pp. 1025-1043
    • Berryman, M.1    Franck, Z.2    Bretscher, A.3
  • 54
    • 0032541338 scopus 로고    scopus 로고
    • P160ROCK mediates RhoA activation of Na-H exchange
    • Tominaga T., Ishizaki T., Narumiya S., Barber D.L. p160ROCK mediates RhoA activation of Na-H exchange. EMBO J. 17:1998;4712-4722.
    • (1998) EMBO J. , vol.17 , pp. 4712-4722
    • Tominaga, T.1    Ishizaki, T.2    Narumiya, S.3    Barber, D.L.4
  • 55
    • 0034997092 scopus 로고    scopus 로고
    • Rho proteins: Linking signaling with membrane trafficking
    • Ridley A.J. Rho proteins: linking signaling with membrane trafficking. Traffic. 2:2001;303-310.
    • (2001) Traffic , vol.2 , pp. 303-310
    • Ridley, A.J.1
  • 56
    • 0033939039 scopus 로고    scopus 로고
    • Everything you wanted to know about the bladder epithelium but were afraid to ask
    • Lewis S.A. Everything you wanted to know about the bladder epithelium but were afraid to ask. Am. J. Physiol., Renal. Physiol. 278:2000;F867-F874.
    • (2000) Am. J. Physiol., Renal. Physiol. , vol.278
    • Lewis, S.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.