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Volumn 57, Issue 5, 2000, Pages 976-983

Pharmacological properties of Y-27632, a specific inhibitor of Rho- associated kinases

Author keywords

[No Author keywords available]

Indexed keywords

4 (1 AMINOETHYL) N (1H PYRROLO[2,3 B]PYRIDIN 4 YL)CYCLOHEXANECARBOXAMIDE; 4 (1 AMINOETHYL) N (4 PYRIDYL)CYCLOHEXANECARBOXAMIDE; PROTEIN KINASE INHIBITOR; RHO FACTOR; UNCLASSIFIED DRUG;

EID: 0034017744     PISSN: 0026895X     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (857)

References (41)
  • 1
    • 0032502680 scopus 로고    scopus 로고
    • Analysis of RhoA-binding proteins reveals an interaction domain conserved in heterotrimeric G protein β subunits and the yeast response regulator protein Skn7
    • Alberts AS, Bouquin N, Johnston LH and Treisman R (1998) Analysis of RhoA-binding proteins reveals an interaction domain conserved in heterotrimeric G protein β subunits and the yeast response regulator protein Skn7. J Biol Chem 273:8616-8622.
    • (1998) J Biol Chem , vol.273 , pp. 8616-8622
    • Alberts, A.S.1    Bouquin, N.2    Johnston, L.H.3    Treisman, R.4
  • 4
    • 0031037187 scopus 로고    scopus 로고
    • A requirement for Rho and Cdc42 during cytokinesis in Xenopus embryos
    • Drechsel DN, Hyman AA, Hall A and Glotzer M (1997) A requirement for Rho and Cdc42 during cytokinesis in Xenopus embryos. Curr Biol 7:12-23.
    • (1997) Curr Biol , vol.7 , pp. 12-23
    • Drechsel, D.N.1    Hyman, A.A.2    Hall, A.3    Glotzer, M.4
  • 6
    • 15644378138 scopus 로고    scopus 로고
    • Geranylgeranylated rho small GTPase(s) are essential for the degradation of p27Kip1 and facilitate the progression from G1 to S phase in growth-stimulated rat FRTL-5 cells
    • Hirai A, Nakamura S, Noguchi Y, Yasuda T, Kitagawa M, Tatsuno I, Oeda T, Tahara K, Terano T, Narumiya S, Kohn, LD and Saito Y (1997) Geranylgeranylated rho small GTPase(s) are essential for the degradation of p27Kip1 and facilitate the progression from G1 to S phase in growth-stimulated rat FRTL-5 cells. J Biol Chem 272:13-16.
    • (1997) J Biol Chem , vol.272 , pp. 13-16
    • Hirai, A.1    Nakamura, S.2    Noguchi, Y.3    Yasuda, T.4    Kitagawa, M.5    Tatsuno, I.6    Oeda, T.7    Tahara, K.8    Terano, T.9    Narumiya, S.10    Kohn, L.D.11    Saito, Y.12
  • 9
    • 0030615004 scopus 로고    scopus 로고
    • p160ROCK, a Rho-associated coiled-coil forming protein kinase, works downstream of Rho and induces focal adhesions
    • Ishizaki T, Naito M, Fujisawa K, Maekawa M, Watanabe N, Saito Y and Narumiya S (1997) p160ROCK, a Rho-associated coiled-coil forming protein kinase, works downstream of Rho and induces focal adhesions. FEBS Lett 404:118-124.
    • (1997) FEBS Lett , vol.404 , pp. 118-124
    • Ishizaki, T.1    Naito, M.2    Fujisawa, K.3    Maekawa, M.4    Watanabe, N.5    Saito, Y.6    Narumiya, S.7
  • 10
    • 0032935495 scopus 로고    scopus 로고
    • An essential part for Rho-associated kinase in the transcellular invasion of tumor cells
    • Itoh K, Yoshioka K, Akedo H, Uehata M, Ishizaki T and Narumiya S (1999) An essential part for Rho-associated kinase in the transcellular invasion of tumor cells. Nat Med 5:221-225.
    • (1999) Nat Med , vol.5 , pp. 221-225
    • Itoh, K.1    Yoshioka, K.2    Akedo, H.3    Uehata, M.4    Ishizaki, T.5    Narumiya, S.6
  • 12
    • 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 and Takai Y (1993) Regulation of cytoplasmic division of Xenopus embryo by rho p21 and its inhibitory GDP/GTP exchange protein (rho GDI). J Cell Biol 120:1187-1195.
    • (1993) J Cell Biol , vol.120 , pp. 1187-1195
    • Kishi, K.1    Sasaki, T.2    Kuroda, S.3    Itoh, T.4    Takai, Y.5
  • 13
    • 0033593667 scopus 로고    scopus 로고
    • Activation of G12/G13 results in shape change and Rho/Rho-kinase-mediated myosin light chain phosphorylation in mouse platelets
    • Klages B, Brandt U, Simon MI, Schultz G and Offermanns S (1999) Activation of G12/G13 results in shape change and Rho/Rho-kinase-mediated myosin light chain phosphorylation in mouse platelets. J Cell Biol 144:745-754.
    • (1999) J Cell Biol , vol.144 , pp. 745-754
    • Klages, B.1    Brandt, U.2    Simon, M.I.3    Schultz, G.4    Offermanns, S.5
  • 15
    • 0029789678 scopus 로고    scopus 로고
    • The p160 RhoA-binding kinase ROK alpha is a member of a kinase family and is involved in the reorganization of the cytoskeleton
    • Leung T, Chen XQ, Manser E and Lim L (1996) The p160 RhoA-binding kinase ROK alpha is a member of a kinase family and is involved in the reorganization of the cytoskeleton. Mol Cell Biol 16:5313-5327.
    • (1996) Mol Cell Biol , vol.16 , pp. 5313-5327
    • Leung, T.1    Chen, X.Q.2    Manser, E.3    Lim, L.4
  • 16
    • 0028863142 scopus 로고
    • A novel serine/threonine kinase binding the Ras-related RhoA GTPase which translocates the kinase to peripheral membranes
    • Leung T, Manser E, Tan L and Lim L (1995) A novel serine/threonine kinase binding the Ras-related RhoA GTPase which translocates the kinase to peripheral membranes. J Biol Chem 270:29051-29054.
    • (1995) J Biol Chem , vol.270 , pp. 29051-29054
    • Leung, T.1    Manser, E.2    Tan, L.3    Lim, L.4
  • 17
    • 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 and Narumiya S (1993) A rho-like protein is involved in the organization of the contractile ring in dividing sand dollar eggs. Zygote 1:325-331.
    • (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
  • 22
    • 0030945871 scopus 로고    scopus 로고
    • Structures of the tyrosine kinase domain of fibroblast growth factor receptor in complex with inhibitors
    • Mohammadi M, McMahon G, Sun L, Tang C, Hirth P, Yeh BK, Hubbard SR and Schlessinger J (1997) Structures of the tyrosine kinase domain of fibroblast growth factor receptor in complex with inhibitors. Science 276:955-960.
    • (1997) Science , vol.276 , pp. 955-960
    • Mohammadi, M.1    McMahon, G.2    Sun, L.3    Tang, C.4    Hirth, P.5    Yeh, B.K.6    Hubbard, S.R.7    Schlessinger, J.8
  • 23
    • 0030603119 scopus 로고    scopus 로고
    • ROCK-I and ROCK-II, two isoforms of Rho-associated coiled-coil forming protein serine/threonine kinase in mice
    • Nakagawa O, Fujisawa K, Ishizaki T, Saito Y, Nakao K and Narumiya S (1996) ROCK-I and ROCK-II, two isoforms of Rho-associated coiled-coil forming protein serine/threonine kinase in mice. FEBS Lett 392:189-193.
    • (1996) FEBS Lett , vol.392 , pp. 189-193
    • Nakagawa, O.1    Fujisawa, K.2    Ishizaki, T.3    Saito, Y.4    Nakao, K.5    Narumiya, S.6
  • 24
    • 0029791373 scopus 로고    scopus 로고
    • The small GTPase Rho: Cellular functions and signal transduction
    • Narumiya S (1996) The small GTPase Rho: Cellular functions and signal transduction. J Biochem 120:215-228.
    • (1996) J Biochem , vol.120 , pp. 215-228
    • Narumiya, S.1
  • 25
    • 0032991828 scopus 로고    scopus 로고
    • Rho-kinase in human neutrophils: A role in signalling for myosin light chain phosphorylation and cell migration
    • Niggli V (1999) Rho-kinase in human neutrophils: A role in signalling for myosin light chain phosphorylation and cell migration. FEBS Lett 445:69-72.
    • (1999) FEBS Lett , vol.445 , pp. 69-72
    • Niggli, V.1
  • 26
  • 27
    • 0033594123 scopus 로고    scopus 로고
    • Rho GTPases control polarity, protrusion, and adhesion during cell movement
    • Nobes CD and Hall A (1999) Rho GTPases control polarity, protrusion, and adhesion during cell movement. J Cell Biol 144:1235-1244.
    • (1999) J Cell Biol , vol.144 , pp. 1235-1244
    • Nobes, C.D.1    Hall, A.2
  • 28
    • 0029101360 scopus 로고
    • An essential role for Rho, Rac, and Cdc42 GTPases in cell cycle progression through G1
    • Olson MF, Ashworth A and Hall A (1995) An essential role for Rho, Rac, and Cdc42 GTPases in cell cycle progression through G1. Science 269:1270-1272.
    • (1995) Science , vol.269 , pp. 1270-1272
    • Olson, M.F.1    Ashworth, A.2    Hall, A.3
  • 29
    • 0032537819 scopus 로고    scopus 로고
    • Signals from Ras and Rho GTPases interact to regulate expression of p21Waf1/Cip1
    • Olson MF, Paterson HF and Marshall CJ (1998) Signals from Ras and Rho GTPases interact to regulate expression of p21Waf1/Cip1. Nature 394:295-299.
    • (1998) Nature , vol.394 , pp. 295-299
    • Olson, M.F.1    Paterson, H.F.2    Marshall, C.J.3
  • 30
    • 0033545354 scopus 로고    scopus 로고
    • Transformation mediated by RhoA requires activity of ROCK kinases. Curr
    • Sahai E, Ishizaki T, Narumiya S and Treisman R (1999) Transformation mediated by RhoA requires activity of ROCK kinases. Curr Biol 9:136-145.
    • (1999) Biol , vol.9 , pp. 136-145
    • Sahai, E.1    Ishizaki, T.2    Narumiya, S.3    Treisman, R.4
  • 31
    • 0033612371 scopus 로고    scopus 로고
    • Rho and Rho kinase mediate thrombin-stimulated vascular smooth muscle cell DNA synthesis and migration
    • Seasholtz TM, Majumdar M, Kaplan DD and Brown JH (1999) Rho and Rho kinase mediate thrombin-stimulated vascular smooth muscle cell DNA synthesis and migration. Cir Res 84:1186-1193.
    • (1999) Cir Res , vol.84 , pp. 1186-1193
    • Seasholtz, T.M.1    Majumdar, M.2    Kaplan, D.D.3    Brown, J.H.4
  • 33
    • 0033562781 scopus 로고    scopus 로고
    • Agonist-induced regulation of myosin phosphatase activity in human platelets through activation of Rho-kinase
    • Suzuki Y, Yamamoto M, Wada H, Ito M, Nakano T, Sasaki Y, Narumiya S, Shiku H and Nishikawa M (1999) Agonist-induced regulation of myosin phosphatase activity in human platelets through activation of Rho-kinase. Blood 93:3408-3417.
    • (1999) Blood , vol.93 , pp. 3408-3417
    • Suzuki, Y.1    Yamamoto, M.2    Wada, H.3    Ito, M.4    Nakano, T.5    Sasaki, Y.6    Narumiya, S.7    Shiku, H.8    Nishikawa, M.9
  • 34
    • 0028143584 scopus 로고
    • Physiological concentrations of purines and pyrimidines
    • Traut TW (1994) Physiological concentrations of purines and pyrimidines. Mol Cell Biochem 140:1-22.
    • (1994) Mol Cell Biochem , vol.140 , pp. 1-22
    • Traut, T.W.1
  • 35
    • 0032854118 scopus 로고    scopus 로고
    • The structure-based design of ATP-site directed protein kinase inhibitors
    • Toledo LM, Lydon NB and Elbaum D (1999) The structure-based design of ATP-site directed protein kinase inhibitors. Curr Med Chem 6:775-805.
    • (1999) Curr Med Chem , vol.6 , pp. 775-805
    • Toledo, L.M.1    Lydon, N.B.2    Elbaum, D.3
  • 39
    • 0027280575 scopus 로고
    • ADP-ribosylation of the rhoA gene product by botulimim C3 exoenzyme causes Swiss 3T3 cells to accumulate in the G1 phase of the cell cycle
    • Yamamoto M, Marui N, Sakai T, Morii N, Kozaki S, Ikai K, Imamura S and Narumiya S (1993) ADP-ribosylation of the rhoA gene product by botulimim C3 exoenzyme causes Swiss 3T3 cells to accumulate in the G1 phase of the cell cycle. Oncogene 8:1449-1455.
    • (1993) Oncogene , vol.8 , pp. 1449-1455
    • Yamamoto, M.1    Marui, N.2    Sakai, T.3    Morii, N.4    Kozaki, S.5    Ikai, K.6    Imamura, S.7    Narumiya, S.8
  • 40
    • 0032583123 scopus 로고    scopus 로고
    • Roles of Rho-associated kinase in cytokinesis; mutations in Rho-associated kinase phosphorylation sites impair cytokinetic segregation of glial filaments
    • Yasui Y, Amano M, Nagata K, Inagaki N, Nakamura H, Saya H, Kaibuchi K and Inagaki M (1998) Roles of Rho-associated kinase in cytokinesis; mutations in Rho-associated kinase phosphorylation sites impair cytokinetic segregation of glial filaments. J Cell Biol 143:1249-1258.
    • (1998) J Cell Biol , vol.143 , pp. 1249-1258
    • Yasui, Y.1    Amano, M.2    Nagata, K.3    Inagaki, N.4    Nakamura, H.5    Saya, H.6    Kaibuchi, K.7    Inagaki, M.8


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