Formation of actin stress fibers and focal adhesions enhanced by Rho-kinase

The Protein Kinase Family: Conserved Features and Deduced Phylogeny of the Catalytic Domains

Hanks, S. K., Quinn, A. M., & Hunter, T. R. (1988) · Science · doi:10.1126/science.3291115 · Cited by 5,040 · see citing works

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. (1992) · Cell · doi:10.1016/0092-8674(92)90163-7 · Cited by 4,469 · see citing works

Rho, Rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia

Nobes, C. D., & Hall, A. (1995) · Cell · doi:10.1016/0092-8674(95)90370-4 · Cited by 4,414 · see citing works

The molecular heterogeneity of protein kinase C and its implications for cellular regulation

Nishizuka, Y. (1988) · Nature · doi:10.1038/334661a0 · Cited by 4,213 · see citing works

Regulation of Myosin Phosphatase by Rho and Rho-Associated Kinase (Rho-Kinase)

Kimura, K., Ito, M., Amano, M., Chihara, K., Fukata, Y., Nakafuku, M., Yamamori, B., Feng, J., Nakano, T., Okawa, K., et al. (1996) · Science · doi:10.1126/science.273.5272.245 · Cited by 2,889 · see citing works

Phosphorylation and Activation of Myosin by Rho-associated Kinase (Rho-kinase)

Amano, M., Ito, M., Kimura, K., Fukata, Y., Chihara, K., Nakano, T., Matsuura, Y., & Kaibuchi, K. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.34.20246 · Cited by 2,009 · see citing works

Rho‐associated kinase, a novel serine/threonine kinase, as a putative target for small GTP binding protein Rho.

Matsui, T., Amano, M., Yamamoto, T., Chihara, K., Nakafuku, M., Ito, M., Nakano, T., Okawa, K., Iwamatsu, A., & Kaibuchi, K. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00574.x · Cited by 1,062 · see citing works

The small GTP‐binding protein Rho binds to and activates a 160 kDa Ser/Thr protein kinase homologous to myotonic dystrophy kinase.

Ishizaki, T., Maekawa, M., Fujisawa, K., Okawa, K., Iwamatsu, A., Fujita, A., Watanabe, N., Saito, Y., Kakizuka, A., Morii, N., et al. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00539.x · Cited by 882 · see citing works

A Novel Serine/Threonine Kinase Binding the Ras-related RhoA GTPase Which Translocates the Kinase to Peripheral Membranes

LEUNG, T. K. C., Manser, E. J., Tan, L. H.-P., & Lim, L. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.49.29051 · Cited by 720 · see citing works

Microinjection of recombinant p21rho induces rapid changes in cell morphology.

Paterson, H. F., Self, A. J., Garrett, M. D., Just, I., Aktories, K., & Hall, A. (1990) · The Journal of Cell Biology · doi:10.1083/jcb.111.3.1001 · Cited by 719 · see citing works

The small GTP-binding protein Rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells

Chong, L. D., Traynor‐Kaplan, A., Bokoch, G., & Schwartz, M. A. (1994) · Cell · doi:10.1016/0092-8674(94)90259-3 · Cited by 641 · see citing works

Asparagine residue in the rho Gene Product Is the Modification Site for Botulinum ADP-ribosyltransferase

Sekine, A., Fujiwara, M., & Narumiya, S. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)81834-8 · Cited by 541 · see citing works

Regulation of Scatter Factor/Hepatocyte Growth Factor Responses by Ras, Rac, and Rho in MDCK Cells

Ridley, A. J., Comoglio, P. M., & Hall, A. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.2.1110 · Cited by 535 · see citing works

Raf-1 protein kinase is required for growth of induced NIH/3T3 cells

Kölch, W., Heidecker, G., Lloyd, P. A., & Rapp, U. R. (1991) · Nature · doi:10.1038/349426a0 · Cited by 474 · see citing works

Signal transduction pathways regulating Rho‐mediated stress fibre formation: requirement for a tyrosine kinase.

Ridley, A. J., & Hall, A. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06550.x · Cited by 469 · see citing works

Involvement of rho p21 in the GTP-enhanced calcium ion sensitivity of smooth muscle contraction.

Hirata, K., Kikuchi, A., Sasaki, T., Kuroda, S., Kaibuchi, K., Matsuura, Y., Seki, H., Saida, K., & Takai, Y. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50337-4 · Cited by 447 · see citing works

Identification of a Putative Target for Rho as the Serine-Threonine Kinase Protein Kinase N

Amano, M., Mukai, H., Ono, Y., Chihara, K., Matsui, T., Hamajima, Y., Okawa, K., Iwamatsu, A., & Kaibuchi, K. (1996) · Science · doi:10.1126/science.271.5249.648 · Cited by 417 · see citing works

Function of Ras as a molecular switch in signal transduction.

Satoh, T., Nakafuku, M., & Kaziro, Y. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)35739-9 · Cited by 409 · see citing works

Rho as a regulator of the cytoskeleton

Takai, Y., Sasaki, T., Tanaka, K., & Nakanishi, H. (1995) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)89022-2 · Cited by 379 · see citing works

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., et al. (1993) · The Journal of Cell Biology · doi:10.1083/jcb.120.5.1187 · Cited by 367 · see citing works

Role of guanine nucleotide-binding proteins--ras-family or trimeric proteins or both--in Ca2+ sensitization of smooth muscle.

Gong, M. C., Iizuka, K., Nixon, G. F., Browne, J. P., Hall, A., Eccleston, J. F., Sugai, M., Kobayashi, S., Somlyo, A. V., & Somlyo, A. P. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.3.1340 · Cited by 276 · see citing works

The rho gene product expressed in E. Coli is a substrate of botulinum ADP-ribosyltransferase C3

Aktories, K., Braun, U., Rösener, S., Just, I., & Hall, A. (1989) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(89)80199-8 · Cited by 251 · see citing works

Role of Raf-1 serine/threonine protein kinase in growth factor signal transduction.

Rapp, U. R. (1991) · PubMed · Cited by 243 · see citing works

Regulation and function of the Rho subfamily of small GTPases

Nobes, C. D., & Hall, A. K. (1994) · Current Opinion in Genetics & Development · doi:10.1016/0959-437x(94)90094-9 · Cited by 231 · see citing works

A rho-like protein is involved in the organisation of the contractile ring in dividing sand dollar eggs

Mabuchi, I., Hamaguchi, Y., Fujimoto, H., Morii, N., Mishima, M., & Narumiya, S. (1993) · Zygote · doi:10.1017/s0967199400001659 · Cited by 226 · see citing works

Activators and effectors of ras p21 proteins

McCormick, F. (1994) · Current Opinion in Genetics & Development · doi:10.1016/0959-437x(94)90093-0 · Cited by 224 · see citing works

Involvement of Rho p21 small GTP-binding protein and its regulator in the HGF-induced cell motility.

Takaishi, K., Sasaki, T., Kato, M., et al. (1994) · PubMed · Cited by 199 · see citing works

A novel partner for the GTP‐bound forms of rho and rac

Madaule, P., Furuyashiki, T., Reid, T., Ishizaki, T., Watanabe, G., Morii, N., & Narumiya, S. (1995) · FEBS Letters · doi:10.1016/0014-5793(95)01351-2 · Cited by 168 · see citing works

Molecular Genetic Analysis of the Regulatory and Catalytic Domains of Protein Kinase C

Kaibuchi, K., Fukumoto, Y., Oku, N., Takai, Y., Arai, K., & Muramatsu, M. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)80023-0 · Cited by 134 · see citing works

Ras‐dependent signal transduction is indispensable but not sufficient for the activation of AP1/Jun by PKC delta.

Hirai, S.-I., Izumi, Y., Higa, K., Kaibuchi, K., Mizuno, K., Osada, S., Suzuki, K., & Ohno, S. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06517.x · Cited by 111 · see citing works

Cell Shape Determination: A Pivotal Role for Rho

Bussey, H. (1996) · Science · doi:10.1126/science.272.5259.224 · Cited by 45 · see citing works

Rho-associated coiled-coil containing kinases (ROCK): Structure, regulation, and functions

Julian, L., & Olson, M. F. (2014) · Small GTPases · doi:10.4161/sgtp.29846 · Cited by 550 · see citing works

Hepatic stellate cells: role in microcirculation and pathophysiology of portal hypertension

Reynaert, H., Thompson, M. G., Thomas, T., & Geerts, A. (2002) · Gut · doi:10.1136/gut.50.4.571 · Cited by 289 · see citing works

Rho-mediated regulation of tight junctions during monocyte migration across the blood-brain barrier in HIV-1 encephalitis (HIVE)

Persidsky, Y., Heilman, D., Haorah, J., Zelivyanskaya, M., Persidsky, R., Weber, G. A., Shimokawa, H., Kaibuchi, K., & Ikezu, T. (2006) · Blood · doi:10.1182/blood-2005-11-4721 · Cited by 200 · see citing works

Tetrahydrobiopterin Radical Enzymology

Wei, C.-C., Crane, B. R., & Stuehr, D. J. (2003) · Chemical Reviews · doi:10.1021/cr0204350 · Cited by 175 · see citing works

Regulation of fibroblast functions by lysophospholipid mediators: Potential roles in wound healing

Watterson, K. R., Lanning, D. A., Diegelmann, R. F., & Spiegel, S. (2007) · Wound Repair and Regeneration · doi:10.1111/j.1524-475x.2007.00292.x · Cited by 113 · see citing works

A selective ROCK inhibitor, Y27632, prevents dimethylnitrosamine-induced hepatic fibrosis in rats

Tada, S., Iwamoto, H., Nakamuta, M., Sugimoto, R., Enjoji, M., Nakashima, Y., & Nawata, H. (2001) · Journal of Hepatology · doi:10.1016/s0168-8278(00)00059-3 · Cited by 102 · see citing works

Tumor Treating Fields (TTFields) Hinder Cancer Cell Motility through Regulation of Microtubule and Actin Dynamics

Voloshin, T., Schneiderman, R. S., Volodin, A., Shamir, R. R., Kaynan, N., Zeevi, E., Koren, L., Klein-Goldberg, A., Paz, R., Giladi, M., et al. (2020) · Cancers · doi:10.3390/cancers12103016 · Cited by 94 · see citing works

Regulation of Cyr61 gene expression by mechanical stretch through multiple signaling pathways

Tamura, I., Rosenbloom, J., Macarak, E., & Chaqour, B. (2001) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.2001.281.5.c1524 · Cited by 90 · see citing works

Ethanol disrupts intestinal epithelial tight junction integrity through intracellular calcium-mediated Rho/ROCK activation

Elamin, E., Masclee, A., Dekker, J., & Jonkers, D. (2014) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00236.2013 · Cited by 72 · see citing works

Syntheses, Spectroscopy, and Redox Chemistry of Encapsulated Oxo−Mo(V) Centers:  Implications for Pyranopterin-Containing Molybdoenzymes

Basu, P., Nemykin, V. N., & Sengar, R. S. (2003) · Inorganic Chemistry · doi:10.1021/ic034821r · Cited by 42 · see citing works

Actin cytoskeleton organization, cell surface modification and invasion rate of 5 glioblastoma cell lines differing in PTEN and p53 status

Djuzenova, C. S., Fiedler, V., Memmel, S., Katzer, A., Hartmann, S., Krohne, G., Zimmermann, H., Scholz, C.-J., Polat, B., Flentje, M., et al. (2015) · Experimental Cell Research · doi:10.1016/j.yexcr.2014.08.013 · Cited by 34 · see citing works

RPGR protein complex regulates proteasome activity and mediates store-operated calcium entry

Patnaik, S. R., Zhang, X., Biswas, L., Akhtar, S., Zhou, X., Kusuluri, D. K., Reilly, J., May-Simera, H., Chalmers, S., McCarron, J. G., et al. (2018) · Oncotarget · doi:10.18632/oncotarget.25259 · Cited by 17 · see citing works

Echovirus 30 Induced Neuronal Cell Death through TRIO-RhoA Signaling Activation

Lee, J.-W., Yeo, S.-G., Kang, B.-H., Lee, H.-K., Kim, J.-W., Lee, S.-H., Kim, K.-S., & Cheon, D.-S. (2012) · PLoS ONE · doi:10.1371/journal.pone.0036656 · Cited by 12 · see citing works

Ca2+ transient is not necessary for Y-27632- sensitive stress fiber formation induced by lysophosphatidic acid in NIH 3T3 cell

Yasutsune, T., Nishimura, J., Hirano, K., et al. (2000) · The Japanese Journal of Pharmacology · doi:10.1016/s0021-5198(19)48283-8

Wnt-signaling mediates the anti-adipogenic action of lysophosphatidic acid through cross talking with the Rho/Rho associated kinase (ROCK) pathway

Li, L., Tam, L.-F., Liu, L., et al. (2011) · Biochemistry and Cell Biology · doi:10.1139/o11-048 · Cited by 26 · see citing works

Uni-axial stretch induces actin stress fiber reorganization and activates c-Jun NH2 terminal kinase via RhoA and Rho kinase in human bladder smooth muscle cells

Kushida, N., Yamaguchi, O., Kawashima, Y., et al. (2016) · BMC Urology · doi:10.1186/s12894-016-0127-9 · Cited by 15 · see citing works

Distinct roles for DH and PH domains in the Lbc oncogene

Olson, M. F., Sterpetti, P., Nagata, K., et al. (1997) · Oncogene · doi:10.1038/sj.onc.1201594 · Cited by 65 · see citing works

Different regulation of the Trio Dbl‐Homology domains by their associated PH domains

Bellanger, J., Estrach, S., Schmidt, S., Briançon‐Marjollet, A., Zugasti, O., Fromont, S., & Debant, A. (2003) · Biology of the Cell · doi:10.1016/j.biolcel.2003.10.002 · Cited by 42 · see citing works