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Rho GTPases and the Actin Cytoskeleton
Abstract
The actin cytoskeleton mediates a variety of essential biological functions in all eukaryotic cells. In addition to providing a structural framework around which cell shape and polarity are defined, its dynamic properties provide the driving force for cells to move and to divide. Understanding the biochemical mechanisms that control the organization of actin is thus a major goal of contemporary cell biology, with implications for health and disease. Members of the Rho family of small guanosine triphosphatases have emerged as key regulators of the actin cytoskeleton, and furthermore, through their interaction with multiple target proteins, they ensure coordinated control of other cellular activities such as gene transcription and adhesion.
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Cites
Activation of Rac1, RhoA, and mitogen-activated protein kinases is required for Ras transformation
Khosravi-Far, R., Solski, P. A., Clark, G. J., Kinch, M. S., & Der, C. J. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.11.6443 · Cited by 683
Cited by
Items 101–199 of 199
The modular logic of signaling proteins: building allosteric switches from simple binding domains
Lim, W. A. (2002) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(02)00290-7 · Cited by 151
Kim, C., & Dinauer, M. C. (2001) · The Journal of Immunology · doi:10.4049/jimmunol.166.2.1223 · Cited by 151
Raghu, H., Sharma-Walia, N., Veettil, M. V., Sadagopan, S., & Chandran, B. (2009) · Journal of Virology · doi:10.1128/jvi.02498-08 · Cited by 149
Chin, A. C., Vergnolle, N., MacNaughton, W. K., Wallace, J. L., Hollenberg, M. D., & Buret, A. G. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1831452100 · Cited by 149
Bacterial virulence factors targeting Rho GTPases: Parasitism or symbiosis?
Boquet, P., & Lemichez, E. (2003) · Trends in Cell Biology · doi:10.1016/s0962-8924(03)00037-0 · Cited by 149
Nalbant, P., Chang, Y.-C., Birkenfeld, J., Chang, Z.-F., & Bokoch, G. M. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-01-0041 · Cited by 148
Johansson, A.-S., Driessens, M., & Aspenström, P. (2000) · Journal of Cell Science · doi:10.1242/jcs.113.18.3267 · Cited by 146
Structure and mutagenesis of the Dbl homology domain
Aghazadeh, B., Zhu, K., Kubiseski, T. J., Liu, G. A., Pawson, T., Zheng, Y., & Rosen, M. K. (1998) · Nature Structural Biology · doi:10.1038/4209 · Cited by 145
Sculpting Organs: Mechanical Regulation of Tissue Development
Nelson, C. M., & Gleghorn, J. P. (2012) · Annual Review of Biomedical Engineering · doi:10.1146/annurev-bioeng-071811-150043 · Cited by 130
Polarized Distribution of Endogenous Rac1 and RhoA at the Cell Surface
Michaely, P. A., Mineo, C., Ying, Y.-S., & Anderson, R. G. W. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.30.21430 · Cited by 139
Structural basis for the reversible activation of a Rho protein by the bacterial toxin SopE
Buchwald, G., Friebel, A., Galán, J. E., Hardt, W., Wittinghofer, A., & Scheffzek, K. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf329 · Cited by 135
Preudhomme, C., Roumier, C., Hildebrand, M. P., Dallery-Prudhomme, E., Lantoine, D., Laï, J. L., Daudignon, A., Adenis, C., Bauters, F., Fenaux, P., et al. (2000) · Oncogene · doi:10.1038/sj.onc.1203521 · Cited by 135
Actin dynamics: Assembly and disassembly of actin networks
Wear, M. A., Schafer, D. A., & Cooper, J. A. (2000) · Current Biology · doi:10.1016/s0960-9822(00)00845-9 · Cited by 131
Abl-dependent tyrosine phosphorylation of Sos-1 mediates growth-factor-induced Rac activation
Sini, P., Cannas, A., Koleske, A. J., Di Fiore, P. P., & Scita, G. (2004) · Nature Cell Biology · doi:10.1038/ncb1096 · Cited by 130
Critical Role of Actin in Modulating BBB Permeability
Lai, C.-H., Kuo, K.-H., & Leo, J. M. (2005) · Brain Research Reviews · doi:10.1016/j.brainresrev.2005.03.007 · Cited by 129
Yang, F.-C., Kapur, R., King, A. J., Tao, W., Kim, C., Borneo, J., Breese, R., Marshall, M., Dinauer, M. C., & Williams, D. A. (2000) · Immunity · doi:10.1016/s1074-7613(00)80207-1 · Cited by 126
IQGAP1 as signal integrator: Ca 2+ , calmodulin, Cdc42 and the cytoskeleton
Briggs, M. W., & Sacks, D. B. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00333-8 · Cited by 125
Thurnherr, T., Benninger, Y., Wu, X., Chrostek, A., Krause, S. M., Nave, K.-A., Franklin, R. J. M., Brakebusch, C., Suter, U., & Relvas, J. B. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.2158-06.2006 · Cited by 142
“…known for their roles in regulating signaling pathways linking extracellular stimuli to the assembly and organization of the actin cytoskeleton (Hall, 1998), also control microtubule dynamics, cell polarity, membrane trafficking, and gene transcription (Etienne-Manneville and Hall, 2002; Jaffe…”
BackgroundWGEF activates Rho in the Wnt–PCP pathway and controls convergent extension in Xenopus gastrulation
Tanegashima, K., Zhao, H., & Dawid, I. B. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.9 · Cited by 121
Quilliam, L. A., Castro, A. F., Rogers-Graham, K. S., Martin, C. B., Der, C. J., & Bi, C. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.34.23850 · Cited by 119
Trp56 of Rac1 Specifies Interaction with a Subset of Guanine Nucleotide Exchange Factors
Gao, Y., Xing, J., Streuli, M., Leto, T. L., & Zheng, Y. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m108865200 · Cited by 115
Shepard, L. W., Yang, M., Xie, P., Browning, D. D., Voyno-Yasenetskaya, T., Kozasa, T., & Ye, R. D. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104783200 · Cited by 114
Ridsdale, A., Denis, M., Gougeon, P.-Y., Ngsee, J. K., Presley, J. F., & Zha, X. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-02-0100 · Cited by 113
Rac1 Induces the Clustering of AMPA Receptors during Spinogenesis
Wiens, K. M., Lin, H., & Liao, D. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.1947-05.2005 · Cited by 111
Li, S., Yamauchi, A., Marchal, C. C., Molitoris, J. K., Quilliam, L. A., & Dinauer, M. C. (2002) · The Journal of Immunology · doi:10.4049/jimmunol.169.9.5043 · Cited by 109
A Ral GAP complex links PI 3-kinase/Akt signaling to RalA activation in insulin action
Chen, X.-W., Leto, D., Xiong, T., Yu, G., Cheng, A., Decker, S., & Saltiel, A. R. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-08-0665 · Cited by 108
Antitumorigenesis of antioxidants in a transgenic Rac1 model of Kaposi's sarcoma
Ma, Q., Cavallin, L. E., Yan, B., Zhu, S., Duran, E. M., Wang, H., Hale, L. P., Dong, C., Cesarman, E., Mesri, E. A., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0812688106 · Cited by 105
Regulation of TOR by small GTPases
Durán, R. V., & Hall, M. N. (2012) · The EMBO Reports · doi:10.1038/embor.2011.257 · Cited by 102
Gu, Y., Jia, B., Yang, F.-C., D'Souza, M., Harris, C. E., Derrow, C. W., Zheng, Y., & Williams, D. A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010445200 · Cited by 100
Nakazawa, T., Watabe, A. M., Tezuka, T., Yoshida, Y., Yokoyama, K., Umemori, H., Inoue, A., Okabe, S., Manabe, T., & Yamamoto, T. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-09-0623 · Cited by 100
Rac GTPase isoforms Rac1 and Rac2 play a redundant and crucial role in T-cell development
Guo, F., Cancelas, J. A., Hildeman, D., Williams, D. A., & Zheng, Y. (2008) · Blood · doi:10.1182/blood-2008-01-132068 · Cited by 100
C-terminal EH-domain-containing proteins: consensus for a role in endocytic trafficking, EH?
Naslavsky, N., & Caplan, S. (2005) · Journal of Cell Science · doi:10.1242/jcs.02595 · Cited by 98
Miyamoto, Y., Yamauchi, J., Sanbe, A., & Tanoue, A. (2007) · Experimental Cell Research · doi:10.1016/j.yexcr.2006.11.017 · Cited by 95
Role of Rho GTPase in astrocyte morphology and migratory response during in vitro wound healing
Höltje, M., Hoffmann, A., Hofmann, F., Mucke, C., Große, G., Van Rooijen, N., Kettenmann, H., Just, I., & Ahnert‐Hilger, G. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03443.x · Cited by 94
Pan, J., Kao, Y., Joshi, S., Jeetendran, S., DiPette, D., & Singh, U. S. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03106.x · Cited by 94
Molecular basis for Rac1 recognition by guanine nucleotide exchange factors.
(2001) · Nature Structural Biology · doi:10.1038/nsb719 · Cited by 93
A new mechanism of RhoA ubiquitination and degradation: Roles of SCF(FBXL19) E3 ligase and Erk2
Wei, J., Mialki, R. K., Dong, S., Khoo, A., Mallampalli, R. K., Zhao, Y., & Zhao, J. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.07.005 · Cited by 92
The C-terminal Domain of Rac1 Contains Two Motifs That Control Targeting and Signaling Specificity
van Hennik, P. B., Klooster, J. P. T., Halstead, J. R., Voermans, C., Anthony, E. C., Divecha, N., & Hordijk, P. L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m307001200 · Cited by 90
Pai, S.-Y., Kim, C., & Williams, D. A. (2010) · Disease Markers · doi:10.1155/2010/380291 · Cited by 85
Hansen, S. H., Zegers, M. M. P., Woodrow, M., Rodriguez-Viciana, P., Chardin, P., Mostov, K. E., & McMahon, M. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.24.9364-9375.2000 · Cited by 85
Protein kinase N3 promotes bone resorption by osteoclasts in response to Wnt5a-Ror2 signaling
Uehara, S., Udagawa, N., Mukai, H., Ishihara, A., Maeda, K., Yamashita, T., Murakami, K., Nishita, M., Nakamura, T., Kato, S., et al. (2017) · Science Signaling · doi:10.1126/scisignal.aan0023 · Cited by 83
Chen, S., Chen, J., Shi, H., Wei, M., Castaneda-Castellanos, D. R., Bultje, R. S., Pei, X., Kriegstein, A. R., Zhang, M., & Shi, S.-H. (2013) · Developmental Cell · doi:10.1016/j.devcel.2012.11.014 · Cited by 82
Altered Rho GTPase Signaling Pathways in Breast Cancer Cells
Burbelo, P., Wellstein, A., & Pestell, R. G. (2004) · Breast Cancer Research and Treatment · doi:10.1023/b:brea.0000018422.02237.f9 · Cited by 82
Raynaud’s Phenomenon: A Brief Review of the Underlying Mechanisms
Fardoun, M. M., Nassif, J., Issa, K., Baydoun, E., & Eid, A. H. (2016) · Frontiers in Pharmacology · doi:10.3389/fphar.2016.00438 · Cited by 80
Camera, P., Da Silva, J. S., Griffiths, G., Giuffrida, M. G., Ferrara, L., Schubert, V., Imarisio, S., Silengo, L., Dotti, C. G., & Di Cunto, F. (2003) · Nature Cell Biology · doi:10.1038/ncb1064 · Cited by 78
Goldfinger, L. E., Ptak, C., Jeffery, E. D., Shabanowitz, J., Hunt, D. F., & Ginsberg, M. H. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200603111 · Cited by 78
Modulation of actin dynamics by Rac1 to target cognitive function
Tejada‐Simon, M. V. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13100 · Cited by 76
Maruvada, R., Zhu, L., Pearce, D., Zheng, Y., Perfect, J., Kwon-Chung, K. J., & Kim, K. S. (2012) · Cellular Microbiology · doi:10.1111/j.1462-5822.2012.01819.x · Cited by 75
NYAP: a phosphoprotein family that links PI3K to WAVE1 signalling in neurons
Yokoyama, K., Tezuka, T., Kotani, M., Nakazawa, T., Hoshina, N., Shimoda, Y., Kakuta, S., Sudo, K., Watanabe, K., Iwakura, Y., et al. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.348 · Cited by 75
Hematopoietic-specific Rho GTPases Rac2 and RhoH and human blood disorders
Troeger, A., & Williams, D. A. (2013) · Experimental Cell Research · doi:10.1016/j.yexcr.2013.07.002 · Cited by 73
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
Dendritic spine actin cytoskeleton in autism spectrum disorder
Joensuu, M., Lanoue, V., & Hotulainen, P. (2018) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2017.08.023 · Cited by 65
Kallmann’s syndrome, a neuronal migration defect
Cariboni, A., & Maggi, R. (2006) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-5604-3 · Cited by 65
Small GTPase RhoD suppresses cell migration and cytokinesis
Tsubakimoto, K., Matsumoto, K., Abe, H., Ishii, J., Amano, M., Kaibuchi, K., & Endo, T. (1999) · Oncogene · doi:10.1038/sj.onc.1202604 · Cited by 64
Nakazawa, T., Kuriu, T., Tezuka, T., Umemori, H., Okabe, S., & Yamamoto, T. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05335.x · Cited by 63
Weiser, D. C., Pyati, U. J., & Kimelman, D. (2007) · Genes & Development · doi:10.1101/gad.1535007 · Cited by 62
Dey, N., De, P. K., Wang, M., Zhang, H., Dobrota, E. A., Robertson, K. A., & Durden, D. L. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01352-06 · Cited by 62
Seipel, K., Medley, Q. G., Kedersha, N. L., Zhang, X. A., O’Brien, S. P., Serra-Pages, C., Hemler, M. E., & Streuli, M. (1999) · Journal of Cell Science · doi:10.1242/jcs.112.12.1825 · Cited by 62
Miyamoto, Y., Torii, T., Yamamori, N., Ogata, T., Tanoue, A., & Yamauchi, J. (2013) · Science Signaling · doi:10.1126/scisignal.2003661 · Cited by 61
Kurokawa, K., Nakamura, T., Aoki, K., & Matsuda, M. (2005) · Biochemical Society Transactions · doi:10.1042/bst0330631 · Cited by 61
Su, L., Lineberry, N., Huh, Y., Soares, L., & Fathman, C. G. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.11.7559 · Cited by 61
Stansell, E., Apkarian, R., Haubova, S., Diehl, W. E., Tytler, E. M., & Hunter, E. (2007) · Journal of Virology · doi:10.1128/jvi.00657-07 · Cited by 59
Characterization of a Brain-specific Rho GTPase-activating Protein, p200RhoGAP
Moon, S. Y., Zang, H., & Zheng, Y. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m207789200 · Cited by 58
Integrins, Rafts, Rac, and Rho
Guan, J.-L. (2004) · Science · doi:10.1126/science.1094376 · Cited by 58
Ras-related GTPase RhoB Represses NF-κB Signaling
Fritz, G., & Kaina, B. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m005058200 · Cited by 57
Dock GEFs and their therapeutic potential: Neuroprotection and axon regeneration
Namekata, K., Kimura, A., Kawamura, K., Harada, C., & Harada, T. (2014) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2014.06.005 · Cited by 57
Sato, N., Fukui, T., Taniguchi, T., Yokoyama, T., Kondo, M., Nagasaka, T., Goto, Y., Gao, W., Ueda, Y., Yokoi, K., et al. (2007) · International Journal of Cancer · doi:10.1002/ijc.22328 · Cited by 56
Qian, Y., Baisden, J. M., Zot, H. G., Van Winkle, W. B., & Flynn, D. C. (2000) · Experimental Cell Research · doi:10.1006/excr.1999.4795 · Cited by 51
Generation of rac3 Null Mutant Mice: Role of Rac3 in Bcr/Abl-Caused Lymphoblastic Leukemia
Cho, Y. J., Zhang, B., Kaartinen, V., Haataja, L., de Curtis, I., Groffen, J., & Heisterkamp, N. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.13.5777-5785.2005 · Cited by 50
Rac2 Specificity in Macrophage Integrin Signaling
Pradip, D., Peng, X., & Durden, D. L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306491200 · Cited by 49
Thrombin receptor and RhoA mediate cell proliferation through integrins and cysteine‐rich protein 61
Walsh, C. T., Radeff‐Huang, J., Matteo, R., Hsiao, A., Subramaniam, S., Stupack, D., & Brown, J. H. (2008) · The FASEB Journal · doi:10.1096/fj.08-113266 · Cited by 47
Kim, J.-C., Crary, B., Chang, Y. C., Kwon-Chung, K. J., & Kim, K. J. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.389676 · Cited by 47
Rac GEF Dock4 interacts with cortactin to regulate dendritic spine formation.
Ueda, S., Negishi, M., & Katoh, H. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-11-0782 · Cited by 47
Novak, C. M., Horst, E. N., Lin, E., & Mehta, G. (2020) · Cancers · doi:10.3390/cancers12061521 · Cited by 47
Yamauchi, J., Miyamoto, Y., Hamasaki, H., Sanbe, A., Kusakawa, S., Nakamura, A., Tsumura, H., Maeda, M., Nemoto, N., Kawahara, K., et al. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.2738-11.2011 · Cited by 45
Dual Roles for RHOA/RHO-Kinase In the Regulated Trafficking of a Voltage-sensitive Potassium Channel
Stirling, L., Williams, M. R., & Morielli, A. D. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-10-1074 · Cited by 45
Regulation of Microglial Phagocytosis by RhoA/ROCK-Inhibiting Drugs
Scheiblich, H., & Bicker, G. (2017) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-016-0379-7 · Cited by 44
Kong, M., Bui, T. V., Ditsworth, D., Gruber, J. J., Goncharov, D., Krymskaya, V. P., Lindsten, T., & Thompson, C. B. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703159200 · Cited by 43
The small GTPase RhoH is an atypical regulator of haematopoietic cells
Fueller, F., & Kubatzky, K. F. (2008) · Cell Communication and Signaling · doi:10.1186/1478-811x-6-6 · Cited by 40
Kitamura, Y., Shibagaki, K., Takata, K., Tsuchiya, D., Taniguchi, T., Gebicke-Haerter, P. J., Miki, H., Takenawa, T., & Shimohama, S. (2003) · Journal of Pharmacological Sciences · doi:10.1254/jphs.92.115 · Cited by 39
Lu, T.-L., Han, C.-K., Chang, Y.-S., Lu, T.-J., Huang, H.-C., Bao, B.-Y., Wu, H.-Y., Huang, C.-H., Li, C.-Y., & Wu, T.-S. (2014) · The American Journal of Chinese Medicine · doi:10.1142/s0192415x14500967 · Cited by 37
RHO Family GTPases in the Biology of Lymphoma
Voena, C., & Chiarle, R. (2019) · Cells · doi:10.3390/cells8070646 · Cited by 35
Fang, Y., Wang, J., Yao, L., Li, C., Wang, J., Liu, Y., Tao, X., Sun, H., & Liao, H. (2018) · Journal of Neuroinflammation · doi:10.1186/s12974-018-1250-1 · Cited by 35
Pasten, C., Cerda, J., Jausoro, I., Court, F. A., Cáceres, A., & Marzolo, M.-P. (2015) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2015.09.004 · Cited by 29
Structural Basis of Nonenveloped Virus Cell Entry
Stewart, P. L., Dermody, T. S., & Nemerow, G. R. (2003) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(03)01013-1 · Cited by 26
Golgi-resident TRIO regulates membrane trafficking during neurite outgrowth
Tao, T., Sun, J., Peng, Y., Li, Y., Wang, P., Chen, X., Zhao, W., Zheng, Y.-Y., Wei, L., Wang, W., et al. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.007318 · Cited by 26
RAC2 GTPase deficiency and myeloid cell dysfunction in human and mouse
Gu, Y., & Williams, D. A. (2002) · Journal of Pediatric Hematology/Oncology · doi:10.1097/00043426-200212000-00027 · Cited by 25
RhoGDIα Acetylation at K127 and K141 Affects Binding toward Nonprenylated RhoA
Kuhlmann, N., Wroblowski, S., Scislowski, L., & Lammers, M. (2016) · Biochemistry · doi:10.1021/acs.biochem.5b01242 · Cited by 24
Nishimura, Y., Itoh, K., Yoshioka, K., Ikeda, K., & Himeno, M. (2002) · The Histochemical Journal · doi:10.1023/a:1021702812146 · Cited by 24
Wardecki, T., Werner, P., Thomas, M., Templin, M. F., Schmidt, G., Brandner, J. M., & Merfort, I. (2016) · Journal of Natural Products · doi:10.1021/acs.jnatprod.6b00027 · Cited by 23
Thompson, A. P., Bitsina, C., Gray, J. L., von Delft, F., & Brennan, P. E. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100521 · Cited by 21
Salivary proteomic profile of dogs with and without dental calculus
Bringel, M., Jorge, P. K., Francisco, P. A., Lowe, C., Sabino-Silva, R., Colombini-Ishikiriama, B. L., Machado, M. A. D. A. M., & Siqueira, W. L. (2020) · BMC Veterinary Research · doi:10.1186/s12917-020-02514-0 · Cited by 17
Lefort, R. (2015) · Neurotherapeutics · doi:10.1007/s13311-014-0328-4 · Cited by 17
Zizimin and Dock guanine nucleotide exchange factors in cell function and disease
Pakes, N. K., Veltman, D. M., & Williams, R. S. B. (2013) · Small GTPases · doi:10.4161/sgtp.22087 · Cited by 17
Biological activity of neurotrophins is dependent on recruitment of Rac1 to lipid rafts
Fujitani, M., Honda, A., Hata, K., Yamagishi, S., Tohyama, M., & Yamashita, T. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.11.151 · Cited by 14
Gαz Inhibits Serum Response Factor-Dependent Transcription by Inhibiting Rho Signaling
Dutt, P., Jaffe, A. B., Merdek, K. D., Hall, A., & Toksoz, D. (2004) · Molecular Pharmacology · doi:10.1124/mol.104.002949 · Cited by 13
Self-citationOn how Rac controls hematopoietic stem cell activity
Cancelas, J. A. (2011) · Transfusion · doi:10.1111/j.1537-2995.2011.03378.x · Cited by 6
Carrizales, M. G., Boulton, A. D., & Koleske, A. J. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110429 · Cited by 2
(2000) · PubMed
Metadata
- Authors
- Hall, A.
- Venue
- Science
- Published
- 1998-01-23
- Volume
- 279
- Issue
- 5350
- Pages
- 509-514
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2096791952
- Cited by
- 6,140
- References
- 1
- FWCI
- 147.22
- Type
- journal article
- Language
- en
- Open access
- closed
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Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.