{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,21]],"date-time":"2026-05-21T06:02:44Z","timestamp":1779343364434,"version":"3.51.4"},"reference-count":73,"publisher":"Elsevier BV","issue":"10","license":[{"start":{"date-parts":[[1996,10,1]],"date-time":"1996-10-01T00:00:00Z","timestamp":844128000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2013,7,17]],"date-time":"2013-07-17T00:00:00Z","timestamp":1374019200000},"content-version":"vor","delay-in-days":6133,"URL":"https:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Current Biology"],"published-print":{"date-parts":[[1996,10]]},"DOI":"10.1016\/s0960-9822(02)70711-2","type":"journal-article","created":{"date-parts":[[2004,8,10]],"date-time":"2004-08-10T15:56:00Z","timestamp":1092153360000},"page":"1256-1264","source":"Crossref","is-referenced-by-count":241,"title":["Rho: theme and variations"],"prefix":"10.1016","volume":"6","author":[{"given":"Anne J.","family":"Ridley","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/S0960-9822(02)70711-2_BIB1","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1146\/annurev.cb.10.110194.000335","article-title":"Small GTP-binding proteins and the regulation of the actin cytoskeleton","volume":"10","author":"Hall","year":"1994","journal-title":"Annu Rev Cell Biol"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB2","doi-asserted-by":"crossref","first-page":"2689","DOI":"10.1128\/MCB.16.6.2689","article-title":"Identification of a novel human Rho protein with unusual properties: GTPase deficiency and in vivo farnesylation","volume":"16","author":"Foster","year":"1996","journal-title":"Mol Cell Biol"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB3","first-page":"2171","article-title":"TTF, a gene encoding a novel small G protein, fuses to the lymphoma-associated LAZ3 gene by t(3;4) chromosomal translocation","volume":"10","author":"Dallery","year":"1995","journal-title":"Oncogene"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB4","doi-asserted-by":"crossref","first-page":"1787","DOI":"10.1101\/gad.8.15.1787","article-title":"Distinct morphogenetic functions of similar small GTPase: Drosophila DRac1 is involved in axonal outgrowth and myoblast fusion","volume":"8","author":"Luo","year":"1994","journal-title":"Genes Dev"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB5","doi-asserted-by":"crossref","first-page":"292","DOI":"10.1002\/j.1460-2075.1995.tb07003.x","article-title":"Characterization of rho GTPase family homologues in Drosophila melanogaster: overexpressing Rho1 in retinal cells causes a late developmental defect","volume":"14","author":"Hariharan","year":"1995","journal-title":"EMBO J"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB6","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1016\/0378-1119(93)90448-C","article-title":"Cloning and characterization of seven novel Dictyostelium discoideum rac-related genes belonging to the rho family of GTPases","volume":"136","author":"Bush","year":"1993","journal-title":"Gene"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB7","doi-asserted-by":"crossref","first-page":"1321","DOI":"10.1083\/jcb.133.6.1321","article-title":"A novel member of the rho family of small GTP-binding proteins is specifically required for cytokinesis","volume":"133","author":"Larochelle","year":"1996","journal-title":"J Cell Biol"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB8","doi-asserted-by":"crossref","first-page":"643","DOI":"10.1038\/366643a0","article-title":"Proteins regulating Ras and its relatives","volume":"366","author":"Boguski","year":"1993","journal-title":"Nature"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB9","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1016\/S0959-437X(95)90049-7","article-title":"Rho-related proteins: actin cytoskeleton and cell cycle","volume":"5","author":"Ridley","year":"1995","journal-title":"Curr Opin Genet Dev"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB10","doi-asserted-by":"crossref","first-page":"710","DOI":"10.1016\/S0960-9822(95)00140-0","article-title":"Rac and Bcr regulate phagocytic phoxes","volume":"5","author":"Ridley","year":"1995","journal-title":"Curr Biol"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB11","doi-asserted-by":"crossref","first-page":"304","DOI":"10.1016\/0962-8924(96)10026-X","article-title":"Rho: a connection between membrane receptor signalling and the cytoskeleton","volume":"6","author":"Machesky","year":"1996","journal-title":"Trends Cell Biol"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB12","doi-asserted-by":"crossref","first-page":"178","DOI":"10.1016\/S0968-0004(96)10022-0","article-title":"Rho family GTPases: the cytoskeleton and beyond","volume":"21","author":"Symons","year":"1996","journal-title":"Trends Biochem Sci"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB13","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1016\/S0955-0674(96)80050-0","article-title":"Signal transduction and actin filament organization","volume":"8","author":"Zigmond","year":"1996","journal-title":"Curr Opin Cell Biol"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB14","doi-asserted-by":"crossref","first-page":"74","DOI":"10.1016\/S0955-0674(96)80051-2","article-title":"Assembly of focal adhesions: progress, paradigms, and portents","volume":"8","author":"Craig","year":"1996","journal-title":"Curr Opin Cell Biol"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB15","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1016\/S0092-8674(00)81280-5","article-title":"Cell migration: a physically integrated molecular process","volume":"84","author":"Lauffenburger","year":"1996","journal-title":"Cell"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB16","doi-asserted-by":"crossref","first-page":"615","DOI":"10.1016\/S0006-291X(05)81110-6","article-title":"ADP-ribosylation of a small size GTP-binding protein in bovine neutrophils by the C3 exoenzyme of Clostridium botulinum and effect on the cell motility","volume":"180","author":"Stasia","year":"1991","journal-title":"Biochem Biophys Res Commun"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB17","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1128\/MCB.13.1.72","article-title":"Involvement of rho p21 and its inhibitory GDP\/GTP exchange protein (rhoGDI) in cell motility","volume":"13","author":"Takaishi","year":"1993","journal-title":"Mol Cell Biol"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB18","doi-asserted-by":"crossref","first-page":"1110","DOI":"10.1128\/MCB.15.2.1110","article-title":"Regulation of scatter factor\/hepatocyte growth factor responses by Ras, Rac and Rho proteins in MDCK cells","volume":"15","author":"Ridley","year":"1995","journal-title":"Mol Cell Biol"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB19","doi-asserted-by":"crossref","first-page":"2208","DOI":"10.1002\/j.1460-2075.1996.tb00574.x","article-title":"Rho-associated kinase, a novel serine\/threonine kinase, as a putative target for the small GTP-binding protein Rho","volume":"15","author":"Matsui","year":"1996","journal-title":"EMBO J"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB20","doi-asserted-by":"crossref","first-page":"29015","DOI":"10.1074\/jbc.270.49.29051","article-title":"A novel serine\/threonine kinase binding the Ras-related RhoA GTPase which translocates the kinase to peripheral membranes","volume":"270","author":"Leung","year":"1995","journal-title":"J Biol Chem"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB21","doi-asserted-by":"crossref","first-page":"1885","DOI":"10.1002\/j.1460-2075.1996.tb00539.x","article-title":"The small GTP-binding protein Rho binds to and activates a 160 kDa Ser\/Thr protein kinase homologous to myotonic dystrophy kinase","volume":"8","author":"Ishizaki","year":"1996","journal-title":"EMBO J"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB22","first-page":"in press","article-title":"The p 160 RhoA-binding kinase ROK\u03b1 is a member of a kinase family and is involved in the reorganization of the cytoskeleton","author":"Leung","year":"1996","journal-title":"Mol Cell Biol"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB23","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1126\/science.273.5272.245","article-title":"Regulation of myosin phosphatase by Rho and Rho-associated kinase (Rho-kinase)","volume":"273","author":"Kimura","year":"1996","journal-title":"Science"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB24","doi-asserted-by":"crossref","first-page":"721","DOI":"10.1146\/annurev.bi.61.070192.003445","article-title":"Control of nonmuscle myosins by phosphorylation","volume":"61","author":"Tan","year":"1992","journal-title":"Annu Rev Biochem"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB25","doi-asserted-by":"crossref","first-page":"2600","DOI":"10.1002\/j.1460-2075.1994.tb06550.x","article-title":"Signal transduction pathways regulating Rho-mediated stress fibre formation: requirement for a tyrosine kinase","volume":"13","author":"Ridley","year":"1994","journal-title":"EMBO J"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB26","doi-asserted-by":"crossref","first-page":"1403","DOI":"10.1083\/jcb.133.6.1403","article-title":"Rho-stimulated contractility drives the formation of stress fibres and focal adhesions","volume":"133","author":"Chrzanowska-Wodnicka","year":"1996","journal-title":"J Cell Biol"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB27","doi-asserted-by":"crossref","first-page":"1955","DOI":"10.1083\/jcb.106.6.1955","article-title":"Regulation of actin microfilament integrity in living nonmuscle cells by the cAMP-dependent kinase and the myosin light chain kinase","volume":"106","author":"Lamb","year":"1988","journal-title":"J Cell Biol"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB28","doi-asserted-by":"crossref","first-page":"8719","DOI":"10.1016\/S0021-9258(19)50337-4","article-title":"Involvement of rho p21 in the GTP-enhanced calcium ion sensitivity of smooth muscle contraction","volume":"267","author":"Hirata","year":"1992","journal-title":"J Biol Chem"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB29","doi-asserted-by":"crossref","first-page":"801","DOI":"10.1083\/jcb.126.3.801","article-title":"Inhibition of lysophosphatidate-\u00a0 and thrombin-induced neurite retraction and neuronal cell rounding by ADP ribosylation of the small GTP-binding protein rho","volume":"126","author":"Jalink","year":"1994","journal-title":"J Cell Biol"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB30","doi-asserted-by":"crossref","first-page":"1005","DOI":"10.1083\/jcb.126.4.1005","article-title":"Actin filament organization in activated mast cells is regulated by heterotrimeric and small GTP-binding proteins","volume":"126","author":"Norman","year":"1994","journal-title":"J Cell Biol"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB31","doi-asserted-by":"crossref","first-page":"3315","DOI":"10.1002\/j.1460-2075.1996.tb00696.x","article-title":"Rho-dependent membrane folding causes Shigella entry into epithelial cells","volume":"15","author":"Adam","year":"1996","journal-title":"EMBO J"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB32","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1091\/mbc.7.3.435","article-title":"Physical association of the small GTPase Rho with a 68-kDa phosphatidylinositol 4-phosphate 5-kinase in Swiss 3T3 cells","volume":"7","author":"Ren","year":"1996","journal-title":"Mol Biol Cell"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB33","doi-asserted-by":"crossref","first-page":"17656","DOI":"10.1074\/jbc.270.30.17656","article-title":"Rho family GTPases bind to phosphoinositide kinases","volume":"270","author":"Tolias","year":"1995","journal-title":"J Biol Chem"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB34","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1016\/0092-8674(94)90259-3","article-title":"The small GTP-binding protein rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells","volume":"79","author":"Chong","year":"1994","journal-title":"Cell"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB35","doi-asserted-by":"crossref","first-page":"531","DOI":"10.1038\/381531a0","article-title":"Regulation of vinculin binding to talin and actin by phosphatidylinositol-4-5-bisphosphate","volume":"381","author":"Gilmore","year":"1996","journal-title":"Nature"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB36","doi-asserted-by":"crossref","first-page":"1133","DOI":"10.1242\/jcs.109.5.1133","article-title":"The small GTP-binding protein Rho stimulates tyrosine phosphorylation of focal adhesion kinase, p130 and paxillin","volume":"109","author":"Flinn","year":"1996","journal-title":"J Cell Sci"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB37","doi-asserted-by":"crossref","first-page":"598","DOI":"10.1016\/S0960-9822(02)00546-8","article-title":"Human Ste20 homologue hPAK1 links GTPases to the JNK MAP kinase pathway","volume":"6","author":"Brown","year":"1996","journal-title":"Curr Biol"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB38","doi-asserted-by":"crossref","first-page":"643","DOI":"10.1016\/0092-8674(95)90036-5","article-title":"Thrombin receptor ligation and activated Rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets","volume":"82","author":"Hartwig","year":"1995","journal-title":"Cell"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB39","doi-asserted-by":"crossref","first-page":"676","DOI":"10.1016\/S0960-9822(09)00447-3","article-title":"Unravelling Wiskott-Aldrich syndrome","volume":"6","author":"Kirchhausen","year":"1996","journal-title":"Curr Biol"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB40","doi-asserted-by":"crossref","first-page":"723","DOI":"10.1016\/S0092-8674(00)81050-8","article-title":"Wiskott-Aldrich syndrome protein, a novel effector for the GTPase Cdc42Hs, is implicated in actin polymerization","volume":"84","author":"Symons","year":"1996","journal-title":"Cell"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB41","doi-asserted-by":"crossref","first-page":"981","DOI":"10.1016\/S0960-9822(02)00642-5","article-title":"Wiskott-Aldrich syndrome protein (WASp) is a binding partner for c-Src family protein-tyrosine kinases","volume":"6","author":"Banin","year":"1996","journal-title":"Curr Biol"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB42","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1038\/376267a0","article-title":"Specific and redundant roles of Src and Fyn in organizing the cytoskeleton","volume":"376","author":"Thomas","year":"1995","journal-title":"Nature"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB43","doi-asserted-by":"crossref","first-page":"5069","DOI":"10.1128\/MCB.16.9.5069","article-title":"The GTPase-activating protein n-chimaerin cooperates with Rac1 and Cdc42Hs to induce the formation of lamellipodia and filopodia","volume":"16","author":"Kozma","year":"1996","journal-title":"Mol Cell Biol"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB44","doi-asserted-by":"crossref","first-page":"76","DOI":"10.1016\/S0960-9822(02)00424-4","article-title":"Rac is required for v-Abl tyrosine kinase to activate mitogenesis","volume":"6","author":"Renshaw","year":"1996","journal-title":"Curr Biol"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB45","doi-asserted-by":"crossref","first-page":"1270","DOI":"10.1126\/science.7652575","article-title":"An essential role for Rho, Rac and Cdc42 GTPases in cell cycle progression through G1","volume":"269","author":"Olsen","year":"1995","journal-title":"Science"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB46","doi-asserted-by":"crossref","first-page":"1159","DOI":"10.1016\/S0092-8674(05)80020-0","article-title":"The rho family GTPases RhoA, Rac1, and Cdc42Hs regulate transcriptional activation by SRF","volume":"81","author":"Hill","year":"1995","journal-title":"Cell"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB47","doi-asserted-by":"crossref","first-page":"5931","DOI":"10.1002\/j.1460-2075.1995.tb00281.x","article-title":"A downstream target of RHO1 small GTP-binding protein is PKC1, a homolog of protein kinase C, which leads to activation of the MAP kinase cascade in Saccharomyces cerevisiae","volume":"14","author":"Nonaka","year":"1995","journal-title":"EMBO J"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB48","doi-asserted-by":"crossref","first-page":"1147","DOI":"10.1016\/S0092-8674(05)80019-4","article-title":"Selective activation of the JNK signaling pathway and c-Jun transcriptional activity by the small GTPases Rac and Cdc42Hs","volume":"81","author":"Minden","year":"1995","journal-title":"Cell"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB49","doi-asserted-by":"crossref","first-page":"1137","DOI":"10.1016\/S0092-8674(05)80018-2","article-title":"The small GTP-binding proteins Rac1 and Cdc42 regulate the activity of the JNK\/SAPK signaling pathway","volume":"81","author":"Coso","year":"1995","journal-title":"Cell"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB50","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1016\/0092-8674(95)90402-6","article-title":"MAP kinase pathways in yeast: for mating and more","volume":"80","author":"Herskowitz","year":"1995","journal-title":"Cell"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB51","doi-asserted-by":"crossref","first-page":"567","DOI":"10.1002\/bies.950180708","article-title":"Protein kinase cascades activated by stress and inflammatory cytokines","volume":"18","author":"Kyriakis","year":"1996","journal-title":"BioEssays"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB52","doi-asserted-by":"crossref","first-page":"27995","DOI":"10.1074\/jbc.270.47.27995","article-title":"Cdc42 and PAK-mediated signaling leads to Jun kinase and p38 mitogen-activated protein kinase activation","volume":"270","author":"Bagrodia","year":"1995","journal-title":"J Biol Chem"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB53","doi-asserted-by":"crossref","first-page":"23934","DOI":"10.1074\/jbc.270.41.23934","article-title":"Rho family GTPases regulate p38 mitogen-activated protein kinase through the downstream mediator Pak1","volume":"270","author":"Zhang","year":"1995","journal-title":"J Biol Chem"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB54","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1016\/S0955-0674(96)80067-6","article-title":"Regulation of transcription by MAP kinase cascades","volume":"8","author":"Treisman","year":"1996","journal-title":"Curr Opin Cell Biol"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB55","doi-asserted-by":"crossref","first-page":"569","DOI":"10.1002\/j.1460-2075.1992.tb05088.x","article-title":"Activation of extracellular signal-regulated kinase, ERK2, by p21ras oncoprotein","volume":"11","author":"Leevers","year":"1992","journal-title":"EMBO J"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB56","doi-asserted-by":"crossref","first-page":"306","DOI":"10.1016\/0076-6879(95)56035-1","article-title":"Growth factor-induced actin reorganization in Swiss 3T3 cells","volume":"256","author":"Ridley","year":"1995","journal-title":"Methods Enzymol"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB57","doi-asserted-by":"crossref","first-page":"573","DOI":"10.1016\/S0092-8674(00)81257-X","article-title":"The 70 kDa S6 kinase complexes with and is activated by the Rho family G proteins Cdc42 and Rac1","volume":"85","author":"Chou","year":"1996","journal-title":"Cell"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB58","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1016\/S0968-0004(96)10016-5","article-title":"p70 S6 kinases: an enigma with variations","volume":"21","author":"Proud","year":"1996","journal-title":"Trends Biochem Sci"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB59","doi-asserted-by":"crossref","first-page":"18727","DOI":"10.1016\/S0021-9258(17)32226-3","article-title":"Activation of phosphoinositide-3 kinase activity by Cdc42Hs binding to p85","volume":"269","author":"Zheng","year":"1994","journal-title":"J Biol Chem"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB60","doi-asserted-by":"crossref","first-page":"849","DOI":"10.1016\/0092-8674(95)90005-5","article-title":"Rac mediates growth factor-induced arachidonic acid release","volume":"81","author":"Peppelenbosch","year":"1995","journal-title":"Cell"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB61","doi-asserted-by":"crossref","first-page":"7883","DOI":"10.1074\/jbc.271.14.7883","article-title":"Rac-dependent and independent pathways mediate growth factor-induced Ca2+ influx","volume":"271","author":"Peppelenbosch","year":"1996","journal-title":"J Biol Chem"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB62","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1016\/S0960-9822(95)00018-2","article-title":"Rac and rho as regulators of secretion in mast cells","volume":"5","author":"Price","year":"1995","journal-title":"Curr Biol"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB63","doi-asserted-by":"crossref","first-page":"397","DOI":"10.1091\/mbc.7.3.397","article-title":"Purification and identification of FOAD-II, a cytosolic protein that regulates secretion in streptolysin-O-permeabilized mast cells, as a rac\/rhoGDI complex","volume":"7","author":"O'Sullivan","year":"1996","journal-title":"Mol Biol Cell"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB64","first-page":"in press","article-title":"The small GTP-binding proteins, Rac and Rho, regulate cytoskeletal organization and exocytosis in mast cells by parallel pathways","author":"Norman","year":"1996","journal-title":"Mol Biol Cell"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB65","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1038\/382177a0","article-title":"Regulation of receptor-mediated endocytosis by Rho and Rac","volume":"382","author":"Lamaze","year":"1996","journal-title":"Nature"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB66","doi-asserted-by":"crossref","first-page":"1319","DOI":"10.1083\/jcb.130.6.1319","article-title":"Involvement of the GTP binding protein Rho in constitutive endocytosis in Xenopus laevis oocytes","volume":"130","author":"Schmalzing","year":"1995","journal-title":"J Cell Biol"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB67","doi-asserted-by":"crossref","first-page":"617","DOI":"10.1083\/jcb.119.3.617","article-title":"Intracellular localization of the p21rho proteins","volume":"119","author":"Adamson","year":"1992","journal-title":"J Cell Biol"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB68","doi-asserted-by":"crossref","first-page":"945","DOI":"10.1016\/S0960-9822(02)00634-6","article-title":"Rho is only ARF the story","volume":"6","author":"Frohman","year":"1996","journal-title":"Curr Biol"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB69","doi-asserted-by":"crossref","first-page":"1533","DOI":"10.1126\/science.271.5255.1533","article-title":"Phosphoinositides as regulators in membrane traffic","volume":"271","author":"De Camilli","year":"1996","journal-title":"Science"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB70","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1016\/0092-8674(95)90401-8","article-title":"Specificity of receptor tyrosine kinase signaling: transient versus sustained extracellular signal-regulated kinase activation","volume":"80","author":"Marshall","year":"1995","journal-title":"Cell"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB71","doi-asserted-by":"crossref","first-page":"510","DOI":"10.1002\/j.1460-2075.1996.tb00383.x","article-title":"Protein kinase A phosphorylation of RhoA mediates the morphological and functional effects of cyclic AMP in cytotoxic lymphocytes","volume":"15","author":"Lang","year":"1996","journal-title":"EMBO J"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB72","doi-asserted-by":"crossref","first-page":"810","DOI":"10.1126\/science.271.5250.810","article-title":"Stimulation of membrane ruffling and MAP kinase activation by distinct effectors of Ras","volume":"271","author":"Joneson","year":"1996","journal-title":"Science"},{"key":"10.1016\/S0960-9822(02)70711-2_BIB73","doi-asserted-by":"crossref","first-page":"3923","DOI":"10.1128\/MCB.16.7.3923","article-title":"Oncogenic Ras activation of Ras\/mitogen-activated kinase-independent pathways is sufficient to cause tumorigenic transformation","volume":"16","author":"Khosravi-Far","year":"1996","journal-title":"Mol Cell Biol"}],"container-title":["Current Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0960982202707112?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0960982202707112?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2021,6,24]],"date-time":"2021-06-24T18:37:42Z","timestamp":1624559862000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0960982202707112"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1996,10]]},"references-count":73,"journal-issue":{"issue":"10","published-print":{"date-parts":[[1996,10]]}},"alternative-id":["S0960982202707112"],"URL":"https:\/\/doi.org\/10.1016\/s0960-9822(02)70711-2","relation":{},"ISSN":["0960-9822"],"issn-type":[{"value":"0960-9822","type":"print"}],"subject":[],"published":{"date-parts":[[1996,10]]}}}