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Tapon N, Hall A. Rho, Rac and Cdc42 GTPases regulate the organization of the actin cytoskeleton. Curr Opin Cell Biol. 9:1997;86-92.
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Tapon, N.1
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Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia
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Nobes CD, Hall A. Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell. 81:1995;53-62.
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Nobes, C.D.1
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The phosphatidylinositol 4-phosphate 5-kinase family
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of special interest. A good review on the biochemistry, cloning and function of PIP5Ks.
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Loijens JC, Boronenkov IV, Parker GJ, Anderson RA. The phosphatidylinositol 4-phosphate 5-kinase family. of special interest Adv Enzyme Regul. 36:1996;115-140 A good review on the biochemistry, cloning and function of PIP5Ks.
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Loijens, J.C.1
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4
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The cloning and sequence of the C isoform of Ptdlns4P 5-kinase
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Divecha N, Truong O, Hsuan JJ, Hinchliffe KA, Irvine RF. The cloning and sequence of the C isoform of Ptdlns4P 5-kinase. Biochem J. 309:1995;715-719.
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Divecha, N.1
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5
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Boronenkov IV, Anderson RA. The sequence of phosphatidylinositol-4-phosphate 5-kinase defines a novel family of lipid kinases. J Biol Chem. 270:1995;2881-2884.
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Boronenkov, I.V.1
Anderson, R.A.2
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6
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0031047829
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A novel interaction between the juxtamembrane region of the p55 tumor necrosis factor receptor and phosphatidylinositol-4-phosphate 5-kinase
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Castellino AM, Parker GJ, Boronenkov IV, Anderson RA, Chao MV. A novel interaction between the juxtamembrane region of the p55 tumor necrosis factor receptor and phosphatidylinositol-4-phosphate 5-kinase. J Biol Chem. 272:1997;5861-5870.
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Castellino, A.M.1
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7
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0029795811
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Cloning of cDNAs encoding two isoforms of 68 kDa type I phosphatidylinositol-4-phospahte 5-kinase
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of special interest. Two mouse type-I PIP5Ks (PIP5K-Iα and PIP5K-Iβ) of 68 kDa PIP5Ks were cloned by PCR using conserved sequences from human and yeast type-II clones as primers. When expressed in COS cells, they show PIP5K activity and can be stimulated by phosphatidic acid. Tissue distribution of these clones were also studied.
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Ishihara H, Shibasaki Y, Kizuki N, Katagiri H, Yazaki Y, Asano T, Oka Y. Cloning of cDNAs encoding two isoforms of 68 kDa type I phosphatidylinositol-4-phospahte 5-kinase. of special interest J Biol Chem. 271:1996;23611-23614 Two mouse type-I PIP5Ks (PIP5K-Iα and PIP5K-Iβ) of 68 kDa PIP5Ks were cloned by PCR using conserved sequences from human and yeast type-II clones as primers. When expressed in COS cells, they show PIP5K activity and can be stimulated by phosphatidic acid. Tissue distribution of these clones were also studied.
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Ishihara, H.1
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Oka, Y.7
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8
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16944365378
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Type I phosphatidylinositol-4-phosphate 5-kinases are distinct members of this novel lipid kinase family
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of special interest. Multiple human type-I PIP5Ks were cloned on the basis of peptide sequences from purified bovine erythrocyte PIP5K. Six independent PIP5K-Iα (homologues to mouse PIP5K-Iβ) clones were identified, three of them were sequenced. Three PIP5K-Iβ (homologues to mouse PIP5K-Iα) were found. All with a predicted molecular weight close to 68 kDa.
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Loijens JC, Anderson RA. Type I phosphatidylinositol-4-phosphate 5-kinases are distinct members of this novel lipid kinase family. of special interest J Biol Chem. 271:1996;32937-32943 Multiple human type-I PIP5Ks were cloned on the basis of peptide sequences from purified bovine erythrocyte PIP5K. Six independent PIP5K-Iα (homologues to mouse PIP5K-Iβ) clones were identified, three of them were sequenced. Three PIP5K-Iβ (homologues to mouse PIP5K-Iα) were found. All with a predicted molecular weight close to 68 kDa.
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Loijens, J.C.1
Anderson, R.A.2
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9
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Chong LD, Traynor-Kaplan A, Bokoch GM, Schwartz MA. The small GTP-binding protein Rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells. Cell. 79:1994;507-513.
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Chong, L.D.1
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10
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0030001638
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Physical association of the small GTPase Rho with a 68-kDa phosphatidylinositol 4-phosphate 5-kinase in Swiss 3T3 cells
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of special interest. Recombinant Rho-bound PIP5K is identified as a 68 kDa type-I PIP5K by western blotting. ADP-ribosylated Rho has higher affinity to the PIP5K.
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Ren X-D, Bokoch GM, Traynor-Kaplan A, Jenkins GH, Anderson RA, Schwartz MA. Physical association of the small GTPase Rho with a 68-kDa phosphatidylinositol 4-phosphate 5-kinase in Swiss 3T3 cells. of special interest Mol Biol Cell. 7:1996;435-442 Recombinant Rho-bound PIP5K is identified as a 68 kDa type-I PIP5K by western blotting. ADP-ribosylated Rho has higher affinity to the PIP5K.
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Ren X-D1
Bokoch, G.M.2
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11
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0029117595
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Thrombin receptor ligation and activated Rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets
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Hartwig JH, Bokoch GM, Carpenter CL, Janmey PA, Taylor LA, Toker A, Stossel TP. Thrombin receptor ligation and activated Rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets. Cell. 82:1995;643-653.
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Hartwig, J.H.1
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Tolias KF, Cantley LC, Carpenter CL. Rho family GTPases bind to phosphoinositde kinases. J Biol Chem. 270:1995;17656-17659.
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Tolias, K.F.1
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A role for Rho in receptor- And G protein-stimulated phospholipase C. Reduction in phosphatidylinositol 4,5-bisphosphate by Clostridium difficile toxin B
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Schmidt M, Bienek C, Rümenapp U, Zhang C, Lümmen G, Jakobs KH, Just I, Aktories K, Moos M, von Eichel-Streiber C. A role for Rho in receptor- and G protein-stimulated phospholipase C. Reduction in phosphatidylinositol 4,5-bisphosphate by Clostridium difficile toxin B. Naunyn Schmiedebergs Arch Pharmacol. 354:1996;87-94.
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Schmidt, M.1
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Aktories, K.8
Moos, M.9
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14
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0029054398
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Glucosylation of Rho proteins by Clostridium difficile toxin B
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Just I, Selzer J, Wilm M, von Eichel-Streiber C, Mann M, Aktories K. Glucosylation of Rho proteins by Clostridium difficile toxin B. Nature. 375:1995;500-503.
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Just, I.1
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15
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0029741569
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Restoration of Clostridium difficile toxin-B-inhibited phospholipase D by phosphatidylinositol 4,5-bisphosphate
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Schmidt M, Rümenapp U, Nehls C, Ott S, Keller J, Von Eichel-Streiber C, Jakobs KH. Restoration of Clostridium difficile toxin-B-inhibited phospholipase D by phosphatidylinositol 4,5-bisphosphate. Eur J Biochem. 240:1996;707-712.
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Schmidt, M.1
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16
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0029912023
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Inhibition by toxin B of inositol phosphate formation induced by G protein-coupled and tyrosine kinase receptors in N1E-115 neuroblastoma cells: Involvement of Rho proteins
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Zhang C, Schmidt M, von Eichel-Streiber C, Jakobs KH. Inhibition by toxin B of inositol phosphate formation induced by G protein-coupled and tyrosine kinase receptors in N1E-115 neuroblastoma cells: involvement of Rho proteins. Mol Pharmacol. 50:1996;864-869.
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Zhang, C.1
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Escherichia coli cytotoxic necrotizing factor 1 (CNF1), a toxin that activates the Rho GTPase
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Florentini C, Fabbri A, Flatau G, Donelli G, Matarrese P, Lemichez E, Falzano L, Boquet P. Escherichia coli cytotoxic necrotizing factor 1 (CNF1), a toxin that activates the Rho GTPase. J Biol Chem. 272:1997;19532-19537.
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Florentini, C.1
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Boquet, P.8
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18
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0029131982
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Translocation of activated Rho from the cytoplasm to membrane ruffling areas, cell-cell adhesion sites and cleavage furrows
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Takaishi K, Sasaki T, Kameyama T, Tsukita S, Tsukita S, Takai Y. Translocation of activated Rho from the cytoplasm to membrane ruffling areas, cell-cell adhesion sites and cleavage furrows. Oncogene. 11:1995;39-48.
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Takaishi, K.1
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19
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0027299745
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On the crawling of animal cells
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Stossel TP. On the crawling of animal cells. Science. 260:1993;1086-1094.
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Stossel, T.P.1
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Regulation of vinculin binding to talin and actin by phosphatidylinositol-4-5-bisphosphate
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2 is critical for Rho-induced stress fiber formation.
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2 is critical for Rho-induced stress fiber formation.
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Gilmore, A.P.1
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Shibasaki Y, Ishihara H, Kizuki N, Asano T, Oka Y, Yazaki Y. Massive actin polymerization induced by phosphatidylinositol-4-phosphate 5-kinase in vivo. J Biol Chem. 272:1997;7578-7581.
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Shibasaki, Y.1
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Role of actin polymerization and adhesion to extracellular matrix in rac- And rho-induced cytoskeletal reorganization
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of outstanding interest. An elegant demonstration that Rac induces actin polymerization, presumably through activation of PIP5K, leading to the formation of membrane ruffles.
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MacHesky, L.M.1
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Formation of actin stress fibers and focal adhesions enhanced by Rho-kinase
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Amano, M.1
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Actin filament organization in activated mast cells is regulated by heterotrimeric and small GTP-binding proteins
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Norman, J.C.1
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The protein kinase encoded by the Akt proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase
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Franke TF, Yang S-I, Chan TO, Datta K, Kazlauskas A, Morrison DK, Kaplan DR, Tsichlis PN. The protein kinase encoded by the Akt proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase. Cell. 81:1995;727-736.
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29
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Transformation by Rho exchange factor oncogenes is mediated by activation of an integrin-dependent pathway
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of special interest. PIP2 level decreases when cells are kept in suspension; however, when Rho is activated by overexpressing a Rho-specific exchange factor Lbc (an oncogene isolated from lymphoid blast crisis with nucleotide exchange activity to Rho but not Rac and Cdc42), suspended cells show increased PIP2 level, suggesting that Rho stimulates PIP5K activity in vivo.
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PDGF stimulates an increase in GTP-Rac via activation of phosphoinositide 3-kinase
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Hawkins PT, Eguinoa A, Qiu RG, Stokoe D, Cooke FT, Walters R, Wennström S, Claesson-Welsh L, Evans T, Symons M, et al. PDGF stimulates an increase in GTP-Rac via activation of phosphoinositide 3-kinase. Curr Biol. 5:1995;393-403.
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