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Hynes, R.O.1
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Signal transduction through integrins: A central role for focal adhesion kinase?
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Richardson A, Parsons JT: Signal transduction through integrins: a central role for focal adhesion kinase? Bioessays 1995, 17:229-236. Several different signal transduction pathways are activated by association of integrins with the ECM. This review discusses the previous literature, and attempts to link integrin activation with activation of distinct pathways.
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Richardson, A.1
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Integrins: Emerging paradigms of signal transduction
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Schwartz MA, Schaller MD, Ginsberg MH: Integrins: emerging paradigms of signal transduction. Annu Rev Cell Dev Biol 1995, 11:549-600. This recent review provides an in-depth discussion of many of the aspects of integrin signalling, including inside-out and outside-in signalling and the roles both of GTP-binding proteins of the Rho family and of PTKs in integrin signalling.
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Schwartz, M.A.1
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Focal adhesion kinase and associated proteins
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Schaller MD, Parsons JT: Focal adhesion kinase and associated proteins. Curr Opin Cell Biol 1994, 6:705-710. Early studies on FAK and its link to cell signalling are discussed in this review.
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Schaller, M.D.1
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Focal adhesions: Transmembrane junctions between the extracellular matrix and the cytoskeleton
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Burridge K, Fath K, Kelly T, Nuckolls G, Turner C: Focal adhesions: transmembrane junctions between the extracellular matrix and the cytoskeleton. Annu Rev Cell Biol 1988, 4:487-525.
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FAK, a structurally distinctive protein-tyrosine kinase associated with focal adhesions
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FAK, a structurally distinctive protein-tyrosine kinase associated with focal adhesions. Proc Natl Acad Sci USA 1992, 89:5192-5196.
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Schaller, M.D.1
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Vines, R.R.4
Reynolds, A.B.5
Parsons, J.T.6
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0026674919
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Focal adhesion protein-tyrosine kinase phosphorylated in response to cell attachment to fibronectin
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Hanks SK, Calalb MB, Harper MC, Patel SK: Focal adhesion protein-tyrosine kinase phosphorylated in response to cell attachment to fibronectin. Proc Natl Acad Sci USA 1992, 89:8487-8491.
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Hanks, S.K.1
Calalb, M.B.2
Harper, M.C.3
Patel, S.K.4
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8
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Expression of an N-terminally truncated form of human focal adhesion kinase in brain
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Andre E, Becker-Andre M: Expression of an N-terminally truncated form of human focal adhesion kinase in brain. Biochem Biophys Res Commun 1993, 190:140-147.
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Andre, E.1
Becker-Andre, M.2
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10
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2+-induced regulation of ion channel and MAP kinase functions
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•] describe a new member of the FAK family of kinases, and discuss the possible function of this family in controlling intracellular signalling.
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Nature
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Lev, S.1
Moreno, H.2
Martinez, R.3
Canoll, P.4
Peles, E.5
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Plowman, G.D.7
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12
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0028987936
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Integrins and signal transduction pathways: The road taken
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Clark EA, Brugge JS: Integrins and signal transduction pathways: the road taken. Science 1995, 268:233-239. This is an excellent review of the literature pertaining to integrin signalling, particularly with respect to integrin signalling in platelets.
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Science
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Clark, E.A.1
Brugge, J.S.2
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Cell adhesion or integrin clustering increases phosphorylation of a focal adhesion-associated tyrosine kinase
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Kornberg L, Earp HS, Parsons JT, Schaller MD, Juliano RL: Cell adhesion or integrin clustering increases phosphorylation of a focal adhesion-associated tyrosine kinase. J Biol Chem 1992, 267:23439-23442.
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Kornberg, L.1
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Parsons, J.T.3
Schaller, M.D.4
Juliano, R.L.5
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14
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0026445719
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FAK accompanies cell adhesion to extracellular matrix: A role in cytoskeletal assembly
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FAK accompanies cell adhesion to extracellular matrix: a role in cytoskeletal assembly. J Cell Biol 1992, 119:893-903.
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J Cell Biol
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Burridge, K.1
Turner, C.E.2
Romer, L.H.3
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15
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Cell spreading on extracellular matrix proteins induces tyrosine phosphorylation of tensin
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Bockholt SM, Burridge K: Cell spreading on extracellular matrix proteins induces tyrosine phosphorylation of tensin. J Biol Chem 1993, 268:14565-14567.
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Bockholt, S.M.1
Burridge, K.2
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16
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0028954797
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Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function
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FAK and tensin, but not the accumulation of other cytoskeletal proteins such as talin. In contrast, combining monovalent antibody mediated clustering with monovalent ligand occupancy resulted in accumulation of seven cytoskeletal proteins, including α actinin, talin and F-actin. The combined clustering mimics the multivalent interactions of integrins with fibronectin or polyvalent peptides.
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Science
, vol.267
, pp. 883-885
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Miyamoto, S.1
Akiyama, S.K.2
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Ras-related GTPases and the cytoskeleton
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Hall A: Ras-related GTPases and the cytoskeleton. Mol Biol Cell 1992, 3:475-479.
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Mol Biol Cell
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Hall, A.1
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18
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0026778133
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The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
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Ridley AJ, Hall A: The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 1992, 70:389-399.
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Ridley, A.J.1
Hall, A.2
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19
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0028961293
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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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FAK, but are distinct from and form independently of Rho-induced focal adhesions.
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Cell
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Nobes, C.D.1
Hall, A.2
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Activation of the small GTP-binding proteins rho and rac by growth factor receptors
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Nobes CD, Hawkins P, Stephens L, Hall A: Activation of the small GTP-binding proteins rho and rac by growth factor receptors. J Cell Sci 1995, 108:225-233.
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Nobes, C.D.1
Hawkins, P.2
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Hall, A.4
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Transmembrane signal transduction by integrin cytoplasmic domains expressed in single-subunit chimeras
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Akiyama SK, Yamada SS, Yamada KM, LaFlamme SE: Transmembrane signal transduction by integrin cytoplasmic domains expressed in single-subunit chimeras. J Biol Chem 1994, 269:15961-15964.
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Akiyama, S.K.1
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LaFlamme, S.E.4
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Mapping in vivo association of cytoplasmic proteins with integrin beta 1 cytoplasmic domain mutants
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Lewis JM, Schwartz MA: Mapping in vivo association of cytoplasmic proteins with integrin beta 1 cytoplasmic domain mutants. Mol Biol Cell 1995, 6:151-160.
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Lewis, J.M.1
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Focal adhesion kinase and paxillin bind to peptides mimicking beta integrin cytoplasmic domains
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Schaller MD, Otey CA, Hildebrand JD, Parsons JT: Focal adhesion kinase and paxillin bind to peptides mimicking beta integrin cytoplasmic domains. J Cell Biol 1995, 130:1181-1187. This paper presents evidence for the direct interaction between integrin's cytoplasmic domains and FAK. In vitro, beads bearing synthetic peptides that mimic the sequence of β integrin cytoplasmic domains efficiently bind FAK and paxillin. FAK binds to sequences within the cytoplasmic domain of integrin that are distinct from those involved in binding to a actinin.
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J Cell Biol
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Schaller, M.D.1
Otey, C.A.2
Hildebrand, J.D.3
Parsons, J.T.4
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Direct Interaction of v-Src with the focal adhesion kinase mediated by the Src SH2 domain
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Xing Z, Chen H-C, Nowlen JK, Taylor SJ, Shalloway D, Guan J-L: Direct Interaction of v-Src with the focal adhesion kinase mediated by the Src SH2 domain. Mol Biol Cell 1994, 5:413-421.
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Chen, H.-C.2
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Taylor, S.J.4
Shalloway, D.5
Guan, J.-L.6
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Tyrosine phosphorylation of focal adhesion kinase at sites in the catalytic domain regulates kinase activity: A role of Src family kinases
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Calalb MB, Polte TR, Hanks SK: Tyrosine phosphorylation of focal adhesion kinase at sites in the catalytic domain regulates kinase activity: a role of Src family kinases. Mol Cell Biol 1995, 15:954-963.
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Hanks, S.K.3
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Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase
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Schlaepfer DD, Hanks SK, Hunter T, Van der Geer P: Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase. Nature 1994, 372:786-791.
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Schlaepfer, D.D.1
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FAK-dependent tyrosine phosphorylation of paxillin creates a high-affinity binding site for Crk
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FAK-dependent tyrosine phosphorylation of paxillin creates a high-affinity binding site for Crk. Mol Cell Biol 1995, 15:2635-2645.
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Mol Cell Biol
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Mapping of the alpha-actinin binding site within the beta 1 integrin cytoplasmic domain
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Interaction of plasma membrane fibronectin receptor with talin-a transmembrane linkage
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Nature
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Horwitz, A.1
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0029055784
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Paxillin, a tyrosine phosphorylated focal adhesion-associated protein binds to the carboxyl terminal domain of focal adhesion kinase
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Hildebrand JD, Schaller MD, Parsons JT: Paxillin, a tyrosine phosphorylated focal adhesion-associated protein binds to the carboxyl terminal domain of focal adhesion kinase. Mol Biol Cell 1995, 6:637-647.
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Hildebrand, J.D.1
Schaller, M.D.2
Parsons, J.T.3
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34
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0029034873
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Cas, a Src homology 3-containing molecule having multiple Src homology 2-binding motifs
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Cas, together with its tyrosine phosphorylation in adherent cells, indicates that it may play a role in regulating focal adhesion structure.
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J Biol Chem
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Nojima, Y.1
Morino, N.2
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Sato, T.7
Tachibana, K.8
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Hirai, H.11
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35
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Adhesion-induced tyrosine phosphorylation of the p130 SRC substrate
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Petch LA, Bockholt SM, Bouton A, Parsons JT, Burridge K: Adhesion-induced tyrosine phosphorylation of the p130 SRC substrate. J Cell Sci 1995, 108:1371-1379.
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Petch, L.A.1
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Morino, N.1
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Kadowaki, T.8
Yazaki, Y.9
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40
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Association of focal adhesion kinase with its potential substrate phosphatidylinositol 3-kinase
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Chen H-C, Guan J-L: Association of focal adhesion kinase with its potential substrate phosphatidylinositol 3-kinase. Proc Natl Acad Sci USA 1994, 91:10148-10152.
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Chen, H.-C.1
Guan, J.-L.2
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0029562867
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The assembly of integrin adhesion complexes requires both extracellular matrix and intracellular RHO/RAC GTPases
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Hotchin NA, Hall A: The assembly of integrin adhesion complexes requires both extracellular matrix and intracellular RHO/RAC GTPases. J Cell Biol 1995, 131:1857-1865.
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J Cell Biol
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Hotchin, N.A.1
Hall, A.2
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42
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0028557424
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Tyrosine phosphorylation is involved in reorganization of the actin cytoskeleton in response to serum of LPA stimulation
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Chrzanowska-Wodnicka M, Burridge K: Tyrosine phosphorylation is involved in reorganization of the actin cytoskeleton In response to serum of LPA stimulation. J Cell Sci 1994, 107:3643-3654.
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J Cell Sci
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Burridge, K.2
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44
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0028036684
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The small GTP-binding protein Rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells
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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 1994, 7984:507-513. The direct targets of Rho are not well characterized. This paper shows that the block in growth factor signalling observed when cells are maintained in suspension can be overcome by addition of activated Rho. The authors also show that Rho interacts with an enzyme that mediates the phosphorylation of phosphatidylinositol 4-phosphate.
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(1994)
Cell
, vol.7984
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Chong, L.D.1
Traynor-Kaplan, A.2
Bokoch, G.M.3
Schwartz, M.A.4
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45
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0028464361
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Profilin: At the crossroads of signal transduction and the actin cytoskeleton
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2 and the consequences of such interactions in linking cell signalling to regulation of the actin cytoskeleton are of importance.
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(1994)
Bioessays
, vol.16
, pp. 465-472
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Sohn, R.H.1
Goldschmidt-Clermont, P.J.2
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46
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0029120440
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Reduced cell motility and enhanced focal adhesion contact formation in cells from FAK-deficient mice
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Ilic D, Furuta Y, Kanazawa S, Takeda N, Sobue K, Nakatsujl N, Nomura S, Fujlmoto J, Okada M, Yamamoto T, Alzawa S: Reduced cell motility and enhanced focal adhesion contact formation in cells from FAK-deficient mice. Nature 1995, 377:539-543. This paper shows that FAK-deficient mice, generated by gene targeting, display a general defect of mesoderm development, and cells from these embryos exhibit reduced mobility in vitro.
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Nature
, vol.377
, pp. 539-543
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Ilic, D.1
Furuta, Y.2
Kanazawa, S.3
Takeda, N.4
Sobue, K.5
Nakatsujl, N.6
Nomura, S.7
Fujlmoto, J.8
Okada, M.9
Yamamoto, T.10
Alzawa, S.11
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47
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0029034939
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C-Src enhances the spreading of src-/- Fibroblasts on fibronectin by a kinase independent mechanism
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Kaplan KB, Swedlow JR, Morgan DO, Varmus HE: C-Src enhances the spreading of src-/- fibroblasts on fibronectin by a kinase independent mechanism. Genes Dev 9:1505-1517.
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Kaplan, K.B.1
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Morgan, D.O.3
Varmus, H.E.4
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