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1
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0028825531
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Ras target proteins in eukaryotic cells
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Marshall MS. Ras target proteins in eukaryotic cells. FASEB J. 9:1995;1311-1318.
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(1995)
FASEB J
, vol.9
, pp. 1311-1318
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Marshall, M.S.1
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2
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0028137615
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Activators and effectors of Ras p21 proteins
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McCormick F. Activators and effectors of Ras p21 proteins. Curr Opin Genet Dev. 4:1994;71-76.
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(1994)
Curr Opin Genet Dev
, vol.4
, pp. 71-76
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McCormick, F.1
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3
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0029089593
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Ras-effector interactions, the problem of specificity
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Wittinghofer A, Herrmann C. Ras-effector interactions, the problem of specificity. FEBS Lett. 369:1995;52-56.
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(1995)
FEBS Lett
, vol.369
, pp. 52-56
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Wittinghofer, A.1
Herrmann, C.2
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4
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0028948382
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Multiple Ras functions can contribute to mammalian cell transformation
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of outstanding interest. This paper introduces the approach of using different mutations in the effector region of Ras to identify and dissect the multiple pathways originating from activated Ras. It shows that Raf activation is not sufficient to induce cell transformation (see [7] for a further application of the approach).
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White MA, Nicolette C, Minden A, Polverino A, Van Aelst L, Karin M, Wigler MH. Multiple Ras functions can contribute to mammalian cell transformation. of outstanding interest Cell. 80:1995;1-20 This paper introduces the approach of using different mutations in the effector region of Ras to identify and dissect the multiple pathways originating from activated Ras. It shows that Raf activation is not sufficient to induce cell transformation (see [7] for a further application of the approach).
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(1995)
Cell
, vol.80
, pp. 1-20
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-
White, M.A.1
Nicolette, C.2
Minden, A.3
Polverino, A.4
Van Aelst, L.5
Karin, M.6
Wigler, M.H.7
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6
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0028903247
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An essential role for Rac in Ras transformation
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of outstanding interest. This paper, together with [5], shows that Ras induces transformation by activating both the MAPK and the Rac pathway. As a consequence, activated Rac and membrane-localized (Raf-CAAX) can synergize in focus formation by substituting oncogenic Ras.
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Qiu RG, Chen J, Kirn D, McCormick F, Symons M. An essential role for Rac in Ras transformation. of outstanding interest Nature. 374:1995;457-459 This paper, together with [5], shows that Ras induces transformation by activating both the MAPK and the Rac pathway. As a consequence, activated Rac and membrane-localized (Raf-CAAX) can synergize in focus formation by substituting oncogenic Ras.
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(1995)
Nature
, vol.374
, pp. 457-459
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Qiu, R.G.1
Chen, J.2
Kirn, D.3
McCormick, F.4
Symons, M.5
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7
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0030052368
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Stimulation of membrane ruffling and MAP kinase activation by distinct effectors of RAS
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of special interest. Uses different effector mutants of Ras to show that there are at least two signalling pathways initiating from activated Ras.
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Joneson T, White MA, Wigler MH, Bar-Sagi D. Stimulation of membrane ruffling and MAP kinase activation by distinct effectors of RAS. of special interest Science. 271:1996;810-812 Uses different effector mutants of Ras to show that there are at least two signalling pathways initiating from activated Ras.
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(1996)
Science
, vol.271
, pp. 810-812
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Joneson, T.1
White, M.A.2
Wigler, M.H.3
Bar-Sagi, D.4
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8
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0028800305
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Activation of Rac1, RhoA, and mitogen-activated protein kinases is required for Ras transformation
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of special interest. Ras activation of Rac and Rho together with the activation of the MAPK/Erk pathway is required for full transforming activity of Ras.
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Khosravi-Far R, Solski PA, Clark GJ, Kinch MS, Der CJ. Activation of Rac1, RhoA, and mitogen-activated protein kinases is required for Ras transformation. of special interest Mol Cell Biol. 15:1995;6443-6453 Ras activation of Rac and Rho together with the activation of the MAPK/Erk pathway is required for full transforming activity of Ras.
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(1995)
Mol Cell Biol
, vol.15
, pp. 6443-6453
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Khosravi-Far, R.1
Solski, P.A.2
Clark, G.J.3
Kinch, M.S.4
Der, C.J.5
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9
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0028153277
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Activated Ras interacts with the Ral guanine nucleotide dissociation stimulator
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Hofer F, Fields S, Schneider C, Martin GS. Activated Ras interacts with the Ral guanine nucleotide dissociation stimulator. Proc Natl Acad Sci USA. 91:1994;11089-11093.
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(1994)
Proc Natl Acad Sci USA
, vol.91
, pp. 11089-11093
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Hofer, F.1
Fields, S.2
Schneider, C.3
Martin, G.S.4
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11
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0028577298
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Identification of the guanine nucleotide dissociation stimulator for Ral as a putative effector molecule of R-ras, H-ras, K-ras, and Rap
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Spaargaren M, Bischoff JR. Identification of the guanine nucleotide dissociation stimulator for Ral as a putative effector molecule of R-ras, H-ras, K-ras, and Rap. Proc Natl Acad Sci USA. 91:1994;12609-12613.
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(1994)
Proc Natl Acad Sci USA
, vol.91
, pp. 12609-12613
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Spaargaren, M.1
Bischoff, J.R.2
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12
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0029831581
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RalGDS-like factor (Rlf) is a novel Ras and Rap 1A-associating protein
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in press
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Wolthuis RMF, Bauer B, Van't Veer LJ, De Vries-Smiths AMM, Cool RH, Spaargaren M, Wittinghofer A, Burgering BMT, Bos JL. RalGDS-like factor (Rlf) is a novel Ras and Rap 1A-associating protein. Oncogene. 12:1996;. in press.
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(1996)
Oncogene
, vol.12
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Wolthuis, R.M.F.1
Bauer, B.2
Van't Veer, L.J.3
De Vries-Smiths, A.M.M.4
Cool, R.H.5
Spaargaren, M.6
Wittinghofer, A.7
Burgering, B.M.T.8
Bos, J.L.9
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13
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0028859266
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A human protein selected for interference with Ras function interacts directly with Ras and competes with Raf1
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Han L, Colicelli J. A human protein selected for interference with Ras function interacts directly with Ras and competes with Raf1. Mol Cell Biol. 15:1995;1318-1323.
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(1995)
Mol Cell Biol
, vol.15
, pp. 1318-1323
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Han, L.1
Colicelli, J.2
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14
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13344281006
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Identification of AF-6 and canoe as putative targets of Ras
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Kuriyama M, Harada N, Kuroda S, Yamamoto T, Nakafuku M, Iwamatsu A, Yamamoto D, Prasad R, Croce C, Canaani E, Kaibuchi K. Identification of AF-6 and canoe as putative targets of Ras. J Biol Chem. 271:1996;607-610.
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(1996)
J Biol Chem
, vol.271
, pp. 607-610
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Kuriyama, M.1
Harada, N.2
Kuroda, S.3
Yamamoto, T.4
Nakafuku, M.5
Iwamatsu, A.6
Yamamoto, D.7
Prasad, R.8
Croce, C.9
Canaani, E.10
Kaibuchi, K.11
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16
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0029077563
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Direct interaction between Ras and the kinase domain of mitogen-activated protein kinase kinase kinase (MEKK1)
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Russell M, Lange-Carter CA, Johnson GL. Direct interaction between Ras and the kinase domain of mitogen-activated protein kinase kinase kinase (MEKK1). J Biol Chem. 270:1995;11757-11760.
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(1995)
J Biol Chem
, vol.270
, pp. 11757-11760
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Russell, M.1
Lange-Carter, C.A.2
Johnson, G.L.3
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17
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0028063391
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Evidence for the in vitro and in vivo interaction of Ras with protein kinase C
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Diaz-Meco MT, Lozano J, Municio MM, Berra E, Frutos S, Sanz L, Moscat J. Evidence for the in vitro and in vivo interaction of Ras with protein kinase C. J Biol Chem. 269:1994;31706-31710.
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(1994)
J Biol Chem
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, pp. 31706-31710
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Diaz-Meco, M.T.1
Lozano, J.2
Municio, M.M.3
Berra, E.4
Frutos, S.5
Sanz, L.6
Moscat, J.7
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18
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0028892105
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Rac GTPase interacts with GAPs and target proteins through multiple effector sites
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of outstanding interest. This paper describes the approach of using different mutants to dissect the multiple effector pathways applied to Rac.
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Diekmann D, Nobes CD, Burbelo PD, Abo A, Hall A. Rac GTPase interacts with GAPs and target proteins through multiple effector sites. of outstanding interest EMBO J. 14:1995;5297-5305 This paper describes the approach of using different mutants to dissect the multiple effector pathways applied to Rac.
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(1995)
EMBO J
, vol.14
, pp. 5297-5305
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Diekmann, D.1
Nobes, C.D.2
Burbelo, P.D.3
Abo, A.4
Hall, A.5
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19
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0028829555
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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
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of outstanding interest. This paper genetically and biochemically identifies PKC1, an activator of a MAPK pathway, as the effector of yeast Rho1, which activates the kinase by binding to the pseudosubstrate region. It also demonstrates by using different Rho effector mutants that yeast Rho1 regulates at least two signaling pathways.
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Nonaka H, Tanaka K, Hirano H, Fujiwara T, Kohno H, Umikawa M, Mino A, Takai Y. 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. of outstanding interest EMBO J. 14:1995;5931-5938 This paper genetically and biochemically identifies PKC1, an activator of a MAPK pathway, as the effector of yeast Rho1, which activates the kinase by binding to the pseudosubstrate region. It also demonstrates by using different Rho effector mutants that yeast Rho1 regulates at least two signaling pathways.
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(1995)
EMBO J
, vol.14
, pp. 5931-5938
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Nonaka, H.1
Tanaka, K.2
Hirano, H.3
Fujiwara, T.4
Kohno, H.5
Umikawa, M.6
Mino, A.7
Takai, Y.8
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20
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0028241777
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Chemical shift assignments and folding topology of the RAS-binding domain of human RAF-1 as determined by heteronuclear three-dimension NMR spectroscopy
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Emerson SD, Waugh DS, Scheffler JE, Tsao K-L, Prinzo KM, Fry DC. Chemical shift assignments and folding topology of the RAS-binding domain of human RAF-1 as determined by heteronuclear three-dimension NMR spectroscopy. Biochemistry. 33:1994;7745-7752.
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(1994)
Biochemistry
, vol.33
, pp. 7745-7752
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Emerson, S.D.1
Waugh, D.S.2
Scheffler, J.E.3
Tsao K-L4
Prinzo, K.M.5
Fry, D.C.6
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21
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0027956706
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Critical binding and regulatory interactions between Ras and Raf occur through a small, stable N-terminal domain of Raf and specific Ras effector residues
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Chuang E, Barnard D, Hettich L, Zhang X-F, Avruch J, Marshall MS. Critical binding and regulatory interactions between Ras and Raf occur through a small, stable N-terminal domain of Raf and specific Ras effector residues. Mol Cell Biol. 14:1994;5318-5325.
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(1994)
Mol Cell Biol
, vol.14
, pp. 5318-5325
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Chuang, E.1
Barnard, D.2
Hettich, L.3
Zhang X-F4
Avruch, J.5
Marshall, M.S.6
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22
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0028128442
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Characterization of a 78-residue fragment of c-Raf-1 that comprises a minimal binding domain for the interaction with Ras-GTP
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Scheffler JE, Waugh DS, Bekesi E, Kiefer SE, LoSardo JE, Neri A, Prinzo KM, Tsao K-L, Wegrzynski B, Emerson SD, Fry DC. Characterization of a 78-residue fragment of c-Raf-1 that comprises a minimal binding domain for the interaction with Ras-GTP. J Biol Chem. 269:1994;22340-22346.
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J Biol Chem
, vol.269
, pp. 22340-22346
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Scheffler, J.E.1
Waugh, D.S.2
Bekesi, E.3
Kiefer, S.E.4
LoSardo, J.E.5
Neri, A.6
Prinzo, K.M.7
Tsao K-L8
Wegrzynski, B.9
Emerson, S.D.10
Fry, D.C.11
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23
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0028019830
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The minimal fragments of c-Raf-1 and NF1 that can suppress v-Ha-Ras-induced malignant phenotype
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Fridman M, Tikoo A, Varga M, Murphy A, Nur-E-Kamal MSA, Maruta H. The minimal fragments of c-Raf-1 and NF1 that can suppress v-Ha-Ras-induced malignant phenotype. J Biol Chem. 269:1994;30105-30108.
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(1994)
J Biol Chem
, vol.269
, pp. 30105-30108
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Fridman, M.1
Tikoo, A.2
Varga, M.3
Murphy, A.4
Nur-E-Kamal, M.S.A.5
Maruta, H.6
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24
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0028795913
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Quantitative analysis of the complex between p21 ras and the Ras-binding domain of the human Raf-1 protein kinase
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Hermann C, Martin GA, Wittinghofer A. Quantitative analysis of the complex between p21 ras and the Ras-binding domain of the human Raf-1 protein kinase. J Biol Chem. 270:1995;2901-2905.
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(1995)
J Biol Chem
, vol.270
, pp. 2901-2905
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Hermann, C.1
Martin, G.A.2
Wittinghofer, A.3
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25
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0028927010
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Identification of the sites of interaction between c-Raf-1 and Ras-GTP
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Barnard D, Diaz B, Hettich L, Chuang E, Zhang X-f, Avruch J, Marshall M. Identification of the sites of interaction between c-Raf-1 and Ras-GTP. Oncogene. 10:1995;1283-1290.
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(1995)
Oncogene
, vol.10
, pp. 1283-1290
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Barnard, D.1
Diaz, B.2
Hettich, L.3
Chuang, E.4
Zhang X-f5
Avruch, J.6
Marshall, M.7
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26
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0029864175
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Equilibrium and kinetic measurements reveal rapidly reversible binding of Ras to Raf
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Gorman C, Skinner RH, Skelly JV, Neidle S, Lowe PN. Equilibrium and kinetic measurements reveal rapidly reversible binding of Ras to Raf. J Biol Chem. 271:1996;6713-6719.
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(1996)
J Biol Chem
, vol.271
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Gorman, C.1
Skinner, R.H.2
Skelly, J.V.3
Neidle, S.4
Lowe, P.N.5
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27
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-
0029041347
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Solution structure of the Ras-binding domain of c-Raf-1 and identification of its Ras interaction surface
-
of special interest. Reports the NMR structure of the Ras-binding domain of c-Raf-1 and suggests how it might interact with Ras.
-
Emerson SD, Madison VS, Palermo RE, Waugh DS, Scheffler JE, Tsao K-L, Kiefer SE, Liu SP, Fry DC. Solution structure of the Ras-binding domain of c-Raf-1 and identification of its Ras interaction surface. of special interest Biochemistry. 34:1995;6911-6918 Reports the NMR structure of the Ras-binding domain of c-Raf-1 and suggests how it might interact with Ras.
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(1995)
Biochemistry
, vol.34
, pp. 6911-6918
-
-
Emerson, S.D.1
Madison, V.S.2
Palermo, R.E.3
Waugh, D.S.4
Scheffler, J.E.5
Tsao K-L6
Kiefer, S.E.7
Liu, S.P.8
Fry, D.C.9
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28
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0029107760
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The 2.2 Å crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue
-
of outstanding interest. The first three-dimensional structure of a complex between a GTP-binding protein (Rap1A) and its effector Raf - RBD supports a wealth of mutational studies about the role of the effector region in this interaction. The structure of Raf - RBD alone has also been solved by NMR [27].
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Nassar N, Horn G, Herrmann C, Scherer A, McCormick F, Wittinghofer A. The 2.2 Å crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue. of outstanding interest Nature. 375:1995;554-560 The first three-dimensional structure of a complex between a GTP-binding protein (Rap1A) and its effector Raf - RBD supports a wealth of mutational studies about the role of the effector region in this interaction. The structure of Raf - RBD alone has also been solved by NMR [27].
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(1995)
Nature
, vol.375
, pp. 554-560
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-
Nassar, N.1
Horn, G.2
Herrmann, C.3
Scherer, A.4
McCormick, F.5
Wittinghofer, A.6
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29
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0011280923
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Conformational switch and structural basis for oncogenic mutations of Ras proteins
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B.F. Dickey, Birnbaumer L. Berlin, Heidelberg, New York: Springer-Verlag
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Kim S-H, Privé GG, Milburn MV. Conformational switch and structural basis for oncogenic mutations of Ras proteins. Dickey BF, Birnbaumer L. GTPases in Biology I. 1993;Springer-Verlag, Berlin, Heidelberg, New York.
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GTPases in Biology I
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Kim S-H1
Privé, G.G.2
Milburn, M.V.3
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30
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0025740753
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The structure of Ras protein: A model for a universal molecular switch
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Wittinghofer A, Pai E. The structure of Ras protein: a model for a universal molecular switch. Trends Biochem Sci. 16:1991;383-387.
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Wittinghofer, A.1
Pai, E.2
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31
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0028956033
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Two distinct Raf domains mediate interaction with Ras
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of special interest. Suggests that in addition to the Ras-binding domain, the cysteine-rich region in the amino terminus of c-Raf-1 is also required for Ras interaction
-
Brtva TR, Drugan JK, Ghosh S, Terrell RS, Campbell-Burk S, Bell RM, Der CJ. Two distinct Raf domains mediate interaction with Ras. of special interest J Biol Chem. 270:1995;9809-9812 Suggests that in addition to the Ras-binding domain, the cysteine-rich region in the amino terminus of c-Raf-1 is also required for Ras interaction.
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(1995)
J Biol Chem
, vol.270
, pp. 9809-9812
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Brtva, T.R.1
Drugan, J.K.2
Ghosh, S.3
Terrell, R.S.4
Campbell-Burk, S.5
Bell, R.M.6
Der, C.J.7
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32
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0029587739
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Cysteine-rich region of Raf-1 interacts with activator domain of post-translationally modified Ha-Ras
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Hu C-D, Kariya K-i, Tamada M, Akasaka K, Shirouzu M, Yokoyama S, Kataoka T. Cysteine-rich region of Raf-1 interacts with activator domain of post-translationally modified Ha-Ras. J Biol Chem. 270:1995;30274-30277.
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J Biol Chem
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Hu C-D1
Kariya K-i2
Tamada, M.3
Akasaka, K.4
Shirouzu, M.5
Yokoyama, S.6
Kataoka, T.7
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33
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0029147166
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Different structural requirements within the switch II region of the Ras protein for interactions with specific downstream targets
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Moodie SA, Paris M, Villafranca E, Kirshmeier P, Willumsen BM, Wolfman A. Different structural requirements within the switch II region of the Ras protein for interactions with specific downstream targets. Oncogene. 11:1995;447-454.
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Oncogene
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Moodie, S.A.1
Paris, M.2
Villafranca, E.3
Kirshmeier, P.4
Willumsen, B.M.5
Wolfman, A.6
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34
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0030053105
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Ras interaction with two distinct binding domains in Raf-1 may be required for Ras transformation
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Drugan JK, Khosravi-Far R, White MA, Der CJ, Sung Y-J, Hwang Y-W, Campbell SL. Ras interaction with two distinct binding domains in Raf-1 may be required for Ras transformation. J Biol Chem. 271:1996;233-237.
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J Biol Chem
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Drugan, J.K.1
Khosravi-Far, R.2
White, M.A.3
Der, C.J.4
Sung Y-J5
Hwang Y-W6
Campbell, S.L.7
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35
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0028206113
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Mutations that abolish the ability of Ha-Ras to associate with Raf-1
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Shirouzu M, Koide H, Fujita-Yoshigaki J, Oshio H, Toyama Y, Yamasaki K, Furhman SA, Villafranca E, Kaziro Y, Yokoyama S. Mutations that abolish the ability of Ha-Ras to associate with Raf-1. Oncogene. 9:1994;2153-2157.
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Oncogene
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Shirouzu, M.1
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Oshio, H.4
Toyama, Y.5
Yamasaki, K.6
Furhman, S.A.7
Villafranca, E.8
Kaziro, Y.9
Yokoyama, S.10
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36
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0029058730
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Purification of a Ras-dependent mitogen-activated protein kinase kinase kinase from bovine brain cytosol and its identification as a complex of B-Raf and 14-3-3 proteins
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of outstanding interest. This is the latest in a series of papers that show that the kinase activity of B-Raf can be stimulated in vitro by incubation with carboxy-terminally modified Ras in the GTP-bound form, similar to the activation of PAK kinase by the addition of Rac-GTP [54-56].
-
Yamamori B, Kuroda S, Shimizu K, Fukui K, Ohtsuka T, Takai Y. Purification of a Ras-dependent mitogen-activated protein kinase kinase kinase from bovine brain cytosol and its identification as a complex of B-Raf and 14-3-3 proteins. of outstanding interest J Biol Chem. 270:1995;11723-11726 This is the latest in a series of papers that show that the kinase activity of B-Raf can be stimulated in vitro by incubation with carboxy-terminally modified Ras in the GTP-bound form, similar to the activation of PAK kinase by the addition of Rac-GTP [54-56].
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(1995)
J Biol Chem
, vol.270
, pp. 11723-11726
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Yamamori, B.1
Kuroda, S.2
Shimizu, K.3
Fukui, K.4
Ohtsuka, T.5
Takai, Y.6
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37
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0029919472
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Post-translational modification of H-Ras is required for activation of, but not for association with, B-Raf
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Okada T, Masuda T, Shinkai M, Kariya K-i, Kataoka T. Post-translational modification of H-Ras is required for activation of, but not for association with, B-Raf. J Biol Chem. 271:1996;4671-4678.
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J Biol Chem
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Okada, T.1
Masuda, T.2
Shinkai, M.3
Kariya K-i4
Kataoka, T.5
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38
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0028074316
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Phosphatidylinositol-3-OH kinase as a direct target of Ras
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Rodriguez-Viciana P, Warne PH, Dhand R, Vanhaesebroeck B, Gout I, Fry MJ, Waterfield MD, Downward J. Phosphatidylinositol-3-OH kinase as a direct target of Ras. Nature. 370:1994;527-532.
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Nature
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Rodriguez-Viciana, P.1
Warne, P.H.2
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Vanhaesebroeck, B.4
Gout, I.5
Fry, M.J.6
Waterfield, M.D.7
Downward, J.8
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39
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0028500187
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The activation of phosphatidylinositol 3-kinase by Ras
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Kodaki T, Woscholski R, Hallberg B, Rodriguez-Viciana P, Downward J, Parker PJ. The activation of phosphatidylinositol 3-kinase by Ras. Curr Biol. 4:1994;798-806.
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Curr Biol
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Kodaki, T.1
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Rodriguez-Viciana, P.4
Downward, J.5
Parker, P.J.6
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40
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Cloning and characterization of a G protein-activated human phosphoinositide-3 kinase
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Stoyanov B, Volinia S, Hanck T, Rubio I, Loubtchenkov M, Malek D, Stoyanova S, Vanhaesebroeck B, Dhand R, Nürnberg B, et al. Cloning and characterization of a G protein-activated human phosphoinositide-3 kinase. Science. 269:1995;690-693.
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Science
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Stoyanov, B.1
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41
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Differential structural requirements for interaction of Ras protein with its distinct downstream effectors
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of special interest. Shows that interaction between Ras and the different effectors Raf-1, Byr2 and adenylyl cyclase is mediated by different amino acids inside and outside the effector region.
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Akasaka K, Tamada M, Wang F, Kariya K-i, Shima F, Kikuchi A, Yamamoto M, Shirouzu M, Yokoyama S, Kataoka T. Differential structural requirements for interaction of Ras protein with its distinct downstream effectors. of special interest J Biol Chem. 271:1996;5353-5360 Shows that interaction between Ras and the different effectors Raf-1, Byr2 and adenylyl cyclase is mediated by different amino acids inside and outside the effector region.
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The differential effects of the Gly-60 to Ala mutation on the interaction of H-Ras p21 with different downstream targets
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Hwang M-CC, Sung YJ, Hwang Y-W. The differential effects of the Gly-60 to Ala mutation on the interaction of H-Ras p21 with different downstream targets. J Biol Chem. 271:1996;8196-8202.
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Hwang M-CC1
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43
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0029913467
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Differential interaction of the Ras family GTP-binding proteins H-Ras, Rap1A and R-Ras with the putative effector molecules Raf-kinase and Ral-guanine nucleotide exchange factor
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Herrmann C, Horn G, Spaargaren M, Wittinghofer A. Differential interaction of the Ras family GTP-binding proteins H-Ras, Rap1A and R-Ras with the putative effector molecules Raf-kinase and Ral-guanine nucleotide exchange factor. of special interest J Biol Chem. 271:1996;6794-6800 Shows by equilibrium measurements that the Ras-binding domains of c-Raf-1 and Ral - GEF have opposite binding characteristics towards Ras and Rap.
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50
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The post-translational processing of ras p21 is critical for its stimulation of mitogen-activated protein kinase
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52
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Lim, L.5
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55
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Molecular cloning of a new member of the p21-Cdc42/Rac-activated kinase (PAK) family
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Manser E, Chong C, Zhao Z-S, Leung T, Michael G, Hall C, Lim L. Molecular cloning of a new member of the p21-Cdc42/Rac-activated kinase (PAK) family. J Biol Chem. 270:1995;25070-25078.
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Manser, E.1
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Zhao Z-S3
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Michael, G.5
Hall, C.6
Lim, L.7
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56
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A novel serine kinase activated by rac1/CDC42Hs-dependent autophosphorylation is related to PAK65 and STE20
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Martin GA, Bollag G, McCormick F, Abo A. A novel serine kinase activated by rac1/CDC42Hs-dependent autophosphorylation is related to PAK65 and STE20. EMBO J. 14:1995;1970-1978.
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57
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N-terminally myristoylated Ras proteins require palmitoylation or a polybasic domain for plasma membrane localization
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Cadwallader KA, Paterson H, MacDonald SG, Hancock JF. N-terminally myristoylated Ras proteins require palmitoylation or a polybasic domain for plasma membrane localization. Mol Cell Biol. 14:1994;4722-4730.
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Hancock, J.F.4
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58
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0028786020
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A conserved binding motif defines numerous candidate target proteins for both Cdc42 and Rac GTPases
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of special interest. Defines a short sequence motif that is found in many identified and unidentified effector proteins for Rac and Cdc42.
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Burbelo PD, Drechsel D, Hall A. A conserved binding motif defines numerous candidate target proteins for both Cdc42 and Rac GTPases. of special interest J Biol Chem. 270:1995;29071-29074 Defines a short sequence motif that is found in many identified and unidentified effector proteins for Rac and Cdc42.
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Hall, A.3
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59
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0030006284
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Wiskott - Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization
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of special interest. Deminstrates that a genetically determined disease that codes for a (non-kinase) protein with a hitherto unknown function is an effector for Cdc42.
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Symons M, Derry JMJ, Karlak B, Jiang S, Lemahieu V, McCormick F, Francke U, Abo A. Wiskott - Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization. of special interest Cell. 84:1996;723-734 Deminstrates that a genetically determined disease that codes for a (non-kinase) protein with a hitherto unknown function is an effector for Cdc42.
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Cell
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Symons, M.1
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McCormick, F.6
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60
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0030035043
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Identification of a putative target for Rho as the serine-threonine kinase protein kinase N
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of outstanding interest. Using different approaches, both this paper and [61] identify PKN, a serine/threonine kinase, as the effector of Rho, which becomes activated several fold by the GTP-dependent interaction. A sequence motif of the Rho binding domain of PKN, called REM-1 for Rho-effector motif class 1, is also found in other putative effectors of Rho such as rhophilin and rhotekin, from the Japanese teki, which means target [86].
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Amano M, Mukai H, Ono Y, Chihara K, Matsui T, Hamajima Y, Okawa K, Iwamatsu A, Kaibuchi K. Identification of a putative target for Rho as the serine-threonine kinase protein kinase N. of outstanding interest Science. 271:1996;648-650 Using different approaches, both this paper and [61] identify PKN, a serine/threonine kinase, as the effector of Rho, which becomes activated several fold by the GTP-dependent interaction. A sequence motif of the Rho binding domain of PKN, called REM-1 for Rho-effector motif class 1, is also found in other putative effectors of Rho such as rhophilin and rhotekin, from the Japanese teki, which means target [86].
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Science
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Amano, M.1
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Okawa, K.7
Iwamatsu, A.8
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61
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Protein kinase N (PKN) and PKN-related protein, rhophilin, as targets of small GTPase Rho
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of outstanding interest. See annotation [60].
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Watanabe G, Saito Y, Madaule P, Ishizaki T, Fujisawa K, Morii N, Mukai H, Ono Y, Kakizuka A, Narumiya S. Protein kinase N (PKN) and PKN-related protein, rhophilin, as targets of small GTPase Rho. of outstanding interest Science. 271:1996;645-648 See annotation [60].
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Watanabe, G.1
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62
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0029117229
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A family of Ran binding proteins that includes nucleoporins
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of special interest. See annotation [64].
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Dingwall C, Kandels-Lewis S, Séraphin B. A family of Ran binding proteins that includes nucleoporins. of special interest Proc Natl Acad Sci USA. 92:1995;7525-7529 See annotation [64].
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Dingwall, C.1
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63
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A Ran-binding motif in nuclear pore proteins
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of special interest. See annotation [64].
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Hartmann E, Görlich D. A Ran-binding motif in nuclear pore proteins. of special interest Trends Cell Biol. 5:1995;192-193 See annotation [64].
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Hartmann, E.1
Görlich, D.2
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64
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0028955712
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The Ran/TC4 GTPase-binding domain: Identification by expression cloning and characterization of a conserved sequence motif
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of special interest. This paper, together with [62,63], shows that the Ran-binding protein 1 (RanBP1) contains a sequence motif that is found in a number of nuclear pore proteins that are thus potential candidate effectors for Ran.
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Beddow AL, Richards SA, Orem NR, Macara IG. The Ran/TC4 GTPase-binding domain: identification by expression cloning and characterization of a conserved sequence motif. of special interest Proc Natl Acad Sci USA. 92:1995;3328-3332 This paper, together with [62,63], shows that the Ran-binding protein 1 (RanBP1) contains a sequence motif that is found in a number of nuclear pore proteins that are thus potential candidate effectors for Ran.
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Proc Natl Acad Sci USA
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Beddow, A.L.1
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Macara, I.G.4
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65
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0028842508
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Identification and molecular cloning of a p21cdc42/rac1-activated serine/threonine kinase that is rapidly activated by thrombin in platelets
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Teo M, Manser E, Lim L. Identification and molecular cloning of a p21cdc42/rac1-activated serine/threonine kinase that is rapidly activated by thrombin in platelets. J Biol Chem. 270:1995;26690-26697.
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Teo, M.1
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Lim, L.3
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66
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0028928791
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Protein kinase Byr2 is a target of Ras1 in the fission yeast Schizosaccharomyces pombe
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of special interest. Demonstrates that the protein kinase Byr2, genetically defined as a molecule downstrean of S. pombe, is indeed a direct effector.
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Masuda T, Kariya K-I, Shinkai M, Okada T, Kataoka T. Protein kinase Byr2 is a target of Ras1 in the fission yeast Schizosaccharomyces pombe. of special interest J Biol Chem. 270:1995;1979-1982 Demonstrates that the protein kinase Byr2, genetically defined as a molecule downstrean of S. pombe, is indeed a direct effector.
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J Biol Chem
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Masuda, T.1
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Shinkai, M.3
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67
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0028955710
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Interactions among proteins involved in Bud-site selection and Bud-site assembly in Saccharomyces cerevisiae
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Xu H-P5
Wigler, M.H.6
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69
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Identification and characterization of Ral-binding protein 1, a potential downstream target of Ral GTPases
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Cantor SB, Urano T, Feig LA. Identification and characterization of Ral-binding protein 1, a potential downstream target of Ral GTPases. Mol Cell Biol. 15:1995;4578-4584.
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Cantor, S.B.1
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70
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Bridging Ral GTPase to Rho pathways
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Jullien-Flores V, Dorseuil O, Romero F, Letourneur F, Saragosti S, Berger R, Tavitian A, Gacon G, Camonis JH. Bridging Ral GTPase to Rho pathways. J Biol Chem. 270:1995;22473-22477.
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Jullien-Flores, V.1
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71
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0029066439
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Molecular characterization of Ste20p, a potential mitogen-activated protein or extracellular signal regulated kinase kinase (MEK) kinase kinase from Saccharomyces cerevisiae
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of special interest. This paper, together with [72], defines genetically for S. cerevisiae and S. pombe the signal transduction pathways involving the interaction between Ste20/PAK and Rac/Cdc42.
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Wu C, Whiteway M, Thomas DY, Leberer E. Molecular characterization of Ste20p, a potential mitogen-activated protein or extracellular signal regulated kinase kinase (MEK) kinase kinase from Saccharomyces cerevisiae. of special interest J Biol Chem. 270:1995;15984-15992 This paper, together with [72], defines genetically for S. cerevisiae and S. pombe the signal transduction pathways involving the interaction between Ste20/PAK and Rac/Cdc42.
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Wu, C.1
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72
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0029044903
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Shk1, a homolog of the Saccharomyces cerevisiae Ste20 and mammalian p65PAK protein kinases, is a component of a Ras/Cdc42 signaling module in the fission yeast Schizosaccharomyces pombe
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of special interest. See annotation [71].
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Marcus S, Polverino A, Chang E, Robbins D, Cobb MH, Wigler MH. Shk1, a homolog of the Saccharomyces cerevisiae Ste20 and mammalian p65PAK protein kinases, is a component of a Ras/Cdc42 signaling module in the fission yeast Schizosaccharomyces pombe. of special interest Proc Natl Acad Sci USA. 92:1995;6180-6184 See annotation [71].
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Proc Natl Acad Sci USA
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Marcus, S.1
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Chang, E.3
Robbins, D.4
Cobb, M.H.5
Wigler, M.H.6
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74
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0029680639
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Two GTPases, Cdc42 and Rac, bind directly to a protein implicated in the immunodeficiency disorder Wiskott - Aldrich syndrome
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Aspenström P, Lindberg U, Hall A. Two GTPases, Cdc42 and Rac, bind directly to a protein implicated in the immunodeficiency disorder Wiskott - Aldrich syndrome. Curr Biol. 6:1996;70-75.
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Aspenström, P.1
Lindberg, U.2
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0030029804
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The Rac target NADPH oxidase p67 phox interacts preferentially with Rac2 rather than Rac 1
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Dorseuil O, Reibel L, Bokoch GM, Camonis J, Gacon G. The Rac target NADPH oxidase p67 phox interacts preferentially with Rac2 rather than Rac 1. J Biol Chem. 271:1996;83-88.
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Dorseuil, O.1
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Gacon, G.5
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77
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0028110120
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A novel oncogene, ost, encodes a guanine nucleotide exchange factor that potentially links Rho and Rac signaling pathways
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Horii Y, Beeler JF, Sakaguchi K, Tachibana M, Miki T. A novel oncogene, ost, encodes a guanine nucleotide exchange factor that potentially links Rho and Rac signaling pathways. EMBO J. 13:1994;4776-4786.
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Horii, Y.1
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78
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IQGAP1, a calmodulin-binding protein with a rasGAP-related domain, is a potential effector for cdc42Hs
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Hart MJ, Callow MG, Souza B, Polakis P. IQGAP1, a calmodulin-binding protein with a rasGAP-related domain, is a potential effector for cdc42Hs. EMBO J. 15:1995;2997-3005.
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EMBO J
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Hart, M.J.1
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0030040856
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The Ras-related GTPase Rac1 binds tubulin
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Best A, Ahmed S, Kozma R, Lim L. The Ras-related GTPase Rac1 binds tubulin. J Biol Chem. 271:1996;3756-3762.
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Best, A.1
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Lim, L.4
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80
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9244220646
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The small GTP-binding protein Rho binds to and activates a 160 kDa Ser/Thr protein kinase homologous to myotonic dystrophy kinase
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of special interest. Define a protein kinase homologous to myotonic dystrophy kinase that interacts with and is activated by Rho. See also [81].
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Ishizaki T, Maekawa M, Fujisawa K, Okawa K, Iwamatsu A, Fujita A, Watanabe N, Saito Y, Kakizuka A, Morii N, Narumiya S. The small GTP-binding protein Rho binds to and activates a 160 kDa Ser/Thr protein kinase homologous to myotonic dystrophy kinase. of special interest EMBO J. 15:1996;1885-1893 Define a protein kinase homologous to myotonic dystrophy kinase that interacts with and is activated by Rho. See also [81].
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EMBO J
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Ishizaki, T.1
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Fujita, A.6
Watanabe, N.7
Saito, Y.8
Kakizuka, A.9
Morii, N.10
Narumiya, S.11
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81
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9244257348
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Rho-associated kinase, a novel serine/threonine kinase, as a putative target for the small GTP binding protein Rho
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of special interest. See annotation [80].
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Matsui T, Amano M, Yamamoto T, Chihara K, Nakafuku M, Ito M, Nakano T, Okawa K, Iwamatsu A, Kaibuchi K. Rho-associated kinase, a novel serine/threonine kinase, as a putative target for the small GTP binding protein Rho. of special interest EMBO J. 15:1996;2208-2216 See annotation [80].
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Matsui, T.1
Amano, M.2
Yamamoto, T.3
Chihara, K.4
Nakafuku, M.5
Ito, M.6
Nakano, T.7
Okawa, K.8
Iwamatsu, A.9
Kaibuchi, K.10
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82
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0028260527
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Novel protein kinase with Leucine zipper-like sequences: Its catalytic domain is highly homologous to that of protein kinase C
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Mukai H, Ono Y. Novel protein kinase with Leucine zipper-like sequences: its catalytic domain is highly homologous to that of protein kinase C. Biochem Biophys Res Commun. 199:1994;897-904.
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Mukai, H.1
Ono, Y.2
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83
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0028863142
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A novel serine/threonine kinase binding the Ras-related RhoA GTPase which translocates the kinase to peripheral membranes
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Leung T, Manser E, Tan L, Lim L. A novel serine/threonine kinase binding the Ras-related RhoA GTPase which translocates the kinase to peripheral membranes. J Biol Chem. 270:1995;29051-29054.
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J Biol Chem
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Leung, T.1
Manser, E.2
Tan, L.3
Lim, L.4
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84
-
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0028902594
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The Drosophila tumor suppressor gene warts encodes a homolog of human myotonic dystrophy kinase and is required for the control of cell shape and proliferation
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Justice RW, Zilian O, Woods DF, Noll M, Bryant PJ. The Drosophila tumor suppressor gene warts encodes a homolog of human myotonic dystrophy kinase and is required for the control of cell shape and proliferation. Genes Dev. 9:1995;534-546.
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Justice, R.W.1
Zilian, O.2
Woods, D.F.3
Noll, M.4
Bryant, P.J.5
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85
-
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0029559573
-
A novel partner for the GTP-bound forms of rho and rac
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Madaule P, Furuyashiki T, Reid T, Ishizaki T, Watanabe G, Morii N, Narumiya S. A novel partner for the GTP-bound forms of rho and rac. FEBS Lett. 377:1995;243-248.
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FEBS Lett
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Madaule, P.1
Furuyashiki, T.2
Reid, T.3
Ishizaki, T.4
Watanabe, G.5
Morii, N.6
Narumiya, S.7
-
86
-
-
0029889591
-
Rhotekin, a new putative target for Rho bearing homology to a serine/threonine kinase, PKN, and rhophillin in the Rho-binding domain
-
of special interest. Identifies a conserved sequence element in Rho effector proteins which appears in protein kinases and other proteins.
-
Reid T, Furuyashiki T, Ishizaki T, Watanabe G, Watanabe N, Fujisawa K, Morii N, Madaule P, Narumiya S. Rhotekin, a new putative target for Rho bearing homology to a serine/threonine kinase, PKN, and rhophillin in the Rho-binding domain. of special interest J Biol Chem. 271:1996;13556-13560 Identifies a conserved sequence element in Rho effector proteins which appears in protein kinases and other proteins.
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(1996)
J Biol Chem
, vol.271
, pp. 13556-13560
-
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Reid, T.1
Furuyashiki, T.2
Ishizaki, T.3
Watanabe, G.4
Watanabe, N.5
Fujisawa, K.6
Morii, N.7
Madaule, P.8
Narumiya, S.9
-
87
-
-
0030005716
-
Rho1p, a yeast protein at the interface between cell polarization and morphogenesis
-
of special interest. This paper, together with [88], shows that Rho is a subunit of an enzyme involved in cell wall biosynthesis.
-
Drgonová J, Drgon T, Tanaka K, Kollár R, Chen G-C, Ford RA, Chan CSM, Takai Y, Cabib E. Rho1p, a yeast protein at the interface between cell polarization and morphogenesis. of special interest Science. 272:1996;277-279 This paper, together with [88], shows that Rho is a subunit of an enzyme involved in cell wall biosynthesis.
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Science
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, pp. 277-279
-
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Drgonová, J.1
Drgon, T.2
Tanaka, K.3
Kollár, R.4
Chen G-C5
Ford, R.A.6
Chan, C.S.M.7
Takai, Y.8
Cabib, E.9
-
88
-
-
0029892037
-
Identification of yeast Rho1p GTPase as a regulatory subunit of 1,3β-glucan synthase
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of special interest. See annotation [87].
-
Qadota H, Python CP, Inoue SB, Arisawa M, Anraku Y, Zheng Y, Watanabe T, Levin DE, Ohya Y. Identification of yeast Rho1p GTPase as a regulatory subunit of 1,3β-glucan synthase. of special interest Science. 272:1996;279-281 See annotation [87].
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Science
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, pp. 279-281
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-
Qadota, H.1
Python, C.P.2
Inoue, S.B.3
Arisawa, M.4
Anraku, Y.5
Zheng, Y.6
Watanabe, T.7
Levin, D.E.8
Ohya, Y.9
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89
-
-
0027461829
-
Rabphilin-3A, a putative target protein for smg p25A/rab3A p25 small GTP-binding protein related to synaptotagmin
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Shirataki H, Kaibuchi K, Sakoda T, Kishida S, Yamaguchi T, Wada K, Miyazaki M, Takai Y. Rabphilin-3A, a putative target protein for smg p25A/rab3A p25 small GTP-binding protein related to synaptotagmin. Mol Cell Biol. 13:1993;2061-2068.
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Mol Cell Biol
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Shirataki, H.1
Kaibuchi, K.2
Sakoda, T.3
Kishida, S.4
Yamaguchi, T.5
Wada, K.6
Miyazaki, M.7
Takai, Y.8
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90
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-
0029935431
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Rab3 reversibly recruits rabphilin to synaptic vesicles by a mechanism analogous to Raf recruitment by Ras
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Stahl B, Chou JH, Li C, Südhof TC, Jahn R. Rab3 reversibly recruits rabphilin to synaptic vesicles by a mechanism analogous to Raf recruitment by Ras. EMBO J. 15:1996;1799-1809.
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EMBO J
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, pp. 1799-1809
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Stahl, B.1
Chou, J.H.2
Li, C.3
Südhof, T.C.4
Jahn, R.5
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91
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-
0028860327
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Interaction cloning of rabin3, a novel protein that associates with the Ras-like GTPase Rab3A
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Brondyk WH, McKiernan CJ, Fortner KA, Stabila P, Holz RW, Macara IG. Interaction cloning of rabin3, a novel protein that associates with the Ras-like GTPase Rab3A. Mol Cell Biol. 15:1995;1137-1143.
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Mol Cell Biol
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Brondyk, W.H.1
McKiernan, C.J.2
Fortner, K.A.3
Stabila, P.4
Holz, R.W.5
Macara, I.G.6
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92
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0029043804
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Two-hybrid system screen with the small GTP-binding protein Rab6
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Janoueix-Lerosey I, Jollivet F, Camonis J, Marche PN, Goud B. Two-hybrid system screen with the small GTP-binding protein Rab6. J Biol Chem. 270:1995;14801-14808.
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J Biol Chem
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Janoueix-Lerosey, I.1
Jollivet, F.2
Camonis, J.3
Marche, P.N.4
Goud, B.5
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93
-
-
0028791634
-
Rabaptin-5 is a direct effector of the small GTPase Rab5 in endocytic membrane fusion
-
of outstanding interest. From the various Rab effector proteins identified by the yeast two-hybrid method, only Rabaptin-5, the effector of Rab5, has functionally been described, showing that the molecule is involved in endosome fusion.
-
Stenmark H, Vitale G, Ullrich O, Zerial M. Rabaptin-5 is a direct effector of the small GTPase Rab5 in endocytic membrane fusion. of outstanding interest Cell. 83:1995;423-432 From the various Rab effector proteins identified by the yeast two-hybrid method, only Rabaptin-5, the effector of Rab5, has functionally been described, showing that the molecule is involved in endosome fusion.
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(1995)
Cell
, vol.83
, pp. 423-432
-
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Stenmark, H.1
Vitale, G.2
Ullrich, O.3
Zerial, M.4
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94
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0027732054
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Characterization of proteins that interact with the cell-cycle regulatory protein Ran/TC4
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Coutavas E, Ren M, Oppenheim JD, D'Eustachio P, Rush MG. Characterization of proteins that interact with the cell-cycle regulatory protein Ran/TC4. Nature. 366:1993;585-587.
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Nature
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, pp. 585-587
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Coutavas, E.1
Ren, M.2
Oppenheim, J.D.3
D'Eustachio, P.4
Rush, M.G.5
-
95
-
-
0028937195
-
Co-activation of Ran GTPase and inhibition of GTP dissociation by Ran-GTP binding protein RanBP1
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Bischoff FR, Krebber H, Smirnova E, Dong W, Ponstingl H. Co-activation of Ran GTPase and inhibition of GTP dissociation by Ran-GTP binding protein RanBP1. EMBO J. 14:1995;705-715.
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EMBO J
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Bischoff, F.R.1
Krebber, H.2
Smirnova, E.3
Dong, W.4
Ponstingl, H.5
-
96
-
-
0029032954
-
A giant nucleopore protein that binds Ran/TC4
-
of outstanding interest. See annotation [97].
-
Yokoyama N, Hayashi N, Seki T, Panté N, Ohba T, Nishii K, Kuma K, Hayashida T, Miyat T, Aebi U, et al. A giant nucleopore protein that binds Ran/TC4. of outstanding interest Nature. 376:1995;184-188 See annotation [97].
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(1995)
Nature
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, pp. 184-188
-
-
Yokoyama, N.1
Hayashi, N.2
Seki, T.3
Panté, N.4
Ohba, T.5
Nishii, K.6
Kuma, K.7
Hayashida, T.8
Miyat, T.9
Aebi, U.10
-
97
-
-
0029070074
-
Nup358, a cytoplasmically exposed nucleoporin with peptide repeats, Ran-GTP binding sites, zinc fingers, a cyclophilin A homologous domain, and a leucine-rich region
-
of outstanding interest. This paper, together with [96], identifies a nuclear pore protein that has, among many other domains, four consecutive Ran-binding domains, all of which have been shown to bind in a GTP-dependent manner to Ran. In addition, it contains the XFXFG (single letter amino acid code) pentapeptide repeats characteristic of nucleoporin. The data support a functional role in protein import.
-
Wu J, Matunis MJ, Kraemer D, Blobel G, Coutavas E. Nup358, a cytoplasmically exposed nucleoporin with peptide repeats, Ran-GTP binding sites, zinc fingers, a cyclophilin A homologous domain, and a leucine-rich region. of outstanding interest J Biol Chem. 270:1995;14209-14213 This paper, together with [96], identifies a nuclear pore protein that has, among many other domains, four consecutive Ran-binding domains, all of which have been shown to bind in a GTP-dependent manner to Ran. In addition, it contains the XFXFG (single letter amino acid code) pentapeptide repeats characteristic of nucleoporin. The data support a functional role in protein import.
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(1995)
J Biol Chem
, vol.270
, pp. 14209-14213
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-
Wu, J.1
Matunis, M.J.2
Kraemer, D.3
Blobel, G.4
Coutavas, E.5
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98
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0028170744
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Purification of a Ran-interacting protein that is required for protein import into the nucleus
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Moore MS, Blobel G. Purification of a Ran-interacting protein that is required for protein import into the nucleus. Proc Natl Acad Sci USA. 91:1994;10212-10216.
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Proc Natl Acad Sci USA
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, pp. 10212-10216
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Moore, M.S.1
Blobel, G.2
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99
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-
0028206481
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A family of proteins that stabilize the Ran/TC4 GTPase in its GTP-bound conformation
-
Lounsbury KM, Beddow AL, Macara IG. A family of proteins that stabilize the Ran/TC4 GTPase in its GTP-bound conformation. J Biol Chem. 269:1994;11285-11290.
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(1994)
J Biol Chem
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, pp. 11285-11290
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-
Lounsbury, K.M.1
Beddow, A.L.2
Macara, I.G.3
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100
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-
0029920934
-
The nuclear transport factor karyopherin β binds stoichiometrically to Ran-FTP and inhibits the Ran GTPase activating protein
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Floer M, Blobel G. The nuclear transport factor karyopherin β binds stoichiometrically to Ran-FTP and inhibits the Ran GTPase activating protein. J Biol Chem. 271:1996;5313-5315.
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J Biol Chem
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Floer, M.1
Blobel, G.2
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101
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-
0028834428
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Protein import into nuclei: Association and dissociation reactions involving transport substrate, transport factors, and nucleoporins
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Rexach M, Blobel G. Protein import into nuclei: association and dissociation reactions involving transport substrate, transport factors, and nucleoporins. Cell. 83:1995;683-692.
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Cell
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, pp. 683-692
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Rexach, M.1
Blobel, G.2
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