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Volumn 71, Issue , 2002, Pages 391-444

A growing family of guanine nucleotide exchange factors is responsible for activation of ras-family GTPases

Author keywords

[No Author keywords available]

Indexed keywords

GUANINE NUCLEOTIDE EXCHANGE FACTOR; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; RAS PROTEIN;

EID: 0036364408     PISSN: 00796603     EISSN: None     Source Type: Book Series    
DOI: 10.1016/s0079-6603(02)71047-7     Document Type: Review
Times cited : (222)

References (289)
  • 1
    • 85112928969 scopus 로고
    • The ras oncogene
    • J.C Lacal S.R Tronick The ras oncogene E.P Reddy A.M Skalka T Curran The Oncogene Handbook 1988 Elsevier Science Publishers Amsterdam 257 304
    • (1988) , pp. 257-304
    • Lacal, J.C1    Tronick, S.R2
  • 2
    • 0025908897 scopus 로고
    • The ras protein family: Evolutionary tree and role of conserved amino acids
    • A Valencia P Chardin A Wittinghofer C Sander The ras protein family: Evolutionary tree and role of conserved amino acids Biochemistry 30 1991 4637 4648
    • (1991) Biochemistry , vol.30 , pp. 4637-4648
    • Valencia, A1    Chardin, P2    Wittinghofer, A3    Sander, C4
  • 5
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • A Hall Rho GTPases and the actin cytoskeleton Science 279 1998 509 514
    • (1998) Science , vol.279 , pp. 509-514
    • Hall, A1
  • 6
    • 0032541613 scopus 로고    scopus 로고
    • Rho family proteins and Ras transformation: The RHOad less traveled gets congested
    • I.M Zohn S.L Campbell R Khosravi-Far K.L Rossman C.J Der Rho family proteins and Ras transformation: The RHOad less traveled gets congested Oncogene 17 1998 1415 1438
    • (1998) Oncogene , vol.17 , pp. 1415-1438
    • Zohn, I.M1    Campbell, S.L2    Khosravi-Far, R3    Rossman, K.L4    Der, C.J5
  • 7
    • 0032860424 scopus 로고    scopus 로고
    • Regulation of the cytoskeleton and cell adhesion by the Rho family GTPases in mammalian cells
    • K Kaibuchi S Kuroda M Amano Regulation of the cytoskeleton and cell adhesion by the Rho family GTPases in mammalian cells Annu. Rev. Biochem. 68 1999 459 486
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 459-486
    • Kaibuchi, K1    Kuroda, S2    Amano, M3
  • 8
    • 0033180113 scopus 로고    scopus 로고
    • The role of ARF and Rab GTPases in membrane transport
    • P Chavrier B Goud The role of ARF and Rab GTPases in membrane transport Curr. Opin. Cell Biol. 11 1999 466 475
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 466-475
    • Chavrier, P1    Goud, B2
  • 10
    • 0034065954 scopus 로고    scopus 로고
    • The role of Ran in nuclear function
    • Y Azuma M Dasso The role of Ran in nuclear function Curr. Opin. Cell Biol. 12 2000 302 307
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 302-307
    • Azuma, Y1    Dasso, M2
  • 11
    • 0035445281 scopus 로고    scopus 로고
    • Ran GTPase: A master regulator of nuclear structure and function during the eukaryotic cell division cycle?
    • P.R Clarke C Zhang Ran GTPase: A master regulator of nuclear structure and function during the eukaryotic cell division cycle? Trends Cell. Biol. 11 2001 366 371
    • (2001) Trends Cell. Biol. , vol.11 , pp. 366-371
    • Clarke, P.R1    Zhang, C2
  • 12
    • 0033392946 scopus 로고    scopus 로고
    • Enzymology and biology of CaaX protein prenylation
    • H.W Fu P.J Casey Enzymology and biology of CaaX protein prenylation Rec. Prog. Horm. Res. 54 1999 315 342
    • (1999) Rec. Prog. Horm. Res. , vol.54 , pp. 315-342
    • Fu, H.W1    Casey, P.J2
  • 13
    • 0031687777 scopus 로고    scopus 로고
    • Signal transduction via Ras
    • A Wittinghofer Signal transduction via Ras Biol. Chem. 379 1998 933 937
    • (1998) Biol. Chem. , vol.379 , pp. 933-937
    • Wittinghofer, A1
  • 14
    • 0029294676 scopus 로고
    • Guanine nucleotide exchange factors: activators of the Ras superfamily of proteins
    • L.A Quilliam R Khosravi-Far S.Y Huff C.J Der Guanine nucleotide exchange factors: activators of the Ras superfamily of proteins Bioessays 17 1995 395 404
    • (1995) Bioessays , vol.17 , pp. 395-404
    • Quilliam, L.A1    Khosravi-Far, R2    Huff, S.Y3    Der, C.J4
  • 16
    • 0027732538 scopus 로고
    • Proteins regulating Ras and its relatives
    • M.S Boguski F McCormick Proteins regulating Ras and its relatives Nature 366 1993 643 654
    • (1993) Nature , vol.366 , pp. 643-654
    • Boguski, M.S1    McCormick, F2
  • 17
    • 0002457485 scopus 로고
    • Ras proto-oncogene activation in human malignancy
    • G.J Clark C.J Der Ras proto-oncogene activation in human malignancy C Garrett S Sell Cellular Cancer Markers 1995 Humana Press Totowa, NJ 17 52
    • (1995) , pp. 17-52
    • Clark, G.J1    Der, C.J2
  • 18
    • 0031844181 scopus 로고    scopus 로고
    • Ras-related TC21 is activated by mutation in a breast cancer cell line, but infrequently in breast carcinomas in vivo
    • K.T Barker M.R Crompton Ras-related TC21 is activated by mutation in a breast cancer cell line, but infrequently in breast carcinomas in vivo Br. J. Cancer 78 1998 296 300
    • (1998) Br. J. Cancer , vol.78 , pp. 296-300
    • Barker, K.T1    Crompton, M.R2
  • 23
    • 0034104590 scopus 로고    scopus 로고
    • The Ras branch of small GTPases: Ras family members don't fall far from the tree
    • G.W Reuther C.J Der The Ras branch of small GTPases: Ras family members don't fall far from the tree Curr. Opin. Cell Biol. 12 2000 157 165
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 157-165
    • Reuther, G.W1    Der, C.J2
  • 25
    • 0034177553 scopus 로고    scopus 로고
    • Rem2, a new member of the Rem/Rad/Gem/Kir family of Ras-related GTPases
    • B.S Finlin H Shao K Kadono-Okuda N Guo D.A Andres Rem2, a new member of the Rem/Rad/Gem/Kir family of Ras-related GTPases Biochem. J. 347 2000 223 231 Pt 1
    • (2000) Biochem. J. , vol.347 , pp. 223-231
    • Finlin, B.S1    Shao, H2    Kadono-Okuda, K3    Guo, N4    Andres, D.A5
  • 27
    • 0034603021 scopus 로고    scopus 로고
    • A subclass of Ras proteins that regulate the degradation of IkappaB
    • C Fenwick S.Y Na R.E Voll H Zhong S.Y Im J.W Lee S Ghosh A subclass of Ras proteins that regulate the degradation of IkappaB Science 287 2000 869 873
    • (2000) Science , vol.287 , pp. 869-873
    • Fenwick, C1    Na, S.Y2    Voll, R.E3    Zhong, H4    Im, S.Y5    Lee, J.W6    Ghosh, S7
  • 28
    • 0026611269 scopus 로고
    • Erythropoietin induces p21ras activation and p120GAP tyrosine phosphorylation in human erythroleukemia cells
    • M Torti K.B Marti D Altschuler K Yamamoto E.G Lapetina Erythropoietin induces p21ras activation and p120GAP tyrosine phosphorylation in human erythroleukemia cells J. Biol. Chem. 267 1992 8293 8298
    • (1992) J. Biol. Chem. , vol.267 , pp. 8293-8298
    • Torti, M1    Marti, K.B2    Altschuler, D3    Yamamoto, K4    Lapetina, E.G5
  • 29
    • 0030806174 scopus 로고    scopus 로고
    • Chemotactic peptide-induced activation of Ras in human neutrophils is associated with inhibition of p120-GAP activity
    • L Zheng J Eckerdal I Dimitrijevic T Andersson Chemotactic peptide-induced activation of Ras in human neutrophils is associated with inhibition of p120-GAP activity J. Biol. Chem. 272 1997 23,448 23,454
    • (1997) J. Biol. Chem. , vol.272
    • Zheng, L1    Eckerdal, J2    Dimitrijevic, I3    Andersson, T4
  • 30
    • 0034609756 scopus 로고    scopus 로고
    • A permissive function of phosphoinositide 3-kinase in Ras activation mediated by inhibition of GTPase-activating proteins
    • I Rubio R Wetzker A permissive function of phosphoinositide 3-kinase in Ras activation mediated by inhibition of GTPase-activating proteins Curr. Biol. 10 2000 1225 1228
    • (2000) Curr. Biol. , vol.10 , pp. 1225-1228
    • Rubio, I1    Wetzker, R2
  • 32
    • 0033618396 scopus 로고    scopus 로고
    • Modulation of rap activity by direct interaction of Galpha(o) with Rapl GTPase-activating protein
    • J.D Jordan K.D Carey P.J Stork R Iyengar Modulation of rap activity by direct interaction of Galpha(o) with Rapl GTPase-activating protein J. Biol. Chem. 274 1999 21,07 21510
    • (1999) J. Biol. Chem. , vol.274
    • Jordan, J.D1    Carey, K.D2    Stork, P.J3    Iyengar, R4
  • 34
    • 0033756553 scopus 로고    scopus 로고
    • CD28 and the tyrosine kinase lck stimulate mitogen-activated protein kinase activity in T cells via inhibition of the small G protein Rapl
    • K.D Carey T.J Dillon J.M Schmitt A.M Baird A.D Holdorf D.B Straus A.S Shaw P.J Stork CD28 and the tyrosine kinase lck stimulate mitogen-activated protein kinase activity in T cells via inhibition of the small G protein Rapl Mol. Cell. Biol. 20 2000 8409 8419
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 8409-8419
    • Carey, K.D1    Dillon, T.J2    Schmitt, J.M3    Baird, A.M4    Holdorf, A.D5    Straus, D.B6    Shaw, A.S7    Stork, P.J8
  • 36
    • 0026315383 scopus 로고
    • The CDC25 protein of Saccharomyces cerevisiae promotes exchange of guanine nucleotides bound to ras
    • S Jones M.L Vignais J.R Broach The CDC25 protein of Saccharomyces cerevisiae promotes exchange of guanine nucleotides bound to ras Mol. Cell. Biol. 11 1991 2641 2646
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 2641-2646
    • Jones, S1    Vignais, M.L2    Broach, J.R3
  • 37
    • 0025043199 scopus 로고
    • Purification and characterization from bovine brain cytosol of proteins that regulate the GDP/GTP exchange reaction of smg p21s, ras p21-like GTP-binding proteins
    • T Yamamoto K Kaibuchi T Mizuno M Hiroyoshi H Shirataki Y Takai Purification and characterization from bovine brain cytosol of proteins that regulate the GDP/GTP exchange reaction of smg p21s, ras p21-like GTP-binding proteins J. Biol. Chem. 265 1990 16,626 16,634
    • (1990) J. Biol. Chem. , vol.265
    • Yamamoto, T1    Kaibuchi, K2    Mizuno, T3    Hiroyoshi, M4    Shirataki, H5    Takai, Y6
  • 38
    • 0026050653 scopus 로고
    • A stimulatory GDP/GTP exchange protein for smg p21 is active on the posttranslationally processed form of c-Ki-ras p21 and rhoA p21
    • T Mizuno K Kaibuchi T Yamamoto M Kawamura T Sakoda H Fujioka Y Matsuura Y Takai A stimulatory GDP/GTP exchange protein for smg p21 is active on the posttranslationally processed form of c-Ki-ras p21 and rhoA p21 Proc. Natl. Acad. Sci. U.S.A. 88 1991 6442 6446
    • (1991) , pp. 6442-6446
    • Mizuno, T1    Kaibuchi, K2    Yamamoto, T3    Kawamura, M4    Sakoda, T5    Fujioka, H6    Matsuura, Y7    Takai, Y8
  • 39
    • 0027972965 scopus 로고
    • SmgGDS stabilizes nucleotide-bound and -free forms of the Racl GTP-binding protein and stimulates GTP/GDP exchange through a substituted enzyme mechanism
    • T.H Chuang X Xu L.A Quilliam G.M Bokoch SmgGDS stabilizes nucleotide-bound and -free forms of the Racl GTP-binding protein and stimulates GTP/GDP exchange through a substituted enzyme mechanism Biochem. J. 303 1994 761 767
    • (1994) Biochem. J. , vol.303 , pp. 761-767
    • Chuang, T.H1    Xu, X2    Quilliam, L.A3    Bokoch, G.M4
  • 40
    • 0026341908 scopus 로고
    • Molecular cloning of the cDNA for stimulatory GDP/GTP exchange protein for smg p21s (ras p21-like small GTP-binding proteins) and characterization of stimulatory GDP/GTP exchange protein
    • K Kaibuchi T Mizuno H Fujioka T Yamamoto K Kishi Y Fukumoto Y Hori Y Takai Molecular cloning of the cDNA for stimulatory GDP/GTP exchange protein for smg p21s (ras p21-like small GTP-binding proteins) and characterization of stimulatory GDP/GTP exchange protein Mol. Cell. Biol. 11 1991 2873 2880
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 2873-2880
    • Kaibuchi, K1    Mizuno, T2    Fujioka, H3    Yamamoto, T4    Kishi, K5    Fukumoto, Y6    Hori, Y7    Takai, Y8
  • 41
    • 0026608238 scopus 로고
    • The Son of sevenless gene product: A putative activator of Ras
    • L Bonfini C.A Karlovich C Dasgupta U Banerjee The Son of sevenless gene product: A putative activator of Ras Science 255 1992 603 606
    • (1992) Science , vol.255 , pp. 603-606
    • Bonfini, L1    Karlovich, C.A2    Dasgupta, C3    Banerjee, U4
  • 42
    • 0025997867 scopus 로고
    • Rasl and a putative guanine nucleotide exchange factor perform crucial steps in signaling by the sevenless protein tyrosine kinase
    • M.A Simon D.D Bowtell G.S Dodson T.R Laverty G.M Rubin Rasl and a putative guanine nucleotide exchange factor perform crucial steps in signaling by the sevenless protein tyrosine kinase Cell 67 1991 701 716
    • (1991) Cell , vol.67 , pp. 701-716
    • Simon, M.A1    Bowtell, D.D2    Dodson, G.S3    Laverty, T.R4    Rubin, G.M5
  • 43
    • 0026627960 scopus 로고
    • Identification of murine homologues of the Drosophila son of sevenless gene: Potential activators of ras
    • D Bowtell P Fu M Simon P Senior Identification of murine homologues of the Drosophila son of sevenless gene: Potential activators of ras Proc. Nail. Acad. Sci. U.S.A. 89 1992 6511 6515
    • (1992) , pp. 6511-6515
    • Bowtell, D1    Fu, P2    Simon, M3    Senior, P4
  • 45
    • 0026523616 scopus 로고
    • Cloning by functional complementation of a mouse cDNA encoding a homologue of CDC25, a Saccharomyces cerevisiae RAS activator
    • E Martegani M Vanoni R Zippel P Coccetti R Brambilla C Ferrari E Sturani L Alberghina Cloning by functional complementation of a mouse cDNA encoding a homologue of CDC25, a Saccharomyces cerevisiae RAS activator EMBO J. 11 1992 2151 2157
    • (1992) EMBO J. , vol.11 , pp. 2151-2157
    • Martegani, E1    Vanoni, M2    Zippel, R3    Coccetti, P4    Brambilla, R5    Ferrari, C6    Sturani, E7    Alberghina, L8
  • 46
    • 0026659515 scopus 로고
    • Molecular cloning of cDNAs encoding a guanine-nucleotide-releasing factor for Ras p21 [see comments
    • C Shou C.L Farnsworth B.G Neel L.A Feig Molecular cloning of cDNAs encoding a guanine-nucleotide-releasing factor for Ras p21 [see comments Nature 358 1992 351 354
    • (1992) Nature , vol.358 , pp. 351-354
    • Shou, C1    Farnsworth, C.L2    Neel, B.G3    Feig, L.A4
  • 47
    • 0026695971 scopus 로고
    • Identification of a mammalian gene structurally and functionally related to the CDC25 gene of Saccharomyces cerevisiae
    • W Wei R.D Mosteller P Sanyal E Gonzales D McKinney C Dasgupta P Li B.X Liu D Broek Identification of a mammalian gene structurally and functionally related to the CDC25 gene of Saccharomyces cerevisiae Proc. Natl. Acad. Sci. U.S.A. 89 1992 7100 7104
    • (1992) , pp. 7100-7104
    • Wei, W1    Mosteller, R.D2    Sanyal, P3    Gonzales, E4    McKinney, D5    Dasgupta, C6    Li, P7    Liu, B.X8    Broek, D9
  • 48
    • 0026768072 scopus 로고
    • Isolation of multiple mouse cDNAs with coding homology to Saccharomyces cerevisiae CDC25: identification of a region related to Bcr, Vav, Dbl and CDC24
    • H Cen A.G Papageorge R Zippel D.R Lowy K Zhang Isolation of multiple mouse cDNAs with coding homology to Saccharomyces cerevisiae CDC25: identification of a region related to Bcr, Vav, Dbl and CDC24 EMBO J. 11 1992 4007 4015
    • (1992) EMBO J. , vol.11 , pp. 4007-4015
    • Cen, H1    Papageorge, A.G2    Zippel, R3    Lowy, D.R4    Zhang, K5
  • 49
    • 0027518574 scopus 로고
    • Characterization of a guanine nucleotide dissociation stimulator for a ras-related GTPase
    • C.F Albright B.W Giddings J Liu M Vito R.A Weinberg Characterization of a guanine nucleotide dissociation stimulator for a ras-related GTPase EMBO J. 12 1993 339 347
    • (1993) EMBO J. , vol.12 , pp. 339-347
    • Albright, C.F1    Giddings, B.W2    Liu, J3    Vito, M4    Weinberg, R.A5
  • 50
    • 0028264812 scopus 로고
    • C3G, a guanine nucleotide-releasing protein expressed ubiquitously, binds to the Src homology 3 domains of CRK and GRB2/ASH proteins
    • S Tanaka T Morishita Y Hashimoto S Hattori S Nakamura M Shibuya K Matuoka T Takenawa T Kurata K Nagashima C3G, a guanine nucleotide-releasing protein expressed ubiquitously, binds to the Src homology 3 domains of CRK and GRB2/ASH proteins Proc. Natl. Acad. Sci. U.S.A. 91 1994 3443 3447
    • (1994) , pp. 3443-3447
    • Tanaka, S1    Morishita, T2    Hashimoto, Y3    Hattori, S4    Nakamura, S5    Shibuya, M6    Matuoka, K7    Takenawa, T8    Kurata, T9    Nagashima, K10
  • 51
    • 0028606468 scopus 로고
    • Four proline-rich sequences of the guanine-nucleotide exchange factor C3G bind with unique specificity to the first Src homology 3 domain of Crk
    • B.S Knudsen S.M Feller H Hanafusa Four proline-rich sequences of the guanine-nucleotide exchange factor C3G bind with unique specificity to the first Src homology 3 domain of Crk J. Biol. Chem. 269 1994 32,781 32,787
    • (1994) J. Biol. Chem. , vol.269
    • Knudsen, B.S1    Feller, S.M2    Hanafusa, H3
  • 54
    • 0027502176 scopus 로고
    • Influence of guanine nucleotides on complex formation between Ras and CDC25 proteins
    • C.C Lai M Boguski D Broek S Powers Influence of guanine nucleotides on complex formation between Ras and CDC25 proteins Mol. Cell. Biol. 13 1993 1345 1352
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 1345-1352
    • Lai, C.C1    Boguski, M2    Broek, D3    Powers, S4
  • 55
    • 0034607989 scopus 로고    scopus 로고
    • Identification and characterization of a new family of guanine nucleotide exchange factors for the Ras-related GTPase Ral
    • J.F Rebhun H Chen L.A Quilliam Identification and characterization of a new family of guanine nucleotide exchange factors for the Ras-related GTPase Ral J. Biol. Chem. 275 2000 13,406 13,410
    • (2000) J. Biol. Chem. , vol.275
    • Rebhun, J.F1    Chen, H2    Quilliam, L.A3
  • 57
    • 0025117674 scopus 로고
    • Molecular switch for signal transduction: Structural differences between active and inactive forms of protooncogenic ras proteins
    • M.V Milburn L Tong A.M deVos A Brunger Z Yamaizumi S Nishimura S.H Kim Molecular switch for signal transduction: Structural differences between active and inactive forms of protooncogenic ras proteins Science 247 1990 939 945
    • (1990) Science , vol.247 , pp. 939-945
    • Milburn, M.V1    Tong, L2    deVos, A.M3    Brunger, A4    Yamaizumi, Z5    Nishimura, S6    Kim, S.H7
  • 58
    • 0035920116 scopus 로고    scopus 로고
    • Structure-based mutagenesis reveals distinct functions for ras switch 1 and switch 2 in Sos-catalyzed guanine nucleotide exchange
    • B.E Hall S.S Yang P.A Boriack-Sjodin J Kuriyan D Bar-Sagi Structure-based mutagenesis reveals distinct functions for ras switch 1 and switch 2 in Sos-catalyzed guanine nucleotide exchange J. Biol. Chem. 276 2001 27,629 27,637
    • (2001) J. Biol. Chem. , vol.276
    • Hall, B.E1    Yang, S.S2    Boriack-Sjodin, P.A3    Kuriyan, J4    Bar-Sagi, D5
  • 59
    • 0343965776 scopus 로고    scopus 로고
    • Ras signalling. Caught in the act of the switch-on
    • F Wittinghofer Ras signalling. Caught in the act of the switch-on Nature 394 317 1998 319 320
    • (1998) Nature , vol.394 , Issue.317 , pp. 319-320
    • Wittinghofer, F1
  • 60
    • 0032104449 scopus 로고    scopus 로고
    • GEF-mediated GDP/GTP exchange by monomeric GTPases: A regulatory role for Mg2+?
    • 2+? Bioessays 20 1998 516 521
    • (1998) Bioessays , vol.20 , pp. 516-521
    • Pan, J.Y1    Wessling-Resnick, M2
  • 61
    • 0032546533 scopus 로고    scopus 로고
    • Kinetic analysis by fluorescence of the interaction between Ras and the catalytic domain of the guanine nucleotide exchange factor Cdc25Mm
    • C Lenzen R.H Cool H Prinz J Kuhlmann A Wittinghofer Kinetic analysis by fluorescence of the interaction between Ras and the catalytic domain of the guanine nucleotide exchange factor Cdc25Mm Biochemistry 37 1998 7420 7430
    • (1998) Biochemistry , vol.37 , pp. 7420-7430
    • Lenzen, C1    Cool, R.H2    Prinz, H3    Kuhlmann, J4    Wittinghofer, A5
  • 62
    • 0031724355 scopus 로고    scopus 로고
    • Distinct subclasses of small GTPases interact with guanine nucleotide exchange factors in a similar manner
    • G.J Day R.D Mosteller D Broek Distinct subclasses of small GTPases interact with guanine nucleotide exchange factors in a similar manner Mol. Cell. Biol. 18 1998 7444 7454
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 7444-7454
    • Day, G.J1    Mosteller, R.D2    Broek, D3
  • 63
    • 0034619877 scopus 로고    scopus 로고
    • Crystal structure of Racl in complex with the guanine nucleotide exchange region of Tiaml
    • D.K Worthylake K.L Rossman J Sondek Crystal structure of Racl in complex with the guanine nucleotide exchange region of Tiaml Nature 408 2000 682 688
    • (2000) Nature , vol.408 , pp. 682-688
    • Worthylake, D.K1    Rossman, K.L2    Sondek, J3
  • 64
    • 0032538317 scopus 로고    scopus 로고
    • Structural basis for activation of ARF GTPase: Mechanisms of guanine nucleotide exchange and GTP-myristoyl switching
    • J Goldberg Structural basis for activation of ARF GTPase: Mechanisms of guanine nucleotide exchange and GTP-myristoyl switching Cell 95 1998 237 248
    • (1998) Cell , vol.95 , pp. 237-248
    • Goldberg, J1
  • 65
    • 0031026133 scopus 로고    scopus 로고
    • Cloning and characterization of Ras-GRF2, a novel guanine nucleotide exchange factor for Ras
    • N.P Fam W.T Fan Z Wang L.J Zhang H Chen M.F Moran Cloning and characterization of Ras-GRF2, a novel guanine nucleotide exchange factor for Ras Mol. Cell. Biol. 17 1997 1396 1406
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1396-1406
    • Fam, N.P1    Fan, W.T2    Wang, Z3    Zhang, L.J4    Chen, H5    Moran, M.F6
  • 66
    • 0034634534 scopus 로고    scopus 로고
    • Identification of guanine nucleotide exchange factors (GEFs) for the rapl GTPase. Regulation of MR-GEF by M-Ras-GTP interaction
    • J.F Rebhun A.F Castro L.A Quilliam Identification of guanine nucleotide exchange factors (GEFs) for the rapl GTPase. Regulation of MR-GEF by M-Ras-GTP interaction J. Biol. Chem. 275 2000 34,901 34,908
    • (2000) J. Biol. Chem. , vol.275
    • Rebhun, J.F1    Castro, A.F2    Quilliam, L.A3
  • 67
    • 0003000807 scopus 로고    scopus 로고
    • Tools of the trade: Use of dominant-inhibitory mutants of ras-family GTPases
    • L.A Feig Tools of the trade: Use of dominant-inhibitory mutants of ras-family GTPases Nat. Cell Biol. 1 1999 E25 E27
    • (1999) Nat. Cell Biol. , vol.1 , pp. E25-E27
    • Feig, L.A1
  • 68
    • 0028122478 scopus 로고
    • Ras-15A protein shares highly similar dominant-negative biological properties with Ras-17N and forms a stable, guanine-nucleotide resistant complex with CDC25 exchange factor
    • S.Y Chen S.Y Huff C.C Lai C.J Der S Powers Ras-15A protein shares highly similar dominant-negative biological properties with Ras-17N and forms a stable, guanine-nucleotide resistant complex with CDC25 exchange factor Oncogene 9 1994 2691 2698
    • (1994) Oncogene , vol.9 , pp. 2691-2698
    • Chen, S.Y1    Huff, S.Y2    Lai, C.C3    Der, C.J4    Powers, S5
  • 72
    • 0034710567 scopus 로고    scopus 로고
    • The GTPase Rapl controls functional activation of macrophage integrin alphaMbeta2 by LPS and other inflammatory mediators
    • E Caron A.J Self A Hall The GTPase Rapl controls functional activation of macrophage integrin alphaMbeta2 by LPS and other inflammatory mediators Curr. Biol. 10 2000 974 978
    • (2000) Curr. Biol. , vol.10 , pp. 974-978
    • Caron, E1    Self, A.J2    Hall, A3
  • 73
    • 0030793873 scopus 로고    scopus 로고
    • Biochemical characterization of C3G: An exchange factor that discriminates between Rapl and Rapt and is not inhibited by Rap1A(S17N)
    • N van den Berghe R.H Cool G Hom A Wittinghofer Biochemical characterization of C3G: An exchange factor that discriminates between Rapl and Rapt and is not inhibited by Rap1A(S17N) Oncogene 15 1997 845 850
    • (1997) Oncogene , vol.15 , pp. 845-850
    • van den Berghe, N1    Cool, R.H2    Hom, G3    Wittinghofer, A4
  • 74
    • 0025883047 scopus 로고
    • Dominant inhibitory Ras mutants selectively inhibit the activity of either cellular or oncogenic Ras
    • D.W Stacey L.A Feig J.B Gibbs Dominant inhibitory Ras mutants selectively inhibit the activity of either cellular or oncogenic Ras Mol. Cell. Biol. 11 1991 4053 4064
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 4053-4064
    • Stacey, D.W1    Feig, L.A2    Gibbs, J.B3
  • 76
    • 0029931169 scopus 로고    scopus 로고
    • Ras-interacting domain of Ral GDP dissociation stimulator like (RGL) reverses v-Ras-induced transformation and Raf-1 activation in NIH3T3 cells
    • M Okazaki S Kishida H Murai T Hinoi A Kikuchi Ras-interacting domain of Ral GDP dissociation stimulator like (RGL) reverses v-Ras-induced transformation and Raf-1 activation in NIH3T3 cells Cancer Res. 56 1996 2387 2392
    • (1996) Cancer Res. , vol.56 , pp. 2387-2392
    • Okazaki, M1    Kishida, S2    Murai, H3    Hinoi, T4    Kikuchi, A5
  • 77
    • 0029156085 scopus 로고
    • Determination of guanine nucleotides bound to Ras in mammalian cells
    • J.B Gibbs Determination of guanine nucleotides bound to Ras in mammalian cells Methods Enzymol. 255 1995 118 125
    • (1995) Methods Enzymol. , vol.255 , pp. 118-125
    • Gibbs, J.B1
  • 78
    • 0028872684 scopus 로고
    • Determination of absolute amounts of GDP and GTP bound to Ras in mammalian cells: Comparison of parental and Ras-overproducing NIH 3T3 fibroblasts
    • J.S Scheele J.M Rhee G.R Boss Determination of absolute amounts of GDP and GTP bound to Ras in mammalian cells: Comparison of parental and Ras-overproducing NIH 3T3 fibroblasts Proc. Natl. Acad. Sci. U.S.A. 92 1995 1097 1100
    • (1995) , pp. 1097-1100
    • Scheele, J.S1    Rhee, J.M2    Boss, G.R3
  • 79
    • 0030461098 scopus 로고    scopus 로고
    • Cell cycle-dependent activation of Ras
    • S.J Taylor D Shalloway Cell cycle-dependent activation of Ras Curr. Biol. 6 1996 1621 1627
    • (1996) Curr. Biol. , vol.6 , pp. 1621-1627
    • Taylor, S.J1    Shalloway, D2
  • 80
    • 0031055415 scopus 로고    scopus 로고
    • Minimal Ras-binding domain of Raft can be used as an activationspecific probe for Ras
    • J de Rooij J.L Bos Minimal Ras-binding domain of Raft can be used as an activationspecific probe for Ras Oncogene 14 1997 623 625
    • (1997) Oncogene , vol.14 , pp. 623-625
    • de Rooij, J1    Bos, J.L2
  • 81
    • 0034981546 scopus 로고    scopus 로고
    • Measurement of GTP-bound Ras-like GTPases by activation-specific probes
    • M van Triest J de Rooij J.L Bos Measurement of GTP-bound Ras-like GTPases by activation-specific probes Methods Enzymol. 333 2001 343 348
    • (2001) Methods Enzymol. , vol.333 , pp. 343-348
    • van Triest, M1    de Rooij, J2    Bos, J.L3
  • 82
    • 0034985396 scopus 로고    scopus 로고
    • Nonradioactive determination of Ras-GTP levels using activated ras interaction assay
    • S.J Taylor R.J Resnick D Shalloway Nonradioactive determination of Ras-GTP levels using activated ras interaction assay Methods Enzymol. 333 2001 333 342
    • (2001) Methods Enzymol. , vol.333 , pp. 333-342
    • Taylor, S.J1    Resnick, R.J2    Shalloway, D3
  • 83
    • 0032578560 scopus 로고    scopus 로고
    • Structure determination of the Ras-binding domain of the Ral-specific guanine nucleotide exchange factor Rlf
    • D Esser B Bauer R.M Wolthuis A Wittinghofer R.H Cool P Bayer Structure determination of the Ras-binding domain of the Ral-specific guanine nucleotide exchange factor Rlf Biochemistry 37 1998 13,453 13,462
    • (1998) Biochemistry , vol.37
    • Esser, D1    Bauer, B2    Wolthuis, R.M3    Wittinghofer, A4    Cool, R.H5    Bayer, P6
  • 88
  • 90
    • 0030666849 scopus 로고    scopus 로고
    • The Ras-specific exchange factors mouse Sosl (mSos1) and mSos2 are regulated differently: mSos2 contains ubiquitination signals absent in mSosl
    • K.H Nielsen A.G Papageorge W.C Vass B.M Willumsen D.R Lowy The Ras-specific exchange factors mouse Sosl (mSos1) and mSos2 are regulated differently: mSos2 contains ubiquitination signals absent in mSosl Mol. Cell. Biol. 17 1997 7132 7138
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 7132-7138
    • Nielsen, K.H1    Papageorge, A.G2    Vass, W.C3    Willumsen, B.M4    Lowy, D.R5
  • 92
    • 0027910431 scopus 로고
    • Association of Sos Ras exchange protein with Grb2 is implicated in tyrosine kinase signal transduction and transformation
    • S.E Egan B.W Giddings M.W Brooks L Buday A.M Sizeland R.A Weinberg Association of Sos Ras exchange protein with Grb2 is implicated in tyrosine kinase signal transduction and transformation Nature 363 1993 45 51
    • (1993) Nature , vol.363 , pp. 45-51
    • Egan, S.E1    Giddings, B.W2    Brooks, M.W3    Buday, L4    Sizeland, A.M5    Weinberg, R.A6
  • 93
    • 0027153103 scopus 로고
    • Epidermal growth factor regulates p21ras through the formation of a complex of receptor, Grb2 adapter protein, and Sos nucleotide exchange factor
    • L Buday J Downward Epidermal growth factor regulates p21ras through the formation of a complex of receptor, Grb2 adapter protein, and Sos nucleotide exchange factor Cell 73 1993 611 620
    • (1993) Cell , vol.73 , pp. 611-620
    • Buday, L1    Downward, J2
  • 94
    • 0027229556 scopus 로고
    • Grb2 mediates the EGF-dependent activation of guanine nucleotide exchange on Ras
    • N.W Gale S Kaplan E.J Lowenstein J Schlessinger D Bar-Sagi Grb2 mediates the EGF-dependent activation of guanine nucleotide exchange on Ras Nature 363 1993 88 92
    • (1993) Nature , vol.363 , pp. 88-92
    • Gale, N.W1    Kaplan, S2    Lowenstein, E.J3    Schlessinger, J4    Bar-Sagi, D5
  • 96
    • 0027422247 scopus 로고
    • The pathway to signal achievement [news]
    • S.E Egan R.A Weinberg The pathway to signal achievement [news] Nature 365 1993 781 783
    • (1993) Nature , vol.365 , pp. 781-783
    • Egan, S.E1    Weinberg, R.A2
  • 97
    • 0029791452 scopus 로고    scopus 로고
    • Identification of the mitogen-activated protein kinase phosphorylation sites on human Sosl that regulate interaction with Grb2
    • S Corbalan-Garcia S.S Yang K.R Degenhardt D Bar-Sagi Identification of the mitogen-activated protein kinase phosphorylation sites on human Sosl that regulate interaction with Grb2 Mol. Cell. Biol. 16 1996 5674 5682
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5674-5682
    • Corbalan-Garcia, S1    Yang, S.S2    Degenhardt, K.R3    Bar-Sagi, D4
  • 99
    • 0030028790 scopus 로고    scopus 로고
    • A Grb2-associated docking protein in EGF- and insulin-receptor signalling
    • M Holgado-Madruga D.R Emlet D.K Moscatello A.K Godwin A.J Wong A Grb2-associated docking protein in EGF- and insulin-receptor signalling Nature 379 1996 560 564
    • (1996) Nature , vol.379 , pp. 560-564
    • Holgado-Madruga, M1    Emlet, D.R2    Moscatello, D.K3    Godwin, A.K4    Wong, A.J5
  • 101
    • 0027279176 scopus 로고
    • How receptor tyrosine kinases activate Ras
    • J Schlessinger How receptor tyrosine kinases activate Ras Trends Biochem. Sci. 18 1993 273 275
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 273-275
    • Schlessinger, J1
  • 102
    • 0030464110 scopus 로고    scopus 로고
    • Signal transduction from the extracellular matrix-a role for the focal adhesion protein-tyrosine kinase FAK
    • D.D Schlaepfer T Hunter Signal transduction from the extracellular matrix-a role for the focal adhesion protein-tyrosine kinase FAK Cell Structure Function 21 1996 445 450
    • (1996) Cell Structure Function , vol.21 , pp. 445-450
    • Schlaepfer, D.D1    Hunter, T2
  • 103
    • 0029907265 scopus 로고    scopus 로고
    • A role for Pyk2 and Src in linking G-protein-coupled receptors with MAP kinase activation
    • I Dikic G Tokiwa S Lev S.A Courtneidge J Schlessinger A role for Pyk2 and Src in linking G-protein-coupled receptors with MAP kinase activation Nature 383 1996 547 550
    • (1996) Nature , vol.383 , pp. 547-550
    • Dikic, I1    Tokiwa, G2    Lev, S3    Courtneidge, S.A4    Schlessinger, J5
  • 104
    • 0035952645 scopus 로고    scopus 로고
    • New mechanisms in heptahelical receptor signaling to mitogen activated protein kinase cascades
    • K.L Pierce L.M Luttrell R.J Lefkowitz New mechanisms in heptahelical receptor signaling to mitogen activated protein kinase cascades Oncogene 20 2001 1532 1539
    • (2001) Oncogene , vol.20 , pp. 1532-1539
    • Pierce, K.L1    Luttrell, L.M2    Lefkowitz, R.J3
  • 105
    • 0028122345 scopus 로고
    • Prenylation of Ras proteins is required for efficient hSOSI-promoted guanine nucleotide exchange
    • E Porfiri T Evans P Chardin J.F Hancock Prenylation of Ras proteins is required for efficient hSOSI-promoted guanine nucleotide exchange J. Biol. Chem. 269 1994 22672 22677
    • (1994) J. Biol. Chem. , vol.269 , pp. 22672-22677
    • Porfiri, E1    Evans, T2    Chardin, P3    Hancock, J.F4
  • 106
    • 0027999033 scopus 로고
    • Membrane-targeting potentiates guanine nucleotide exchange factor CDC25 and SOS1 activation of Ras transforming activity
    • L.A Quilliam S.Y Huff K.M Rabun W Wei W Park D Broek C.J Der Membrane-targeting potentiates guanine nucleotide exchange factor CDC25 and SOS1 activation of Ras transforming activity Proc. Natl. Acad. Sci. U.S.A. 91 1994 8512 8516
    • (1994) , pp. 8512-8516
    • Quilliam, L.A1    Huff, S.Y2    Rabun, K.M3    Wei, W4    Park, W5    Broek, D6    Der, C.J7
  • 107
    • 0027931640 scopus 로고
    • Membrane targeting of the nucleotide exchange factor Sos is sufficient for activating the Ras signaling pathway
    • A Aronheim D Engelberg N Li N al-Alawi J Schlessinger M Karin Membrane targeting of the nucleotide exchange factor Sos is sufficient for activating the Ras signaling pathway Cell 78 1994 949 961
    • (1994) Cell , vol.78 , pp. 949-961
    • Aronheim, A1    Engelberg, D2    Li, N3    al-Alawi, N4    Schlessinger, J5    Karin, M6
  • 108
    • 0028832658 scopus 로고
    • Signal transduction in T lymphocytes using a conditional allele of Sos
    • L.J Holsinger D.M Spencer D.J Austin S.L Schreiber G.R Crabtree Signal transduction in T lymphocytes using a conditional allele of Sos Proc. Natl. Acad. Sci. U.S.A. 92 1995 9810 9814
    • (1995) , pp. 9810-9814
    • Holsinger, L.J1    Spencer, D.M2    Austin, D.J3    Schreiber, S.L4    Crabtree, G.R5
  • 109
    • 0029031112 scopus 로고
    • The Grb2 binding domain of mSosl is not required for downstream signal transduction
    • W Wang E.M Fisher Q Jia J.M Dunn E Porfiri J Downward S.E Egan The Grb2 binding domain of mSosl is not required for downstream signal transduction Nat. Genet. 10 1995 294 300
    • (1995) Nat. Genet. , vol.10 , pp. 294-300
    • Wang, W1    Fisher, E.M2    Jia, Q3    Dunn, J.M4    Porfiri, E5    Downward, J6    Egan, S.E7
  • 111
    • 0031929680 scopus 로고    scopus 로고
    • N terminus of Sosl Ras exchange factor: critical roles for the Dbl and pleckstrin homology domains
    • X Qian W.C Vass A.G Papageorge P.H Anborgh D.R Lowy N terminus of Sosl Ras exchange factor: critical roles for the Dbl and pleckstrin homology domains Mol. Cell. Biol. 18 1998 771 778
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 771-778
    • Qian, X1    Vass, W.C2    Papageorge, A.G3    Anborgh, P.H4    Lowy, D.R5
  • 112
    • 0031002348 scopus 로고    scopus 로고
    • The role of the PH domain in the signal-dependent membrane targeting of Sos
    • R.H Chen S Corbalan-Garcia D Bar-Sagi The role of the PH domain in the signal-dependent membrane targeting of Sos EMBO J. 16 1997 1351 1359
    • (1997) EMBO J. , vol.16 , pp. 1351-1359
    • Chen, R.H1    Corbalan-Garcia, S2    Bar-Sagi, D3
  • 113
    • 0032493134 scopus 로고    scopus 로고
    • Inhibition of mSOS-activity by binding of phosphatidylinositol 4,5-P2 to the mSOS pleckstrin homology domain
    • A.B Jefferson A Klippel L.T Williams Inhibition of mSOS-activity by binding of phosphatidylinositol 4,5-P2 to the mSOS pleckstrin homology domain Oncogene 16 1998 2303 2310
    • (1998) Oncogene , vol.16 , pp. 2303-2310
    • Jefferson, A.B1    Klippel, A2    Williams, L.T3
  • 114
    • 0032559211 scopus 로고    scopus 로고
    • Coupling of Ras and Rae guanosine triphosphatases through the Ras exchanger Sos
    • A.S Nimnual B.A Yatsula D Bar-Sagi Coupling of Ras and Rae guanosine triphosphatases through the Ras exchanger Sos Science 279 1998 560 563
    • (1998) Science , vol.279 , pp. 560-563
    • Nimnual, A.S1    Yatsula, B.A2    Bar-Sagi, D3
  • 116
    • 15144353776 scopus 로고    scopus 로고
    • Role of substrates and products of PI 3-kinase in regulating activation of Rac-related guanosine triphosphatases by Vav
    • J Han K Luby-Phelps B Das X Shu Y Xia R.D Mosteller U.M Krishna J.R Falck M.A White D Broek Role of substrates and products of PI 3-kinase in regulating activation of Rac-related guanosine triphosphatases by Vav Science 279 1998 558 560
    • (1998) Science , vol.279 , pp. 558-560
    • Han, J1    Luby-Phelps, K2    Das, B3    Shu, X4    Xia, Y5    Mosteller, R.D6    Krishna, U.M7    Falck, J.R8    White, M.A9    Broek, D10
  • 117
    • 0032538316 scopus 로고    scopus 로고
    • Crystal structure of the Dbl and pleckstrin homology domains from the human Son of sevenless protein
    • S.M Soisson A.S Nimnual M Uy J Bar-Sagi J Kuriyan Crystal structure of the Dbl and pleckstrin homology domains from the human Son of sevenless protein Cell 95 1998 259 268
    • (1998) Cell , vol.95 , pp. 259-268
    • Soisson, S.M1    Nimnual, A.S2    Uy, M3    Bar-Sagi, J4    Kuriyan, J5
  • 119
    • 0035802118 scopus 로고    scopus 로고
    • An effector region in Eps8 is responsible for the activation of the Rac-specific GEF activity of Sos-1 and for the proper localization of the Rac-based actin-polymerizing machine
    • G Scita P Tenca L.B Areces A Tocchetti E Frittoli G Giardina I Ponzanelli P Sini M Innocenti P.P Di Fiore An effector region in Eps8 is responsible for the activation of the Rac-specific GEF activity of Sos-1 and for the proper localization of the Rac-based actin-polymerizing machine J. Cell. Biol. 154 2001 1031 1044
    • (2001) J. Cell. Biol. , vol.154 , pp. 1031-1044
    • Scita, G1    Tenca, P2    Areces, L.B3    Tocchetti, A4    Frittoli, E5    Giardina, G6    Ponzanelli, I7    Sini, P8    Innocenti, M9    Di Fiore, P.P10
  • 120
    • 0027365376 scopus 로고
    • A murine CDC25/ras-GRF-related protein implicated in Ras regulation
    • L Chen L.J Zhang P Greer P.S Tung M.F Moran A murine CDC25/ras-GRF-related protein implicated in Ras regulation Dev. Genet. 14 1993 339 346
    • (1993) Dev. Genet. , vol.14 , pp. 339-346
    • Chen, L1    Zhang, L.J2    Greer, P3    Tung, P.S4    Moran, M.F5
  • 121
    • 0027367141 scopus 로고
    • Regulated and constitutive activity by CDC25Mm (GRF), a Ras-specific exchange factor
    • H Cen A.G Papageorge W.C Vass K.E Zhang D.R Lowy Regulated and constitutive activity by CDC25Mm (GRF), a Ras-specific exchange factor Mol. Cell. Biol. 13 1993 7718 7724
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 7718-7724
    • Cen, H1    Papageorge, A.G2    Vass, W.C3    Zhang, K.E4    Lowy, D.R5
  • 122
  • 123
    • 0031917171 scopus 로고    scopus 로고
    • Ras-GRF activates Ha-Ras, but not N-Ras or K-Ras 4B, protein in vivo
    • M.K Jones J.H Jackson Ras-GRF activates Ha-Ras, but not N-Ras or K-Ras 4B, protein in vivo J. Biol. Chem. 273 1998 1782 1787
    • (1998) J. Biol. Chem. , vol.273 , pp. 1782-1787
    • Jones, M.K1    Jackson, J.H2
  • 124
    • 0035912081 scopus 로고    scopus 로고
    • Sensitivity of wild type and mutant ras alleles to Ras specific exchange factors: Identification of factor specific requirements
    • K.H Nielsen L Gredsted J.R Broach B.M Willumsen Sensitivity of wild type and mutant ras alleles to Ras specific exchange factors: Identification of factor specific requirements Oncogene 20 2001 2091 2100
    • (2001) Oncogene , vol.20 , pp. 2091-2100
    • Nielsen, K.H1    Gredsted, L2    Broach, J.R3    Willumsen, B.M4
  • 126
    • 0033588299 scopus 로고    scopus 로고
    • M-Ras/R-Ras3, a novel transforming Ras protein regulated by Sosl and p120 GAP, interacts with the putative Ras effector AF6
    • L.A Quilliam K.R Graham A.F Castro C.B Martin C.J Der C Bi M-Ras/R-Ras3, a novel transforming Ras protein regulated by Sosl and p120 GAP, interacts with the putative Ras effector AF6 J. Biol. Chem. 274 1999 23,850 23,857
    • (1999) J. Biol. Chem. , vol.274
    • Quilliam, L.A1    Graham, K.R2    Castro, A.F3    Martin, C.B4    Der, C.J5    Bi, C6
  • 127
    • 0035861736 scopus 로고    scopus 로고
    • Prenylation of target GTPases contributes to signaling specificity of Ras-guanine nucleotide exchange factors
    • T Gotoh X Tian L.A Feig Prenylation of target GTPases contributes to signaling specificity of Ras-guanine nucleotide exchange factors J. Biol. Chem. 276 2001 in press
    • (2001) J. Biol. Chem. , vol.276
    • Gotoh, T1    Tian, X2    Feig, L.A3
  • 128
    • 13144250140 scopus 로고    scopus 로고
    • The exchange factor Ras-GRF2 activates Ras-dependent and Rac-dependent mitogen-activated protein kinase pathways
    • W.T Fan C.A Koch C.L de Hoog N.P Fam M.F Moran The exchange factor Ras-GRF2 activates Ras-dependent and Rac-dependent mitogen-activated protein kinase pathways Curr. Biol. 8 1998 935 938
    • (1998) Curr. Biol. , vol.8 , pp. 935-938
    • Fan, W.T1    Koch, C.A2    de Hoog, C.L3    Fam, N.P4    Moran, M.F5
  • 129
    • 0029742101 scopus 로고    scopus 로고
    • The N-terminal pleckstrin, coiledcoil, and IQ domains of the exchange factor Ras-GRF act cooperatively to facilitate activation by calcium
    • R Buchsbaum J.B Telliez S Goonesekera L.A Feig The N-terminal pleckstrin, coiledcoil, and IQ domains of the exchange factor Ras-GRF act cooperatively to facilitate activation by calcium Mol. Cell. Biol. 16 1996 4888 4896
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4888-4896
    • Buchsbaum, R1    Telliez, J.B2    Goonesekera, S3    Feig, L.A4
  • 132
    • 0031582212 scopus 로고    scopus 로고
    • Activation of the exchange factor Ras-GRF by calcium requires an intact Dbl homology domain
    • N.W Freshney S.D Goonesekera L.A Feig Activation of the exchange factor Ras-GRF by calcium requires an intact Dbl homology domain FEBS Lett 407 1997 111 115
    • (1997) FEBS Lett , vol.407 , pp. 111-115
    • Freshney, N.W1    Goonesekera, S.D2    Feig, L.A3
  • 133
    • 0033002199 scopus 로고    scopus 로고
    • Ras-specific exchange factor GAF: Oligomerization through its Dbl homology domain and calcium-dependent activation of Raf
    • P.H Anborgh X Qian A.G Papageorge W.C Vass J.E DeClue D.R Lowy Ras-specific exchange factor GAF: Oligomerization through its Dbl homology domain and calcium-dependent activation of Raf Mol. Cell. Biol. 19 1999 4611 4622
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4611-4622
    • Anborgh, P.H1    Qian, X2    Papageorge, A.G3    Vass, W.C4    DeClue, J.E5    Lowy, D.R6
  • 134
    • 0034624783 scopus 로고    scopus 로고
    • Regulation of the protein kinase Raf-1 by oncogenic Ras through phosphatidylinositol 3-kinase, Cdc42/Rac and Pak
    • H Sun A.J King H.B Diaz M.S Marshall Regulation of the protein kinase Raf-1 by oncogenic Ras through phosphatidylinositol 3-kinase, Cdc42/Rac and Pak Curr. Biol. 10 2000 281 284
    • (2000) Curr. Biol. , vol.10 , pp. 281-284
    • Sun, H1    King, A.J2    Diaz, H.B3    Marshall, M.S4
  • 135
    • 0035173480 scopus 로고    scopus 로고
    • Oligomerization of DH domain is essential for Dbl-induced transformation
    • K Zhu B Debreceni F Bi Y Zheng Oligomerization of DH domain is essential for Dbl-induced transformation Mol. Cell. Biol. 21 2001 425 437
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 425-437
    • Zhu, K1    Debreceni, B2    Bi, F3    Zheng, Y4
  • 136
    • 0030855008 scopus 로고    scopus 로고
    • Dimerization of Cdc25p, the guanine-nucleotide exchange factor for Ras from Saccharomyces cerevisiae, and its interaction with Sdc25p
    • C Camus M Geymonat H Garreau S Baudet-Nessler M Jacquet Dimerization of Cdc25p, the guanine-nucleotide exchange factor for Ras from Saccharomyces cerevisiae, and its interaction with Sdc25p Eur. J. Biochem. 247 1997 703 708
    • (1997) Eur. J. Biochem. , vol.247 , pp. 703-708
    • Camus, C1    Geymonat, M2    Garreau, H3    Baudet-Nessler, S4    Jacquet, M5
  • 137
    • 0029017628 scopus 로고
    • Differential response of the Ras exchange factor, Ras-GRF to tyrosine kinase and G protein mediated signals
    • C Shou A Wurmser K.L Suen M Barbacid L.A Feig K Ling Differential response of the Ras exchange factor, Ras-GRF to tyrosine kinase and G protein mediated signals Oncogene 10 1995 1887 1893
    • (1995) Oncogene , vol.10 , pp. 1887-1893
    • Shou, C1    Wurmser, A2    Suen, K.L3    Barbacid, M4    Feig, L.A5    Ling, K6
  • 138
    • 0033057582 scopus 로고    scopus 로고
    • Activation of the Ras-GRF/CDC25Mm exchange factor by lysophosphatidic acid
    • R.R Mattingly V Saini I.G Macara Activation of the Ras-GRF/CDC25Mm exchange factor by lysophosphatidic acid Cell Signal 11 1999 603 610
    • (1999) Cell Signal , vol.11 , pp. 603-610
    • Mattingly, R.R1    Saini, V2    Macara, I.G3
  • 139
    • 0033601374 scopus 로고    scopus 로고
    • Phosphorylation of serine 916 of Ras-GRF1 contributes to the activation of exchange factor activity by muscarinic receptors
    • R.R Mattingly Phosphorylation of serine 916 of Ras-GRF1 contributes to the activation of exchange factor activity by muscarinic receptors J. Biol. Chem. 274 1999 37379 37384
    • (1999) J. Biol. Chem. , vol.274 , pp. 37379-37384
    • Mattingly, R.R1
  • 141
    • 0034192402 scopus 로고    scopus 로고
    • The guanine nucleotide exchange factor CNrasGEF activates ras in response to CAMP and cGMP [In Process Citation]
    • N Pham I Cheglakov C.A Koch C.L de Hoog M.F Moran D Rotin The guanine nucleotide exchange factor CNrasGEF activates ras in response to CAMP and cGMP [In Process Citation] Curr Biol. 10 2000 555 558
    • (2000) Curr Biol. , vol.10 , pp. 555-558
    • Pham, N1    Cheglakov, I2    Koch, C.A3    de Hoog, C.L4    Moran, M.F5    Rotin, D6
  • 142
    • 0035914321 scopus 로고    scopus 로고
    • Cloning and characterization of mouse-UBPy, a deubiquitinating enzyme that interacts with the Ras guanine nucleotide exchange factor CDC25 Mm/RasGRFl
    • N Gnesutta M Ceriani M Innocenti I Mauri R Zippel E Sturani B Borgonovo G Berruti E Martegani Cloning and characterization of mouse-UBPy, a deubiquitinating enzyme that interacts with the Ras guanine nucleotide exchange factor CDC25 Mm/RasGRFl J. Biol. Chem. 276 2001 39,448 39,454
    • (2001) J. Biol. Chem. , vol.276
    • Gnesutta, N1    Ceriani, M2    Innocenti, M3    Mauri, I4    Zippel, R5    Sturani, E6    Borgonovo, B7    Berruti, G8    Martegani, E9
  • 150
    • 0032524389 scopus 로고    scopus 로고
    • RasGRP a Ras guanyl nucleotide-releasing protein with calcium- and diacylglycerol-binding motifs
    • J.O Ebinu D.A Bottorff E.Y Chan S.L Stang R.J Dunn J.C Stone RasGRP a Ras guanyl nucleotide-releasing protein with calcium- and diacylglycerol-binding motifs Science 280 1998 1082 1086
    • (1998) Science , vol.280 , pp. 1082-1086
    • Ebinu, J.O1    Bottorff, D.A2    Chan, E.Y3    Stang, S.L4    Dunn, R.J5    Stone, J.C6
  • 152
    • 0034025493 scopus 로고    scopus 로고
    • Eyes wide shut: Protein kinase C isozymes are not the only receptors for the phorbol ester tumor promoters
    • M.G Kazanietz Eyes wide shut: Protein kinase C isozymes are not the only receptors for the phorbol ester tumor promoters Mol. Carcinog. 28 2000 5 11
    • (2000) Mol. Carcinog. , vol.28 , pp. 5-11
    • Kazanietz, M.G1
  • 153
    • 0034061660 scopus 로고    scopus 로고
    • The guanine nucleotide exchange factor RasGRP is a high-affinity target for diacylglycerol and phorbol esters
    • P.S Lorenzo M Beheshti G.R Pettit J.C Stone P.M Blumberg The guanine nucleotide exchange factor RasGRP is a high-affinity target for diacylglycerol and phorbol esters Mol. Pharmacol. 57 2000 840 846
    • (2000) Mol. Pharmacol. , vol.57 , pp. 840-846
    • Lorenzo, P.S1    Beheshti, M2    Pettit, G.R3    Stone, J.C4    Blumberg, P.M5
  • 154
    • 0034465901 scopus 로고    scopus 로고
    • Distribution of ras guanyl releasing protein (RasGRP) mRNA in the adult rat central nervous system
    • P Pierret R.J Dunn B Djordjevic J.C Stone P.M Richardson Distribution of ras guanyl releasing protein (RasGRP) mRNA in the adult rat central nervous system J Neurocytol 29 2000 485 497
    • (2000) J Neurocytol , vol.29 , pp. 485-497
    • Pierret, P1    Dunn, R.J2    Djordjevic, B3    Stone, J.C4    Richardson, P.M5
  • 156
    • 0035911971 scopus 로고    scopus 로고
    • Diacylglycerol kinase zeta regulates Ras activation by a novel mechanism
    • M.K Topham S.M Prescott Diacylglycerol kinase zeta regulates Ras activation by a novel mechanism J. Cell. Biol. 152 2001 1135 1143
    • (2001) J. Cell. Biol. , vol.152 , pp. 1135-1143
    • Topham, M.K1    Prescott, S.M2
  • 158
    • 0035801950 scopus 로고    scopus 로고
    • Guanine nucleotide exchange factors CaIDAG-GEFI and CalDAG-GEFII are colocalized in striatal projection neurons
    • S Told H Kawasaki N Tashiro D.E Housman A.M Graybiel Guanine nucleotide exchange factors CaIDAG-GEFI and CalDAG-GEFII are colocalized in striatal projection neurons J. Comp. Neurol. 437 2001 398 407
    • (2001) J. Comp. Neurol. , vol.437 , pp. 398-407
    • Told, S1    Kawasaki, H2    Tashiro, N3    Housman, D.E4    Graybiel, A.M5
  • 159
    • 0032894068 scopus 로고    scopus 로고
    • HUGE: A database for human large proteins identified by Kazusa cDNA sequencing project
    • M Suyama T Nagase O Ohara HUGE: A database for human large proteins identified by Kazusa cDNA sequencing project Nucleic Acids Res. 27 1999 338 339
    • (1999) Nucleic Acids Res. , vol.27 , pp. 338-339
    • Suyama, M1    Nagase, T2    Ohara, O3
  • 160
    • 0031588576 scopus 로고    scopus 로고
    • Construction and characterization of human brain cDNA libraries suitable for analysis of cDNA clones encoding relatively large proteins
    • O Ohara T Nagase K Ishikawa D Nakajima M Ohira N Seki N Nomura Construction and characterization of human brain cDNA libraries suitable for analysis of cDNA clones encoding relatively large proteins DNA Res. 4 1997 53 59
    • (1997) DNA Res. , vol.4 , pp. 53-59
    • Ohara, O1    Nagase, T2    Ishikawa, K3    Nakajima, D4    Ohira, M5    Seki, N6    Nomura, N7
  • 161
    • 0033679909 scopus 로고    scopus 로고
    • GRASP-1: A neuronal RasGEF associated with the AMPA receptor/GRIP complex
    • B Ye D Liao X Zhang P Zhang H Dong R.L Huganir GRASP-1: A neuronal RasGEF associated with the AMPA receptor/GRIP complex Neuron 26 2000 603 617
    • (2000) Neuron , vol.26 , pp. 603-617
    • Ye, B1    Liao, D2    Zhang, X3    Zhang, P4    Dong, H5    Huganir, R.L6
  • 163
    • 2442765369 scopus 로고    scopus 로고
    • Identification of a novel splice variant of C3G which shows tissue-specific expression
    • Shivakrupa R Singh G Swarup Identification of a novel splice variant of C3G which shows tissue-specific expression DNA Cell. Biol. 18 1999 701 708
    • (1999) DNA Cell. Biol. , vol.18 , pp. 701-708
    • Singh, Shivakrupa R1    Swarup, G2
  • 164
    • 0032475982 scopus 로고    scopus 로고
    • Direct binding of p130(Cas) to the guanine nucleotide exchange factor C3G
    • K.H Kirsch M.M Georgescu H Hanafusa Direct binding of p130(Cas) to the guanine nucleotide exchange factor C3G J. Biol. Chem. 273 1998 25673 25679
    • (1998) J. Biol. Chem. , vol.273 , pp. 25673-25679
    • Kirsch, K.H1    Georgescu, M.M2    Hanafusa, H3
  • 166
    • 0032080085 scopus 로고    scopus 로고
    • Insulin regulates the dynamic balance between Ras and Rapl signaling by coordinating the assembly states of the Grb2-SOS and CrkII-C3G complexes
    • S Okada M Matsuda M Anafi T Pawson J.E Pessin Insulin regulates the dynamic balance between Ras and Rapl signaling by coordinating the assembly states of the Grb2-SOS and CrkII-C3G complexes EMBO J. 17 1998 2554 2565
    • (1998) EMBO J. , vol.17 , pp. 2554-2565
    • Okada, S1    Matsuda, M2    Anafi, M3    Pawson, T4    Pessin, J.E5
  • 168
    • 0032510263 scopus 로고    scopus 로고
    • Identification of Tyr-762 in the platelet-derived growth factor alpha-receptor as the binding site for Crk proteins
    • K Yokote U Hellman S Ekman Y Saito L Ronnstrand C.H Heldin S Mori Identification of Tyr-762 in the platelet-derived growth factor alpha-receptor as the binding site for Crk proteins Oncogene 16 1998 1229 1239
    • (1998) Oncogene , vol.16 , pp. 1229-1239
    • Yokote, K1    Hellman, U2    Ekman, S3    Saito, Y4    Ronnstrand, L5    Heldin, C.H6    Mori, S7
  • 169
    • 0033520278 scopus 로고    scopus 로고
    • Fibroblast growth factor receptor- lmediated endothelial cell proliferation is dependent on the Src homology (SH) 2/SH3 domain-containing adaptor protein Crk
    • H Larsson P Klint E Landgren L Claesson-Welsh Fibroblast growth factor receptor- lmediated endothelial cell proliferation is dependent on the Src homology (SH) 2/SH3 domain-containing adaptor protein Crk J. Biol. Chem. 274 1999 25726 25734
    • (1999) J. Biol. Chem. , vol.274 , pp. 25726-25734
    • Larsson, H1    Klint, P2    Landgren, E3    Claesson-Welsh, L4
  • 171
    • 0034646610 scopus 로고    scopus 로고
    • Signaling of hepatocyte growth factor/scatter factor (HGF) to the small GTPase Rapl via the large docking protein Gab1 and the adapter protein CRKL
    • D Sakkab M Lewitzky G Posern U Schaeper M Sachs W Birchmeier S.M Feller Signaling of hepatocyte growth factor/scatter factor (HGF) to the small GTPase Rapl via the large docking protein Gab1 and the adapter protein CRKL J. Biol. Chem. 275 2000 10772 10778
    • (2000) J. Biol. Chem. , vol.275 , pp. 10772-10778
    • Sakkab, D1    Lewitzky, M2    Posern, G3    Schaeper, U4    Sachs, M5    Birchmeier, W6    Feller, S.M7
  • 172
    • 0034693268 scopus 로고    scopus 로고
    • Engagement of the CrkL adapter in interleukin-5 signaling in eosinophils
    • J Du Y.M Alsayed F Xin S.J Ackerman L.C Platanias Engagement of the CrkL adapter in interleukin-5 signaling in eosinophils J. Biol. Chem. 275 2000 33167 33175
    • (2000) J. Biol. Chem. , vol.275 , pp. 33167-33175
    • Du, J1    Alsayed, Y.M2    Xin, F3    Ackerman, S.J4    Platanias, L.C5
  • 173
    • 0034649516 scopus 로고    scopus 로고
    • The Crk signaling pathway contributes to the bombesin-induced activation of the small GTPase Rapl in Swiss 3T3 cells
    • G Posern U.R Rapp S.M Feller The Crk signaling pathway contributes to the bombesin-induced activation of the small GTPase Rapl in Swiss 3T3 cells Oncogene 19 2000 6361 6368
    • (2000) Oncogene , vol.19 , pp. 6361-6368
    • Posern, G1    Rapp, U.R2    Feller, S.M3
  • 174
    • 0035947724 scopus 로고    scopus 로고
    • Identification of the mechanisms regulating the differential activation of the mapk cascade by epidermal growth factor and nerve growth factor in PC 12 cells
    • S Kao R.K Jaiswal W Kolch G.E Landreth Identification of the mechanisms regulating the differential activation of the mapk cascade by epidermal growth factor and nerve growth factor in PC 12 cells J. Biol. Chem. 276 2001 18169 18177
    • (2001) J. Biol. Chem. , vol.276 , pp. 18169-18177
    • Kao, S1    Jaiswal, R.K2    Kolch, W3    Landreth, G.E4
  • 175
    • 0033569897 scopus 로고    scopus 로고
    • CrkL mediates Ras-dependent activation of the Raf/ERK pathway through the guanine nucleotide exchange factor C3G in hematopoietic cells stimulated with erythropoietin or interleukin-3
    • Y Nosaka A Arai N Miyasaka O Miura CrkL mediates Ras-dependent activation of the Raf/ERK pathway through the guanine nucleotide exchange factor C3G in hematopoietic cells stimulated with erythropoietin or interleukin-3 J. Biol. Chem. 274 1999 30154 30162
    • (1999) J. Biol. Chem. , vol.274 , pp. 30154-30162
    • Nosaka, Y1    Arai, A2    Miyasaka, N3    Miura, O4
  • 176
    • 0032569839 scopus 로고    scopus 로고
    • C3G is tyrosine-phosphorylated after integrin-mediated cell adhesion in normal but not in Bcr/Abl expressing cells
    • R de Jong A van Wijk N Heisterkamp J Groffen C3G is tyrosine-phosphorylated after integrin-mediated cell adhesion in normal but not in Bcr/Abl expressing cells Oncogene 17 1998 2805 2810
    • (1998) Oncogene , vol.17 , pp. 2805-2810
    • de Jong, R1    van Wijk, A2    Heisterkamp, N3    Groffen, J4
  • 177
    • 0029664531 scopus 로고    scopus 로고
    • Introduction of p130cas signaling complex formation upon integrin-mediated cell adhesion: A role for Src family kinases
    • K Vuori H Hirai S Aizawa E Ruoslahti Introduction of p130cas signaling complex formation upon integrin-mediated cell adhesion: A role for Src family kinases Mol. Cell. Biol. 16 1996 2606 2613
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 2606-2613
    • Vuori, K1    Hirai, H2    Aizawa, S3    Ruoslahti, E4
  • 178
    • 0033152359 scopus 로고    scopus 로고
    • CrkL activates integrin-mediated hematopoietic cell adhesion through the guanine nucleotide exchange factor C3G
    • A Arai Y Nosaka H Kohsaka N Miyasaka O Miura CrkL activates integrin-mediated hematopoietic cell adhesion through the guanine nucleotide exchange factor C3G Blood 93 1999 3713 3722
    • (1999) Blood , vol.93 , pp. 3713-3722
    • Arai, A1    Nosaka, Y2    Kohsaka, H3    Miyasaka, N4    Miura, O5
  • 179
    • 0033621446 scopus 로고    scopus 로고
    • The adapter protein Crkl links Cbl to C3G after integrin ligation and enhances cell migration
    • N Uemura J.D Griffin The adapter protein Crkl links Cbl to C3G after integrin ligation and enhances cell migration J. Biol. Chem. 274 1999 37525 37532
    • (1999) J. Biol. Chem. , vol.274 , pp. 37525-37532
    • Uemura, N1    Griffin, J.D2
  • 180
    • 0034724873 scopus 로고    scopus 로고
    • The association of CRKII with c3g can be regulated by integrins and defines a novel means to regulate the mitogen-activated protein kinases
    • C.S Buensuceso T.E O'Toole The association of CRKII with c3g can be regulated by integrins and defines a novel means to regulate the mitogen-activated protein kinases J. Biol. Chem. 275 2000 13118 13125
    • (2000) J. Biol. Chem. , vol.275 , pp. 13118-13125
    • Buensuceso, C.S1    O'Toole, T.E2
  • 181
    • 0029876948 scopus 로고    scopus 로고
    • Stimulation through the T cell receptor induces Cbl association with Crk proteins and the guanine nucleotide exchange protein C3G
    • K.A Reedquist T Fukazawa G Panchamoorthy W.Y Langdon S.E Shoelson B.J Druker H Band Stimulation through the T cell receptor induces Cbl association with Crk proteins and the guanine nucleotide exchange protein C3G J. Biol. Chem. 271 1996 8435 8442
    • (1996) J. Biol. Chem. , vol.271 , pp. 8435-8442
    • Reedquist, K.A1    Fukazawa, T2    Panchamoorthy, G3    Langdon, W.Y4    Shoelson, S.E5    Druker, B.J6    Band, H7
  • 182
    • 0025339511 scopus 로고
    • A cell culture model for T lymphocyte clonal anergy
    • R.H Schwartz A cell culture model for T lymphocyte clonal anergy Science 248 1990 1349 1356
    • (1990) Science , vol.248 , pp. 1349-1356
    • Schwartz, R.H1
  • 183
    • 0030812812 scopus 로고    scopus 로고
    • Maintenance of human T cell anergy: Blocking of IL-2 gene transcription by activated Rapl
    • V.A Boussiotis G.J Freeman A Berezovskaya D.L Barber L.M Nadler Maintenance of human T cell anergy: Blocking of IL-2 gene transcription by activated Rapl Science 278 1997 124 128
    • (1997) Science , vol.278 , pp. 124-128
    • Boussiotis, V.A1    Freeman, G.J2    Berezovskaya, A3    Barber, D.L4    Nadler, L.M5
  • 184
    • 0029928127 scopus 로고    scopus 로고
    • Sos, Vav, and C3G participate in B cell receptor-induced signaling pathways and differentially associate with Shc-Grb2, Crk, and Crk-L adaptors
    • L Smit G van der Horst J Borst Sos, Vav, and C3G participate in B cell receptor-induced signaling pathways and differentially associate with Shc-Grb2, Crk, and Crk-L adaptors J. Biol. Chem. 271 1996 8564 8569
    • (1996) J. Biol. Chem. , vol.271 , pp. 8564-8569
    • Smit, L1    van der Horst, G2    Borst, J3
  • 185
    • 0029768637 scopus 로고    scopus 로고
    • B cell antigen receptor signaling induces the formation of complexes containing the Crk adapter proteins
    • R.J Ingham D.L Krebs S.M Barbazuk C.W Turck H Hirai M Matsuda M.R Gold B cell antigen receptor signaling induces the formation of complexes containing the Crk adapter proteins J. Biol. Chem. 271 1996 32306 32314
    • (1996) J. Biol. Chem. , vol.271 , pp. 32306-32314
    • Ingham, R.J1    Krebs, D.L2    Barbazuk, S.M3    Turck, C.W4    Hirai, H5    Matsuda, M6    Gold, M.R7
  • 186
    • 0031941567 scopus 로고    scopus 로고
    • Guanine-nucleotide exchange protein C3G activates JNK1 by a ras-independent mechanism. JNK1 activation inhibited by kinase negative forms of MLK3 and DLK mixed lineage kinases
    • S Tanaka H Hanafusa Guanine-nucleotide exchange protein C3G activates JNK1 by a ras-independent mechanism. JNK1 activation inhibited by kinase negative forms of MLK3 and DLK mixed lineage kinases J. Biol. Chem. 273 1998 1281 1284
    • (1998) J. Biol. Chem. , vol.273 , pp. 1281-1284
    • Tanaka, S1    Hanafusa, H2
  • 187
    • 0031004266 scopus 로고    scopus 로고
    • Downstream of Crk adaptor signaling pathway: Activation of Jun kinase by v-Crk through the guanine nucleotide exchange protein C3G
    • S Tanaka T Ouchi H Hanafusa Downstream of Crk adaptor signaling pathway: Activation of Jun kinase by v-Crk through the guanine nucleotide exchange protein C3G Proc. Nad. Acad. Sci. U.S.A. 94 1997 2356 2361
    • (1997) , pp. 2356-2361
    • Tanaka, S1    Ouchi, T2    Hanafusa, H3
  • 189
    • 0032480885 scopus 로고    scopus 로고
    • Signal transduction. New exchange, new target
    • J Downward Signal transduction. New exchange, new target Nature 396 1998 416 417
    • (1998) Nature , vol.396 , pp. 416-417
    • Downward, J1
  • 193
    • 0035154289 scopus 로고    scopus 로고
    • New signaling pathways for hormones and cyclic adenosine 3′,5′-monophosphate action in endocrine cells
    • J.S Richards New signaling pathways for hormones and cyclic adenosine 3′,5′-monophosphate action in endocrine cells Mol. Endocrinol. 15 2001 209 218
    • (2001) Mol. Endocrinol. , vol.15 , pp. 209-218
    • Richards, J.S1
  • 194
    • 0027296639 scopus 로고
    • Inhibition of thyrotropin-stimulated DNA synthesis by microinjection of inhibitors of cellular Ras and cyclic AMP-dependent protein kinase
    • E Kupperman W Wen J.L Meinkoth Inhibition of thyrotropin-stimulated DNA synthesis by microinjection of inhibitors of cellular Ras and cyclic AMP-dependent protein kinase Mol. Cell. Biol. 13 1993 4477 4484
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 4477-4484
    • Kupperman, E1    Wen, W2    Meinkoth, J.L3
  • 195
    • 0026661582 scopus 로고
    • Physiological and pathological regulation of thyroid cell proliferation and differentiation by thyrotropin and other factors
    • J.E Dumont F Lamy P Roger C Maenhaut Physiological and pathological regulation of thyroid cell proliferation and differentiation by thyrotropin and other factors Physiol. Rev. 72 1992 667 697
    • (1992) Physiol. Rev. , vol.72 , pp. 667-697
    • Dumont, J.E1    Lamy, F2    Roger, P3    Maenhaut, C4
  • 196
    • 0035016611 scopus 로고    scopus 로고
    • Coordinated regulation of Rapl and thyroid differentiation by cyclic AMP and protein kinase A
    • O.M Tsygankova A Saavedra J.F Rebhun L.A Quilliam J.L Meinkoth Coordinated regulation of Rapl and thyroid differentiation by cyclic AMP and protein kinase A Mol. Cell. Biol. 21 2001 1921 1929
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 1921-1929
    • Tsygankova, O.M1    Saavedra, A2    Rebhun, J.F3    Quilliam, L.A4    Meinkoth, J.L5
  • 198
    • 0034463096 scopus 로고    scopus 로고
    • Follicle-Stimulating hormone (FSH) stimulates phosphorylation and activation of protein kinase B (PKB/Akt) and serum and glucocorticoid-Induced kinase (Sgk): evidence for A kinase-independent signaling by FSH in granulosa cells
    • I.J Gonzalez-Robayna A.E Falender S Ochsner G.L Firestone J.S Richards Follicle-Stimulating hormone (FSH) stimulates phosphorylation and activation of protein kinase B (PKB/Akt) and serum and glucocorticoid-Induced kinase (Sgk): evidence for A kinase-independent signaling by FSH in granulosa cells Mol. Endocrinol. 14 2000 1283 1300
    • (2000) Mol. Endocrinol. , vol.14 , pp. 1283-1300
    • Gonzalez-Robayna, I.J1    Falender, A.E2    Ochsner, S3    Firestone, G.L4    Richards, J.S5
  • 199
    • 0031936954 scopus 로고    scopus 로고
    • Glucagon-like peptides
    • D.J Drucker Glucagon-like peptides Diabetes 47 1998 159 169
    • (1998) Diabetes , vol.47 , pp. 159-169
    • Drucker, D.J1
  • 200
    • 0029043139 scopus 로고
    • Cell and molecular biology of the incretin hormones Gucagon-like peptide-I and glucose-dependent insulin releasing polypeptide
    • H.C Fehmann R Coke B Goke Cell and molecular biology of the incretin hormones Gucagon-like peptide-I and glucose-dependent insulin releasing polypeptide Endocr Rev. 16 1995 390 410
    • (1995) Endocr Rev. , vol.16 , pp. 390-410
    • Fehmann, H.C1    Coke, R2    Goke, B3
  • 201
    • 0033947157 scopus 로고    scopus 로고
    • Glucagon-like peptide 1 stimulates insulin gene promoter activity by protein kinase A-independent activation of the rat insulin I gene cAMP response element
    • G Skoglund M.A Hussain G.G Holz Glucagon-like peptide 1 stimulates insulin gene promoter activity by protein kinase A-independent activation of the rat insulin I gene cAMP response element Diabetes 49 2000 1156 1164
    • (2000) Diabetes , vol.49 , pp. 1156-1164
    • Skoglund, G1    Hussain, M.A2    Holz, G.G3
  • 202
    • 0034638602 scopus 로고    scopus 로고
    • Expression of cAMP-regulated guanine nucleotide exchange factors in pancreatic beta-cells
    • C.A Leech G.G Holz O Chepurny J.F Habener Expression of cAMP-regulated guanine nucleotide exchange factors in pancreatic beta-cells Biochem. Biophys. Res. Commun. 278 2000 44 47
    • (2000) Biochem. Biophys. Res. Commun. , vol.278 , pp. 44-47
    • Leech, C.A1    Holz, G.G2    Chepurny, O3    Habener, J.F4
  • 204
    • 0034659736 scopus 로고    scopus 로고
    • Ras mediates the CAMP-dependent activation of extracellular signal-regulated kinases (ERKs) in melanocytes
    • R Busca P Abbe F Mantoux E Aberdam C Peyssonnaux A Eychene J.P Ortonne R Ballotti Ras mediates the CAMP-dependent activation of extracellular signal-regulated kinases (ERKs) in melanocytes EMBO J. 19 2000 2900 2910
    • (2000) EMBO J. , vol.19 , pp. 2900-2910
    • Busca, R1    Abbe, P2    Mantoux, F3    Aberdam, E4    Peyssonnaux, C5    Eychene, A6    Ortonne, J.P7    Ballotti, R8
  • 205
    • 0035813228 scopus 로고    scopus 로고
    • Cyclic AMP inhibits extracellular signal-regulated kinase and phosphatidylinositol 3-kinase/Akt pathways by inhibiting Rapl
    • L Wang F Liu M.L Adamo Cyclic AMP inhibits extracellular signal-regulated kinase and phosphatidylinositol 3-kinase/Akt pathways by inhibiting Rapl J. Biol. Chem. 276 2001 37242 37249
    • (2001) J. Biol. Chem. , vol.276 , pp. 37242-37249
    • Wang, L1    Liu, F2    Adamo, M.L3
  • 206
    • 0032952308 scopus 로고    scopus 로고
    • Elevation of cyclic adenosine 3′,5′-monophosphate potentiates activation of mitogen-activated protein kinase by growth factors in LNCaP prostate cancer cells
    • T Chen R.W Cho P.J Stork M.J Weber Elevation of cyclic adenosine 3′,5′-monophosphate potentiates activation of mitogen-activated protein kinase by growth factors in LNCaP prostate cancer cells Cancer Res. 59 1999 213 218
    • (1999) Cancer Res. , vol.59 , pp. 213-218
    • Chen, T1    Cho, R.W2    Stork, P.J3    Weber, M.J4
  • 207
    • 0032793219 scopus 로고    scopus 로고
    • Characterization of GFR, a novel guanine nucleotide exchange factor for Rapl
    • T Ichiba Y Hoshi Y Eto N Tajima Y Kuraishi Characterization of GFR, a novel guanine nucleotide exchange factor for Rapl FEBS Lett. 457 1999 85 89
    • (1999) FEBS Lett. , vol.457 , pp. 85-89
    • Ichiba, T1    Hoshi, Y2    Eto, Y3    Tajima, N4    Kuraishi, Y5
  • 208
    • 0035958929 scopus 로고    scopus 로고
    • RA-GEF-1, a guanine nucleotide exchange factor for Rap1, is activated by translocation induced by association with Rapl {middle dot}GTP and enhances Rap1-dependent B-Raf activation
    • Y Liao T Satoh X Gao T.G Jin C.D Hu T Kataoka RA-GEF-1, a guanine nucleotide exchange factor for Rap1, is activated by translocation induced by association with Rapl {middle dot}GTP and enhances Rap1-dependent B-Raf activation J. Biol. Chem. 276 2001 28478 28483
    • (2001) J. Biol. Chem. , vol.276 , pp. 28478-28483
    • Liao, Y1    Satoh, T2    Gao, X3    Jin, T.G4    Hu, C.D5    Kataoka, T6
  • 210
  • 211
    • 0033547353 scopus 로고    scopus 로고
    • nRap GEP: A novel neural GDP/GTP exchange protein for rap1 small G protein that interacts with synaptic scaffolding molecule (S-SCAM)
    • T Ohtsuka Y Hata N Ide T Yasuda E Inoue T Inoue A Mizoguchi Y Takai nRap GEP: A novel neural GDP/GTP exchange protein for rap1 small G protein that interacts with synaptic scaffolding molecule (S-SCAM) Biochem. Biophys. Res. Commun. 265 1999 38 44
    • (1999) Biochem. Biophys. Res. Commun. , vol.265 , pp. 38-44
    • Ohtsuka, T1    Hata, Y2    Ide, N3    Yasuda, T4    Inoue, E5    Inoue, T6    Mizoguchi, A7    Takai, Y8
  • 212
    • 0034485413 scopus 로고    scopus 로고
    • Membrane-associated guanylate kinase with inverted orientation (MAGI)-1/brain angiogenesis inhibitor 1-associated protein (BAPI) as a scaffolding molecule for Rap small G protein GDP/GTP exchange protein at tight junctions
    • A Mino T Ohtsuka E Inoue Y Takai Membrane-associated guanylate kinase with inverted orientation (MAGI)-1/brain angiogenesis inhibitor 1-associated protein (BAPI) as a scaffolding molecule for Rap small G protein GDP/GTP exchange protein at tight junctions Genes Cells 5 2000 1009 1016
    • (2000) Genes Cells , vol.5 , pp. 1009-1016
    • Mino, A1    Ohtsuka, T2    Inoue, E3    Takai, Y4
  • 213
    • 0033560065 scopus 로고    scopus 로고
    • PDZ domains: Fundamental building blocks in the organization of protein complexes at the plasma membrane
    • A.S Fanning J.M Anderson PDZ domains: Fundamental building blocks in the organization of protein complexes at the plasma membrane J. Clin. Invest. 103 1999 767 772
    • (1999) J. Clin. Invest. , vol.103 , pp. 767-772
    • Fanning, A.S1    Anderson, J.M2
  • 214
    • 0033081407 scopus 로고    scopus 로고
    • The Rap1 GTPase functions as a regulator of morphogenesis in vivo
    • H Asha N.D de Ruiter M.G Wang I.K Hariharan The Rap1 GTPase functions as a regulator of morphogenesis in vivo EMBO J. 18 1999 605 615
    • (1999) EMBO J. , vol.18 , pp. 605-615
    • Asha, H1    de Ruiter, N.D2    Wang, M.G3    Hariharan, I.K4
  • 215
    • 0033609359 scopus 로고    scopus 로고
    • Sequence analysis identifies a ras-associating (RA)-like domain in the N-termini of band 4. /JEF domains and in the Grb7/10/14 adapter family
    • J Wojcik J.A Girault G Labesse J Chomilier J.P Mornon I Callebaut Sequence analysis identifies a ras-associating (RA)-like domain in the N-termini of band 4. /JEF domains and in the Grb7/10/14 adapter family Biochem. Biophys. Res. Commun. 259 1999 113 120
    • (1999) Biochem. Biophys. Res. Commun. , vol.259 , pp. 113-120
    • Wojcik, J1    Girault, J.A2    Labesse, G3    Chomilier, J4    Mornon, J.P5    Callebaut, I6
  • 216
    • 0035834649 scopus 로고    scopus 로고
    • Identification and characterization of RA-GEF-2, a Rap guanine nucleotide exchange factor that serves as a downstream target of M-Ras
    • X Gao T Satoh Y Liao C Song C.D Hu K Kariya Ki T Kataoka Identification and characterization of RA-GEF-2, a Rap guanine nucleotide exchange factor that serves as a downstream target of M-Ras J. Biol. Chem. 276 2001 42219 42225
    • (2001) J. Biol. Chem. , vol.276 , pp. 42219-42225
    • Gao, X1    Satoh, T2    Liao, Y3    Song, C4    Hu, C.D5    Kariya Ki, K6    Kataoka, T7
  • 217
    • 0022373903 scopus 로고
    • Transformation of BALB/3T3 cells with EJ/T24/H-ras oncogene inhibits adenylate cyclase response to beta-adrenergic agonist while increases muscarinic receptor dependent hydrolysis of inositol lipids
    • V Chiarugi F Porciatti F Pasquali P Bruni Transformation of BALB/3T3 cells with EJ/T24/H-ras oncogene inhibits adenylate cyclase response to beta-adrenergic agonist while increases muscarinic receptor dependent hydrolysis of inositol lipids Biochem. Biophys. Res. Commun. 132 1985 900 907
    • (1985) Biochem. Biophys. Res. Commun. , vol.132 , pp. 900-907
    • Chiarugi, V1    Porciatti, F2    Pasquali, F3    Bruni, P4
  • 218
    • 0023047013 scopus 로고
    • Normal p21 N-ras couples bombesin and other growth factor receptors to inositol phosphate production
    • M.J Wakelam S.A Davies M.D Houslay I McKay C.J Marshall A Hall Normal p21 N-ras couples bombesin and other growth factor receptors to inositol phosphate production Nature 323 1986 173 176
    • (1986) Nature , vol.323 , pp. 173-176
    • Wakelam, M.J1    Davies, S.A2    Houslay, M.D3    McKay, I4    Marshall, C.J5    Hall, A6
  • 219
    • 0024061384 scopus 로고
    • p21ras-induced responsiveness of phosphatidylinositol turnover to bradykinin is a receptor number effect
    • J Downward J de Gunzburg R Riehl R.A Weinberg p21ras-induced responsiveness of phosphatidylinositol turnover to bradykinin is a receptor number effect Proc. Natl. Acad. Sci. U.S.A. 85 1988 5774 5778
    • (1988) , pp. 5774-5778
    • Downward, J1    de Gunzburg, J2    Riehl, R3    Weinberg, R.A4
  • 220
    • 0025598274 scopus 로고
    • GTP-binding protein-stimulated phospholipase C and phospholipase D activities in ras-transformed NIH 3T3 fibroblasts
    • L.A Quilliam C.J Der J.H Brown GTP-binding protein-stimulated phospholipase C and phospholipase D activities in ras-transformed NIH 3T3 fibroblasts Second Messengers dT Phosphoproteins 13 1990 59 67
    • (1990) Second Messengers dT Phosphoproteins , vol.13 , pp. 59-67
    • Quilliam, L.A1    Der, C.J2    Brown, J.H3
  • 221
    • 0032513127 scopus 로고    scopus 로고
    • Identification of PLC210, a Caenorhabditis elegans phospholipase C, as a putative effector of Ras
    • M Shibatohge K Kariya Y Liao C.D Hu Y Watari M Goshima F Shima T Kataoka Identification of PLC210, a Caenorhabditis elegans phospholipase C, as a putative effector of Ras J. Biol. Chem. 273 1998 6218 6222
    • (1998) J. Biol. Chem. , vol.273 , pp. 6218-6222
    • Shibatohge, M1    Kariya, K2    Liao, Y3    Hu, C.D4    Watari, Y5    Goshima, M6    Shima, F7    Kataoka, T8
  • 222
    • 0035839496 scopus 로고    scopus 로고
    • Role of the CDC25 homology domain of PLC{epsilon} in amplification of Rap1-dependent signaling
    • T.G Jin T Satoh Y Liao C Song X Gao K Kariya Ki C.D Hu T Kataoka Role of the CDC25 homology domain of PLC{epsilon} in amplification of Rap1-dependent signaling J. Biol. Chem. 276 2001 30301 30307
    • (2001) J. Biol. Chem. , vol.276 , pp. 30301-30307
    • Jin, T.G1    Satoh, T2    Liao, Y3    Song, C4    Gao, X5    Kariya Ki, K6    Hu, C.D7    Kataoka, T8
  • 224
    • 0035865293 scopus 로고    scopus 로고
    • Phospholipase C(epsilon): A novel Ras effector
    • G.G Kelley S.E Reks J.M Ondrako A.V Smrcka Phospholipase C(epsilon): A novel Ras effector EMBO J. 20 2001 743 754
    • (2001) EMBO J. , vol.20 , pp. 743-754
    • Kelley, G.G1    Reks, S.E2    Ondrako, J.M3    Smrcka, A.V4
  • 225
    • 0035951882 scopus 로고    scopus 로고
    • A novel bifunctional phospholipase c that is regulated by Galpha 12 and stimulates the Ras/mitogen-activated protein kinase pathway
    • I Lopez E.C Mak J Ding H.E Hamm J.W Lomasney A novel bifunctional phospholipase c that is regulated by Galpha 12 and stimulates the Ras/mitogen-activated protein kinase pathway J. Biol. Chem. 276 2001 2758 2765
    • (2001) J. Biol. Chem. , vol.276 , pp. 2758-2765
    • Lopez, I1    Mak, E.C2    Ding, J3    Hamm, H.E4    Lomasney, J.W5
  • 226
    • 0035337097 scopus 로고    scopus 로고
    • Ras effectors: Buying shares in Ras plc
    • P.J Cullen Ras effectors: Buying shares in Ras plc Curr. Biol. 11 2001 R342 R344
    • (2001) Curr. Biol. , vol.11 , pp. R342-R344
    • Cullen, P.J1
  • 227
    • 0027986765 scopus 로고
    • ralGDS family members interact with the effector loop of ras p21
    • A Kikuchi S.D Demo Z.H Ye Y.W Chen L.T Williams ralGDS family members interact with the effector loop of ras p21 Mol. Cell. Biol. 14 1994 7483 7491
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 7483-7491
    • Kikuchi, A1    Demo, S.D2    Ye, Z.H3    Chen, Y.W4    Williams, L.T5
  • 230
    • 0034282408 scopus 로고    scopus 로고
    • A novel RaIGEF-like protein, RGL3, as a candidate effector for rit and Ras
    • H Shao D.A Andres A novel RaIGEF-like protein, RGL3, as a candidate effector for rit and Ras J. Biol. Chem. 275 2000 26914 26924
    • (2000) J. Biol. Chem. , vol.275 , pp. 26914-26924
    • Shao, H1    Andres, D.A2
  • 231
    • 0035843165 scopus 로고    scopus 로고
    • A novel potential effector of M-Ras and p21 Ras negatively regulates p21 Ras-mediated gene induction and cell growth
    • G.R Ehrhardt C Korherr J.S Wieler M Knaus J.W Schrader A novel potential effector of M-Ras and p21 Ras negatively regulates p21 Ras-mediated gene induction and cell growth Oncogene 20 2001 188 197
    • (2001) Oncogene , vol.20 , pp. 188-197
    • Ehrhardt, G.R1    Korherr, C2    Wieler, J.S3    Knaus, M4    Schrader, J.W5
  • 232
    • 0030950471 scopus 로고    scopus 로고
    • rsc: A novel oncogene with structural and functional homology with the gene family of exchange factors for Ral
    • D.R D'Adamo S Novick J.M Kahn P Leonardi A Pellicer rsc: A novel oncogene with structural and functional homology with the gene family of exchange factors for Ral Oncogene 14 1997 1295 1305
    • (1997) Oncogene , vol.14 , pp. 1295-1305
    • D'Adamo, D.R1    Novick, S2    Kahn, J.M3    Leonardi, P4    Pellicer, A5
  • 233
    • 0033020660 scopus 로고    scopus 로고
    • Ral-specific guanine nucleotide exchange factor activity opposes other Ras effectors in PC I2 cells by inhibiting neurite outgrowth
    • T Goi G Rusanescu T Urano L.A Feig Ral-specific guanine nucleotide exchange factor activity opposes other Ras effectors in PC I2 cells by inhibiting neurite outgrowth Mol. Cell. Biol. 19 1999 1731 1741
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1731-1741
    • Goi, T1    Rusanescu, G2    Urano, T3    Feig, L.A4
  • 234
    • 0034713356 scopus 로고    scopus 로고
    • The Rgr oncogene (homologous to RalGDS) induces transformation and gene expression by activating Ras, Ral and Rho mediated pathways
    • I Hernandez-Munoz M Malumbres P Leonardi A Pellicer The Rgr oncogene (homologous to RalGDS) induces transformation and gene expression by activating Ras, Ral and Rho mediated pathways Oncogene 19 2000 2745 2757
    • (2000) Oncogene , vol.19 , pp. 2745-2757
    • Hernandez-Munoz, I1    Malumbres, M2    Leonardi, P3    Pellicer, A4
  • 236
    • 0030723061 scopus 로고    scopus 로고
    • Identification and characterization of R-ras3: a novel member of the RAS gene family with a non-ubiquitous pattern of tissue distribution
    • A Kimmelman T Tolkacheva M.V Lorenzi M Osada A.M Chan Identification and characterization of R-ras3: a novel member of the RAS gene family with a non-ubiquitous pattern of tissue distribution Oncogene 15 1997 2675 2685
    • (1997) Oncogene , vol.15 , pp. 2675-2685
    • Kimmelman, A1    Tolkacheva, T2    Lorenzi, M.V3    Osada, M4    Chan, A.M5
  • 237
    • 0032531756 scopus 로고    scopus 로고
    • Extracellular signal-regulated activation of Rapl fails to interfere in Ras effector signalling
    • F.J Zwartkruis R.M Wolthuis N.M Nabben B Franke J.L Bos Extracellular signal-regulated activation of Rapl fails to interfere in Ras effector signalling EMBO J. 17 1998 5905 5912
    • (1998) EMBO J. , vol.17 , pp. 5905-5912
    • Zwartkruis, F.J1    Wolthuis, R.M2    Nabben, N.M3    Franke, B4    Bos, J.L5
  • 238
    • 0033545328 scopus 로고    scopus 로고
    • Plasma membrane recruitment of RaIGDS is critical for Ras-dependent Ral activation
    • K Matsubara S Kishida Y Matsuura H Kitayama M Noda A Kikuchi Plasma membrane recruitment of RaIGDS is critical for Ras-dependent Ral activation Oncogene 18 1999 1303 1312
    • (1999) Oncogene , vol.18 , pp. 1303-1312
    • Matsubara, K1    Kishida, S2    Matsuura, Y3    Kitayama, H4    Noda, M5    Kikuchi, A6
  • 239
    • 0030728532 scopus 로고    scopus 로고
    • Stimulation of gene induction and cell growth by the Ras effector Rlf
    • R.M Wolthuis N.D de Ruiter R.H Cool J.L Bos Stimulation of gene induction and cell growth by the Ras effector Rlf EMBO J. 16 1997 6748 6761
    • (1997) EMBO J. , vol.16 , pp. 6748-6761
    • Wolthuis, R.M1    de Ruiter, N.D2    Cool, R.H3    Bos, J.L4
  • 240
    • 0030022174 scopus 로고    scopus 로고
    • Ral-GTPases mediate a distinct downstream signaling pathway from Ras that facilitates cellular transformation
    • T Urano R Emkey L.A Feig Ral-GTPases mediate a distinct downstream signaling pathway from Ras that facilitates cellular transformation EMBO J. 15 1996 810 816
    • (1996) EMBO J. , vol.15 , pp. 810-816
    • Urano, T1    Emkey, R2    Feig, L.A3
  • 242
    • 0031055236 scopus 로고    scopus 로고
    • Synergistic activation of c-fos promoter activity by Raf and Ral GDP dissociation stimulator
    • M Okazaki S Kishida T Hinoi T Hasegawa M Tamada T Kataoka A Kikuchi Synergistic activation of c-fos promoter activity by Raf and Ral GDP dissociation stimulator Oncogene 14 1997 515 521
    • (1997) Oncogene , vol.14 , pp. 515-521
    • Okazaki, M1    Kishida, S2    Hinoi, T3    Hasegawa, T4    Tamada, M5    Kataoka, T6    Kikuchi, A7
  • 243
    • 0033551698 scopus 로고    scopus 로고
    • Specific contributions of the small GTPases Rho, Rae, and Cdc42 to Dbl transformation
    • R Lin R.A Cerione D Manor Specific contributions of the small GTPases Rho, Rae, and Cdc42 to Dbl transformation J. Biol. Chem. 274 1999 23,633 23,641
    • (1999) J. Biol. Chem. , vol.274
    • Lin, R1    Cerione, R.A2    Manor, D3
  • 244
    • 0026488394 scopus 로고
    • GTP-binding mutants of rab1 and rab2 are potent inhibitors of vesicular transport from the endoplasmic reticulum to the Golgi complex
    • E.J Tisdale J.R Bourne R Khosravi-Far C.J Der W.E Balch GTP-binding mutants of rab1 and rab2 are potent inhibitors of vesicular transport from the endoplasmic reticulum to the Golgi complex J. Cell. Biol. 119 1992 749 761
    • (1992) J. Cell. Biol. , vol.119 , pp. 749-761
    • Tisdale, E.J1    Bourne, J.R2    Khosravi-Far, R3    Der, C.J4    Balch, W.E5
  • 245
    • 0032474731 scopus 로고    scopus 로고
    • Ras-independent activation of Ral by a Ca(2+)dependent pathway
    • F Hofer R Berdeaux G.S Martin Ras-independent activation of Ral by a Ca(2+)dependent pathway Curr. Biol. 8 1998 839 842
    • (1998) Curr. Biol. , vol.8 , pp. 839-842
    • Hofer, F1    Berdeaux, R2    Martin, G.S3
  • 247
    • 0030988723 scopus 로고    scopus 로고
    • Identification and characterization of a calmodulin-binding domain in Ral-A, a Ras-related GTP-binding protein purified from human erythrocyte membrane
    • K.L Wang M.T Khan B.D Roufogalis Identification and characterization of a calmodulin-binding domain in Ral-A, a Ras-related GTP-binding protein purified from human erythrocyte membrane J. Biol. Chem. 272 1997 16,002 16,009
    • (1997) J. Biol. Chem. , vol.272
    • Wang, K.L1    Khan, M.T2    Roufogalis, B.D3
  • 248
    • 0029861489 scopus 로고    scopus 로고
    • Rin, a neuron-specific and calmodulin-binding small G-protein, and Rit define a novel subfamily of ras proteins
    • C.H.J Lee N.G Della C.E Chew D.J Zack Rin, a neuron-specific and calmodulin-binding small G-protein, and Rit define a novel subfamily of ras proteins J. Neurosci. 16 1996 6784 6794
    • (1996) J. Neurosci. , vol.16 , pp. 6784-6794
    • Lee, C.H.J1    Della, N.G2    Chew, C.E3    Zack, D.J4
  • 249
    • 0029857106 scopus 로고    scopus 로고
    • RIC, a calmodulin-binding Ras-like GTPase
    • P.D Wes M Yu C Montell RIC, a calmodulin-binding Ras-like GTPase EMBO J. 15 1996 5839 5848
    • (1996) EMBO J. , vol.15 , pp. 5839-5848
    • Wes, P.D1    Yu, M2    Montell, C3
  • 252
    • 85112953346 scopus 로고    scopus 로고
    • Distinct ligand preferences of SH3 domains from Src, Yes, Abl, cortactin, p53bp2, PLC y, Crk and Grb2
    • A.B Sparks J.E Rider N.G Hoffmann D.M Fowlkes L.A Quilliam B.K Kay Distinct ligand preferences of SH3 domains from Src, Yes, Abl, cortactin, p53bp2, PLC y, Crk and Grb2 Proc. Nad. Acad. Sci. U.S.A. 93 1996
    • (1996)
    • Sparks, A.B1    Rider, J.E2    Hoffmann, N.G3    Fowlkes, D.M4    Quilliam, L.A5    Kay, B.K6
  • 254
    • 0034684997 scopus 로고    scopus 로고
    • BCAR1, a human homologue of the adapter protein p130Cas, and antiestrogen resistance in breast cancer cells
    • A Brinkman S van der Flier E.M Kok L.C Dorssers BCAR1, a human homologue of the adapter protein p130Cas, and antiestrogen resistance in breast cancer cells J. Natl. Cancer Inst. 92 2000 112 120
    • (2000) J. Natl. Cancer Inst. , vol.92 , pp. 112-120
    • Brinkman, A1    van der Flier, S2    Kok, E.M3    Dorssers, L.C4
  • 255
    • 0032525138 scopus 로고    scopus 로고
    • Identification of BCAR3 by a random search for genes involved in antiestrogen resistance of human breast cancer cells
    • T van Agthoven T.L van Agthoven A Dekker P.J van der Spek L Vreede L.C Dorssers Identification of BCAR3 by a random search for genes involved in antiestrogen resistance of human breast cancer cells EMBO J. 17 1998 2799 2808
    • (1998) EMBO J. , vol.17 , pp. 2799-2808
    • van Agthoven, T1    van Agthoven, T.L2    Dekker, A3    van der Spek, P.J4    Vreede, L5    Dorssers, L.C6
  • 256
    • 0033566368 scopus 로고    scopus 로고
    • AND-34, a novel p130Cas-binding thymic stromal cell protein regulated by adhesion and inflammatory cytokines
    • D Cai L.K Clayton A Smolyar A Lerner AND-34, a novel p130Cas-binding thymic stromal cell protein regulated by adhesion and inflammatory cytokines J Immunol 163 1999 2104 2112
    • (1999) J Immunol , vol.163 , pp. 2104-2112
    • Cai, D1    Clayton, L.K2    Smolyar, A3    Lerner, A4
  • 257
    • 0033527649 scopus 로고    scopus 로고
    • A novel signaling intermediate, SHEP1, directly couples Eph receptors to R-Ras and Rap1A
    • V.C Dodelet C Pazzagli A.H Zisch C.A Hauser E.B Pasquale A novel signaling intermediate, SHEP1, directly couples Eph receptors to R-Ras and Rap1A J. Biol. Chem. 274 1999 31,941 31,946
    • (1999) J. Biol. Chem. , vol.274
    • Dodelet, V.C1    Pazzagli, C2    Zisch, A.H3    Hauser, C.A4    Pasquale, E.B5
  • 258
    • 0033537975 scopus 로고    scopus 로고
    • NSP1 defines a novel family of adaptor proteins linking integrin and tyrosine kinase receptors to the c-Jun N-terminal kinase/stress-activated protein kinase signaling pathway
    • Y Lu J Brush T.A Stewart NSP1 defines a novel family of adaptor proteins linking integrin and tyrosine kinase receptors to the c-Jun N-terminal kinase/stress-activated protein kinase signaling pathway J. Biol. Chem. 274 1999 10,047 10,052
    • (1999) J. Biol. Chem. , vol.274
    • Lu, Y1    Brush, J2    Stewart, T.A3
  • 259
    • 0034052103 scopus 로고    scopus 로고
    • Chat, a Cas/HEFT-associated adaptor protein that integrates multiple signaling pathways
    • A Sakakibara S Hattori Chat, a Cas/HEFT-associated adaptor protein that integrates multiple signaling pathways J. Biol. Chem. 275 2000 6404 6410
    • (2000) J. Biol. Chem. , vol.275 , pp. 6404-6410
    • Sakakibara, A1    Hattori, S2
  • 260
    • 0034730244 scopus 로고    scopus 로고
    • p130Cas regulates the activity of AND34, a novel Ral, Rapl, and R-Ras guanine nucleotide exchange factor
    • T Gotoh D Cai X Tian L.A Feig A Lerner p130Cas regulates the activity of AND34, a novel Ral, Rapl, and R-Ras guanine nucleotide exchange factor J. Biol. Chem. 275 2000 30,118 30,123
    • (2000) J. Biol. Chem. , vol.275
    • Gotoh, T1    Cai, D2    Tian, X3    Feig, L.A4    Lerner, A5
  • 262
    • 0034651872 scopus 로고    scopus 로고
    • An EGF receptor/RalGTPase signaling cascade regulates c-Src activity and substrate specificity
    • T Goi M Shipitsin Z Lu D.A Foster S.G Klinz L.A Feig An EGF receptor/RalGTPase signaling cascade regulates c-Src activity and substrate specificity EMBO J. 19 2000 623 630
    • (2000) EMBO J. , vol.19 , pp. 623-630
    • Goi, T1    Shipitsin, M2    Lu, Z3    Foster, D.A4    Klinz, S.G5    Feig, L.A6
  • 263
    • 0032544537 scopus 로고    scopus 로고
    • Identification and characterization in Xenopus of XsmgGDS, a RalB binding protein
    • N Iouzalen J Camonis J Moreau Identification and characterization in Xenopus of XsmgGDS, a RalB binding protein Biochem. Biophys. Res. Commun. 250 1998 359 363
    • (1998) Biochem. Biophys. Res. Commun. , vol.250 , pp. 359-363
    • Iouzalen, N1    Camonis, J2    Moreau, J3
  • 264
    • 0034629117 scopus 로고    scopus 로고
    • Unique in vivo associations with SmgGDS and RhoGDI and different guanine nucleotide exchange activities exhibited by RhoA, dominant negative RhoA(Asn-19), and activated RhoA(Val-14)
    • D Strassheim R.A Porter S.H Phelps C.L Williams Unique in vivo associations with SmgGDS and RhoGDI and different guanine nucleotide exchange activities exhibited by RhoA, dominant negative RhoA(Asn-19), and activated RhoA(Val-14) J. Biol. Chem. 275 2000 6699 6702
    • (2000) J. Biol. Chem. , vol.275 , pp. 6699-6702
    • Strassheim, D1    Porter, R.A2    Phelps, S.H3    Williams, C.L4
  • 265
    • 0031754774 scopus 로고    scopus 로고
    • The armadillo family of structural proteins
    • M Hatzfeld The armadillo family of structural proteins Int. Rev. Cytol. 186 1999 179 224
    • (1999) Int. Rev. Cytol. , vol.186 , pp. 179-224
    • Hatzfeld, M1
  • 266
    • 0030800831 scopus 로고    scopus 로고
    • Three-dimensional structure of the armadillo repeat region of beta-catenin
    • A.H Huber W.H Nelson W.I Weis Three-dimensional structure of the armadillo repeat region of beta-catenin Cell 90 1997 871 882
    • (1997) Cell , vol.90 , pp. 871-882
    • Huber, A.H1    Nelson, W.H2    Weis, W.I3
  • 267
    • 0033612390 scopus 로고    scopus 로고
    • Structural view of the RanImportin beta interaction at 2.3 A resolution
    • I.R Vetter A Arndt U Kutay D Gorlich A Wittinghofer Structural view of the RanImportin beta interaction at 2.3 A resolution Cell 97 1999 635 646
    • (1999) Cell , vol.97 , pp. 635-646
    • Vetter, I.R1    Arndt, A2    Kutay, U3    Gorlich, D4    Wittinghofer, A5
  • 268
    • 0026760620 scopus 로고
    • The functional domain of the stimulatory GDP/GTP exchange protein (smg GDS) which interacts with the C-terminal geranylgeranylated region of rapl/Krev-1/smg p21
    • K Kotani A Kikuchi K Doi S Kishida T Sakoda K Kishi Y Takai The functional domain of the stimulatory GDP/GTP exchange protein (smg GDS) which interacts with the C-terminal geranylgeranylated region of rapl/Krev-1/smg p21 Oncogene 7 1992 1699 1704
    • (1992) Oncogene , vol.7 , pp. 1699-1704
    • Kotani, K1    Kikuchi, A2    Doi, K3    Kishida, S4    Sakoda, T5    Kishi, K6    Takai, Y7
  • 269
    • 0025895931 scopus 로고
    • The smg GDS-induced activation of smg p21 is initiated by cyclic AMP-dependent protein kinase-catalyzed phosphorylation of smg p21
    • T Itoh K Kaibuchi T Sasaki Y Takai The smg GDS-induced activation of smg p21 is initiated by cyclic AMP-dependent protein kinase-catalyzed phosphorylation of smg p21 Biochem. Biophys. Res. Commun. 177 1991 1319 1324
    • (1991) Biochem. Biophys. Res. Commun. , vol.177 , pp. 1319-1324
    • Itoh, T1    Kaibuchi, K2    Sasaki, T3    Takai, Y4
  • 271
    • 0030987069 scopus 로고    scopus 로고
    • How receptors talk to trimeric G proteins
    • H.R Bourne How receptors talk to trimeric G proteins Curr. Opin. Cell Biol. 9 1997 134 142
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 134-142
    • Bourne, H.R1
  • 272
    • 0028239341 scopus 로고
    • The Dbl oncogene product as a GDP/GTP exchange protein for the Rho family: its properties in comparison with those of Smg GDS
    • H Yaku T Sasaki Y Takai The Dbl oncogene product as a GDP/GTP exchange protein for the Rho family: its properties in comparison with those of Smg GDS Biochem. Biophys. Res. Commun. 198 1994 811 817
    • (1994) Biochem. Biophys. Res. Commun. , vol.198 , pp. 811-817
    • Yaku, H1    Sasaki, T2    Takai, Y3
  • 273
    • 0028365660 scopus 로고
    • Different functions of Smg GDP dissociation stimulator and mammalian counterpart of yeast Cdc25
    • H Nakanishi K Kaibuchi S Orita N Ueno Y Takai Different functions of Smg GDP dissociation stimulator and mammalian counterpart of yeast Cdc25 J. Biol. Chem. 269 1994 15,085 15,091
    • (1994) J. Biol. Chem. , vol.269
    • Nakanishi, H1    Kaibuchi, K2    Orita, S3    Ueno, N4    Takai, Y5
  • 274
    • 0032549628 scopus 로고    scopus 로고
    • Complex formation of SMAP/ KAP3, a KIF3A/B ATPase motor-associated protein, with a human chromosome-associated polypeptide
    • K Shimizu H Shirataki T Honda S Minami Y Takai Complex formation of SMAP/ KAP3, a KIF3A/B ATPase motor-associated protein, with a human chromosome-associated polypeptide J. Biol. Chem. 273 1998 6591 6594
    • (1998) J. Biol. Chem. , vol.273 , pp. 6591-6594
    • Shimizu, K1    Shirataki, H2    Honda, T3    Minami, S4    Takai, Y5
  • 277
    • 0031769082 scopus 로고    scopus 로고
    • Identification of darlin, a Dictyostelium protein with Armadillo-like repeats that binds to small GTPases and is important for the proper aggregation of developing cells
    • K.K Vithalani C.A Parent E.M Thorn M Penn D.A Larochelle P.N Devreotes A De Lozanne Identification of darlin, a Dictyostelium protein with Armadillo-like repeats that binds to small GTPases and is important for the proper aggregation of developing cells Mol. Biol. Cell. 9 1998 3095 3106
    • (1998) Mol. Biol. Cell. , vol.9 , pp. 3095-3106
    • Vithalani, K.K1    Parent, C.A2    Thorn, E.M3    Penn, M4    Larochelle, D.A5    Devreotes, P.N6    De Lozanne, A7
  • 279
    • 0031034106 scopus 로고    scopus 로고
    • HER-2/neu signal transduction in human breast and ovarian cancer
    • D.M Reese D.J Slamon HER-2/neu signal transduction in human breast and ovarian cancer Stem Cells 15 1997 1 8
    • (1997) Stem Cells , vol.15 , pp. 1-8
    • Reese, D.M1    Slamon, D.J2
  • 280
    • 0030754123 scopus 로고    scopus 로고
    • The significance of Ras guanine nucleotide exchange factor, son of sevenless protein, in renal cell carcinoma cell lines
    • N Shinohara Y Ogiso M Tanaka A Sazawa T Harabayashi T Koyanagi The significance of Ras guanine nucleotide exchange factor, son of sevenless protein, in renal cell carcinoma cell lines J. Urol. 158 1997 908 911
    • (1997) J. Urol. , vol.158 , pp. 908-911
    • Shinohara, N1    Ogiso, Y2    Tanaka, M3    Sazawa, A4    Harabayashi, T5    Koyanagi, T6
  • 283
    • 0033568581 scopus 로고    scopus 로고
    • The (4;11)(q2I;p15) translocation fuses the NUP98 and RAP1GDS1 genes and is recurrent in T-cell acute lymphocytic leukemia
    • D.J Hussey M Nicola S Moore G.B Peters A Dobrovic The (4;11)(q2I;p15) translocation fuses the NUP98 and RAP1GDS1 genes and is recurrent in T-cell acute lymphocytic leukemia Blood 94 1999 2072 2079
    • (1999) Blood , vol.94 , pp. 2072-2079
    • Hussey, D.J1    Nicola, M2    Moore, S3    Peters, G.B4    Dobrovic, A5
  • 284
  • 285
    • 0027294981 scopus 로고
    • The SH2 and SH3 domains of mammalian Grb2 couple the EGF receptor to the Ras activator mSosl
    • M Rozakis-Adcock R Fernley J Wade T Pawson D Bowtell The SH2 and SH3 domains of mammalian Grb2 couple the EGF receptor to the Ras activator mSosl Nature 363 1993 83 85
    • (1993) Nature , vol.363 , pp. 83-85
    • Rozakis-Adcock, M1    Fernley, R2    Wade, J3    Pawson, T4    Bowtell, D5
  • 286
    • 0029132697 scopus 로고
    • Differential interactions of human Sosl and Sos2 with Grb2
    • S.S Yang L Van Aelst D Bar-Sagi Differential interactions of human Sosl and Sos2 with Grb2 J. Biol. Chem. 270 1995 18,212 18,215
    • (1995) J. Biol. Chem. , vol.270
    • Yang, S.S1    Van Aelst, L2    Bar-Sagi, D3
  • 288
    • 0029913467 scopus 로고    scopus 로고
    • 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
    • C Herrmann G Hom M Spaargaren A Wittinghofer 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 J. Biol. Chem. 271 1996 6794 6800
    • (1996) J. Biol. Chem. , vol.271 , pp. 6794-6800
    • Herrmann, C1    Hom, G2    Spaargaren, M3    Wittinghofer, A4
  • 289
    • 0028577298 scopus 로고
    • Identification of the guanine nucleotide dissociation stimulator for Ral as a putative effector molecule of R-ras, H-ras, K-ras, and Rap
    • M Spaargaren J.R Bischoff Identification of the guanine nucleotide dissociation stimulator for Ral as a putative effector molecule of R-ras, H-ras, K-ras, and Rap Proc. Nad. Acad. Sci. U.S.A. 91 1994 12,609 12,613
    • (1994)
    • Spaargaren, M1    Bischoff, J.R2


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