메뉴 건너뛰기




Volumn 107, Issue 24, 2010, Pages 10920-10925

Erratum: Pseudopodium-enriched atypical kinase 1 regulates the cytoskeleton and cancer progession (Proceedings of the National Academy of Sciences of the United States of America (2010) 107, 24 (10920-10925) DOI: 10.1073/pnas.0914776107);Pseudopodium-enriched atypical kinase 1 regulates the cytoskeleton and cancer progression

Author keywords

Cancer; Cell migration; Phosphoproteomics

Indexed keywords

EPIDERMAL GROWTH FACTOR RECEPTOR; INTEGRIN; MITOGEN ACTIVATED PROTEIN KINASE; PAXILLIN; PSEUDOPODIUM ENRICHED ATYPICAL KINASE 1; TUMOR PROTEIN; UNCLASSIFIED DRUG;

EID: 77954643220     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1008849107     Document Type: Erratum
Times cited : (92)

References (65)
  • 1
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • Hall A (1998) Rho GTPases and the actin cytoskeleton. Science 279:509-514.
    • (1998) Science , vol.279 , pp. 509-514
    • Hall, A.1
  • 2
    • 36749024118 scopus 로고    scopus 로고
    • Filopodia: The fingers that do the walking
    • Gupton SL, Gertler FB (2007) Filopodia: The fingers that do the walking. Sci STKE 2007:re5.
    • (2007) Sci STKE , vol.2007
    • Gupton, S.L.1    Gertler, F.B.2
  • 3
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • Pollard TD, Borisy GG (2003) Cellular motility driven by assembly and disassembly of actin filaments. Cell 112:453-465.
    • (2003) Cell , vol.112 , pp. 453-465
    • Pollard, T.D.1    Borisy, G.G.2
  • 4
    • 0344305784 scopus 로고    scopus 로고
    • Cell migration: Integrating signals from front to back
    • Ridley AJ, et al. (2003) Cell migration: Integrating signals from front to back. Science 302:1704-1709.
    • (2003) Science , vol.302 , pp. 1704-1709
    • Ridley, A.J.1
  • 6
    • 6344231716 scopus 로고    scopus 로고
    • Guiding cell migration through directed extension and stabilization of pseudopodia
    • Chodniewicz D, Klemke RL (2004) Guiding cell migration through directed extension and stabilization of pseudopodia. Exp Cell Res 301:31-37.
    • (2004) Exp Cell Res , vol.301 , pp. 31-37
    • Chodniewicz, D.1    Klemke, R.L.2
  • 7
    • 0030045346 scopus 로고    scopus 로고
    • Cell migration: A physically integrated molecular process
    • Lauffenburger DA, Horwitz AF (1996) Cell migration: A physically integrated molecular process. Cell 84:359-369.
    • (1996) Cell , vol.84 , pp. 359-369
    • Lauffenburger, D.A.1    Horwitz, A.F.2
  • 8
    • 0033617576 scopus 로고    scopus 로고
    • A cell's sense of direction
    • Parent CA, Devreotes PN (1999) A cell's sense of direction. Science 284:765-770.
    • (1999) Science , vol.284 , pp. 765-770
    • Parent, C.A.1    Devreotes, P.N.2
  • 9
    • 0037128213 scopus 로고    scopus 로고
    • Purification of pseudopodia from polarized cells reveals redistribution and activation of Rac through assembly of a CAS/Crk scaffold
    • Cho SY, Klemke RL (2002) Purification of pseudopodia from polarized cells reveals redistribution and activation of Rac through assembly of a CAS/Crk scaffold. J Cell Biol 156:725-736.
    • (2002) J Cell Biol , vol.156 , pp. 725-736
    • Cho, S.Y.1    Klemke, R.L.2
  • 10
    • 34347257820 scopus 로고    scopus 로고
    • Profiling signaling polarity in chemotactic cells
    • Wang Y, et al. (2007) Profiling signaling polarity in chemotactic cells. Proc Natl Acad Sci USA 104:8328-8333.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 8328-8333
    • Wang, Y.1
  • 11
    • 38449107248 scopus 로고    scopus 로고
    • Methods for pseudopodia purification and proteomic analysis
    • Wang Y, et al. (2007) Methods for pseudopodia purification and proteomic analysis. Sci STKE 2007:pl4.
    • (2007) Sci STKE , vol.2007
    • Wang, Y.1
  • 12
    • 0034383949 scopus 로고    scopus 로고
    • The regulation of protein function by multisite phosphorylation - A 25 year update
    • Cohen P (2000) The regulation of protein function by multisite phosphorylation - a 25 year update. Trends Biochem Sci 25:596-601.
    • (2000) Trends Biochem Sci , vol.25 , pp. 596-601
    • Cohen, P.1
  • 13
    • 0036605185 scopus 로고    scopus 로고
    • Analysis of protein phosphorylation using mass spectrometry: Deciphering the phosphoproteome
    • DOI 10.1016/S0167-7799(02)01944-3, PII S0167779902019443
    • Mann M, et al. (2002) Analysis of protein phosphorylation using mass spectrometry: Deciphering the phosphoproteome. Trends Biotechnol 20:261-268. (Pubitemid 34451062)
    • (2002) Trends in Biotechnology , vol.20 , Issue.6 , pp. 261-268
    • Mann, M.1    Ong, S.-E.2    Gronborg, M.3    Steen, H.4    Jensen, O.N.5    Pandey, A.6
  • 14
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • DOI 10.1038/85686
    • Washburn MP, Wolters D, Yates JR, 3rd (2001) Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat Biotechnol 19:242-247. (Pubitemid 32220565)
    • (2001) Nature Biotechnology , vol.19 , Issue.3 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates, J.R.3
  • 15
    • 0031047981 scopus 로고    scopus 로고
    • Complexes of focal adhesion kinase (FAK) and Crk-associated substrate (p130(Cas)) are elevated in cytoskeleton-associated fractions following adhesion and Src transformation. Requirements for Src kinase activity and FAK proline-rich motifs
    • Polte TR, Hanks SK (1997) Complexes of focal adhesion kinase (FAK) and Crk-associated substrate (p130(Cas)) are elevated in cytoskeleton-associated fractions following adhesion and Src transformation. Requirements for Src kinase activity and FAK proline-rich motifs. J Biol Chem 272:5501-5509.
    • (1997) J Biol Chem , vol.272 , pp. 5501-5509
    • Polte, T.R.1    Hanks, S.K.2
  • 16
    • 33747859675 scopus 로고    scopus 로고
    • BABELOMICS: A systems biology perspective in the functional annotation of genome-scale experiments
    • Al-Shahrour F, et al. (2006) BABELOMICS: A systems biology perspective in the functional annotation of genome-scale experiments. Nucleic Acids Res 34:W472-W476.
    • (2006) Nucleic Acids Res , vol.34
    • Al-Shahrour, F.1
  • 17
    • 0032559562 scopus 로고    scopus 로고
    • CAS/Crk coupling serves as a "molecular switch" for induction of cell migration
    • Klemke RL, et al. (1998) CAS/Crk coupling serves as a "molecular switch" for induction of cell migration. J Cell Biol 140:961-972.
    • (1998) J Cell Biol , vol.140 , pp. 961-972
    • Klemke, R.L.1
  • 18
    • 1642586962 scopus 로고    scopus 로고
    • FAK-Src signalling through paxillin, ERK and MLCK regulates adhesion disassembly
    • Webb DJ, et al. (2004) FAK-Src signalling through paxillin, ERK and MLCK regulates adhesion disassembly. Nat Cell Biol 6:154-161.
    • (2004) Nat Cell Biol , vol.6 , pp. 154-161
    • Webb, D.J.1
  • 19
    • 50249107474 scopus 로고    scopus 로고
    • Paxillin comes of age
    • Deakin NO, Turner CE (2008) Paxillin comes of age. J Cell Sci 121:2435-2444.
    • (2008) J Cell Sci , vol.121 , pp. 2435-2444
    • Deakin, N.O.1    Turner, C.E.2
  • 20
    • 0034529411 scopus 로고    scopus 로고
    • Paxillin interactions
    • Turner CE (2000) Paxillin interactions. J Cell Sci 113:4139-4140.
    • (2000) J Cell Sci , vol.113 , pp. 4139-4140
    • Turner, C.E.1
  • 21
    • 46149093439 scopus 로고    scopus 로고
    • Structural basis for the autoinhibition of talin in regulating integrin activation
    • Goksoy E, et al. (2008) Structural basis for the autoinhibition of talin in regulating integrin activation. Mol Cell 31:124-133.
    • (2008) Mol Cell , vol.31 , pp. 124-133
    • Goksoy, E.1
  • 22
    • 5444239061 scopus 로고    scopus 로고
    • Calpain-mediated proteolysis of talin regulates adhesion dynamics
    • Franco SJ, et al. (2004) Calpain-mediated proteolysis of talin regulates adhesion dynamics. Nat Cell Biol 6:977-983.
    • (2004) Nat Cell Biol , vol.6 , pp. 977-983
    • Franco, S.J.1
  • 23
    • 65449148205 scopus 로고    scopus 로고
    • Talin phosphorylation by Cdk5 regulates Smurf1-mediated talin head ubiquitylation and cell migration
    • Huang C, et al. (2009) Talin phosphorylation by Cdk5 regulates Smurf1-mediated talin head ubiquitylation and cell migration. Nat Cell Biol 11:624-630.
    • (2009) Nat Cell Biol , vol.11 , pp. 624-630
    • Huang, C.1
  • 24
    • 34249320529 scopus 로고    scopus 로고
    • Cortactin is an essential regulator of matrix metalloproteinase secretion and extracellular matrix degradation in invadopodia
    • Clark ES, Whigham AS, Yarbrough WG, Weaver AM (2007) Cortactin is an essential regulator of matrix metalloproteinase secretion and extracellular matrix degradation in invadopodia. Cancer Res 67:4227-4235.
    • (2007) Cancer Res , vol.67 , pp. 4227-4235
    • Clark, E.S.1    Whigham, A.S.2    Yarbrough, W.G.3    Weaver, A.M.4
  • 25
    • 0035475450 scopus 로고    scopus 로고
    • Cortactin: Coupling membrane dynamics to cortical actin assembly
    • Weed SA, Parsons JT (2001) Cortactin: Coupling membrane dynamics to cortical actin assembly. Oncogene 20:6418-6434.
    • (2001) Oncogene , vol.20 , pp. 6418-6434
    • Weed, S.A.1    Parsons, J.T.2
  • 26
    • 33646705915 scopus 로고    scopus 로고
    • The multifunctional GIT family of proteins
    • Hoefen RJ, Berk BC (2006) The multifunctional GIT family of proteins. J Cell Sci 119: 1469-1475.
    • (2006) J Cell Sci , vol.119 , pp. 1469-1475
    • Hoefen, R.J.1    Berk, B.C.2
  • 27
    • 0042622251 scopus 로고    scopus 로고
    • Scansite 2.0: Proteome-wide prediction of cell signaling interactions using short sequence motifs
    • Obenauer JC, Cantley LC, Yaffe MB (2003) Scansite 2.0: Proteome-wide prediction of cell signaling interactions using short sequence motifs. Nucleic Acids Res 31:3635-3641.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3635-3641
    • Obenauer, J.C.1    Cantley, L.C.2    Yaffe, M.B.3
  • 28
    • 0036923947 scopus 로고    scopus 로고
    • Characterization of size-fractionated cDNA libraries generated by the in vitro recombination-assisted method
    • Ohara O, et al. (2002) Characterization of size-fractionated cDNA libraries generated by the in vitro recombination-assisted method. DNA Res 9:47-57.
    • (2002) DNA Res , vol.9 , pp. 47-57
    • Ohara, O.1
  • 29
    • 33646343494 scopus 로고    scopus 로고
    • Deregulation of proteasome function induces Abl-mediated cell death by uncoupling p130CAS and c-CrkII
    • Holcomb M, Rufini A, Barilà D, Klemke RL (2006) Deregulation of proteasome function induces Abl-mediated cell death by uncoupling p130CAS and c-CrkII. J Biol Chem 281:2430-2440.
    • (2006) J Biol Chem , vol.281 , pp. 2430-2440
    • Holcomb, M.1    Rufini, A.2    Barilà, D.3    Klemke, R.L.4
  • 30
    • 0030931217 scopus 로고    scopus 로고
    • Regulation of cell motility by mitogen-activated protein kinase
    • Klemke RL, et al. (1997) Regulation of cell motility by mitogen-activated protein kinase. J Cell Biol 137:481-492.
    • (1997) J Cell Biol , vol.137 , pp. 481-492
    • Klemke, R.L.1
  • 32
    • 36849065315 scopus 로고    scopus 로고
    • Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer
    • Rikova K, et al. (2007) Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell 131:1190-1203.
    • (2007) Cell , vol.131 , pp. 1190-1203
    • Rikova, K.1
  • 33
    • 0037032835 scopus 로고    scopus 로고
    • The protein kinase complement of the human genome
    • DOI 10.1126/science.1075762
    • Manning G, Whyte DB, Martinez R, Hunter T, Sudarsanam S (2002) The protein kinase complement of the human genome. Science 298:1912-1934. (Pubitemid 35425239)
    • (2002) Science , vol.298 , Issue.5600 , pp. 1912-1934
    • Manning, G.1    Whyte, D.B.2    Martinez, R.3    Hunter, T.4    Sudarsanam, S.5
  • 34
    • 0029834447 scopus 로고    scopus 로고
    • Evidence for in vivo phosphorylation of the Grb2 SH2-domain binding site on focal adhesion kinase by Src-family protein-tyrosine kinases
    • Schlaepfer DD, Hunter T (1996) Evidence for in vivo phosphorylation of the Grb2 SH2-domain binding site on focal adhesion kinase by Src-family protein-tyrosine kinases. Mol Cell Biol 16:5623-5633.
    • (1996) Mol Cell Biol , vol.16 , pp. 5623-5633
    • Schlaepfer, D.D.1    Hunter, T.2
  • 35
    • 0032400508 scopus 로고    scopus 로고
    • Autophosphorylation and protein kinase activity of p21-activated protein kinase gamma-PAK are differentially affected by magnesium and manganese
    • DOI 10.1021/bi982103o
    • Tuazon PT, Chinwah M, Traugh JA (1998) Autophosphorylation and protein kinase activity of p21-activated protein kinase gamma-PAK are differentially affected by magnesium and manganese. Biochemistry 37:17024-17029. (Pubitemid 28566781)
    • (1998) Biochemistry , vol.37 , Issue.48 , pp. 17024-17029
    • Tuazon, P.T.1    Chinwah, M.2    Traugh, J.A.3
  • 36
    • 0037044198 scopus 로고    scopus 로고
    • In-gel kinase assay as a method to identify kinase substrates
    • Wooten MW (2002) In-gel kinase assay as a method to identify kinase substrates. Sci STKE 2002:pl15.
    • (2002) Sci STKE , vol.2002
    • Wooten, M.W.1
  • 37
    • 33846781373 scopus 로고    scopus 로고
    • A paxillin tyrosine phosphorylation switch regulates the assembly and form of cell-matrix adhesions
    • DOI 10.1242/jcs.03314
    • Zaidel-Bar R, Milo R, Kam Z, Geiger B (2007) A paxillin tyrosine phosphorylation switch regulates the assembly and form of cell-matrix adhesions. J Cell Sci 120:137-148. (Pubitemid 46206656)
    • (2007) Journal of Cell Science , vol.120 , Issue.1 , pp. 137-148
    • Zaidel-Bar, R.1    Milo, R.2    Kam, Z.3    Geiger, B.4
  • 38
    • 0345306687 scopus 로고    scopus 로고
    • Src phosphorylates Cas on tyrosine 253 to promote migration of transformed cells
    • Goldberg GS, et al. (2003) Src phosphorylates Cas on tyrosine 253 to promote migration of transformed cells. J Biol Chem 278:46533-46540.
    • (2003) J Biol Chem , vol.278 , pp. 46533-46540
    • Goldberg, G.S.1
  • 39
    • 3142619126 scopus 로고    scopus 로고
    • EphB1-mediated cell migration requires the phosphorylation of paxillin at Tyr-31/Tyr-118
    • DOI 10.1074/jbc.M401295200
    • Vindis C, Teli T, Cerretti DP, Turner CE, Huynh-Do U (2004) EphB1-mediated cell migration requires the phosphorylation of paxillin at Tyr-31/Tyr-118. J Biol Chem 279: 27965-27970. (Pubitemid 38900065)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.27 , pp. 27965-27970
    • Vindis, C.1    Teli, T.2    Cerretti, D.P.3    Turner, C.E.4    Huynh-Do, U.5
  • 40
    • 0034610997 scopus 로고    scopus 로고
    • Phosphorylation of tyrosine residues 31 and 118 on paxillin regulates cell migration through an association with CRK in NBT-II cells
    • Petit V, et al. (2000) Phosphorylation of tyrosine residues 31 and 118 on paxillin regulates cell migration through an association with CRK in NBT-II cells. J Cell Biol 148:957-970.
    • (2000) J Cell Biol , vol.148 , pp. 957-970
    • Petit, V.1
  • 41
    • 0029036124 scopus 로고
    • The SH3 domain of Crk binds specifically to a conserved proline-rich motif in Eps15 and Eps15R
    • Schumacher C, et al. (1995) The SH3 domain of Crk binds specifically to a conserved proline-rich motif in Eps15 and Eps15R. J Biol Chem 270:15341-15347.
    • (1995) J Biol Chem , vol.270 , pp. 15341-15347
    • Schumacher, C.1
  • 42
    • 0035902180 scopus 로고    scopus 로고
    • Oncogenic kinase signalling
    • Blume-Jensen P, Hunter T (2001) Oncogenic kinase signalling. Nature 411:355-365.
    • (2001) Nature , vol.411 , pp. 355-365
    • Blume-Jensen, P.1    Hunter, T.2
  • 43
    • 0016318441 scopus 로고
    • Cellular tumorigenicity in nude mice: Correlation with cell growth in semi-solid medium
    • Freedman VH, Shin SI (1974) Cellular tumorigenicity in nude mice: Correlation with cell growth in semi-solid medium. Cell 3:355-359.
    • (1974) Cell , vol.3 , pp. 355-359
    • Freedman, V.H.1    Shin, S.I.2
  • 44
    • 0017402399 scopus 로고
    • In vitro traits of adenovirus-transformed cell lines and their relevance to tumorigenicity in nude mice
    • Gallimore PH, McDougall JK, Chen LB (1977) In vitro traits of adenovirus-transformed cell lines and their relevance to tumorigenicity in nude mice. Cell 10:669-678.
    • (1977) Cell , vol.10 , pp. 669-678
    • Gallimore, P.H.1    McDougall, J.K.2    Chen, L.B.3
  • 45
    • 0006224409 scopus 로고
    • Tumorigenicity of virus-transformed cells in nude mice is correlated specifically with anchorage independent growth in vitro
    • Shin SI, Freedman VH, Risser R, Pollack R (1975) Tumorigenicity of virus-transformed cells in nude mice is correlated specifically with anchorage independent growth in vitro. Proc Natl Acad Sci USA 72:4435-4439.
    • (1975) Proc Natl Acad Sci USA , vol.72 , pp. 4435-4439
    • Shin, S.I.1    Freedman, V.H.2    Risser, R.3    Pollack, R.4
  • 46
    • 34247342742 scopus 로고    scopus 로고
    • Whole body imaging with fluorescent proteins
    • Hoffman RM, Yang M (2006) Whole body imaging with fluorescent proteins. Nat Protoc 1:1429-1438.
    • (2006) Nat Protoc , vol.1 , pp. 1429-1438
    • Hoffman, R.M.1    Yang, M.2
  • 47
    • 3042717667 scopus 로고    scopus 로고
    • Regulation of integrin-mediated cellular responses through assembly of a CAS/Crk scaffold
    • Chodniewicz D, Klemke RL (2004) Regulation of integrin-mediated cellular responses through assembly of a CAS/Crk scaffold. Biochim Biophys Acta 1692:63-76.
    • (2004) Biochim Biophys Acta , vol.1692 , pp. 63-76
    • Chodniewicz, D.1    Klemke, R.L.2
  • 49
    • 0034599542 scopus 로고    scopus 로고
    • Extracellular-regulated kinase activation and CAS/Crk coupling regulate cell migration and suppress apoptosis during invasion of the extracellular matrix
    • Cho SY, Klemke RL (2000) Extracellular-regulated kinase activation and CAS/Crk coupling regulate cell migration and suppress apoptosis during invasion of the extracellular matrix. J Cell Biol 149:223-236.
    • (2000) J Cell Biol , vol.149 , pp. 223-236
    • Cho, S.Y.1    Klemke, R.L.2
  • 50
    • 4644285487 scopus 로고    scopus 로고
    • The prognostic value of BCAR1 in patients with primary breast cancer
    • Dorssers LC, et al. (2004) The prognostic value of BCAR1 in patients with primary breast cancer. Clin Cancer Res 10:6194-6202.
    • (2004) Clin Cancer Res , vol.10 , pp. 6194-6202
    • Dorssers, L.C.1
  • 51
    • 0033797764 scopus 로고    scopus 로고
    • BCAR1/p130Cas expression in untreated and acquired tamoxifen-resistant human breast carcinomas
    • van der Flier S, et al. (2000) BCAR1/p130Cas expression in untreated and acquired tamoxifen-resistant human breast carcinomas. Int J Cancer 89:465-468.
    • (2000) Int J Cancer , vol.89 , pp. 465-468
    • Van Der Flier, S.1
  • 52
    • 0031032777 scopus 로고    scopus 로고
    • Fibronectin-stimulated signaling from a focal adhesion kinase-c-Src complex: Involvement of the Grb2, p130cas, and Nck adaptor proteins
    • Schlaepfer DD, Broome MA, Hunter T (1997) Fibronectin-stimulated signaling from a focal adhesion kinase-c-Src complex: Involvement of the Grb2, p130cas, and Nck adaptor proteins. Mol Cell Biol 17:1702-1713.
    • (1997) Mol Cell Biol , vol.17 , pp. 1702-1713
    • Schlaepfer, D.D.1    Broome, M.A.2    Hunter, T.3
  • 53
    • 0029664531 scopus 로고    scopus 로고
    • Introduction of p130cas signaling complex formation upon integrin-mediated cell adhesion: A role for Src family kinases
    • Vuori K, Hirai H, Aizawa S, Ruoslahti E (1996) Introduction of p130cas signaling complex formation upon integrin-mediated cell adhesion: A role for Src family kinases. Mol Cell Biol 16:2606-2613.
    • (1996) Mol Cell Biol , vol.16 , pp. 2606-2613
    • Vuori, K.1    Hirai, H.2    Aizawa, S.3    Ruoslahti, E.4
  • 54
    • 0035474419 scopus 로고    scopus 로고
    • Functions of the adapter protein Cas: Signal convergence and the determination of cellular responses
    • Bouton AH, Riggins RB, Bruce-Staskal PJ (2001) Functions of the adapter protein Cas: Signal convergence and the determination of cellular responses. Oncogene 20:6448-6458.
    • (2001) Oncogene , vol.20 , pp. 6448-6458
    • Bouton, A.H.1    Riggins, R.B.2    Bruce-Staskal, P.J.3
  • 55
    • 0034769929 scopus 로고    scopus 로고
    • Mechanisms of CAS substrate domain tyrosine phosphorylation by FAK and Src
    • DOI 10.1128/MCB.21.22.7641-7652.2001
    • Ruest PJ, Shin NY, Polte TR, Zhang X, Hanks SK (2001) Mechanisms of CAS substrate domain tyrosine phosphorylation by FAK and Src. Mol Cell Biol 21:7641-7652. (Pubitemid 32988775)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.22 , pp. 7641-7652
    • Ruest, P.J.1    Shin, N.-Y.2    Polte, T.R.3    Zhang, X.4    Hanks, S.K.5
  • 56
    • 21344443681 scopus 로고    scopus 로고
    • Crk-associated substrate tyrosine phosphorylation sites are critical for invasion and metastasis of Src-transformed cells
    • DOI 10.1158/1541-7786.MCR-05-0015
    • Brábek J, et al. (2005) Crk-associated substrate tyrosine phosphorylation sites are critical for invasion and metastasis of SRC-transformed cells. Mol Cancer Res 3:307-315. (Pubitemid 40905622)
    • (2005) Molecular Cancer Research , vol.3 , Issue.6 , pp. 307-315
    • Brabek, J.1    Constancio, S.S.2    Siesser, P.F.3    Shin, N.-Y.4    Pozzi, A.5    Hanks, S.K.6
  • 57
    • 14744267471 scopus 로고    scopus 로고
    • The LIM protein Ajuba influences p130Cas localization and Rac1 activity during cell migration
    • Pratt SJ, et al. (2005) The LIM protein Ajuba influences p130Cas localization and Rac1 activity during cell migration. J Cell Biol 168:813-824.
    • (2005) J Cell Biol , vol.168 , pp. 813-824
    • Pratt, S.J.1
  • 58
    • 53149139896 scopus 로고    scopus 로고
    • Phosphorylation of p130Cas initiates Rac activation and membrane ruffling
    • Sharma A, Mayer BJ (2008) Phosphorylation of p130Cas initiates Rac activation and membrane ruffling. BMC Cell Biol 9:50.
    • (2008) BMC Cell Biol , vol.9 , pp. 50
    • Sharma, A.1    Mayer, B.J.2
  • 59
    • 50249145697 scopus 로고    scopus 로고
    • UPAR promotes formation of the p130Cas-Crk complex to activate Rac through DOCK180
    • Smith HW, Marra P, Marshall CJ (2008) uPAR promotes formation of the p130Cas-Crk complex to activate Rac through DOCK180. J Cell Biol 182:777-790.
    • (2008) J Cell Biol , vol.182 , pp. 777-790
    • Smith, H.W.1    Marra, P.2    Marshall, C.J.3
  • 60
    • 65549140324 scopus 로고    scopus 로고
    • Quantitative phosphoproteomics reveals a cluster of tyrosine kinases that mediates SRC invasive activity in advanced colon carcinoma cells
    • Leroy C, et al. (2009) Quantitative phosphoproteomics reveals a cluster of tyrosine kinases that mediates SRC invasive activity in advanced colon carcinoma cells. Cancer Res 69:2279-2286.
    • (2009) Cancer Res , vol.69 , pp. 2279-2286
    • Leroy, C.1
  • 61
    • 33744549035 scopus 로고    scopus 로고
    • Pragmin, a novel effector of Rnd2 GTPase, stimulates RhoA activity
    • Tanaka H, Katoh H, Negishi M (2006) Pragmin, a novel effector of Rnd2 GTPase, stimulates RhoA activity. J Biol Chem 281:10355-10364.
    • (2006) J Biol Chem , vol.281 , pp. 10355-10364
    • Tanaka, H.1    Katoh, H.2    Negishi, M.3
  • 62
    • 38849098442 scopus 로고    scopus 로고
    • Cancer proliferation gene discovery through functional genomics
    • Schlabach MR, et al. (2008) Cancer proliferation gene discovery through functional genomics. Science 319:620-624.
    • (2008) Science , vol.319 , pp. 620-624
    • Schlabach, M.R.1
  • 63
    • 0037089589 scopus 로고    scopus 로고
    • Short hairpin RNAs (shRNAs) induce sequence-specific silencing in mammalian cells
    • DOI 10.1101/gad.981002
    • Paddison PJ, Caudy AA, Bernstein E, Hannon GJ, Conklin DS (2002) Short hairpin RNAs (shRNAs) induce sequence-specific silencing in mammalian cells. Genes Dev 16:948-958. (Pubitemid 34408544)
    • (2002) Genes and Development , vol.16 , Issue.8 , pp. 948-958
    • Paddison, P.J.1    Caudy, A.A.2    Bernstein, E.3    Hannon, G.J.4    Conklin, D.S.5
  • 64
    • 0038505214 scopus 로고    scopus 로고
    • Cytoplasmic c-Abl provides a molecular 'Rheostat' controlling carcinoma cell survival and invasion
    • Kain KH, Gooch S, Klemke RL (2003) Cytoplasmic c-Abl provides a molecular 'Rheostat' controlling carcinoma cell survival and invasion. Oncogene 22:6071-6080.
    • (2003) Oncogene , vol.22 , pp. 6071-6080
    • Kain, K.H.1    Gooch, S.2    Klemke, R.L.3
  • 65
    • 1642313625 scopus 로고    scopus 로고
    • An imageable highly metastatic orthotopic red fluorescent protein model of pancreatic cancer
    • Katz MH, et al. (2004) An imageable highly metastatic orthotopic red fluorescent protein model of pancreatic cancer. Clin Exp Metastasis 21:7-12.
    • (2004) Clin Exp Metastasis , vol.21 , pp. 7-12
    • Katz, M.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.