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Volumn 11, Issue 23, 2011, Pages 4514-4528

Identifying transient protein-protein interactions in EphB2 signaling by blue native PAGE and mass spectrometry

Author keywords

Animal proteomics; BN PAGE; MS; Protein protein interactions; Signal transduction

Indexed keywords

EPHRIN RECEPTOR B1; EPHRIN RECEPTOR B2; LIGAND; PHOSPHOTYROSINE;

EID: 81855192712     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201000819     Document Type: Article
Times cited : (70)

References (66)
  • 1
    • 0029851690 scopus 로고    scopus 로고
    • Bidirectional signalling through the EPH-family receptor Nuk and its transmembrane ligands
    • Holland, S. J., Gale, N. W., Mbamalu, G., Yancopoulos, G. D. et al., Bidirectional signalling through the EPH-family receptor Nuk and its transmembrane ligands. Nature 1996, 383, 722-725.
    • (1996) Nature , vol.383 , pp. 722-725
    • Holland, S.J.1    Gale, N.W.2    Mbamalu, G.3    Yancopoulos, G.D.4
  • 2
    • 0031947718 scopus 로고    scopus 로고
    • Cell-contact-dependent signalling in axon growth and guidance: Eph receptor tyrosine kinases and receptor protein tyrosine phosphatase beta
    • Holland, S. J., Peles, E., Pawson, T., Schlessinger, J., Cell-contact-dependent signalling in axon growth and guidance: Eph receptor tyrosine kinases and receptor protein tyrosine phosphatase beta. Curr. Opin. Neurobiol. 1998, 8, 117-127.
    • (1998) Curr. Opin. Neurobiol. , vol.8 , pp. 117-127
    • Holland, S.J.1    Peles, E.2    Pawson, T.3    Schlessinger, J.4
  • 3
    • 0035287473 scopus 로고    scopus 로고
    • Multiple roles of EPH receptors and ephrins in neural development
    • Wilkinson, D. G., Multiple roles of EPH receptors and ephrins in neural development. Nat. Rev. Neurosci. 2001, 2, 155-164.
    • (2001) Nat. Rev. Neurosci. , vol.2 , pp. 155-164
    • Wilkinson, D.G.1
  • 4
    • 0033635736 scopus 로고    scopus 로고
    • EphB receptors interact with NMDA receptors and regulate excitatory synapse formation
    • Dalva, M. B., Takasu, M. A., Lin, M. Z., Shamah, S. M. et al., EphB receptors interact with NMDA receptors and regulate excitatory synapse formation. Cell 2000, 103, 945-956.
    • (2000) Cell , vol.103 , pp. 945-956
    • Dalva, M.B.1    Takasu, M.A.2    Lin, M.Z.3    Shamah, S.M.4
  • 5
    • 0030831565 scopus 로고    scopus 로고
    • Roles of Eph receptors and ephrins in neural crest pathfinding
    • Robinson, V., Smith, A., Flenniken, A. M., Wilkinson, D. G., Roles of Eph receptors and ephrins in neural crest pathfinding. Cell Tissue Res. 1997, 290, 265-274.
    • (1997) Cell Tissue Res. , vol.290 , pp. 265-274
    • Robinson, V.1    Smith, A.2    Flenniken, A.M.3    Wilkinson, D.G.4
  • 6
    • 0037272448 scopus 로고    scopus 로고
    • Molecular control of arterial-venous blood vessel identity
    • Adams, R. H., Molecular control of arterial-venous blood vessel identity. J. Anat. 2003, 202, 105-112.
    • (2003) J. Anat. , vol.202 , pp. 105-112
    • Adams, R.H.1
  • 8
    • 33645795212 scopus 로고    scopus 로고
    • Proteomic analysis reveals novel molecules involved in insulin signaling pathway
    • Wang, Y., Li, R., Du, D., Zhang, C. et al., Proteomic analysis reveals novel molecules involved in insulin signaling pathway. J. Proteome Res. 2006, 5, 846-855.
    • (2006) J. Proteome Res. , vol.5 , pp. 846-855
    • Wang, Y.1    Li, R.2    Du, D.3    Zhang, C.4
  • 9
    • 0032577571 scopus 로고    scopus 로고
    • Vasculogenesis, angiogenesis, and growth factors: ephrins enter the fray at the border
    • Yancopoulos, G. D., Klagsbrun, M., Folkman, J., Vasculogenesis, angiogenesis, and growth factors: ephrins enter the fray at the border. Cell 1998, 93, 661-664.
    • (1998) Cell , vol.93 , pp. 661-664
    • Yancopoulos, G.D.1    Klagsbrun, M.2    Folkman, J.3
  • 10
    • 15844429889 scopus 로고    scopus 로고
    • Eph receptors and ligands comprise two major specificity subclasses and are reciprocally compartmentalized during embryogenesis
    • Gale, N. W., Holland, S. J., Valenzuela, D. M., Flenniken, A. et al., Eph receptors and ligands comprise two major specificity subclasses and are reciprocally compartmentalized during embryogenesis. Neuron 1996, 17, 9-19.
    • (1996) Neuron , vol.17 , pp. 9-19
    • Gale, N.W.1    Holland, S.J.2    Valenzuela, D.M.3    Flenniken, A.4
  • 11
    • 0036045804 scopus 로고    scopus 로고
    • EphrinA1-induced cytoskeletal re-organization requires FAK and p130(cas)
    • Carter, N., Nakamoto, T., Hirai, H., Hunter, T., EphrinA1-induced cytoskeletal re-organization requires FAK and p130(cas). Nat. Cell Biol. 2002, 4, 565-573.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 565-573
    • Carter, N.1    Nakamoto, T.2    Hirai, H.3    Hunter, T.4
  • 12
    • 0033785409 scopus 로고    scopus 로고
    • Activation of EphA2 kinase suppresses integrin function and causes focal-adhesion-kinase dephosphorylation
    • Miao, H., Burnett, E., Kinch, M., Simon, E., Wang, B., Activation of EphA2 kinase suppresses integrin function and causes focal-adhesion-kinase dephosphorylation. Nat. Cell Biol. 2000, 2, 62-69.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 62-69
    • Miao, H.1    Burnett, E.2    Kinch, M.3    Simon, E.4    Wang, B.5
  • 13
    • 25144472138 scopus 로고    scopus 로고
    • Eph receptor signalling; dimerisation just isn't enough
    • Vearing, C. J., Lackmann, M., Eph receptor signalling; dimerisation just isn't enough. Growth Factors 2005, 23, 67-76.
    • (2005) Growth Factors , vol.23 , pp. 67-76
    • Vearing, C.J.1    Lackmann, M.2
  • 14
    • 0030891962 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of transmembrane ligands for Eph receptors
    • Bruckner, K., Pasquale, E. B., Klein, R., Tyrosine phosphorylation of transmembrane ligands for Eph receptors. Science 1997, 275, 1640-1643.
    • (1997) Science , vol.275 , pp. 1640-1643
    • Bruckner, K.1    Pasquale, E.B.2    Klein, R.3
  • 15
    • 0035855819 scopus 로고    scopus 로고
    • The SH2/SH3 adaptor Grb4 transduces B-ephrin reverse signals
    • Cowan, C. A., Henkemeyer, M., The SH2/SH3 adaptor Grb4 transduces B-ephrin reverse signals. Nature 2001, 413, 174-179.
    • (2001) Nature , vol.413 , pp. 174-179
    • Cowan, C.A.1    Henkemeyer, M.2
  • 16
    • 20444434349 scopus 로고    scopus 로고
    • Isolation and structural characterization of the Ndh complex from mesophyll and bundle sheath chloroplasts of Zea mays
    • Darie, C. C., Biniossek, M. L., Winter, V., Mutschler, B., Haehnel, W., Isolation and structural characterization of the Ndh complex from mesophyll and bundle sheath chloroplasts of Zea mays. FEBS J. 2005, 272, 2705-2716.
    • (2005) FEBS J. , vol.272 , pp. 2705-2716
    • Darie, C.C.1    Biniossek, M.L.2    Winter, V.3    Mutschler, B.4    Haehnel, W.5
  • 17
    • 38549147576 scopus 로고    scopus 로고
    • Purified trout egg vitelline envelope proteins VEbeta and VEgamma polymerize into homomeric fibrils from dimers in vitro
    • Darie, C. C., Janssen, W. G., Litscher, E. S., Wassarman, P. M., Purified trout egg vitelline envelope proteins VEbeta and VEgamma polymerize into homomeric fibrils from dimers in vitro. Biochim. Biophys. Acta 2008, 1784, 385-392.
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 385-392
    • Darie, C.C.1    Janssen, W.G.2    Litscher, E.S.3    Wassarman, P.M.4
  • 18
    • 0028214450 scopus 로고
    • Analysis of molecular masses and oligomeric states of protein complexes by Blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis
    • Schagger, H., Cramer, W. A., von Jagow, G., Analysis of molecular masses and oligomeric states of protein complexes by Blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis. Anal. Biochem. 1994, 217, 220-230.
    • (1994) Anal. Biochem. , vol.217 , pp. 220-230
    • Schagger, H.1    Cramer, W.A.2    von Jagow, G.3
  • 19
    • 0026409298 scopus 로고
    • Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form
    • Schagger, H., von Jagow, G., Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form. Anal. Biochem. 1991, 199, 223-231.
    • (1991) Anal. Biochem. , vol.199 , pp. 223-231
    • Schagger, H.1    von Jagow, G.2
  • 20
    • 2642529334 scopus 로고    scopus 로고
    • Two-dimensional Blue native/SDS gel electrophoresis of multi-protein complexes from whole cellular lysates: a proteomics approach
    • Camacho-Carvajal, M. M., Wollscheid, B., Aebersold, R., Steimle, V., Schamel, W. W., Two-dimensional Blue native/SDS gel electrophoresis of multi-protein complexes from whole cellular lysates: a proteomics approach. Mol. Cell. Proteomics 2004, 3, 176-182.
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 176-182
    • Camacho-Carvajal, M.M.1    Wollscheid, B.2    Aebersold, R.3    Steimle, V.4    Schamel, W.W.5
  • 21
    • 36849049826 scopus 로고    scopus 로고
    • Purified mouse egg zona pellucida glycoproteins polymerize into homomeric fibrils under non-denaturing conditions
    • Litscher, E. S., Janssen, W. G., Darie, C. C., Wassarman, P. M., Purified mouse egg zona pellucida glycoproteins polymerize into homomeric fibrils under non-denaturing conditions. J. Cell. Physiol. 2008, 214, 153-157.
    • (2008) J. Cell. Physiol. , vol.214 , pp. 153-157
    • Litscher, E.S.1    Janssen, W.G.2    Darie, C.C.3    Wassarman, P.M.4
  • 22
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold, R., Mann, M., Mass spectrometry-based proteomics. Nature 2003, 422, 198-207.
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 25
    • 33644836196 scopus 로고    scopus 로고
    • Quantitative phosphotyrosine proteomics of EphB2 signaling by stable isotope labeling with amino acids in cell culture (SILAC)
    • Zhang, G., Spellman, D. S., Skolnik, E. Y., Neubert, T. A., Quantitative phosphotyrosine proteomics of EphB2 signaling by stable isotope labeling with amino acids in cell culture (SILAC). J. Proteome Res. 2006, 5, 581-588.
    • (2006) J. Proteome Res. , vol.5 , pp. 581-588
    • Zhang, G.1    Spellman, D.S.2    Skolnik, E.Y.3    Neubert, T.A.4
  • 27
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko, A., Wilm, M., Vorm, O., Mann, M., Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal. Chem. 1996, 68, 850-858.
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 28
    • 45749144385 scopus 로고    scopus 로고
    • Stable isotopic labeling by amino acids in cultured primary neurons: application to brain-derived neurotrophic factor-dependent phosphotyrosine-associated signaling
    • Spellman, D. S., Deinhardt, K., Darie, C. C., Chao, M. V., Neubert, T. A., Stable isotopic labeling by amino acids in cultured primary neurons: application to brain-derived neurotrophic factor-dependent phosphotyrosine-associated signaling. Mol. Cell. Proteomics 2008, 7, 1067-1076.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 1067-1076
    • Spellman, D.S.1    Deinhardt, K.2    Darie, C.C.3    Chao, M.V.4    Neubert, T.A.5
  • 29
    • 0141507032 scopus 로고    scopus 로고
    • Complete structure of p97/valosin-containing protein reveals communication between nucleotide domains
    • DeLaBarre, B., Brunger, A. T., Complete structure of p97/valosin-containing protein reveals communication between nucleotide domains. Nat. Struct. Biol. 2003, 10, 856-863.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 856-863
    • DeLaBarre, B.1    Brunger, A.T.2
  • 31
    • 58149382072 scopus 로고    scopus 로고
    • Screening for EphB signaling effectors using SILAC with a linear ion trap-orbitrap mass spectrometer
    • Zhang, G., Fenyo, D., Neubert, T. A., Screening for EphB signaling effectors using SILAC with a linear ion trap-orbitrap mass spectrometer. J. Proteome Res. 2008, 7, 4715-4726.
    • (2008) J. Proteome Res. , vol.7 , pp. 4715-4726
    • Zhang, G.1    Fenyo, D.2    Neubert, T.A.3
  • 32
    • 0028889436 scopus 로고
    • Interaction between focal adhesion kinase and Crk-associated tyrosine kinase substrate p130Cas
    • Polte, T. R., Hanks, S. K., Interaction between focal adhesion kinase and Crk-associated tyrosine kinase substrate p130Cas. Proc. Natl. Acad. Sci. USA 1995, 92, 10678-10682.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10678-10682
    • Polte, T.R.1    Hanks, S.K.2
  • 33
    • 23644446185 scopus 로고    scopus 로고
    • Growth factors induce differential phosphorylation profiles of the Hrs-STAM complex: a common node in signalling networks with signal-specific properties
    • Row, P. E., Clague, M. J., Urbe, S., Growth factors induce differential phosphorylation profiles of the Hrs-STAM complex: a common node in signalling networks with signal-specific properties. Biochem. J. 2005, 389, 629-636.
    • (2005) Biochem. J. , vol.389 , pp. 629-636
    • Row, P.E.1    Clague, M.J.2    Urbe, S.3
  • 34
    • 0038323973 scopus 로고    scopus 로고
    • STAM and Hrs are subunits of a multivalent ubiquitin-binding complex on early endosomes
    • Bache, K. G., Raiborg, C., Mehlum, A., Stenmark, H., STAM and Hrs are subunits of a multivalent ubiquitin-binding complex on early endosomes. J. Biol. Chem. 2003, 278, 12513-12521.
    • (2003) J. Biol. Chem. , vol.278 , pp. 12513-12521
    • Bache, K.G.1    Raiborg, C.2    Mehlum, A.3    Stenmark, H.4
  • 35
    • 79955791663 scopus 로고    scopus 로고
    • Study of neurotrophin-3 signaling in primary cultured neurons using multiplex stable isotope labeling with amino acids in cell culture
    • Zhang, G., Deinhardt, K., Chao, M. V., Neubert, T. A. Study of neurotrophin-3 signaling in primary cultured neurons using multiplex stable isotope labeling with amino acids in cell culture. J. Proteome Res. 2011, 10, 2546-2554.
    • (2011) J. Proteome Res , vol.10 , pp. 2546-2554
    • Zhang, G.1    Deinhardt, K.2    Chao, M.V.3    Neubert, T.A.4
  • 36
    • 2342483041 scopus 로고    scopus 로고
    • Abi1 is essential for the formation and activation of a WAVE2 signalling complex
    • Innocenti, M., Zucconi, A., Disanza, A., Frittoli, E. et al., Abi1 is essential for the formation and activation of a WAVE2 signalling complex. Nat. Cell. Biol. 2004, 6, 319-327.
    • (2004) Nat. Cell. Biol. , vol.6 , pp. 319-327
    • Innocenti, M.1    Zucconi, A.2    Disanza, A.3    Frittoli, E.4
  • 37
    • 0037102301 scopus 로고    scopus 로고
    • Mechanism of regulation of WAVE1-induced actin nucleation by Rac1 and Nck
    • Eden, S., Rohatgi, R., Podtelejnikov, A. V., Mann, M., Kirschner, M. W., Mechanism of regulation of WAVE1-induced actin nucleation by Rac1 and Nck. Nature 2002, 418, 790-793.
    • (2002) Nature , vol.418 , pp. 790-793
    • Eden, S.1    Rohatgi, R.2    Podtelejnikov, A.V.3    Mann, M.4    Kirschner, M.W.5
  • 38
    • 0030905009 scopus 로고    scopus 로고
    • Interaction of Nck-associated protein 1 with activated GTP-binding protein Rac
    • Kitamura, Y., Kitamura, T., Sakaue, H., Maeda, T. et al., Interaction of Nck-associated protein 1 with activated GTP-binding protein Rac. Biochem. J. 1997, 322, 873-878.
    • (1997) Biochem. J. , vol.322 , pp. 873-878
    • Kitamura, Y.1    Kitamura, T.2    Sakaue, H.3    Maeda, T.4
  • 39
    • 0036499989 scopus 로고    scopus 로고
    • The GEX-2 and GEX-3 proteins are required for tissue morphogenesis and cell migrations in C. elegans
    • Soto, M. C., Qadota, H., Kasuya, K., Inoue, M. et al., The GEX-2 and GEX-3 proteins are required for tissue morphogenesis and cell migrations in C. elegans. Genes Dev. 2002, 16, 620-632.
    • (2002) Genes Dev. , vol.16 , pp. 620-632
    • Soto, M.C.1    Qadota, H.2    Kasuya, K.3    Inoue, M.4
  • 40
    • 12844251861 scopus 로고    scopus 로고
    • Abelson-interactor-1 promotes WAVE2 membrane translocation and Abelson-mediated tyrosine phosphorylation required for WAVE2 activation
    • Leng, Y., Zhang, J., Badour, K., Arpaia, E. et al., Abelson-interactor-1 promotes WAVE2 membrane translocation and Abelson-mediated tyrosine phosphorylation required for WAVE2 activation. Proc. Natl. Acad. Sci. USA 2005, 102, 1098-1103.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 1098-1103
    • Leng, Y.1    Zhang, J.2    Badour, K.3    Arpaia, E.4
  • 41
    • 0034282711 scopus 로고    scopus 로고
    • Scar/WAVE-1, a Wiskott-Aldrich syndrome protein, assembles an actin-associated multi-kinase scaffold
    • Westphal, R. S., Soderling, S. H., Alto, N. M., Langeberg, L. K., Scott, J. D., Scar/WAVE-1, a Wiskott-Aldrich syndrome protein, assembles an actin-associated multi-kinase scaffold. EMBO J. 2000, 19, 4589-4600.
    • (2000) EMBO J. , vol.19 , pp. 4589-4600
    • Westphal, R.S.1    Soderling, S.H.2    Alto, N.M.3    Langeberg, L.K.4    Scott, J.D.5
  • 42
    • 0042564472 scopus 로고    scopus 로고
    • Nischarin inhibits Rac induced migration and invasion of epithelial cells by affecting signaling cascades involving PAK
    • Alahari, S. K., Nischarin inhibits Rac induced migration and invasion of epithelial cells by affecting signaling cascades involving PAK. Exp. Cell Res. 2003, 288, 415-424.
    • (2003) Exp. Cell Res. , vol.288 , pp. 415-424
    • Alahari, S.K.1
  • 43
    • 3543034637 scopus 로고    scopus 로고
    • The integrin-binding protein Nischarin regulates cell migration by inhibiting PAK
    • Alahari, S. K., Reddig, P. J., Juliano, R. L., The integrin-binding protein Nischarin regulates cell migration by inhibiting PAK. EMBO J. 2004, 23, 2777-2788.
    • (2004) EMBO J. , vol.23 , pp. 2777-2788
    • Alahari, S.K.1    Reddig, P.J.2    Juliano, R.L.3
  • 44
    • 1342326666 scopus 로고    scopus 로고
    • Cell signaling by imidazoline-1 receptor candidate, IRAS, and the nischarin homologue
    • Piletz, J. E., Wang, G., Zhu, H., Cell signaling by imidazoline-1 receptor candidate, IRAS, and the nischarin homologue. Ann. N Y Acad. Sci. 2003, 1009, 392-399.
    • (2003) Ann. N Y Acad. Sci. , vol.1009 , pp. 392-399
    • Piletz, J.E.1    Wang, G.2    Zhu, H.3
  • 45
    • 0034638831 scopus 로고    scopus 로고
    • Nischarin, a novel protein that interacts with the integrin alpha5 subunit and inhibits cell migration
    • Alahari, S. K., Lee, J. W., Juliano, R. L., Nischarin, a novel protein that interacts with the integrin alpha5 subunit and inhibits cell migration. J. Cell. Biol. 2000, 151, 1141-1154.
    • (2000) J. Cell. Biol. , vol.151 , pp. 1141-1154
    • Alahari, S.K.1    Lee, J.W.2    Juliano, R.L.3
  • 46
    • 0037205482 scopus 로고    scopus 로고
    • Insulin receptor substrate 4 associates with the protein IRAS
    • Sano, H., Liu, S. C., Lane, W. S., Piletz, J. E., Lienhard, G. E., Insulin receptor substrate 4 associates with the protein IRAS. J. Biol. Chem. 2002, 277, 19439-19447.
    • (2002) J. Biol. Chem. , vol.277 , pp. 19439-19447
    • Sano, H.1    Liu, S.C.2    Lane, W.S.3    Piletz, J.E.4    Lienhard, G.E.5
  • 47
    • 24744462314 scopus 로고    scopus 로고
    • Regulation of p21-activated kinase-independent Rac1 signal transduction by nischarin
    • Reddig, P. J., Xu, D., Juliano, R. L., Regulation of p21-activated kinase-independent Rac1 signal transduction by nischarin. J. Biol. Chem. 2005, 280, 30994-31002.
    • (2005) J. Biol. Chem. , vol.280 , pp. 30994-31002
    • Reddig, P.J.1    Xu, D.2    Juliano, R.L.3
  • 48
    • 0034619877 scopus 로고    scopus 로고
    • Crystal structure of Rac1 in complex with the guanine nucleotide exchange region of Tiam1
    • Worthylake, D. K., Rossman, K. L., Sondek, J., Crystal structure of Rac1 in complex with the guanine nucleotide exchange region of Tiam1. Nature 2000, 408, 682-688.
    • (2000) Nature , vol.408 , pp. 682-688
    • Worthylake, D.K.1    Rossman, K.L.2    Sondek, J.3
  • 49
    • 26844559000 scopus 로고    scopus 로고
    • Exponentially modified protein abundance index (emPAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptides per protein
    • Ishihama, Y., Oda, Y., Tabata, T., Sato, T. et al., Exponentially modified protein abundance index (emPAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptides per protein. Mol. Cell. Proteomics 2005, 4, 1265-1272.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1265-1272
    • Ishihama, Y.1    Oda, Y.2    Tabata, T.3    Sato, T.4
  • 50
    • 58149299336 scopus 로고    scopus 로고
    • Significance analysis of spectral count data in label-free shotgun proteomics
    • Choi, H., Fermin, D., Nesvizhskii, A. I., Significance analysis of spectral count data in label-free shotgun proteomics. Mol. Cell. Proteomics 2008, 7, 2373-2385.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 2373-2385
    • Choi, H.1    Fermin, D.2    Nesvizhskii, A.I.3
  • 51
    • 0032510108 scopus 로고    scopus 로고
    • Role of the TFG N-terminus and coiled-coil domain in the transforming activity of the thyroid TRK-T3 oncogene
    • Greco, A., Fusetti, L., Miranda, C., Villa, R. et al., Role of the TFG N-terminus and coiled-coil domain in the transforming activity of the thyroid TRK-T3 oncogene. Oncogene 1998, 16, 809-816.
    • (1998) Oncogene , vol.16 , pp. 809-816
    • Greco, A.1    Fusetti, L.2    Miranda, C.3    Villa, R.4
  • 52
    • 0028805220 scopus 로고
    • The DNA rearrangement that generates the TRK-T3 oncogene involves a novel gene on chromosome 3 whose product has a potential coiled-coil domain
    • Greco, A., Mariani, C., Miranda, C., Lupas, A. et al., The DNA rearrangement that generates the TRK-T3 oncogene involves a novel gene on chromosome 3 whose product has a potential coiled-coil domain. Mol. Cell. Biol. 1995, 15, 6118-6127.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6118-6127
    • Greco, A.1    Mariani, C.2    Miranda, C.3    Lupas, A.4
  • 53
    • 77950939830 scopus 로고    scopus 로고
    • Rearrangements of NTRK1 gene in papillary thyroid carcinoma
    • Greco, A., Miranda, C., Pierotti, M. A., Rearrangements of NTRK1 gene in papillary thyroid carcinoma. Mol. Cell. Endocrinol. 2010, 321, 44-49.
    • (2010) Mol. Cell. Endocrinol. , vol.321 , pp. 44-49
    • Greco, A.1    Miranda, C.2    Pierotti, M.A.3
  • 54
    • 33744904714 scopus 로고    scopus 로고
    • The TFG protein, involved in oncogenic rearrangements, interacts with TANK and NEMO, two proteins involved in the NF-kappaB pathway
    • Miranda, C., Roccato, E., Raho, G., Pagliardini, S. et al., The TFG protein, involved in oncogenic rearrangements, interacts with TANK and NEMO, two proteins involved in the NF-kappaB pathway. J. Cell. Physiol. 2006, 208, 154-160.
    • (2006) J. Cell. Physiol. , vol.208 , pp. 154-160
    • Miranda, C.1    Roccato, E.2    Raho, G.3    Pagliardini, S.4
  • 55
    • 34248651568 scopus 로고    scopus 로고
    • Effect of WAVE2 phosphorylation on activation of the Arp2/3 complex
    • Nakanishi, O., Suetsugu, S., Yamazaki, D., Takenawa, T., Effect of WAVE2 phosphorylation on activation of the Arp2/3 complex. J. Biochem. 2007, 141, 319-325.
    • (2007) J. Biochem. , vol.141 , pp. 319-325
    • Nakanishi, O.1    Suetsugu, S.2    Yamazaki, D.3    Takenawa, T.4
  • 56
    • 1842562381 scopus 로고    scopus 로고
    • Sra-1 and Nap1 link Rac to actin assembly driving lamellipodia formation
    • Steffen, A., Rottner, K., Ehinger, J., Innocenti, M. et al., Sra-1 and Nap1 link Rac to actin assembly driving lamellipodia formation. EMBO J. 2004, 23, 749-759.
    • (2004) EMBO J. , vol.23 , pp. 749-759
    • Steffen, A.1    Rottner, K.2    Ehinger, J.3    Innocenti, M.4
  • 57
    • 0025924674 scopus 로고
    • Activation of tyrosinase kinase and microfilament-binding functions of c-abl by bcr sequences in bcr/abl fusion proteins
    • McWhirter, J. R., Wang, J. Y., Activation of tyrosinase kinase and microfilament-binding functions of c-abl by bcr sequences in bcr/abl fusion proteins. Mol. Cell. Biol. 1991, 11, 1553-1565.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 1553-1565
    • McWhirter, J.R.1    Wang, J.Y.2
  • 58
    • 0029924347 scopus 로고    scopus 로고
    • Nuclear tyrosine kinases: from Abl to WEE1
    • Pendergast, A. M., Nuclear tyrosine kinases: from Abl to WEE1. Curr. Opin. Cell Biol. 1996, 8, 174-181.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 174-181
    • Pendergast, A.M.1
  • 59
    • 0032486386 scopus 로고    scopus 로고
    • Integrins regulate the association and phosphorylation of paxillin by c-Abl
    • Lewis, J. M., Schwartz, M. A., Integrins regulate the association and phosphorylation of paxillin by c-Abl. J. Biol. Chem. 1998, 273, 14225-14230.
    • (1998) J. Biol. Chem. , vol.273 , pp. 14225-14230
    • Lewis, J.M.1    Schwartz, M.A.2
  • 60
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • Hall, A., Rho GTPases and the actin cytoskeleton. Science 1998, 279, 509-514.
    • (1998) Science , vol.279 , pp. 509-514
    • Hall, A.1
  • 61
    • 0032702259 scopus 로고    scopus 로고
    • Regulation of actin polymerization by Arp2/3 complex and WASp/Scar proteins
    • Higgs, H. N., Pollard, T. D., Regulation of actin polymerization by Arp2/3 complex and WASp/Scar proteins. J. Biol. Chem. 1999, 274, 32531-32534.
    • (1999) J. Biol. Chem. , vol.274 , pp. 32531-32534
    • Higgs, H.N.1    Pollard, T.D.2
  • 62
    • 0031952518 scopus 로고    scopus 로고
    • Induction of filopodium formation by a WASP-related actin-depolymerizing protein N-WASP
    • Miki, H., Sasaki, T., Takai, Y., Takenawa, T., Induction of filopodium formation by a WASP-related actin-depolymerizing protein N-WASP. Nature 1998, 391, 93-96.
    • (1998) Nature , vol.391 , pp. 93-96
    • Miki, H.1    Sasaki, T.2    Takai, Y.3    Takenawa, T.4
  • 63
    • 0032403083 scopus 로고    scopus 로고
    • WAVE, a novel WASP-family protein involved in actin reorganization induced by Rac
    • Miki, H., Suetsugu, S., Takenawa, T., WAVE, a novel WASP-family protein involved in actin reorganization induced by Rac. EMBO J. 1998, 17, 6932-6941.
    • (1998) EMBO J. , vol.17 , pp. 6932-6941
    • Miki, H.1    Suetsugu, S.2    Takenawa, T.3
  • 64
    • 0034619847 scopus 로고    scopus 로고
    • IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling
    • Miki, H., Yamaguchi, H., Suetsugu, S., Takenawa, T., IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling. Nature 2000, 408, 732-735.
    • (2000) Nature , vol.408 , pp. 732-735
    • Miki, H.1    Yamaguchi, H.2    Suetsugu, S.3    Takenawa, T.4
  • 65
    • 0037415574 scopus 로고    scopus 로고
    • Mechanism of filopodia initiation by reorganization of a dendritic network
    • Svitkina, T. M., Bulanova, E. A., Chaga, O. Y., Vignjevic, D. M. et al., Mechanism of filopodia initiation by reorganization of a dendritic network. J. Cell. Biol. 2003, 160, 409-421.
    • (2003) J. Cell. Biol. , vol.160 , pp. 409-421
    • Svitkina, T.M.1    Bulanova, E.A.2    Chaga, O.Y.3    Vignjevic, D.M.4
  • 66
    • 44349130374 scopus 로고    scopus 로고
    • Nischarin inhibits LIM kinase to regulate cofilin phosphorylation and cell invasion
    • Ding, Y., Milosavljevic, T., Alahari, S. K., Nischarin inhibits LIM kinase to regulate cofilin phosphorylation and cell invasion. Mol. Cell. Biol. 2008, 28, 3742-3756.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 3742-3756
    • Ding, Y.1    Milosavljevic, T.2    Alahari, S.K.3


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