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Volumn 2, Issue , 2001, Pages

Dimerization of receptor protein-tyrosine phosphatase alpha in living cells

Author keywords

[No Author keywords available]

Indexed keywords

CHIMERIC PROTEIN; CYAN FLUORESCENT PROTEIN; HYBRID PROTEIN; MEMBRANE PROTEIN; MEMBRANE RECEPTOR; MUTANT PROTEIN; PROTEIN TYROSINE PHOSPHATASE; PROTEIN TYROSINE PHOSPHATASE ALPHA; RECEPTOR PROTEIN; UNCLASSIFIED DRUG; YELLOW FLUORESCENT PROTEIN; CELL SURFACE RECEPTOR; CROSS LINKING REAGENT; GREEN FLUORESCENT PROTEIN; LEUKOCYTE COMMON ANTIGEN RELATED PHOSPHATASE; LEUKOCYTE COMMON ANTIGEN-RELATED PHOSPHATASE; PHOTOPROTEIN;

EID: 18744408187     PISSN: 14712121     EISSN: None     Source Type: Journal    
DOI: 10.1186/1471-2121-2-8     Document Type: Article
Times cited : (80)

References (57)
  • 1
    • 0028838971 scopus 로고
    • Protein kinases and phosphatases: The yin and yang of protein phosphorylation and signaling
    • Hunter T: Protein kinases and phosphatases: the yin and yang of protein phosphorylation and signaling. Cell 1995, 80:225-236
    • (1995) Cell , vol.80 , pp. 225-236
    • Hunter, T.1
  • 2
    • 0033167111 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatases in development
    • den Hertog J: Protein-tyrosine phosphatases in development. Mech. Dev. 1999, 85:3-14
    • (1999) Mech. Dev. , vol.85 , pp. 3-14
    • den Hertog, J.1
  • 3
    • 0030953448 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases in signal transduction
    • Neel BG, Tonks NK: Protein tyrosine phosphatases in signal transduction. Curr. Opin. Cell Biol. 1997, 9:193-204
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 193-204
    • Neel, B.G.1    Tonks, N.K.2
  • 5
    • 0034646459 scopus 로고    scopus 로고
    • Pleiotrophin signals increased tyrosine phosphorylation of beta beta-catenin through inactivation of the intrinsic catalytic activity of the receptor-type protein tyrosine phosphatase beta/zeta
    • Meng K, Rodriguez-Pena A, Dimitrov T, Chen W, Yamin M, Noda M, Deuel TF: Pleiotrophin signals increased tyrosine phosphorylation of beta beta-catenin through inactivation of the intrinsic catalytic activity of the receptor-type protein tyrosine phosphatase beta/zeta. Proc. Natl. Acad. Sci. U.S.A. 2000, 97:2603-2608
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 2603-2608
    • Meng, K.1    Rodriguez-Pena, A.2    Dimitrov, T.3    Chen, W.4    Yamin, M.5    Noda, M.6    Deuel, T.F.7
  • 6
    • 0028104202 scopus 로고
    • Regulation of signal transduction and signal diversity by receptor oligomerization
    • Lemmon MA, Schlessinger J: Regulation of signal transduction and signal diversity by receptor oligomerization. Trends. Biochem. Sci. 1994, 19:459-463
    • (1994) Trends. Biochem. Sci. , vol.19 , pp. 459-463
    • Lemmon, M.A.1    Schlessinger, J.2
  • 7
    • 0032493859 scopus 로고    scopus 로고
    • Switching signals on or off by receptor dimerization
    • Weiss A, Schlessinger J: Switching signals on or off by receptor dimerization. Cell 1998, 94:277-280
    • (1998) Cell , vol.94 , pp. 277-280
    • Weiss, A.1    Schlessinger, J.2
  • 8
    • 0028231388 scopus 로고
    • Crystal structure of human protein tyrosine phosphatase 1B
    • Barford D, Flint AJ, Tonks NK: Crystal structure of human protein tyrosine phosphatase 1B. Science 1994, 263:1397-1404
    • (1994) Science , vol.263 , pp. 1397-1404
    • Barford, D.1    Flint, A.J.2    Tonks, N.K.3
  • 9
    • 0029759927 scopus 로고    scopus 로고
    • Structural basis for inhibition of receptor protein-tyrosine phosphatase-alpha by dimerization
    • Bilwes AM, den Hertog J, Hunter T, Noel JP: Structural basis for inhibition of receptor protein-tyrosine phosphatase-alpha by dimerization. Nature 1996, 382:555-559
    • (1996) Nature , vol.382 , pp. 555-559
    • Bilwes, A.M.1    den Hertog, J.2    Hunter, T.3    Noel, J.P.4
  • 11
    • 0030735366 scopus 로고    scopus 로고
    • The crystal structure of domain 1 of receptor protein-tyrosine phosphatase mu
    • Hoffmann KM, Tonks NK, Barford D: The crystal structure of domain 1 of receptor protein-tyrosine phosphatase mu. J. Biol. Chem. 1997, 272:27505-27508
    • (1997) J. Biol. Chem. , vol.272 , pp. 27505-27508
    • Hoffmann, K.M.1    Tonks, N.K.2    Barford, D.3
  • 12
    • 0033553515 scopus 로고    scopus 로고
    • Crystal structure of the tandem phosphatase domains of RPTP LAR
    • Nam HJ, Poy F, Krueger NX, Saito H, Frederick CA: Crystal structure of the tandem phosphatase domains of RPTP LAR. Cell 1999, 97:449-457
    • (1999) Cell , vol.97 , pp. 449-457
    • Nam, H.J.1    Poy, F.2    Krueger, N.X.3    Saito, H.4    Frederick, C.A.5
  • 13
    • 0028122711 scopus 로고
    • Crystal structure of Yersinia protein tyrosine phosphatase at 2.5 A and the complex with tungstate
    • Stuckey JA, Schubert HL, Fauman EB, Zhang ZY, Dixon JE, Saper MA: Crystal structure of Yersinia protein tyrosine phosphatase at 2.5 A and the complex with tungstate. Nature 1994, 370:571-575
    • (1994) Nature , vol.370 , pp. 571-575
    • Stuckey, J.A.1    Schubert, H.L.2    Fauman, E.B.3    Zhang, Z.Y.4    Dixon, J.E.5    Saper, M.A.6
  • 14
    • 0032561478 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domain of protein-tyrosine phosphatase SHP-1
    • Yang J, Liang X, Niu T, Meng W, Zhao Z, Zhou GW: Crystal structure of the catalytic domain of protein-tyrosine phosphatase SHP-1. J. Biol. Chem. 1998, 273:28199-28207
    • (1998) J. Biol. Chem. , vol.273 , pp. 28199-28207
    • Yang, J.1    Liang, X.2    Niu, T.3    Meng, W.4    Zhao, Z.5    Zhou, G.W.6
  • 15
    • 0027266773 scopus 로고
    • Ligand-mediated negative regulation of a chimeric transmembrane receptor tyrosine phosphatase
    • Desai DM, Sap J, Schlessinger J, Weiss A: Ligand-mediated negative regulation of a chimeric transmembrane receptor tyrosine phosphatase. Cell 1993, 73:541-554
    • (1993) Cell , vol.73 , pp. 541-554
    • Desai, D.M.1    Sap, J.2    Schlessinger, J.3    Weiss, A.4
  • 16
    • 0032472226 scopus 로고    scopus 로고
    • Dimerization-induced inhibition of receptor protein tyrosine phosphatase function through an inhibitory wedge
    • Majeti R, Bilwes AM, Noel JP, Hunter T, Weiss A: Dimerization-induced inhibition of receptor protein tyrosine phosphatase function through an inhibitory wedge. Science 1998, 279:88-91
    • (1998) Science , vol.279 , pp. 88-91
    • Majeti, R.1    Bilwes, A.M.2    Noel, J.P.3    Hunter, T.4    Weiss, A.5
  • 17
    • 0034704180 scopus 로고    scopus 로고
    • An Inactivating Point Mutation in the Inhibitory Wedge of CD45 Causes Lymphoproliferation and Autoimmunity
    • Majeti R, Xu Z, Parslow TG, Olson JL, Daikh DI, Killeen N, Weiss A: An Inactivating Point Mutation in the Inhibitory Wedge of CD45 Causes Lymphoproliferation and Autoimmunity. Cell 2000, 103:1059-1070
    • (2000) Cell , vol.103 , pp. 1059-1070
    • Majeti, R.1    Xu, Z.2    Parslow, T.G.3    Olson, J.L.4    Daikh, D.I.5    Killeen, N.6    Weiss, A.7
  • 18
    • 0027329003 scopus 로고
    • Receptor protein tyrosine phosphatase alpha activates pp60c-src and is involved in neuronal differentiation
    • den Hertog J, Pals CE, Peppelenbosch MP, Tertoolen LG, de Laat SW, Kruijer W: Receptor protein tyrosine phosphatase alpha activates pp60c-src and is involved in neuronal differentiation. EMBO J. 1993, 12:3789-3798
    • (1993) EMBO J. , vol.12 , pp. 3789-3798
    • den Hertog, J.1    Pals, C.E.2    Peppelenbosch, M.P.3    Tertoolen, L.G.4    de Laat, S.W.5    Kruijer, W.6
  • 19
    • 0033587177 scopus 로고    scopus 로고
    • Targeted disruption of the tyrosine phosphatase PTPalpha leads to constitutive downregulation of the kinases Src and Fyn
    • Ponniah S, Wang DZ, Lim KL, Pallen CJ: Targeted disruption of the tyrosine phosphatase PTPalpha leads to constitutive downregulation of the kinases Src and Fyn. Curr. Biol. 1999, 9:535-538
    • (1999) Curr. Biol. , vol.9 , pp. 535-538
    • Ponniah, S.1    Wang, D.Z.2    Lim, K.L.3    Pallen, C.J.4
  • 20
    • 0033587069 scopus 로고    scopus 로고
    • Receptor protein tyrosine phosphatase alpha activates Src-family kinases and controls integrin-mediated responses in fibroblasts
    • Su J, Muranjan M, Sap J: Receptor protein tyrosine phosphatase alpha activates Src-family kinases and controls integrin-mediated responses in fibroblasts. Curr. Biol. 1999, 9:505-511
    • (1999) Curr. Biol. , vol.9 , pp. 505-511
    • Su, J.1    Muranjan, M.2    Sap, J.3
  • 21
    • 0026705734 scopus 로고
    • Cell transformation and activation of pp60c-src by overexpression of a protein tyrosine phosphatase
    • Zheng XM, Wang Y, Pallen CJ: Cell transformation and activation of pp60c-src by overexpression of a protein tyrosine phosphatase. Nature 1992, 359:336-339
    • (1992) Nature , vol.359 , pp. 336-339
    • Zheng, X.M.1    Wang, Y.2    Pallen, C.J.3
  • 22
    • 0034161405 scopus 로고    scopus 로고
    • A phosphotyrosine displacement mechanism for activation of Src by PTPalpha
    • Zheng XM, Resnick RJ, Shalloway D: A phosphotyrosine displacement mechanism for activation of Src by PTPalpha. EMBO J. 2000, 19:964-978
    • (2000) EMBO J. , vol.19 , pp. 964-978
    • Zheng, X.M.1    Resnick, R.J.2    Shalloway, D.3
  • 23
    • 0033533817 scopus 로고    scopus 로고
    • Dimerization inhibits the activity of receptor-like protein-tyrosine phosphatase-alpha
    • Jiang G, den Hertog J, Su J, Noel J, Sap J, Hunter T: Dimerization inhibits the activity of receptor-like protein-tyrosine phosphatase-alpha. Nature 1999, 401:606-610
    • (1999) Nature , vol.401 , pp. 606-610
    • Jiang, G.1    den Hertog, J.2    Su, J.3    Noel, J.4    Sap, J.5    Hunter, T.6
  • 24
    • 0033859771 scopus 로고    scopus 로고
    • Receptor-like Protein Tyrosine Phosphatase alpha homodimerizes on the cell surface
    • Jiang G, den Hertog J, Hunter T: Receptor-like Protein Tyrosine Phosphatase alpha homodimerizes on the cell surface. Mol. Cell Biol. 2000, 20:5917-5929
    • (2000) Mol. Cell Biol. , vol.20 , pp. 5917-5929
    • Jiang, G.1    den Hertog, J.2    Hunter, T.3
  • 25
    • 1842563953 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer
    • Clegg RM: Fluorescence resonance energy transfer.1996179-252
    • (1996) , pp. 179-252
    • Clegg, R.M.1
  • 26
    • 0028913136 scopus 로고
    • Fluorescence resonance energy transfer
    • Selvin PR: Fluorescence resonance energy transfer. Meth. Enzymol. 1995, 246:300-334
    • (1995) Meth. Enzymol. , vol.246 , pp. 300-334
    • Selvin, P.R.1
  • 27
    • 0028295796 scopus 로고
    • Resonance energy transfer: Methods and applications
    • Wu P, Brand L: Resonance energy transfer: methods and applications. Anal. Biochem. 1994, 218:1-13
    • (1994) Anal. Biochem. , vol.218 , pp. 1-13
    • Wu, P.1    Brand, L.2
  • 29
    • 0033083490 scopus 로고    scopus 로고
    • Using GFP in FRET-based applications
    • Pollok BA, Heim R: Using GFP in FRET-based applications. Trends. Cell Biol. 1999, 9:57-60
    • (1999) Trends. Cell Biol. , vol.9 , pp. 57-60
    • Pollok, B.A.1    Heim, R.2
  • 31
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescent protein
    • Tsien RY: The green fluorescent protein. Annu. Rev. Biochem. 1998, 67:509-544
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 509-544
    • Tsien, R.Y.1
  • 32
    • 0031865351 scopus 로고    scopus 로고
    • Bcl-2 and Bax interactions in mitochondria probed with green fluorescent protein and fluorescence resonance energy transfer
    • Mahajan NP, Linder K, Berry G, Gordon GW, Heim R, Herman B: Bcl-2 and Bax interactions in mitochondria probed with green fluorescent protein and fluorescence resonance energy transfer. Nat. Biotechnol. 1998, 16:547-552
    • (1998) Nat. Biotechnol. , vol.16 , pp. 547-552
    • Mahajan, N.P.1    Linder, K.2    Berry, G.3    Gordon, G.W.4    Heim, R.5    Herman, B.6
  • 33
    • 0032161918 scopus 로고    scopus 로고
    • Visualization of Pit-1 transcription factor interactions in the living cell nucleus by fluorescence resonance energy transfer microscopy
    • Day RN: Visualization of Pit-1 transcription factor interactions in the living cell nucleus by fluorescence resonance energy transfer microscopy. Mol. Endocrinol. 1998, 12:1410-1419
    • (1998) Mol. Endocrinol. , vol.12 , pp. 1410-1419
    • Day, R.N.1
  • 34
    • 0033966543 scopus 로고    scopus 로고
    • Mapping interactions between nuclear transport factors in living cells reveals pathways through the nuclear pore complex
    • Damelin M, Silver PA: Mapping interactions between nuclear transport factors in living cells reveals pathways through the nuclear pore complex. Mol. Cell 2000, 5:133-140
    • (2000) Mol. Cell , vol.5 , pp. 133-140
    • Damelin, M.1    Silver, P.A.2
  • 35
    • 0034704906 scopus 로고    scopus 로고
    • G-protein-coupled receptors function as oligomers in vivo
    • Overton MC, Blumer KJ: G-protein-coupled receptors function as oligomers in vivo. Curr. Biol. 2000, 10:341-344
    • (2000) Curr. Biol. , vol.10 , pp. 341-344
    • Overton, M.C.1    Blumer, K.J.2
  • 36
    • 0034597554 scopus 로고    scopus 로고
    • Interaction of EGF receptor and grb2 in living cells visualized by fluorescence resonance energy transfer (FRET) microscopy
    • Sorkin A, McClure M, Huang F, Carter R: Interaction of EGF receptor and grb2 in living cells visualized by fluorescence resonance energy transfer (FRET) microscopy. Curr. Biol. 2000, 10:1395-1398
    • (2000) Curr. Biol. , vol.10 , pp. 1395-1398
    • Sorkin, A.1    McClure, M.2    Huang, F.3    Carter, R.4
  • 37
    • 0342547337 scopus 로고    scopus 로고
    • Microspectroscopic imaging of nodulation factor-binding sites on living Vicia sativa roots using a novel bioactive fluorescent nodulation factor
    • Gadella TWJ, Vereb GJ, Hadri AE, Rohrig H, Schmidt J, John M, Schell J, Bisseling T: Microspectroscopic imaging of nodulation factor-binding sites on living Vicia sativa roots using a novel bioactive fluorescent nodulation factor. Biophys. J. 1997, 72:1986-1996
    • (1997) Biophys. J. , vol.72 , pp. 1986-1996
    • Gadella, T.W.J.1    Vereb, G.J.2    Hadri, A.E.3    Rohrig, H.4    Schmidt, J.5    John, M.6    Schell, J.7    Bisseling, T.8
  • 40
    • 0034724720 scopus 로고    scopus 로고
    • Multiple interactions between receptor protein-tyrosine phosphatase (RPTP) alpha and membrane-distal protein-tyrosine phosphatase domains of various RPTPs
    • Blanchetot C, den Hertog J: Multiple interactions between receptor protein-tyrosine phosphatase (RPTP) alpha and membrane-distal protein-tyrosine phosphatase domains of various RPTPs. J. Biol. Chem. 2000, 275:12446-12452
    • (2000) J. Biol. Chem. , vol.275 , pp. 12446-12452
    • Blanchetot, C.1    den Hertog, J.2
  • 41
    • 0034686081 scopus 로고    scopus 로고
    • Intramolecular interactions between the juxtamembrane domain and phosphatase domains of receptor protein-tyrosine phosphatase RPTPmu. Regulation of catalytic activity
    • Feiken E, van EI, Gebbink MF, Moolenaar WH, Zondag GC: Intramolecular interactions between the juxtamembrane domain and phosphatase domains of receptor protein-tyrosine phosphatase RPTPmu. Regulation of catalytic activity. J. Biol. Chem. 2000, 275:15350-15356
    • (2000) J. Biol. Chem. , vol.275 , pp. 15350-15356
    • Feiken, E.1    van, E.I.2    Gebbink, M.F.3    Moolenaar, W.H.4    Zondag, G.C.5
  • 42
    • 0032504217 scopus 로고    scopus 로고
    • Characterization of recombinant CD45 cytoplasmic domain proteins. Evidence for intramolecular and intermolecular interactions
    • Felberg J, Johnson P: Characterization of recombinant CD45 cytoplasmic domain proteins. Evidence for intramolecular and intermolecular interactions. J. Biol. Chem. 1998, 273:17839-17845
    • (1998) J. Biol. Chem. , vol.273 , pp. 17839-17845
    • Felberg, J.1    Johnson, P.2
  • 43
    • 0031893012 scopus 로고    scopus 로고
    • The second catalytic domain of protein tyrosine phosphatase delta (PTP delta) binds to and inhibits the first catalytic domain of PTP sigma
    • Wallace MJ, Fladd C, Batt J, Rotin D: The second catalytic domain of protein tyrosine phosphatase delta (PTP delta) binds to and inhibits the first catalytic domain of PTP sigma. Mol. Cell Biol. 1998, 18:2608-2616
    • (1998) Mol. Cell Biol. , vol.18 , pp. 2608-2616
    • Wallace, M.J.1    Fladd, C.2    Batt, J.3    Rotin, D.4
  • 44
    • 0026714979 scopus 로고
    • Evidence for monomeric and dimeric forms of CD45 associated with a 30- kDa phosphorylated protein
    • Takeda A, Wu JJ, Maizel AL: Evidence for monomeric and dimeric forms of CD45 associated with a 30- kDa phosphorylated protein. J. Biol. Chem. 1992, 267:16651-16659
    • (1992) J. Biol. Chem. , vol.267 , pp. 16651-16659
    • Takeda, A.1    Wu, J.J.2    Maizel, A.L.3
  • 45
    • 0028283506 scopus 로고
    • Multiple forms of the human tyrosine phosphatase RPTP alpha. Isozymes and differences in glycosylation
    • Daum G, Regenass S, Sap J, Schlessinger J, Fischer EH: Multiple forms of the human tyrosine phosphatase RPTP alpha. Isozymes and differences in glycosylation. J. Biol. Chem. 1994, 269:10524-10528
    • (1994) J. Biol. Chem. , vol.269 , pp. 10524-10528
    • Daum, G.1    Regenass, S.2    Sap, J.3    Schlessinger, J.4    Fischer, E.H.5
  • 46
    • 0027296921 scopus 로고
    • Homophilic binding of PTP mu, a receptor-type protein tyrosine phosphatase, can mediate cell-cell aggregation
    • Brady-Kalnay SM, Flint AJ, Tonks NK: Homophilic binding of PTP mu, a receptor-type protein tyrosine phosphatase, can mediate cell-cell aggregation. J. Cell Biol. 1993, 122:961-972
    • (1993) J. Cell Biol. , vol.122 , pp. 961-972
    • Brady-Kalnay, S.M.1    Flint, A.J.2    Tonks, N.K.3
  • 48
    • 15444357989 scopus 로고    scopus 로고
    • The laminin-nidogen complex is a ligand for a specific splice isoform of the transmembrane protein tyrosine phosphatase LAR
    • O'Grady P, Thai TC, Saito H: The laminin-nidogen complex is a ligand for a specific splice isoform of the transmembrane protein tyrosine phosphatase LAR. J. Cell Biol. 1998, 141:1675-1684
    • (1998) J. Cell Biol. , vol.141 , pp. 1675-1684
    • O'Grady, P.1    Thai, T.C.2    Saito, H.3
  • 49
    • 0029096048 scopus 로고
    • The carbonic anhydrase domain of receptor tyrosine phosphatase beta is a functional ligand for the axonal cell recognition molecule contactin
    • Peles E, Nativ M, Campbell PL, Sakurai T, Martinez R, Lev S, Clary DO, Schilling J, Barnea G, Plowman GD: The carbonic anhydrase domain of receptor tyrosine phosphatase beta is a functional ligand for the axonal cell recognition molecule contactin. Cell 1995, 82:251-260
    • (1995) Cell , vol.82 , pp. 251-260
    • Peles, E.1    Nativ, M.2    Campbell, P.L.3    Sakurai, T.4    Martinez, R.5    Lev, S.6    Clary, D.O.7    Schilling, J.8    Barnea, G.9    Plowman, G.D.10
  • 50
    • 0033571032 scopus 로고    scopus 로고
    • Protein Tyrosine Phosphatase alpha (PTPalpha) and Contactin Form a Novel Neuronal Receptor Complex Linked to the Intracellular Tyrosine Kinase fyn
    • Zeng L, D'Alessandri L, Kalousek MB, Vaughan L, Pallen CJ: Protein Tyrosine Phosphatase alpha (PTPalpha) and Contactin Form a Novel Neuronal Receptor Complex Linked to the Intracellular Tyrosine Kinase fyn. J. Cell Biol. 1999, 147:707-714
    • (1999) J. Cell Biol. , vol.147 , pp. 707-714
    • Zeng, L.1    D'Alessandri, L.2    Kalousek, M.B.3    Vaughan, L.4    Pallen, C.J.5
  • 51
    • 0029010607 scopus 로고
    • Oligomerization of epidermal growth factor receptors on A431 cells studied by time-resolved fluorescence imaging microscopy. A stereochemical model for tyrosine kinase receptor activation
    • Gadella TWJ, Jovin TM: Oligomerization of epidermal growth factor receptors on A431 cells studied by time-resolved fluorescence imaging microscopy. A stereochemical model for tyrosine kinase receptor activation. J. Cell Biol. 1995, 129:1543-1558
    • (1995) J. Cell Biol. , vol.129 , pp. 1543-1558
    • Gadella, T.W.J.1    Jovin, T.M.2
  • 52
    • 0033615077 scopus 로고    scopus 로고
    • When dimerization is not enough
    • Jiang G, Hunter T: When dimerization is not enough. Curr. Biol. 1999, 9:R568-R571
    • (1999) Curr. Biol. , vol.9
    • Jiang, G.1    Hunter, T.2
  • 53
    • 0028945421 scopus 로고
    • Stimulation of receptor protein-tyrosine phosphatase alpha activity and phosphorylation by phorbol ester
    • den Hertog J, Sap J, Pals CE, Schlessinger J, Kruijer W: Stimulation of receptor protein-tyrosine phosphatase alpha activity and phosphorylation by phorbol ester. Cell Growth Differ. 1995, 6:303-307
    • (1995) Cell Growth Differ , vol.6 , pp. 303-307
    • den Hertog, J.1    Sap, J.2    Pals, C.E.3    Schlessinger, J.4    Kruijer, W.5
  • 54
    • 0028933161 scopus 로고
    • The receptor-like protein-tyrosine phosphatase, RPTP alpha, is phosphorylated by protein kinase C on two serines close to the inner face of the plasma membrane
    • Tracy S, van der Geer P, Hunter T: The receptor-like protein-tyrosine phosphatase, RPTP alpha, is phosphorylated by protein kinase C on two serines close to the inner face of the plasma membrane. J. Biol. Chem. 1995, 270:10587-10594
    • (1995) J. Biol. Chem. , vol.270 , pp. 10587-10594
    • Tracy, S.1    van der Geer, P.2    Hunter, T.3
  • 55
    • 0029949837 scopus 로고    scopus 로고
    • Tight association of GRB2 with receptor protein-tyrosine phosphatase alpha is mediated by the SH2 and C-terminal SH3 domains
    • den Hertog J, Hunter T: Tight association of GRB2 with receptor protein-tyrosine phosphatase alpha is mediated by the SH2 and C-terminal SH3 domains. EMBO J. 1996, 15:3016-3027
    • (1996) EMBO J. , vol.15 , pp. 3016-3027
    • den Hertog, J.1    Hunter, T.2
  • 57
    • 0028285788 scopus 로고
    • Phosphorylation of receptor protein-tyrosine phosphatase alpha on Tyr789, a binding site for the SH3-SH2-SH3 adaptor protein GRB-2 in vivo
    • den Hertog J, Tracy S, Hunter T: Phosphorylation of receptor protein-tyrosine phosphatase alpha on Tyr789, a binding site for the SH3-SH2-SH3 adaptor protein GRB-2 in vivo. EMBO J. 1994, 13:3020-3032
    • (1994) EMBO J. , vol.13 , pp. 3020-3032
    • den Hertog, J.1    Tracy, S.2    Hunter, T.3


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