메뉴 건너뛰기




Volumn 3, Issue 2, 2014, Pages 304-330

Mechanisms of activation of receptor tyrosine kinases: Monomers or dimers

Author keywords

BDNF; Cancer; Dimerization; EGFR; IGF; Ligand; NGF; Phosphorylation; Rotation twist; Transmembrane signaling; Trk

Indexed keywords

BRAIN DERIVED NEUROTROPHIC FACTOR RECEPTOR; DIMER; EPIDERMAL GROWTH FACTOR RECEPTOR; HETERODIMER; INSULIN RECEPTOR; ISOENZYME; MONOMER; NEUROTROPHIN 3 RECEPTOR; NEUROTROPHIN RECEPTOR; PROTEIN TYROSINE KINASE; PROTEIN TYROSINE KINASE A; TYROSINE;

EID: 84908268069     PISSN: None     EISSN: 20734409     Source Type: Journal    
DOI: 10.3390/cells3020304     Document Type: Review
Times cited : (154)

References (213)
  • 1
    • 0035902180 scopus 로고    scopus 로고
    • Oncogenic kinase signaling
    • Blume-Jensen, P.; Hunter, T. Oncogenic kinase signaling. Nature 2001, 411, 355-365.
    • (2001) Nature , vol.411 , pp. 355-365
    • Blume-Jensen, P.1    Hunter, T.2
  • 2
    • 4444371652 scopus 로고    scopus 로고
    • Temporal analysis of phosphotyrosine-dependent signaling networks by quantitative proteomics
    • Blagoev, B.; Ong, S. E.; Kratchmarova, I.; Mann, M. Temporal analysis of phosphotyrosine-dependent signaling networks by quantitative proteomics. Nat. Biotechnol. 2004, 22, 1139-1145.
    • (2004) Nat. Biotechnol , vol.22 , pp. 1139-1145
    • Blagoev, B.1    Ong, S.E.2    Kratchmarova, I.3    Mann, M.4
  • 3
    • 84874009500 scopus 로고    scopus 로고
    • Receptor tyrosine kinase signaling mechanisms: Devolving TrkA responses with phosphoproteomics
    • Bradshaw, R. A.; Chalkley, R. J.; Biarc, J.; Burlingame, A. L. Receptor tyrosine kinase signaling mechanisms: Devolving TrkA responses with phosphoproteomics. Adv. Biol. Regul. 2013, 53, 87-96.
    • (2013) Adv. Biol. Regul , vol.53 , pp. 87-96
    • Bradshaw, R.A.1    Chalkley, R.J.2    Biarc, J.3    Burlingame, A.L.4
  • 4
    • 0026701674 scopus 로고
    • A highly conserved tyrosine residue at codon 845 within the kinase domain is not required for the transforming activity of human epidermal growth factor receptor
    • Gotoh, N.; Tojo, A.; Hino, M.; Yazaki, Y.; Shibuya, M. A highly conserved tyrosine residue at codon 845 within the kinase domain is not required for the transforming activity of human epidermal growth factor receptor. Biochem. Biophys. Res. Commun. 1992, 186, 768-774.
    • (1992) Biochem. Biophys. Res. Commun , vol.186 , pp. 768-774
    • Gotoh, N.1    Tojo, A.2    Hino, M.3    Yazaki, Y.4    Shibuya, M.5
  • 5
    • 0033786922 scopus 로고    scopus 로고
    • Protein tyrosine kinase structure and function
    • Hubbard, S. R.; Till, J. H. Protein tyrosine kinase structure and function. Annu. Rev. Biochem. 2000, 69, 373-398.
    • (2000) Annu. Rev. Biochem , vol.69 , pp. 373-398
    • Hubbard, S.R.1    Till, J.H.2
  • 6
    • 0036769119 scopus 로고    scopus 로고
    • Regulation and targets of receptor tyrosine kinases
    • Pawson, T. Regulation and targets of receptor tyrosine kinases. Eur. J. Cancer 2002, 38, S3-S10.
    • (2002) Eur. J. Cancer , vol.38
    • Pawson, T.1
  • 7
    • 77953896432 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Lemmon, M. A.; Schlessinger, J. Cell signaling by receptor tyrosine kinases. Cell 2010, 141, 1117-1134.
    • (2010) Cell , vol.141 , pp. 1117-1134
    • Lemmon, M.A.1    Schlessinger, J.2
  • 8
    • 0034644539 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Schlessinger, J. Cell signaling by receptor tyrosine kinases. Cell 2000, 103, 211-225.
    • (2000) Cell , vol.103 , pp. 211-225
    • Schlessinger, J.1
  • 9
    • 0025343230 scopus 로고
    • Signal transduction by receptors with tyrosine kinase activity
    • Ullrich, A.; Schlessinger, J. Signal transduction by receptors with tyrosine kinase activity. Cell 1990, 61, 203-212.
    • (1990) Cell , vol.61 , pp. 203-212
    • Ullrich, A.1    Schlessinger, J.2
  • 10
    • 0028838012 scopus 로고
    • Dimerization of cell surface receptors in signal transduction
    • Heldin, C. H. Dimerization of cell surface receptors in signal transduction. Cell 1995, 80, 213-223.
    • (1995) Cell , vol.80 , pp. 213-223
    • Heldin, C.H.1
  • 11
    • 0037145061 scopus 로고    scopus 로고
    • Ligand-induced, receptor-mediated dimerization and activation of EGF receptor
    • Schlessinger, J. Ligand-induced, receptor-mediated dimerization and activation of EGF receptor. Cell 2002, 110, 669-672.
    • (2002) Cell , vol.110 , pp. 669-672
    • Schlessinger, J.1
  • 13
    • 33847718214 scopus 로고    scopus 로고
    • The EGF receptor family: Spearheading a merger of signaling and therapeutics
    • Bublil, E. M.; Yarden, Y. The EGF receptor family: Spearheading a merger of signaling and therapeutics. Curr. Opin. Cell Biol. 2007, 19, 124-134.
    • (2007) Curr. Opin. Cell Biol , vol.19 , pp. 124-134
    • Bublil, E.M.1    Yarden, Y.2
  • 15
    • 0035979763 scopus 로고    scopus 로고
    • Activation of preformed EGF receptor dimers by ligand-induced rotation of the transmembrane domain
    • Moriki, T.; Maruyama, H.; Maruyama, I. N. Activation of preformed EGF receptor dimers by ligand-induced rotation of the transmembrane domain. J. Mol. Biol. 2001, 311, 1011-1026.
    • (2001) J. Mol. Biol , vol.311 , pp. 1011-1026
    • Moriki, T.1    Maruyama, H.2    Maruyama, I.N.3
  • 16
    • 0036225144 scopus 로고    scopus 로고
    • Preformed oligomeric epidermal growth factor receptors undergo an ectodomain structure change during signaling
    • Martin-Fernandez, M.; Clarke, D. T.; Tobin, M. J.; Jones, S. V.; Jones, G. R. Preformed oligomeric epidermal growth factor receptors undergo an ectodomain structure change during signaling. Biophys. J. 2002, 82, 2415-2427.
    • (2002) Biophys. J , vol.82 , pp. 2415-2427
    • Martin-Fernandez, M.1    Clarke, D.T.2    Tobin, M.J.3    Jones, S.V.4    Jones, G.R.5
  • 17
    • 0036320471 scopus 로고    scopus 로고
    • Ligand-independent dimer formation of epidermal growth factor receptor (EGFR) is a step separable from ligand-induced EGFR signaling
    • Yu, X.; Sharma, K. D.; Takahashi, T.; Iwamoto, R.; Mekada, E. Ligand-independent dimer formation of epidermal growth factor receptor (EGFR) is a step separable from ligand-induced EGFR signaling. Mol. Biol. Cell 2002, 13, 2547-2557.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 2547-2557
    • Yu, X.1    Sharma, K.D.2    Takahashi, T.3    Iwamoto, R.4    Mekada, E.5
  • 18
    • 24044436190 scopus 로고    scopus 로고
    • Ligand-induced dimer-tetramer transition during the activation of the cell surface epidermal growth factor receptor-A multidimensional microscopy analysis
    • Clayton, A. H.; Walker, F.; Orchard, S. G.; Henderson, C.; Fuchs, D.; Rothacker, J.; Nice, E. C.; Burgess, A. W. Ligand-induced dimer-tetramer transition during the activation of the cell surface epidermal growth factor receptor-A multidimensional microscopy analysis. J. Biol. Chem. 2005, 280, 30392-30399.
    • (2005) J. Biol. Chem , vol.280 , pp. 30392-30399
    • Clayton, A.H.1    Walker, F.2    Orchard, S.G.3    Henderson, C.4    Fuchs, D.5    Rothacker, J.6    Nice, E.C.7    Burgess, A.W.8
  • 19
    • 33748939242 scopus 로고    scopus 로고
    • Single-molecule analysis of epidermal growth factor binding on the surface of living cells
    • Teramura, Y.; Ichinose, J.; Takagi, H.; Nishida, K.; Yanagida, T.; Sako, Y. Single-molecule analysis of epidermal growth factor binding on the surface of living cells. EMBO J. 2006, 25, 4215-4222.
    • (2006) EMBO J , vol.25 , pp. 4215-4222
    • Teramura, Y.1    Ichinose, J.2    Takagi, H.3    Nishida, K.4    Yanagida, T.5    Sako, Y.6
  • 20
    • 34447299688 scopus 로고    scopus 로고
    • Investigation of the dimerization of proteins from the epidermal growth factor receptor family by single wavelength fluorescence cross-correlation spectroscopy
    • Liu, P.; Sudhaharan, T.; Koh, R. M.; Hwang, L. C.; Ahmed, S.; Maruyama, I. N.; Wohland, T. Investigation of the dimerization of proteins from the epidermal growth factor receptor family by single wavelength fluorescence cross-correlation spectroscopy. Biophys. J. 2007, 93, 684-698.
    • (2007) Biophys. J , vol.93 , pp. 684-698
    • Liu, P.1    Sudhaharan, T.2    Koh, R.M.3    Hwang, L.C.4    Ahmed, S.5    Maruyama, I.N.6    Wohland, T.7
  • 21
    • 34447313361 scopus 로고    scopus 로고
    • Oligomerization of the EGF receptor investigated by live cell fluorescence intensity distribution analysis
    • Saffarian, S.; Li, Y.; Elson, E. L.; Pike, L. J. Oligomerization of the EGF receptor investigated by live cell fluorescence intensity distribution analysis. Biophys. J. 2007, 93, 1021-1031.
    • (2007) Biophys. J , vol.93 , pp. 1021-1031
    • Saffarian, S.1    Li, Y.2    Elson, E.L.3    Pike, L.J.4
  • 22
    • 55449102296 scopus 로고    scopus 로고
    • All EGF(ErbB) receptors have preformed homo-and heterodimeric structures in living cells
    • Tao, R. H.; Maruyama, I. N. All EGF(ErbB) receptors have preformed homo-and heterodimeric structures in living cells. J. Cell Sci. 2008, 121, 3207-3217.
    • (2008) J. Cell Sci , vol.121 , pp. 3207-3217
    • Tao, R.H.1    Maruyama, I.N.2
  • 23
    • 72249114997 scopus 로고    scopus 로고
    • Homo-FRET imaging enables quantification of protein cluster sizes with subcellular resolution
    • Bader, A. N.; Hofman, E. G.; Voortman, J.; En Henegouwen, P. M.; Gerritsen, H. C. Homo-FRET imaging enables quantification of protein cluster sizes with subcellular resolution. Biophys. J. 2009, 97, 2613-2622.
    • (2009) Biophys. J , vol.97 , pp. 2613-2622
    • Bader, A.N.1    Hofman, E.G.2    Voortman, J.3    En Henegouwen, P.M.4    Gerritsen, H.C.5
  • 24
    • 65549138069 scopus 로고    scopus 로고
    • Luciferase fragment complementation imaging of conformational changes in the epidermal growth factor receptor
    • Yang, K. S.; Ilagan, M. X.; Piwnica-Worms, D.; Pike, L. J. Luciferase fragment complementation imaging of conformational changes in the epidermal growth factor receptor. J. Biol. Chem. 2009, 284, 7474-7482.
    • (2009) J. Biol. Chem , vol.284 , pp. 7474-7482
    • Yang, K.S.1    Ilagan, M.X.2    Piwnica-Worms, D.3    Pike, L.J.4
  • 25
    • 79957820213 scopus 로고    scopus 로고
    • EGFR activation monitored by SW-FCCS in live cells
    • Ma, X.; Ahmed, S.; Wohland, T. EGFR activation monitored by SW-FCCS in live cells. Front. Biosci. (Elite Ed.) 2011, 3, 22-32.
    • (2011) Front. Biosci. (Elite Ed.) , vol.3 , pp. 22-32
    • Ma, X.1    Ahmed, S.2    Wohland, T.3
  • 26
    • 78651372868 scopus 로고    scopus 로고
    • Nerve growth factor receptor TrkA exists as a preformed, yet inactive, dimer in living cells
    • Shen, J.; Maruyama, I. N. Nerve growth factor receptor TrkA exists as a preformed, yet inactive, dimer in living cells. FEBS Lett. 2011, 585, 295-299.
    • (2011) FEBS Lett , vol.585 , pp. 295-299
    • Shen, J.1    Maruyama, I.N.2
  • 27
    • 84856072855 scopus 로고    scopus 로고
    • Brain-derived neurotrophic factor receptor TrkB exists as a preformed dimer in living cells
    • Shen, J.; Maruyama, I. N. Brain-derived neurotrophic factor receptor TrkB exists as a preformed dimer in living cells. J. Mol. Signal. 2012, 7, 2.
    • (2012) J. Mol. Signal , vol.7 , pp. 2
    • Shen, J.1    Maruyama, I.N.2
  • 28
    • 84855999013 scopus 로고    scopus 로고
    • Mechanics of EGF receptor/ErbB2 kinase activation revealed by luciferase fragment complementation imaging
    • Macdonald-Obermann, J. L.; Piwnica-Worms, D.; Pike, L. J. Mechanics of EGF receptor/ErbB2 kinase activation revealed by luciferase fragment complementation imaging. Proc. Natl. Acad. Sci. USA 2012, 109, 137-142.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 137-142
    • Macdonald-Obermann, J.L.1    Piwnica-Worms, D.2    Pike, L.J.3
  • 29
    • 84886907697 scopus 로고    scopus 로고
    • Dynamic analysis of the epidermal growth factor (EGF) receptor-ErbB2-ErbB3 protein network by luciferase fragment complementation imaging
    • Macdonald-Obermann, J. L.; Adak, S.; Landgraf, R.; Piwnica-Worms, D.; Pike, L. J. Dynamic analysis of the epidermal growth factor (EGF) receptor-ErbB2-ErbB3 protein network by luciferase fragment complementation imaging. J. Biol. Chem. 2013, 288, 30773-30784.
    • (2013) J. Biol. Chem , vol.288 , pp. 30773-30784
    • Macdonald-Obermann, J.L.1    Adak, S.2    Landgraf, R.3    Piwnica-Worms, D.4    Pike, L.J.5
  • 30
    • 33847619358 scopus 로고    scopus 로고
    • The insulin and EGF receptor structures: New insights into ligand-induced receptor activation
    • Ward, C. W.; Lawrence, M. C.; Streltsov, V. A.; Adams, T. E.; McKern, N. M. The insulin and EGF receptor structures: New insights into ligand-induced receptor activation. Trends Biochem. Sci. 2007, 32, 129-137.
    • (2007) Trends Biochem. Sci , vol.32 , pp. 129-137
    • Ward, C.W.1    Lawrence, M.C.2    Streltsov, V.A.3    Adams, T.E.4    McKern, N.M.5
  • 31
    • 84916265276 scopus 로고
    • Isolation of a mouse submaxillary gland protein accelerating incisor eruption and eyelid opening in the new-born animal
    • Cohen, S. Isolation of a mouse submaxillary gland protein accelerating incisor eruption and eyelid opening in the new-born animal. J. Biol. Chem. 1962, 237, 1555-1562.
    • (1962) J. Biol. Chem , vol.237 , pp. 1555-1562
    • Cohen, S.1
  • 32
    • 0016592056 scopus 로고
    • Characterization of the binding of 125-I-labeled epidermal growth factor to human fibroblasts
    • Carpenter, G.; Lembach, K. J.; Morrison, M. M.; Cohen, S. Characterization of the binding of 125-I-labeled epidermal growth factor to human fibroblasts. J. Biol. Chem. 1975, 250, 4297-4304.
    • (1975) J. Biol. Chem , vol.250 , pp. 4297-4304
    • Carpenter, G.1    Lembach, K.J.2    Morrison, M.M.3    Cohen, S.4
  • 33
    • 1342323632 scopus 로고    scopus 로고
    • ErbB receptors: Directing key signaling networks throughout life
    • Holbro, T.; Hynes, N. E. ErbB receptors: Directing key signaling networks throughout life. Annu. Rev. Pharmacol. Toxicol. 2004, 44, 195-217.
    • (2004) Annu. Rev. Pharmacol. Toxicol , vol.44 , pp. 195-217
    • Holbro, T.1    Hynes, N.E.2
  • 35
    • 0034600849 scopus 로고    scopus 로고
    • The ErbB signaling network: Receptor heterodimerization in development and cancer
    • Olayioye, M. A.; Neve, R. M.; Lane, H. A.; Hynes, N. E. The ErbB signaling network: Receptor heterodimerization in development and cancer. EMBO J. 2000, 19, 3159-3167.
    • (2000) EMBO J , vol.19 , pp. 3159-3167
    • Olayioye, M.A.1    Neve, R.M.2    Lane, H.A.3    Hynes, N.E.4
  • 36
    • 63749086305 scopus 로고    scopus 로고
    • ErbB receptors and signaling pathways in cancer
    • Hynes, N. E.; MacDonald, G. ErbB receptors and signaling pathways in cancer. Curr. Opin. Cell Biol. 2009, 21, 177-184.
    • (2009) Curr. Opin. Cell Biol , vol.21 , pp. 177-184
    • Hynes, N.E.1    McDonald, G.2
  • 37
    • 0028785406 scopus 로고
    • Aberrant neural and cardiac development in mice lacking the ErbB4 neuregulin receptor
    • Gassmann, M.; Casagranda, F.; Orioli, D.; Simon, H.; Lai, C.; Klein, R.; Lemke, G. Aberrant neural and cardiac development in mice lacking the ErbB4 neuregulin receptor. Nature 1995, 378, 390-394.
    • (1995) Nature , vol.378 , pp. 390-394
    • Gassmann, M.1    Casagranda, F.2    Orioli, D.3    Simon, H.4    Lai, C.5    Klein, R.6    Lemke, G.7
  • 39
    • 18344390418 scopus 로고    scopus 로고
    • ERBB receptors and cancer: The complexity of targeted inhibitors
    • Hynes, N. E.; Lane, H. A. ERBB receptors and cancer: The complexity of targeted inhibitors. Nat. Rev. Cancer 2005, 5, 341-354.
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 341-354
    • Hynes, N.E.1    Lane, H.A.2
  • 41
    • 62649159075 scopus 로고    scopus 로고
    • Ligand-induced ErbB receptor dimerization
    • Lemmon, M. A. Ligand-induced ErbB receptor dimerization. Exp. Cell Res. 2009, 315, 638-648.
    • (2009) Exp. Cell Res , vol.315 , pp. 638-648
    • Lemmon, M.A.1
  • 43
    • 2942516509 scopus 로고    scopus 로고
    • The relationship between the L1 and L2 domains of the insulin and epidermal growth factor receptors and leucine-rich repeat modules
    • Ward, C. W.; Garrett, T. P. J. The relationship between the L1 and L2 domains of the insulin and epidermal growth factor receptors and leucine-rich repeat modules. BMC Bioinform. 2001, 2, 4.
    • (2001) BMC Bioinform , vol.2 , pp. 4
    • Ward, C.W.1    Garrett, T.P.J.2
  • 45
    • 63049100044 scopus 로고    scopus 로고
    • Functional selectivity of EGF family peptide growth factors: Implications for cancer
    • Wilson, K. J.; Gilmore, J. L.; Foley, J.; Lemmon, M. A.; Riese, D. J., 2nd. Functional selectivity of EGF family peptide growth factors: Implications for cancer. Pharmacol. Ther. 2009, 122, 1-8.
    • (2009) Pharmacol. Ther , vol.122 , pp. 1-8
    • Wilson, K.J.1    Gilmore, J.L.2    Foley, J.3    Lemmon, M.A.4    Riese II, D.J.5
  • 47
    • 0029814271 scopus 로고    scopus 로고
    • A hierarchical network of interreceptor interactions determines signal transduction by Neu differentiation factor/neuregulin and epidermal growth factor
    • Tzahar, E.; Waterman, H.; Chen, X.; Levkowitz, G.; Karunagaran, D.; Lavi, S.; Ratzkin, B. J.; Yarden, Y. A hierarchical network of interreceptor interactions determines signal transduction by Neu differentiation factor/neuregulin and epidermal growth factor. Mol. Cell. Biol. 1996, 16, 5276-5287.
    • (1996) Mol. Cell. Biol , vol.16 , pp. 5276-5287
    • Tzahar, E.1    Waterman, H.2    Chen, X.3    Levkowitz, G.4    Karunagaran, D.5    Lavi, S.6    Ratzkin, B.J.7    Yarden, Y.8
  • 48
    • 0030944455 scopus 로고    scopus 로고
    • ErbB-2, the preferred heterodimerization partner of all ErbB receptors, is a mediator of lateral signaling
    • Graus-Porta, D.; Beerli, R. R.; Daly, J. M.; Hynes, N. E. ErbB-2, the preferred heterodimerization partner of all ErbB receptors, is a mediator of lateral signaling. EMBO J. 1997, 16, 1647-1655.
    • (1997) EMBO J , vol.16 , pp. 1647-1655
    • Graus-Porta, D.1    Beerli, R.R.2    Daly, J.M.3    Hynes, N.E.4
  • 49
    • 0033608993 scopus 로고    scopus 로고
    • The ErbB-2/HER2 oncoprotein of human carcinomas may function solely as a shared coreceptor for multiple stroma-derived growth factors
    • Klapper, L. N.; Glathe, S.; Vaisman, N.; Hynes, N. E.; Andrews, G. C.; Sela, M.; Yarden, Y. The ErbB-2/HER2 oncoprotein of human carcinomas may function solely as a shared coreceptor for multiple stroma-derived growth factors. Proc. Natl. Acad. Sci. USA 1999, 96, 4995-5000.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 4995-5000
    • Klapper, L.N.1    Glathe, S.2    Vaisman, N.3    Hynes, N.E.4    Andrews, G.C.5    Sela, M.6    Yarden, Y.7
  • 51
    • 0030973939 scopus 로고    scopus 로고
    • Biochemical characterization of the protein tyrosine kinase homology domain of the ErbB3 (HER3) receptor protein
    • Sierke, S. L.; Cheng, K.; Kim, H. H.; Koland, J. G. Biochemical characterization of the protein tyrosine kinase homology domain of the ErbB3 (HER3) receptor protein. Biochem. J. 1997, 322, 757-763.
    • (1997) Biochem. J , vol.322 , pp. 757-763
    • Sierke, S.L.1    Cheng, K.2    Kim, H.H.3    Koland, J.G.4
  • 52
    • 0028216712 scopus 로고
    • Identification of c-erbB-3 binding sites for phosphatidylinositol 3'-kinase and SHC using an EGF receptor/c-erbB-3 chimera
    • Prigent, S. A.; Gullick, W. J. Identification of c-erbB-3 binding sites for phosphatidylinositol 3'-kinase and SHC using an EGF receptor/c-erbB-3 chimera. EMBO J. 1994, 13, 2831-2841.
    • (1994) EMBO J , vol.13 , pp. 2831-2841
    • Prigent, S.A.1    Gullick, W.J.2
  • 53
    • 0029162564 scopus 로고
    • Heregulin-dependent regulation of HER2/neu oncogenic signaling by heterodimerization with HER3
    • Wallasch, C.; Weiss, F. U.; Niederfellner, G.; Jallal, B.; Issing, W.; Ullrich, A. Heregulin-dependent regulation of HER2/neu oncogenic signaling by heterodimerization with HER3. EMBO J. 1995, 14, 4267-4275.
    • (1995) EMBO J , vol.14 , pp. 4267-4275
    • Wallasch, C.1    Weiss, F.U.2    Niederfellner, G.3    Jallal, B.4    Issing, W.5    Ullrich, A.6
  • 54
    • 77952338791 scopus 로고    scopus 로고
    • ErbB3/HER3 intracellular domain is competent to bind ATP and catalyze autophosphorylation
    • Shi, F.; Telesco, S. E.; Liu, Y.; Radhakrishnan, R.; Lemmon, M. A. ErbB3/HER3 intracellular domain is competent to bind ATP and catalyze autophosphorylation. Proc. Natl. Acad. Sci. USA 2010, 107, 7692-7697.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 7692-7697
    • Shi, F.1    Telesco, S.E.2    Liu, Y.3    Radhakrishnan, R.4    Lemmon, M.A.5
  • 55
    • 84865165294 scopus 로고    scopus 로고
    • Functional isolation of activated and unilaterally phosphorylated heterodimers of ERBB2 and ERBB3 as scaffolds in ligand-dependent signaling
    • Zhang, Q.; Park, E.; Kani, K.; Landgraf, R. Functional isolation of activated and unilaterally phosphorylated heterodimers of ERBB2 and ERBB3 as scaffolds in ligand-dependent signaling. Proc. Natl. Acad. Sci. USA 2012, 109, 13237-13242.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 13237-13242
    • Zhang, Q.1    Park, E.2    Kani, K.3    Landgraf, R.4
  • 56
    • 50549180370 scopus 로고
    • Essential role of the nerve growth factor in the survival and maintenance of dissociated sensory and sympathetic embryonic nerve cells in vitro
    • Levi-Montalcini, R.; Angeletti, P. U. Essential role of the nerve growth factor in the survival and maintenance of dissociated sensory and sympathetic embryonic nerve cells in vitro. Dev. Biol. 1963, 7, 653-659.
    • (1963) Dev. Biol , vol.7 , pp. 653-659
    • Levi-Montalcini, R.1    Angeletti, P.U.2
  • 57
    • 0031861901 scopus 로고    scopus 로고
    • Cloning and expression of a novel neurotrophin, NT-7, from carp
    • Lai, K. O.; Fu, W. Y.; Ip, F. C.; Ip, N. Y. Cloning and expression of a novel neurotrophin, NT-7, from carp. Mol. Cell. Neurosci. 1998, 11, 64-76.
    • (1998) Mol. Cell. Neurosci , vol.11 , pp. 64-76
    • Lai, K.O.1    Fu, W.Y.2    Ip, F.C.3    Ip, N.Y.4
  • 58
    • 0025735392 scopus 로고
    • The trk proto-oncogene product: A signal transducing receptor for nerve growth factor
    • Kaplan, D. R.; Hempstead, B. L.; Martin-Zanca, D.; Chao, M. V.; Parada, L. F. The trk proto-oncogene product: A signal transducing receptor for nerve growth factor. Science 1991, 252, 554-558.
    • (1991) Science , vol.252 , pp. 554-558
    • Kaplan, D.R.1    Hempstead, B.L.2    Martin-Zanca, D.3    Chao, M.V.4    Parada, L.F.5
  • 61
    • 0025944524 scopus 로고
    • trkC, a new member of the trk family of tyrosine protein kinases, is a receptor for neurotrophin-3
    • Lamballe, F.; Klein, R.; Barbacid, M. trkC, a new member of the trk family of tyrosine protein kinases, is a receptor for neurotrophin-3. Cell 1991, 66, 967-979.
    • (1991) Cell , vol.66 , pp. 967-979
    • Lamballe, F.1    Klein, R.2    Barbacid, M.3
  • 62
    • 0025827738 scopus 로고
    • The neurotrophic factors brain-derived neurotrophic factor and neurotrophin-3 are ligands for the trkB tyrosine kinase receptor
    • Soppet, D.; Escandon, E.; Maragos, J.; Middlemas, D. S.; Reid, S. W.; Blair, J.; Burton, L. E.; Stanton, B. R.; Kaplan, D. R.; Hunter, T.; et al. The neurotrophic factors brain-derived neurotrophic factor and neurotrophin-3 are ligands for the trkB tyrosine kinase receptor. Cell 1991, 65, 895-903.
    • (1991) Cell , vol.65 , pp. 895-903
    • Soppet, D.1    Escandon, E.2    Maragos, J.3    Middlemas, D.S.4    Reid, S.W.5    Blair, J.6    Burton, L.E.7    Stanton, B.R.8    Kaplan, D.R.9    Hunter, T.10
  • 64
    • 0026608541 scopus 로고
    • Binding of neurotrophin-3 to its neuronal receptors and interactions with nerve growth factor and brain-derived neurotrophic factor
    • Rodriguez-Tebar, A.; Dechant, G.; Gotz, R.; Barde, Y. A. Binding of neurotrophin-3 to its neuronal receptors and interactions with nerve growth factor and brain-derived neurotrophic factor. EMBO J. 1992, 11, 917-922.
    • (1992) EMBO J , vol.11 , pp. 917-922
    • Rodriguez-Tebar, A.1    Dechant, G.2    Gotz, R.3    Barde, Y.A.4
  • 65
    • 0028090302 scopus 로고
    • The Trk family of neurotrophin receptors
    • Barbacid, M. The Trk family of neurotrophin receptors. J. Neurobiol. 1994, 25, 1386-1403.
    • (1994) J. Neurobiol , vol.25 , pp. 1386-1403
    • Barbacid, M.1
  • 66
    • 0041488911 scopus 로고    scopus 로고
    • Trk receptors: Roles in neuronal signal transduction
    • Huang, E. J.; Reichardt, L. F. Trk receptors: Roles in neuronal signal transduction. Annu. Rev. Biochem. 2003, 72, 609-642.
    • (2003) Annu. Rev. Biochem , vol.72 , pp. 609-642
    • Huang, E.J.1    Reichardt, L.F.2
  • 67
    • 67650450676 scopus 로고    scopus 로고
    • Mechanisms, locations, and kinetics of synaptic BDNF secretion: An update
    • Lessmann, V.; Brigadski, T. Mechanisms, locations, and kinetics of synaptic BDNF secretion: An update. Neurosci. Res. 2009, 65, 11-22.
    • (2009) Neurosci. Res , vol.65 , pp. 11-22
    • Lessmann, V.1    Brigadski, T.2
  • 68
    • 0012315645 scopus 로고    scopus 로고
    • Neurotrophin secretion: Current facts and future prospects
    • Lessmann, V.; Gottmann, K.; Malcangio, M. Neurotrophin secretion: Current facts and future prospects. Prog. Neurobiol. 2003, 69, 341-374.
    • (2003) Prog. Neurobiol , vol.69 , pp. 341-374
    • Lessmann, V.1    Gottmann, K.2    Malcangio, M.3
  • 69
    • 32644451922 scopus 로고    scopus 로고
    • Neurotrophin signalling in health and disease
    • Chao, M. V.; Rajagopal, R.; Lee, F. S. Neurotrophin signalling in health and disease. Clin. Sci. (Lond.) 2006, 110, 167-173.
    • (2006) Clin. Sci. (Lond.) , vol.110 , pp. 167-173
    • Chao, M.V.1    Rajagopal, R.2    Lee, F.S.3
  • 70
    • 0025797396 scopus 로고
    • Tyrosine phosphorylation and tyrosine kinase activity of the trk proto-oncogene product induced by NGF
    • Kaplan, D. R.; Martin-Zanca, D.; Parada, L. F. Tyrosine phosphorylation and tyrosine kinase activity of the trk proto-oncogene product induced by NGF. Nature 1991, 350, 158-160.
    • (1991) Nature , vol.350 , pp. 158-160
    • Kaplan, D.R.1    Martin-Zanca, D.2    Parada, L.F.3
  • 71
    • 0025774207 scopus 로고
    • High-affinity NGF binding requires coexpression of the trk proto-oncogene and the low-affinity NGF receptor
    • Hempstead, B. L.; Martin-Zanca, D.; Kaplan, D. R.; Parada, L. F.; Chao, M. V. High-affinity NGF binding requires coexpression of the trk proto-oncogene and the low-affinity NGF receptor. Nature 1991, 350, 678-683.
    • (1991) Nature , vol.350 , pp. 678-683
    • Hempstead, B.L.1    Martin-Zanca, D.2    Kaplan, D.R.3    Parada, L.F.4    Chao, M.V.5
  • 72
    • 0026703471 scopus 로고
    • The trkB tyrosine protein kinase is a receptor for neurotrophin-4
    • Klein, R.; Lamballe, F.; Bryant, S.; Barbacid, M. The trkB tyrosine protein kinase is a receptor for neurotrophin-4. Neuron 1992, 8, 947-956.
    • (1992) Neuron , vol.8 , pp. 947-956
    • Klein, R.1    Lamballe, F.2    Bryant, S.3    Barbacid, M.4
  • 74
    • 77949735378 scopus 로고    scopus 로고
    • Assembly and activation of neurotrophic factor receptor complexes
    • Simi, A.; Ibáñez, C. F. Assembly and activation of neurotrophic factor receptor complexes. Dev. Neurobiol. 2010, 70, 323-331.
    • (2010) Dev. Neurobiol , vol.70 , pp. 323-331
    • Simi, A.1    Ibáñez, C.F.2
  • 75
    • 0037762690 scopus 로고    scopus 로고
    • Neurotrophins and their receptors: A convergence point for many signaling pathways
    • Chao, M. V. Neurotrophins and their receptors: A convergence point for many signaling pathways. Nat. Rev. Neurosci. 2003, 4, 299-309.
    • (2003) Nat. Rev. Neurosci , vol.4 , pp. 299-309
    • Chao, M.V.1
  • 76
    • 0034044227 scopus 로고    scopus 로고
    • Neurotrophin signal transduction in the nervous system
    • Kaplan, D. R.; Miller, F. D. Neurotrophin signal transduction in the nervous system. Curr. Opin. Neurobiol. 2000, 10, 381-391.
    • (2000) Curr. Opin. Neurobiol , vol.10 , pp. 381-391
    • Kaplan, D.R.1    Miller, F.D.2
  • 77
    • 0035964486 scopus 로고    scopus 로고
    • Trk receptor tyrosine kinases: A bridge between cancer and neural development
    • Nakagawara, A. Trk receptor tyrosine kinases: A bridge between cancer and neural development. Cancer Lett. 2001, 169, 107-114.
    • (2001) Cancer Lett , vol.169 , pp. 107-114
    • Nakagawara, A.1
  • 80
    • 0026009877 scopus 로고
    • A novel modular mosaic of cell adhesion motifs in the extracellular domains of the neurogenic trk and trkB tyrosine kinase receptors
    • Schneider, R.; Schweiger, M. A novel modular mosaic of cell adhesion motifs in the extracellular domains of the neurogenic trk and trkB tyrosine kinase receptors. Oncogene 1991, 6, 1807-1811.
    • (1991) Oncogene , vol.6 , pp. 1807-1811
    • Schneider, R.1    Schweiger, M.2
  • 83
    • 0029017053 scopus 로고
    • NGF binding to the trk tyrosine kinase receptor requires the extracellular immunoglobulin-like domains
    • Perez, P.; Coll, P. M.; Hempstead, B. L.; Martin-Zanca, D.; Chao, M. V. NGF binding to the trk tyrosine kinase receptor requires the extracellular immunoglobulin-like domains. Mol. Cell. Neurosci. 1995, 6, 97-105.
    • (1995) Mol. Cell. Neurosci , vol.6 , pp. 97-105
    • Perez, P.1    Coll, P.M.2    Hempstead, B.L.3    Martin-Zanca, D.4    Chao, M.V.5
  • 84
    • 0030963477 scopus 로고    scopus 로고
    • Specificity determinants in neurotrophin-3 and design of nerve growth factor-based trkC agonists by changing central β-strand bundle residues of their neurotrophin-3 analogs
    • Urfer, R.; Tsoulfas, P.; O'Connell, L.; Presta, L. G. Specificity determinants in neurotrophin-3 and design of nerve growth factor-based trkC agonists by changing central β-strand bundle residues of their neurotrophin-3 analogs. Biochemistry 1997, 36, 4775-4781.
    • (1997) Biochemistry , vol.36 , pp. 4775-4781
    • Urfer, R.1    Tsoulfas, P.2    O'Connell, L.3    Presta, L.G.4
  • 86
    • 0033539065 scopus 로고    scopus 로고
    • Crystal structure of nerve growth factor in complex with the ligand-binding domain of the TrkA receptor
    • Wiesmann, C.; Ultsch, M. H.; Bass, S. H.; de Vos, A. M. Crystal structure of nerve growth factor in complex with the ligand-binding domain of the TrkA receptor. Nature 1999, 401, 184-188.
    • (1999) Nature , vol.401 , pp. 184-188
    • Wiesmann, C.1    Ultsch, M.H.2    Bass, S.H.3    de Vos, A.M.4
  • 87
    • 85136050641 scopus 로고
    • Insulin Today
    • Steiner, D. F. Insulin Today. Diabetes 1976, 26, 322-340.
    • (1976) Diabetes , vol.26 , pp. 322-340
    • Steiner, D.F.1
  • 88
    • 0010989599 scopus 로고
    • The action of insulin on the distribution of galactose in eviscerated nephrectomized dogs
    • Levine, R.; Goldstein, M.; Klein, S.; Huddlestun, B. The action of insulin on the distribution of galactose in eviscerated nephrectomized dogs. J. Biol. Chem. 1949, 179, 985-986.
    • (1949) J. Biol. Chem , vol.179 , pp. 985-986
    • Levine, R.1    Goldstein, M.2    Klein, S.3    Huddlestun, B.4
  • 90
    • 33750172251 scopus 로고    scopus 로고
    • Genetic disorders in the growth hormone-insulin-like growth factor-I axis
    • Walenkamp, M. J. E.; Wit, J. M. Genetic disorders in the growth hormone-insulin-like growth factor-I axis. Horm. Res. 2006, 66, 221-230.
    • (2006) Horm. Res , vol.66 , pp. 221-230
    • Walenkamp, M.J.E.1    Wit, J.M.2
  • 91
    • 33745014194 scopus 로고    scopus 로고
    • Hormonal regulation of fetal growth
    • Gicquel, C.; Le Bouc, Y. Hormonal regulation of fetal growth. Horm. Res. 2006, 65, 28-33.
    • (2006) Horm. Res , vol.65 , pp. 28-33
    • Gicquel, C.1    Le Bouc, Y.2
  • 92
    • 77957241580 scopus 로고    scopus 로고
    • The proliferating role of insulin and insulin-like growth factors in cancer
    • Gallagher, E. J.; LeRoith, D. The proliferating role of insulin and insulin-like growth factors in cancer. Trends Endocrinol. Metab. 2010, 21, 610-618.
    • (2010) Trends Endocrinol. Metab , vol.21 , pp. 610-618
    • Gallagher, E.J.1    LeRoith, D.2
  • 93
    • 0015103371 scopus 로고
    • Insulin receptors in the liver: Specific binding of [125I]insulin to the plasma membrane and its relation to insulin bioactivity
    • Freychet, P.; Roth, J.; Neville, D. M., Jr. Insulin receptors in the liver: Specific binding of [125I]insulin to the plasma membrane and its relation to insulin bioactivity. Proc. Natl. Acad. Sci. USA 1971, 68, 1833-1837.
    • (1971) Proc. Natl. Acad. Sci. USA , vol.68 , pp. 1833-1837
    • Freychet, P.1    Roth, J.2    Neville Jr., D.M.3
  • 94
    • 0346095210 scopus 로고    scopus 로고
    • The insulin receptor isoform exon 11-(IR-A) in cancer and other diseases: A review
    • Denley, A.; Wallace, J. C.; Cosgrove, L. J.; Forbes, B. E. The insulin receptor isoform exon 11-(IR-A) in cancer and other diseases: A review. Horm. Metab. Res. 2003, 35, 778-785.
    • (2003) Horm. Metab. Res , vol.35 , pp. 778-785
    • Denley, A.1    Wallace, J.C.2    Cosgrove, L.J.3    Forbes, B.E.4
  • 95
    • 70849120946 scopus 로고    scopus 로고
    • Insulin receptor isoforms and insulin receptor/insulin-like growth factor receptor hybrids in physiology and disease
    • Belfiore, A.; Frasca, F.; Pandini, G.; Sciacca, L.; Vigneri, R. Insulin receptor isoforms and insulin receptor/insulin-like growth factor receptor hybrids in physiology and disease. Endocr. Rev. 2009, 30, 586-623.
    • (2009) Endocr. Rev , vol.30 , pp. 586-623
    • Belfiore, A.1    Frasca, F.2    Pandini, G.3    Sciacca, L.4    Vigneri, R.5
  • 96
  • 97
    • 5044227353 scopus 로고    scopus 로고
    • Structural determinants for high-affinity binding of insulin-like growth factor II to insulin receptor (IR)-A, the exon 11 minus isoform of the IR
    • Denley, A.; Bonython, E. R.; Booker, G. W.; Cosgrove, L. J.; Forbes, B. E.; Ward, C. W.; Wallace, J. C. Structural determinants for high-affinity binding of insulin-like growth factor II to insulin receptor (IR)-A, the exon 11 minus isoform of the IR. Mol. Endocrinol. 2004, 18, 2502-2512.
    • (2004) Mol. Endocrinol , vol.18 , pp. 2502-2512
    • Denley, A.1    Bonython, E.R.2    Booker, G.W.3    Cosgrove, L.J.4    Forbes, B.E.5    Ward, C.W.6    Wallace, J.C.7
  • 98
    • 33748744723 scopus 로고    scopus 로고
    • Hybrid receptors formed by insulin receptor (IR) and insulin-like growth factor I receptor (IGF-IR) have low insulin and high IGF-1 affinity irrespective of the IR splice variant
    • Slaaby, R.; Schaffer, L.; Lautrup-Larsen, I.; Andersen, A. S.; Shaw, A. C.; Mathiasen, I. S.; Brandt, J. Hybrid receptors formed by insulin receptor (IR) and insulin-like growth factor I receptor (IGF-IR) have low insulin and high IGF-1 affinity irrespective of the IR splice variant. J. Biol. Chem. 2006, 281, 25869-25874.
    • (2006) J. Biol. Chem , vol.281 , pp. 25869-25874
    • Slaaby, R.1    Schaffer, L.2    Lautrup-Larsen, I.3    Andersen, A.S.4    Shaw, A.C.5    Mathiasen, I.S.6    Brandt, J.7
  • 99
    • 34247872895 scopus 로고    scopus 로고
    • Characterization of insulin/IGF hybrid receptors: Contributions of the insulin receptor L2 and Fn1 domains and the alternatively spliced exon 11 sequence to ligand binding and receptor activation
    • Benyoucef, S.; Surinya, K. H.; Hadaschik, D.; Siddle, K. Characterization of insulin/IGF hybrid receptors: Contributions of the insulin receptor L2 and Fn1 domains and the alternatively spliced exon 11 sequence to ligand binding and receptor activation. Biochem. J. 2007, 403, 603-613.
    • (2007) Biochem. J , vol.403 , pp. 603-613
    • Benyoucef, S.1    Surinya, K.H.2    Hadaschik, D.3    Siddle, K.4
  • 100
    • 0036545778 scopus 로고    scopus 로고
    • Insulin and insulin-like growth factors: The paradox of signaling specificity
    • De Meyts, P. Insulin and insulin-like growth factors: The paradox of signaling specificity. Growth Horm. IGF Res. 2002, 12, 81-83.
    • (2002) Growth Horm. IGF Res , vol.12 , pp. 81-83
    • De Meyts, P.1
  • 101
    • 0035742583 scopus 로고    scopus 로고
    • Insulin and insulin-like growth factor I receptors: Similarities and differences in signal transduction
    • Dupont, J.; LeRoith, D. Insulin and insulin-like growth factor I receptors: Similarities and differences in signal transduction. Horm. Res. 2001, 55, 22-26.
    • (2001) Horm. Res , vol.55 , pp. 22-26
    • Dupont, J.1    LeRoith, D.2
  • 102
    • 0027930275 scopus 로고
    • Expression of a cDNA encoding the human insulin receptor-related receptor
    • Jui, H. Y.; Suzuki, Y.; Accili, D.; Taylor, S. I. Expression of a cDNA encoding the human insulin receptor-related receptor. J. Biol. Chem. 1994, 269, 22446-22452.
    • (1994) J. Biol. Chem , vol.269 , pp. 22446-22452
    • Jui, H.Y.1    Suzuki, Y.2    Accili, D.3    Taylor, S.I.4
  • 103
    • 0026693671 scopus 로고
    • The insulin receptor-related receptor. Tissue expression, ligand binding specificity, and signaling capabilities
    • Zhang, B.; Roth, R. A. The insulin receptor-related receptor. Tissue expression, ligand binding specificity, and signaling capabilities. J. Biol. Chem. 1992, 267, 18320-18328.
    • (1992) J. Biol. Chem , vol.267 , pp. 18320-18328
    • Zhang, B.1    Roth, R.A.2
  • 104
    • 0344517365 scopus 로고    scopus 로고
    • Insulin receptor-related receptor is expressed in pancreatic beta-cells and stimulates tyrosine phosphorylation of insulin receptor substrate-1 and-2
    • Hirayama, I.; Tamemoto, H.; Yokota, H.; Kubo, S. K.; Wang, J.; Kuwano, H.; Nagamachi, Y.; Takeuchi, T.; Izumi, T. Insulin receptor-related receptor is expressed in pancreatic beta-cells and stimulates tyrosine phosphorylation of insulin receptor substrate-1 and-2. Diabetes 1999, 48, 1237-1244.
    • (1999) Diabetes , vol.48 , pp. 1237-1244
    • Hirayama, I.1    Tamemoto, H.2    Yokota, H.3    Kubo, S.K.4    Wang, J.5    Kuwano, H.6    Nagamachi, Y.7    Takeuchi, T.8    Izumi, T.9
  • 105
    • 0029097571 scopus 로고
    • Insulin receptor-related receptor messenger ribonucleic acid: Quantitative distribution and localization to subpopulations of epithelial cells in stomach and kidney
    • Mathi, S. K.; Chan, J.; Watt, V. M. Insulin receptor-related receptor messenger ribonucleic acid: Quantitative distribution and localization to subpopulations of epithelial cells in stomach and kidney. Endocrinology 1995, 136, 4125-4132.
    • (1995) Endocrinology , vol.136 , pp. 4125-4132
    • Mathi, S.K.1    Chan, J.2    Watt, V.M.3
  • 108
    • 0033906634 scopus 로고    scopus 로고
    • Structure and function of the type 1 insulin-like growth factor receptor
    • Adams, T. E.; Epa, V. C.; Garrett, T. P.; Ward, C. W. Structure and function of the type 1 insulin-like growth factor receptor. Cell. Mol. Life Sci. 2000, 57, 1050-1093.
    • (2000) Cell. Mol. Life Sci , vol.57 , pp. 1050-1093
    • Adams, T.E.1    Epa, V.C.2    Garrett, T.P.3    Ward, C.W.4
  • 109
    • 4944222159 scopus 로고    scopus 로고
    • Structural relationships between the insulin receptor and epidermal growth factor receptor families and other proteins
    • Ward, C. W.; Garrett, T. P. Structural relationships between the insulin receptor and epidermal growth factor receptor families and other proteins. Curr. Opin. Drug Discov. Dev. 2004, 7, 630-638.
    • (2004) Curr. Opin. Drug Discov. Dev , vol.7 , pp. 630-638
    • Ward, C.W.1    Garrett, T.P.2
  • 110
    • 2942594298 scopus 로고    scopus 로고
    • Juxtamembrane autoinhibition in receptor tyrosine kinases
    • Hubbard, S. R. Juxtamembrane autoinhibition in receptor tyrosine kinases. Nat. Rev. Mol. Cell Biol. 2004, 5, 464-471.
    • (2004) Nat. Rev. Mol. Cell Biol , vol.5 , pp. 464-471
    • Hubbard, S.R.1
  • 112
    • 33750374137 scopus 로고    scopus 로고
    • The twentieth centrury struggle to decipher insulin signaling
    • Cohen, P. The twentieth centrury struggle to decipher insulin signaling. Nat. Rev. Mol. Cell Biol. 2006, 7, 867-873.
    • (2006) Nat. Rev. Mol. Cell Biol , vol.7 , pp. 867-873
    • Cohen, P.1
  • 113
    • 33244464562 scopus 로고    scopus 로고
    • Critical nodes in signaling pathways: Insights into insulin action
    • Taniguchi, C. M.; Emanuelli, B.; Kahn, C. R. Critical nodes in signaling pathways: Insights into insulin action. Nat. Rev. Mol. Cell Biol. 2006, 7, 85-96.
    • (2006) Nat. Rev. Mol. Cell Biol , vol.7 , pp. 85-96
    • Taniguchi, C.M.1    Emanuelli, B.2    Kahn, C.R.3
  • 114
    • 48149100986 scopus 로고    scopus 로고
    • Insulin action on glucose transporters through molecular switches, tracks and tethers
    • Zaid, H.; Antonescu, C. N.; Randhawa, V. K.; Klip, A. Insulin action on glucose transporters through molecular switches, tracks and tethers. Biochem. J. 2008, 413, 201-215.
    • (2008) Biochem. J , vol.413 , pp. 201-215
    • Zaid, H.1    Antonescu, C.N.2    Randhawa, V.K.3    Klip, A.4
  • 115
    • 0023100261 scopus 로고
    • Epidermal growth factor induces rapid, reversible aggregation of the purified epidermal growth factor receptor
    • Yarden, Y.; Schlessinger, J. Epidermal growth factor induces rapid, reversible aggregation of the purified epidermal growth factor receptor. Biochemistry 1987, 26, 1443-1451.
    • (1987) Biochemistry , vol.26 , pp. 1443-1451
    • Yarden, Y.1    Schlessinger, J.2
  • 116
    • 0023443196 scopus 로고
    • Mechanism of epidermal growth factor receptor autophosphorylation and high-affinity binding
    • Boni-Schnetzler, M.; Pilch, P. F. Mechanism of epidermal growth factor receptor autophosphorylation and high-affinity binding. Proc. Natl. Acad. Sci. USA 1987, 84, 7832-7836.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 7832-7836
    • Boni-Schnetzler, M.1    Pilch, P.F.2
  • 118
    • 0026704007 scopus 로고
    • Signal transmission by epidermal growth factor receptor: Coincidence of activation and dimerization
    • Canals, F. Signal transmission by epidermal growth factor receptor: Coincidence of activation and dimerization. Biochemistry 1992, 31, 4493-4501.
    • (1992) Biochemistry , vol.31 , pp. 4493-4501
    • Canals, F.1
  • 119
    • 0029973636 scopus 로고    scopus 로고
    • FACS-optimized mutants of the green fluorescent protein (GFP)
    • Cormack, B. P.; Valdivia, R. H.; Falkow, S. FACS-optimized mutants of the green fluorescent protein (GFP). Gene 1996, 173, 33-38.
    • (1996) Gene , vol.173 , pp. 33-38
    • Cormack, B.P.1    Valdivia, R.H.2    Falkow, S.3
  • 120
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescent protein
    • Tsien, R. Y. The green fluorescent protein. Annu. Rev. Biochem. 1998, 67, 509-544.
    • (1998) Annu. Rev. Biochem , vol.67 , pp. 509-544
    • Tsien, R.Y.1
  • 121
    • 0036138908 scopus 로고    scopus 로고
    • A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications
    • Nagai, T.; Ibata, K.; Park, E. S.; Kubota, M.; Mikoshiba, K.; Miyawaki, A. A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications. Nat. Biotechnol. 2002, 20, 87-90.
    • (2002) Nat. Biotechnol , vol.20 , pp. 87-90
    • Nagai, T.1    Ibata, K.2    Park, E.S.3    Kubota, M.4    Mikoshiba, K.5    Miyawaki, A.6
  • 122
    • 0029790979 scopus 로고    scopus 로고
    • Dephosphorylation of receptor tyrosine kinases as target of regulation by radiation, oxidants or alkylating agents
    • Knebel, A.; Rahmsdorf, H. J.; Ullrich, A.; Herrlich, P. Dephosphorylation of receptor tyrosine kinases as target of regulation by radiation, oxidants or alkylating agents. EMBO J. 1996, 15, 5314-5325.
    • (1996) EMBO J , vol.15 , pp. 5314-5325
    • Knebel, A.1    Rahmsdorf, H.J.2    Ullrich, A.3    Herrlich, P.4
  • 123
    • 78049239930 scopus 로고    scopus 로고
    • Distribution of resting and ligand-bound ErbB1 and ErbB2 receptor tyrosine kinases in living cells using number and brightness analysis
    • Nagy, P.; Claus, J.; Jovin, T. M.; Arndt-Jovin, D. J. Distribution of resting and ligand-bound ErbB1 and ErbB2 receptor tyrosine kinases in living cells using number and brightness analysis. Proc. Natl. Acad. Sci. USA 2010, 107, 16524-16529.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 16524-16529
    • Nagy, P.1    Claus, J.2    Jovin, T.M.3    Arndt-Jovin, D.J.4
  • 124
    • 0036696824 scopus 로고    scopus 로고
    • Lateral propagation of EGF signaling after local stimulation is dependent on receptor density
    • Sawano, A.; Takayama, S.; Matsuda, M.; Miyawaki, A. Lateral propagation of EGF signaling after local stimulation is dependent on receptor density. Dev. Cell 2002, 3, 245-257.
    • (2002) Dev. Cell , vol.3 , pp. 245-257
    • Sawano, A.1    Takayama, S.2    Matsuda, M.3    Miyawaki, A.4
  • 125
    • 0033860103 scopus 로고    scopus 로고
    • TrkA immunoglobulin-like ligand binding domains inhibit spontaneous activation of the receptor
    • Arevalo, J. C.; Conde, B.; Hempstead, B. L.; Chao, M. V.; Martin-Zanca, D.; Perez, P. TrkA immunoglobulin-like ligand binding domains inhibit spontaneous activation of the receptor. Mol. Cell. Biol. 2000, 20, 5908-5916.
    • (2000) Mol. Cell. Biol , vol.20 , pp. 5908-5916
    • Arevalo, J.C.1    Conde, B.2    Hempstead, B.L.3    Chao, M.V.4    Martin-Zanca, D.5    Perez, P.6
  • 126
    • 0035448621 scopus 로고    scopus 로고
    • TrkB dimerization during development of the prefrontal cortex of the macaque
    • Ohira, K.; Shimizu, K.; Hayashi, M. TrkB dimerization during development of the prefrontal cortex of the macaque. J. Neurosci. Res. 2001, 65, 463-469.
    • (2001) J. Neurosci. Res , vol.65 , pp. 463-469
    • Ohira, K.1    Shimizu, K.2    Hayashi, M.3
  • 130
    • 2442434770 scopus 로고    scopus 로고
    • Structure of nerve growth factor complexed with the shared neurotrophin receptor p75
    • He, X. L.; Garcia, K. C. Structure of nerve growth factor complexed with the shared neurotrophin receptor p75. Science 2004, 304, 870-875.
    • (2004) Science , vol.304 , pp. 870-875
    • He, X.L.1    Garcia, K.C.2
  • 131
    • 33845695804 scopus 로고    scopus 로고
    • Structural and mechanistic insights into nerve growth factor interactions with the TrkA and p75 receptors
    • Wehrman, T.; He, X.; Raab, B.; Dukipatti, A.; Blau, H.; Garcia, K. C. Structural and mechanistic insights into nerve growth factor interactions with the TrkA and p75 receptors. Neuron 2007, 53, 25-38.
    • (2007) Neuron , vol.53 , pp. 25-38
    • Wehrman, T.1    He, X.2    Raab, B.3    Dukipatti, A.4    Blau, H.5    Garcia, K.C.6
  • 133
    • 84876553840 scopus 로고    scopus 로고
    • An intracellular domain fragment of the p75 neurotrophin receptor (p75(NTR) enhances tropomyosin receptor kinase A (TrkA) receptor function
    • Matusica, D.; Skeldal, S.; Sykes, A. M.; Palstra, N.; Sharma, A.; Coulson, E. J. An intracellular domain fragment of the p75 neurotrophin receptor (p75(NTR) enhances tropomyosin receptor kinase A (TrkA) receptor function. J. Biol. Chem. 2013, 288, 11144-11154.
    • (2013) J. Biol. Chem , vol.288 , pp. 11144-11154
    • Matusica, D.1    Skeldal, S.2    Sykes, A.M.3    Palstra, N.4    Sharma, A.5    Coulson, E.J.6
  • 134
    • 0009632799 scopus 로고
    • Electrophoretic resolution of three major insulin receptor structures with unique subunit stoichiometries
    • Massague, J.; Pilch, P. F.; Czech, M. P. Electrophoretic resolution of three major insulin receptor structures with unique subunit stoichiometries. Proc. Natl. Acad. Sci. USA 1980, 77, 7137-7141.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 7137-7141
    • Massague, J.1    Pilch, P.F.2    Czech, M.P.3
  • 137
    • 0024358352 scopus 로고
    • Insulin-like growth factor I receptor beta-subunit heterogeneity. Evidence for hybrid tetramers composed of insulin-like growth factor I and insulin receptor heterodimers
    • Moxham, C. P.; Duronio, V.; Jacobs, S. Insulin-like growth factor I receptor beta-subunit heterogeneity. Evidence for hybrid tetramers composed of insulin-like growth factor I and insulin receptor heterodimers. J. Biol. Chem. 1989, 264, 13238-13244.
    • (1989) J. Biol. Chem , vol.264 , pp. 13238-13244
    • Moxham, C.P.1    Duronio, V.2    Jacobs, S.3
  • 138
    • 0024465470 scopus 로고
    • Immunological relationships between receptors for insulin and insulin-like growth factor I. Evidence for structural heterogeneity of insulin-like growth factor I receptors involving hybrids with insulin receptors
    • Soos, M. A.; Siddle, K. Immunological relationships between receptors for insulin and insulin-like growth factor I. Evidence for structural heterogeneity of insulin-like growth factor I receptors involving hybrids with insulin receptors. Biochem. J. 1989, 263, 553-563.
    • (1989) Biochem. J , vol.263 , pp. 553-563
    • Soos, M.A.1    Siddle, K.2
  • 140
    • 0030693249 scopus 로고    scopus 로고
    • Insulin receptor/IGF-I receptor hybrids are widely distributed in mammalian tissues: Quantification of individual receptor species by selective immunoprecipitation and immunoblotting
    • Bailyes, E. M.; Nave, B. T.; Soos, M. A.; Orr, S. R.; Hayward, A. C.; Siddle, K. Insulin receptor/IGF-I receptor hybrids are widely distributed in mammalian tissues: Quantification of individual receptor species by selective immunoprecipitation and immunoblotting. Biochem. J. 1997, 327, 209-215.
    • (1997) Biochem. J , vol.327 , pp. 209-215
    • Bailyes, E.M.1    Nave, B.T.2    Soos, M.A.3    Orr, S.R.4    Hayward, A.C.5    Siddle, K.6
  • 141
    • 0037014743 scopus 로고    scopus 로고
    • Insulin, insulin-like growth factor-I (IGF-I), IGF binding proteins, their biologic interactions, and colorectal cancer
    • Sandhu, M. S.; Dunger, D. B.; Giovannucci, E. L. Insulin, insulin-like growth factor-I (IGF-I), IGF binding proteins, their biologic interactions, and colorectal cancer. J. Natl. Cancer Inst. 2002, 94, 972-980.
    • (2002) J. Natl. Cancer Inst , vol.94 , pp. 972-980
    • Sandhu, M.S.1    Dunger, D.B.2    Giovannucci, E.L.3
  • 142
    • 0037162799 scopus 로고    scopus 로고
    • Structure of the extracellular region of HER3 reveals an interdomain tether
    • Cho, H. S.; Leahy, D. J. Structure of the extracellular region of HER3 reveals an interdomain tether. Science 2002, 297, 1330-1333.
    • (2002) Science , vol.297 , pp. 1330-1333
    • Cho, H.S.1    Leahy, D.J.2
  • 143
    • 0037291769 scopus 로고    scopus 로고
    • EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization
    • Ferguson, K. M.; Berger, M. B.; Mendrola, J. M.; Cho, H. S.; Leahy, D. J.; Lemmon, M. A. EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization. Moll. Cell 2003, 11, 507-517.
    • (2003) Moll. Cell , vol.11 , pp. 507-517
    • Ferguson, K.M.1    Berger, M.B.2    Mendrola, J.M.3    Cho, H.S.4    Leahy, D.J.5    Lemmon, M.A.6
  • 144
    • 27244461099 scopus 로고    scopus 로고
    • The extracellular region of ErbB4 adopts a tethered conformation in the absence of ligand
    • Bouyain, S.; Longo, P. A.; Li, S.; Ferguson, K. M.; Leahy, D. J. The extracellular region of ErbB4 adopts a tethered conformation in the absence of ligand. Proc. Natl. Acad. Sci. USA 2005, 102, 15024-15029.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 15024-15029
    • Bouyain, S.1    Longo, P.A.2    Li, S.3    Ferguson, K.M.4    Leahy, D.J.5
  • 145
    • 48249158391 scopus 로고    scopus 로고
    • Structure-based view of epidermal growth factor receptor regulation
    • Ferguson, K. M. Structure-based view of epidermal growth factor receptor regulation. Annu. Rev. Biophys. 2008, 37, 353-373.
    • (2008) Annu. Rev. Biophys , vol.37 , pp. 353-373
    • Ferguson, K.M.1
  • 146
    • 18644370411 scopus 로고    scopus 로고
    • Crystal structure of a truncated epidermal growth factor receptor extracellular domain bound to transforming growth factor alpha
    • Garrett, T. P.; McKern, N. M.; Lou, M.; Elleman, T. C.; Adams, T. E.; Lovrecz, G. O.; Zhu, H. J.; Walker, F.; Frenkel, M. J.; Hoyne, P. A.; et al. Crystal structure of a truncated epidermal growth factor receptor extracellular domain bound to transforming growth factor alpha. Cell 2002, 110, 763-773.
    • (2002) Cell , vol.110 , pp. 763-773
    • Garrett, T.P.1    McKern, N.M.2    Lou, M.3    Elleman, T.C.4    Adams, T.E.5    Lovrecz, G.O.6    Zhu, H.J.7    Walker, F.8    Frenkel, M.J.9    Hoyne, P.A.10
  • 148
    • 0037008698 scopus 로고    scopus 로고
    • Disabling receptor ensembles with rationally designed interface peptidomimetics
    • Berezov, A.; Chen, J.; Liu, Q.; Zhang, H. T.; Greene, M. I.; Murali, R. Disabling receptor ensembles with rationally designed interface peptidomimetics. J. Biol. Chem. 2002, 277, 28330-28339.
    • (2002) J. Biol. Chem , vol.277 , pp. 28330-28339
    • Berezov, A.1    Chen, J.2    Liu, Q.3    Zhang, H.T.4    Greene, M.I.5    Murali, R.6
  • 150
    • 0037434791 scopus 로고    scopus 로고
    • Structure of the extracellular region of HER2 alone and in complex with the Herceptin Fab
    • Cho, H. S.; Mason, K.; Ramyar, K. X.; Stanley, A. M.; Gabelli, S. B.; Denney, D. W., Jr.; Leahy, D. J. Structure of the extracellular region of HER2 alone and in complex with the Herceptin Fab. Nature 2003, 421, 756-760.
    • (2003) Nature , vol.421 , pp. 756-760
    • Cho, H.S.1    Mason, K.2    Ramyar, K.X.3    Stanley, A.M.4    Gabelli, S.B.5    Denney Jr., D.W.6    Leahy, D.J.7
  • 152
    • 67549145398 scopus 로고    scopus 로고
    • Mechanism for activation of the EGF receptor catalytic domain by the juxtamembrane segment
    • Jura, N.; Endres, N. F.; Engel, K.; Deindl, S.; Das, R.; Lamers, M. H.; Wemmer, D. E.; Zhang, X.; Kuriyan, J. Mechanism for activation of the EGF receptor catalytic domain by the juxtamembrane segment. Cell 2009, 137, 1293-1307.
    • (2009) Cell , vol.137 , pp. 1293-1307
    • Jura, N.1    Endres, N.F.2    Engel, K.3    Deindl, S.4    Das, R.5    Lamers, M.H.6    Wemmer, D.E.7    Zhang, X.8    Kuriyan, J.9
  • 153
    • 33745002702 scopus 로고    scopus 로고
    • An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor
    • Zhang, X.; Gureasko, J.; Shen, K.; Cole, P. A.; Kuriyan, J. An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor. Cell 2006, 125, 1137-1149.
    • (2006) Cell , vol.125 , pp. 1137-1149
    • Zhang, X.1    Gureasko, J.2    Shen, K.3    Cole, P.A.4    Kuriyan, J.5
  • 154
    • 0141599428 scopus 로고    scopus 로고
    • Structure of the epidermal growth factor receptor kinase domain alone and in complex with a 4-anilinoquinazoline inhibitor
    • Stamos, J.; Sliwkowski, M. X.; Eigenbrot, C. Structure of the epidermal growth factor receptor kinase domain alone and in complex with a 4-anilinoquinazoline inhibitor. J. Biol. Chem. 2002, 277, 46265-46272.
    • (2002) J. Biol. Chem , vol.277 , pp. 46265-46272
    • Stamos, J.1    Sliwkowski, M.X.2    Eigenbrot, C.3
  • 155
    • 0037013143 scopus 로고    scopus 로고
    • The conformational plasticity of protein kinases
    • Huse, M.; Kuriyan, J. The conformational plasticity of protein kinases. Cell 2002, 109, 275-282.
    • (2002) Cell , vol.109 , pp. 275-282
    • Huse, M.1    Kuriyan, J.2
  • 158
    • 0027050178 scopus 로고
    • Nerve growth factor mediates signal transduction through trk homodimer receptors
    • Jing, S.; Tapley, P.; Barbacid, M. Nerve growth factor mediates signal transduction through trk homodimer receptors. Neuron 1992, 9, 1067-1079.
    • (1992) Neuron , vol.9 , pp. 1067-1079
    • Jing, S.1    Tapley, P.2    Barbacid, M.3
  • 159
    • 0017705162 scopus 로고
    • Dissociation equilibrium constant of beta nerve growth factor
    • Bothwell, M. A.; Shooter, E. M. Dissociation equilibrium constant of beta nerve growth factor. J. Biol. Chem. 1977, 252, 8532-8536.
    • (1977) J. Biol. Chem , vol.252 , pp. 8532-8536
    • Bothwell, M.A.1    Shooter, E.M.2
  • 160
    • 0025986121 scopus 로고
    • New protein fold revealed by a 2. 3-Å resolution crystal structure of nerve growth factor
    • McDonald, N. Q.; Lapatto, R.; Murray-Rust, J.; Gunning, J.; Wlodawer, A.; Blundell, T. L. New protein fold revealed by a 2. 3-Å resolution crystal structure of nerve growth factor. Nature 1991, 354, 411-414.
    • (1991) Nature , vol.354 , pp. 411-414
    • McDonald, N.Q.1    Lapatto, R.2    Murray-Rust, J.3    Gunning, J.4    Wlodawer, A.5    Blundell, T.L.6
  • 161
    • 0026651549 scopus 로고
    • Dimeric structure and conformational stability of brain-derived neurotrophic factor and neurotrophin-3
    • Radziejewski, C.; Robinson, R. C.; DiStefano, P. S.; Taylor, J. W. Dimeric structure and conformational stability of brain-derived neurotrophic factor and neurotrophin-3. Biochemistry 1992, 31, 4431-4436.
    • (1992) Biochemistry , vol.31 , pp. 4431-4436
    • Radziejewski, C.1    Robinson, R.C.2    DiStefano, P.S.3    Taylor, J.W.4
  • 162
    • 0027315407 scopus 로고
    • An extended surface of binding to Trk tyrosine kinase receptors in NGF and BDNF allows the engineering of a multifunctional pan-neurotrophin
    • Ibanez, C. F.; Ilag, L. L.; Murray-Rust, J.; Persson, H. An extended surface of binding to Trk tyrosine kinase receptors in NGF and BDNF allows the engineering of a multifunctional pan-neurotrophin. EMBO J. 1993, 12, 2281-2293.
    • (1993) EMBO J , vol.12 , pp. 2281-2293
    • Ibanez, C.F.1    Ilag, L.L.2    Murray-Rust, J.3    Persson, H.4
  • 163
    • 84869051908 scopus 로고    scopus 로고
    • Assessing the range of kinase autoinhibition mechanisms in the insulin receptor family
    • Artim, S. C.; Mendrola, J. M.; Lemmon, M. A. Assessing the range of kinase autoinhibition mechanisms in the insulin receptor family. Biochem. J. 2012, 448, 213-220.
    • (2012) Biochem. J , vol.448 , pp. 213-220
    • Artim, S.C.1    Mendrola, J.M.2    Lemmon, M.A.3
  • 165
    • 0038168241 scopus 로고    scopus 로고
    • Structural and biochemical evidence for an autoinhibitory role for tyrosine 984 in the juxtamembrane region of the insulin receptor
    • Li, S.; Covino, N. D.; Stein, E. G.; Till, J. H.; Hubbard, S. R. Structural and biochemical evidence for an autoinhibitory role for tyrosine 984 in the juxtamembrane region of the insulin receptor. J. Biol. Chem. 2003, 278, 26007-26014.
    • (2003) J. Biol. Chem , vol.278 , pp. 26007-26014
    • Li, S.1    Covino, N.D.2    Stein, E.G.3    Till, J.H.4    Hubbard, S.R.5
  • 166
    • 84874727313 scopus 로고    scopus 로고
    • The insulin receptor: Both a prototypical and atypical receptor tyrosine kinase
    • Hubbard, S. R. The insulin receptor: Both a prototypical and atypical receptor tyrosine kinase. Cold Spring Harb. Perspect. Biol. 2013, 5, a008946.
    • (2013) Cold Spring Harb. Perspect. Biol , vol.5
    • Hubbard, S.R.1
  • 167
    • 0028582185 scopus 로고
    • Crystal structure of the tyrosine kinase domain of the human insulin receptor
    • Hubbard, S. R.; Wei, L.; Ellis, L.; Hendrickson, W. A. Crystal structure of the tyrosine kinase domain of the human insulin receptor. Nature 1994, 372, 746-754.
    • (1994) Nature , vol.372 , pp. 746-754
    • Hubbard, S.R.1    Wei, L.2    Ellis, L.3    Hendrickson, W.A.4
  • 168
    • 0037064032 scopus 로고    scopus 로고
    • Crystal structure of the Apo, unactivated insulin-like growth factor-1 receptor kinase. Implication for inhibitor specificity
    • Munshi, S.; Kornienko, M.; Hall, D. L.; Reid, J. C.; Waxman, L.; Stirdivant, S. M.; Darke, P. L.; Kuo, L. C. Crystal structure of the Apo, unactivated insulin-like growth factor-1 receptor kinase. Implication for inhibitor specificity. J. Biol. Chem. 2002, 277, 38797-38802.
    • (2002) J. Biol. Chem , vol.277 , pp. 38797-38802
    • Munshi, S.1    Kornienko, M.2    Hall, D.L.3    Reid, J.C.4    Waxman, L.5    Stirdivant, S.M.6    Darke, P.L.7    Kuo, L.C.8
  • 170
    • 0023024754 scopus 로고
    • Allosteric regulation of the epidermal growth factor receptor kinase
    • Schlessinger, J. Allosteric regulation of the epidermal growth factor receptor kinase. J. Cell Biol. 1986, 103, 2067-2072.
    • (1986) J. Cell Biol , vol.103 , pp. 2067-2072
    • Schlessinger, J.1
  • 171
    • 38349190632 scopus 로고    scopus 로고
    • Heterogeneity in EGF-binding affinities arises from negative cooperativity in an aggregating system
    • Macdonald, J. L.; Pike, L. J. Heterogeneity in EGF-binding affinities arises from negative cooperativity in an aggregating system. Proc. Natl. Acad. Sci. USA 2008, 105, 112-117.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 112-117
    • Macdonald, J.L.1    Pike, L.J.2
  • 172
    • 67649391241 scopus 로고    scopus 로고
    • The intracellular juxtamembrane domain of the epidermal growth factor (EGF) receptor is responsible for the allosteric regulation of EGF binding
    • Macdonald-Obermann, J. L.; Pike, L. J. The intracellular juxtamembrane domain of the epidermal growth factor (EGF) receptor is responsible for the allosteric regulation of EGF binding. J. Biol. Chem. 2009, 284, 13570-13576.
    • (2009) J. Biol. Chem , vol.284 , pp. 13570-13576
    • Macdonald-Obermann, J.L.1    Pike, L.J.2
  • 174
    • 0018774782 scopus 로고
    • Biologically active phorbol esters specifically alter affinity of epidermal growth factor membrane receptors
    • Shoyab, M.; De Larco, J. E.; Todaro, G. J. Biologically active phorbol esters specifically alter affinity of epidermal growth factor membrane receptors. Nature 1979, 279, 387-391.
    • (1979) Nature , vol.279 , pp. 387-391
    • Shoyab, M.1    De Larco, J.E.2    Todaro, G.J.3
  • 175
    • 0019121389 scopus 로고
    • Epidermal growth factor. Ability of tumor promoter to alter its degradation, receptor affinity and receptor number
    • Magun, B. E.; Matrisian, L. M.; Bowden, G. T. Epidermal growth factor. Ability of tumor promoter to alter its degradation, receptor affinity and receptor number. J. Biol. Chem. 1980, 255, 6373-6381.
    • (1980) J. Biol. Chem , vol.255 , pp. 6373-6381
    • Magun, B.E.1    Matrisian, L.M.2    Bowden, G.T.3
  • 176
    • 0020078747 scopus 로고
    • Resolution of high and low affinity epidermal growth factor receptors. Inhibition of high affinity component by low temperature, cycloheximide, and phorbol esters
    • King, A. C.; Cuatrecasas, P. Resolution of high and low affinity epidermal growth factor receptors. Inhibition of high affinity component by low temperature, cycloheximide, and phorbol esters. J. Biol. Chem. 1982, 257, 3053-3060.
    • (1982) J. Biol. Chem , vol.257 , pp. 3053-3060
    • King, A.C.1    Cuatrecasas, P.2
  • 177
    • 0010233988 scopus 로고
    • Growth stimulation of A431 cells by epidermal growth factor: Identification of high-affinity receptors for epidermal growth factor by an anti-receptor monoclonal antibody
    • Kawamoto, T.; Sato, J. D.; Le, A.; Polikoff, J.; Sato, G. H.; Mendelsohn, J. Growth stimulation of A431 cells by epidermal growth factor: Identification of high-affinity receptors for epidermal growth factor by an anti-receptor monoclonal antibody. Proc. Natl. Acad. Sci. USA 1983, 80, 1337-1341.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 1337-1341
    • Kawamoto, T.1    Sato, J.D.2    Le, A.3    Polikoff, J.4    Sato, G.H.5    Mendelsohn, J.6
  • 179
    • 0025020407 scopus 로고
    • High-affinity epidermal growth factor binding is specifically reduced by a monoclonal antibody, and appears necessary for early responses
    • Bellot, F.; Moolenaar, W.; Kris, R.; Mirakhur, B.; Verlaan, I.; Ullrich, A.; Schlessinger, J.; Felder, S. High-affinity epidermal growth factor binding is specifically reduced by a monoclonal antibody, and appears necessary for early responses. J. Cell Biol. 1990, 110, 491-502.
    • (1990) J. Cell Biol , vol.110 , pp. 491-502
    • Bellot, F.1    Moolenaar, W.2    Kris, R.3    Mirakhur, B.4    Verlaan, I.5    Ullrich, A.6    Schlessinger, J.7    Felder, S.8
  • 180
    • 0021220257 scopus 로고
    • Protein kinase C phosphorylation of the EGF receptor at a threonine residue close to the cytoplasmic face of the plasma membrane
    • Hunter, T.; Ling, N.; Cooper, J. A. Protein kinase C phosphorylation of the EGF receptor at a threonine residue close to the cytoplasmic face of the plasma membrane. Nature 1984, 311, 480-483.
    • (1984) Nature , vol.311 , pp. 480-483
    • Hunter, T.1    Ling, N.2    Cooper, J.A.3
  • 182
    • 0023028733 scopus 로고
    • Reconstitution of human epidermal growth factor receptors and its deletion mutants in cultured hamster cells
    • Livneh, E.; Prywes, R.; Kashles, O.; Reiss, N.; Sasson, I.; Mory, Y.; Ullrich, A.; Schlessinger, J. Reconstitution of human epidermal growth factor receptors and its deletion mutants in cultured hamster cells. J. Biol. Chem. 1986, 261, 12490-12497.
    • (1986) J. Biol. Chem , vol.261 , pp. 12490-12497
    • Livneh, E.1    Prywes, R.2    Kashles, O.3    Reiss, N.4    Sasson, I.5    Mory, Y.6    Ullrich, A.7    Schlessinger, J.8
  • 183
    • 0026708050 scopus 로고
    • Implications of epidermal growth factor (EGF) induced egf receptor aggregation
    • Wofsy, C.; Goldstein, B.; Lund, K.; Wiley, H. S. Implications of epidermal growth factor (EGF) induced egf receptor aggregation. Biophys. J. 1992, 63, 98-110.
    • (1992) Biophys. J , vol.63 , pp. 98-110
    • Wofsy, C.1    Goldstein, B.2    Lund, K.3    Wiley, H.S.4
  • 185
    • 0742288415 scopus 로고    scopus 로고
    • A structure-based model for ligand binding and dimerization of EGF receptors
    • Klein, P.; Mattoon, D.; Lemmon, M. A.; Schlessinger, J. A structure-based model for ligand binding and dimerization of EGF receptors. Proc. Natl. Acad. Sci. USA 2004, 101, 929-934.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 929-934
    • Klein, P.1    Mattoon, D.2    Lemmon, M.A.3    Schlessinger, J.4
  • 186
    • 0034668798 scopus 로고    scopus 로고
    • Thermodynamic mixing of molecular states of the epidermal growth factor receptor modulates macroscopic ligand binding affinity
    • Holbrook, M. R.; Slakey, L. L.; Gross, D. J. Thermodynamic mixing of molecular states of the epidermal growth factor receptor modulates macroscopic ligand binding affinity. Biochem. J. 2000, 352, 99-108.
    • (2000) Biochem. J , vol.352 , pp. 99-108
    • Holbrook, M.R.1    Slakey, L.L.2    Gross, D.J.3
  • 187
    • 20444409504 scopus 로고    scopus 로고
    • Heterogeneities in EGF receptor density at the cell surface can lead to concave up scatchard plot of EGF binding
    • Mayawala, K.; Vlachos, D. G.; Edwards, J. S. Heterogeneities in EGF receptor density at the cell surface can lead to concave up scatchard plot of EGF binding. FEBS Lett. 2005, 579, 3043-3047.
    • (2005) FEBS Lett , vol.579 , pp. 3043-3047
    • Mayawala, K.1    Vlachos, D.G.2    Edwards, J.S.3
  • 188
    • 77955627615 scopus 로고    scopus 로고
    • Structural basis for negative cooperativity in growth factor binding to an EGF receptor
    • Alvarado, D.; Klein, D. E.; Lemmon, M. A. Structural basis for negative cooperativity in growth factor binding to an EGF receptor. Cell 2010, 142, 568-579.
    • (2010) Cell , vol.142 , pp. 568-579
    • Alvarado, D.1    Klein, D.E.2    Lemmon, M.A.3
  • 190
    • 0033779765 scopus 로고    scopus 로고
    • Single-molecule imaging of EGFR signalling on the surface of living cells
    • Sako, Y.; Minoghchi, S.; Yanagida, T. Single-molecule imaging of EGFR signalling on the surface of living cells. Nat. Cell Biol. 2000, 2, 168-172.
    • (2000) Nat. Cell Biol , vol.2 , pp. 168-172
    • Sako, Y.1    Minoghchi, S.2    Yanagida, T.3
  • 191
    • 84868323253 scopus 로고    scopus 로고
    • Mechanisms for kinase-mediated dimerization of the epidermal growth factor receptor
    • Lu, C.; Mi, L. Z.; Schurpf, T.; Walz, T.; Springer, T. A. Mechanisms for kinase-mediated dimerization of the epidermal growth factor receptor. J. Biol. Chem. 2012, 287, 38244-38253.
    • (2012) J. Biol. Chem , vol.287 , pp. 38244-38253
    • Lu, C.1    Mi, L.Z.2    Schurpf, T.3    Walz, T.4    Springer, T.A.5
  • 192
    • 78651399024 scopus 로고    scopus 로고
    • The tethering arm of the EGF receptor is required for negative cooperativity and signal transduction
    • Adak, S.; DeAndrade, D.; Pike, L. J. The tethering arm of the EGF receptor is required for negative cooperativity and signal transduction. J. Biol. Chem. 2011, 286, 1545-1555.
    • (2011) J. Biol. Chem , vol.286 , pp. 1545-1555
    • Adak, S.1    DeAndrade, D.2    Pike, L.J.3
  • 193
    • 84455161571 scopus 로고    scopus 로고
    • The membrane-proximal intracellular domain of the epidermal growth factor receptor underlies negative cooperativity in ligand binding
    • Adak, S.; Yang, K. S.; Macdonald-Obermann, J.; Pike, L. J. The membrane-proximal intracellular domain of the epidermal growth factor receptor underlies negative cooperativity in ligand binding. J. Biol. Chem. 2011, 286, 45146-45155.
    • (2011) J. Biol. Chem , vol.286 , pp. 45146-45155
    • Adak, S.1    Yang, K.S.2    Macdonald-Obermann, J.3    Pike, L.J.4
  • 194
    • 0022393612 scopus 로고
    • Autophosphorylation and protein kinase C phosphorylation of the epidermal growth factor receptor. Effect on tyrosine kinase activity and ligand binding affinity
    • Downward, J.; Waterfield, M. D.; Parker, P. J. Autophosphorylation and protein kinase C phosphorylation of the epidermal growth factor receptor. Effect on tyrosine kinase activity and ligand binding affinity. J. Biol. Chem. 1985, 260, 14538-14546.
    • (1985) J. Biol. Chem , vol.260 , pp. 14538-14546
    • Downward, J.1    Waterfield, M.D.2    Parker, P.J.3
  • 195
    • 0028217645 scopus 로고
    • High affinity nerve growth factor binding displays a faster rate of association than p140trk binding. Implications for multi-subunit polypeptide receptors
    • Mahadeo, D.; Kaplan, L.; Chao, M. V.; Hempstead, B. L. High affinity nerve growth factor binding displays a faster rate of association than p140trk binding. Implications for multi-subunit polypeptide receptors. J. Biol. Chem. 1994, 269, 6884-6891.
    • (1994) J. Biol. Chem , vol.269 , pp. 6884-6891
    • Mahadeo, D.1    Kaplan, L.2    Chao, M.V.3    Hempstead, B.L.4
  • 196
    • 0025905180 scopus 로고
    • Keeping track of neurotrophin receptors
    • Bothwell, M. Keeping track of neurotrophin receptors. Cell 1991, 65, 915-918.
    • (1991) Cell , vol.65 , pp. 915-918
    • Bothwell, M.1
  • 197
    • 0026730310 scopus 로고
    • Neurotrophin receptors: A window into neuronal differentiation
    • Chao, M. V. Neurotrophin receptors: A window into neuronal differentiation. Neuron 1992, 9, 583-593.
    • (1992) Neuron , vol.9 , pp. 583-593
    • Chao, M.V.1
  • 198
    • 0034637553 scopus 로고    scopus 로고
    • p75 reduces TrkB tyrosine autophosphorylation in response to brain-derived neurotrophic factor and neurotrophin 4/5
    • Vesa, J.; Kruttgen, A.; Shooter, E. M. p75 reduces TrkB tyrosine autophosphorylation in response to brain-derived neurotrophic factor and neurotrophin 4/5. J. Biol. Chem. 2000, 275, 24414-24420.
    • (2000) J. Biol. Chem , vol.275 , pp. 24414-24420
    • Vesa, J.1    Kruttgen, A.2    Shooter, E.M.3
  • 199
    • 33845707629 scopus 로고    scopus 로고
    • High affinity not in the vicinity?
    • Barker, P. A. High affinity not in the vicinity? Neuron 2007, 53, 1-4.
    • (2007) Neuron , vol.53 , pp. 1-4
    • Barker, P.A.1
  • 200
    • 0035980009 scopus 로고    scopus 로고
    • The cytoplasmic and transmembrane domains of the p75 and Trk A receptors regulate high affinity binding to nerve growth factor
    • Esposito, D.; Patel, P.; Stephens, R. M.; Perez, P.; Chao, M. V.; Kaplan, D. R.; Hempstead, B. L. The cytoplasmic and transmembrane domains of the p75 and Trk A receptors regulate high affinity binding to nerve growth factor. J. Biol. Chem. 2001, 276, 32687-32695.
    • (2001) J. Biol. Chem , vol.276 , pp. 32687-32695
    • Esposito, D.1    Patel, P.2    Stephens, R.M.3    Perez, P.4    Chao, M.V.5    Kaplan, D.R.6    Hempstead, B.L.7
  • 201
    • 0026649556 scopus 로고
    • Transmembrane signaling by the human insulin receptor kinase. Relationship between intramolecular beta subunit trans-and cis-autophosphorylation and substrate kinase activation
    • Frattali, A. L.; Treadway, J. L.; Pessin, J. E. Transmembrane signaling by the human insulin receptor kinase. Relationship between intramolecular beta subunit trans-and cis-autophosphorylation and substrate kinase activation. J. Biol. Chem. 1992, 267, 19521-19528.
    • (1992) J. Biol. Chem , vol.267 , pp. 19521-19528
    • Frattali, A.L.1    Treadway, J.L.2    Pessin, J.E.3
  • 202
    • 0036782071 scopus 로고    scopus 로고
    • Structural biology of insulin and IGF1 receptors: Implication for drug design
    • De Meyts, P.; Whittaker, J. Structural biology of insulin and IGF1 receptors: Implication for drug design. Nat. Rev. Drug Discov. 2002, 1, 769-783.
    • (2002) Nat. Rev. Drug Discov , vol.1 , pp. 769-783
    • De Meyts, P.1    Whittaker, J.2
  • 203
    • 0028146822 scopus 로고
    • The structural basis of insulin and insulin-like growth factor-I receptor binding and negative co-operativity, and its relevance to mitogenic versus metabolic signaling
    • De Meyts, P. The structural basis of insulin and insulin-like growth factor-I receptor binding and negative co-operativity, and its relevance to mitogenic versus metabolic signaling. Diabetologia 1994, 37, S135-S148.
    • (1994) Diabetologia , vol.37
    • De Meyts, P.1
  • 204
    • 48149095486 scopus 로고    scopus 로고
    • The insulin receptor: A prototype for dimeric, allosteric membrane receptors?
    • De Meyts, P. The insulin receptor: A prototype for dimeric, allosteric membrane receptors? Trends Biochem. Sci. 2008, 33, 376-384.
    • (2008) Trends Biochem. Sci , vol.33 , pp. 376-384
    • De Meyts, P.1
  • 205
    • 60749092852 scopus 로고    scopus 로고
    • Harmonic oscillator model of the insulin and IGF1 receptors' allosteric binding and activation
    • Kiselyov, V. V.; Versteyhe, S.; Gauguin, L.; De Meyts, P. Harmonic oscillator model of the insulin and IGF1 receptors' allosteric binding and activation. Mol. Syst. Biol. 2009, 5, 243.
    • (2009) Mol. Syst. Biol , vol.5 , pp. 243
    • Kiselyov, V.V.1    Versteyhe, S.2    Gauguin, L.3    De Meyts, P.4
  • 206
    • 82455186745 scopus 로고    scopus 로고
    • Insight into the molecular basis for the kinetic differences between the two insulin receptor isoforms
    • Knudsen, L.; De Meyts, P.; Kiselyov, V. V. Insight into the molecular basis for the kinetic differences between the two insulin receptor isoforms. Biochem. J. 2011, 440, 397-403.
    • (2011) Biochem. J , vol.440 , pp. 397-403
    • Knudsen, L.1    De Meyts, P.2    Kiselyov, V.V.3
  • 207
    • 0023262816 scopus 로고
    • The insulin receptor. Structural basis for high affinity ligand binding
    • Boni-Schnetzler, M.; Scott, W.; Waugh, S. M.; DiBella, E.; Pilch, P. F. The insulin receptor. Structural basis for high affinity ligand binding. J. Biol. Chem. 1987, 262, 8395-401.
    • (1987) J. Biol. Chem , vol.262 , pp. 8395-8401
    • Boni-Schnetzler, M.1    Scott, W.2    Waugh, S.M.3    DiBella, E.4    Pilch, P.F.5
  • 208
    • 0023267760 scopus 로고
    • Isolation of functional alpha beta heterodimers from the purified human placental alpha 2 beta 2 heterotetrameric insulin receptor complex. A structural basis for insulin binding
    • Sweet, L. J.; Morrison, B. D.; Pessin, J. E. Isolation of functional alpha beta heterodimers from the purified human placental alpha 2 beta 2 heterotetrameric insulin receptor complex. A structural basis for insulin binding. J. Biol. Chem. 1987, 262, 6939-6942.
    • (1987) J. Biol. Chem , vol.262 , pp. 6939-6942
    • Sweet, L.J.1    Morrison, B.D.2    Pessin, J.E.3
  • 209
    • 0020594584 scopus 로고
    • Stoichiometry for the binding of insulin to insulin receptors in adipocyte membranes
    • Pang, D. T.; Shafer, J. A. Stoichiometry for the binding of insulin to insulin receptors in adipocyte membranes. J. Biol. Chem. 1983, 258, 2514-2518.
    • (1983) J. Biol. Chem , vol.258 , pp. 2514-2518
    • Pang, D.T.1    Shafer, J.A.2
  • 210
    • 0021267830 scopus 로고
    • Evidence that insulin receptor from human placenta has a high affinity for only one molecule of insulin
    • Pang, D. T.; Shafer, J. A. Evidence that insulin receptor from human placenta has a high affinity for only one molecule of insulin. J. Biol. Chem. 1984, 259, 8589-8596.
    • (1984) J. Biol. Chem , vol.259 , pp. 8589-8596
    • Pang, D.T.1    Shafer, J.A.2
  • 211
    • 0034598998 scopus 로고    scopus 로고
    • Properties of an insulin receptor with an IGF-1 receptor loop exchange in the cysteine-rich region
    • Hoyne, P. A.; Elleman, T. C.; Adams, T. E.; Richards, K. M.; Ward, C. W. Properties of an insulin receptor with an IGF-1 receptor loop exchange in the cysteine-rich region. FEBS Lett. 2000, 469, 57-60.
    • (2000) FEBS Lett , vol.469 , pp. 57-60
    • Hoyne, P.A.1    Elleman, T.C.2    Adams, T.E.3    Richards, K.M.4    Ward, C.W.5
  • 212
    • 0021164871 scopus 로고
    • Insulin-receptor interactions. Presence of a positive cooperative effect
    • Marsh, J. W.; Westley, J.; Steiner, D. F. Insulin-receptor interactions. Presence of a positive cooperative effect. J. Biol. Chem. 1984, 259, 6641-6649.
    • (1984) J. Biol. Chem , vol.259 , pp. 6641-6649
    • Marsh, J.W.1    Westley, J.2    Steiner, D.F.3
  • 213
    • 0022499546 scopus 로고
    • A chimaeric receptor allows insulin to stimulate tyrosine kinase activity of epidermal growth factor receptor
    • Riedel, H.; Dull, T. J.; Schlessinger, J.; Ullrich, A. A chimaeric receptor allows insulin to stimulate tyrosine kinase activity of epidermal growth factor receptor. Nature 1986, 324, 68-70.
    • (1986) Nature , vol.324 , pp. 68-70
    • Riedel, H.1    Dull, T.J.2    Schlessinger, J.3    Ullrich, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.