메뉴 건너뛰기




Volumn 1800, Issue 9, 2010, Pages 1018-1026

A monovalent agonist of TrkA tyrosine kinase receptors can be converted into a bivalent antagonist

Author keywords

Agonist; Antagonist; Ligand; Linker; Neurotrophin; Tyrosine kinase receptor

Indexed keywords

HOMODIMER; NERVE GROWTH FACTOR RECEPTOR; PEPTIDOMIMETIC AGENT; PROTEIN TYROSINE KINASE A; TYROSINE KINASE RECEPTOR; NERVE GROWTH FACTOR; NGF PROTEIN, HUMAN; OLIGOPEPTIDE; PROTEIN BINDING; PROTEIN KINASE INHIBITOR;

EID: 77955282196     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2010.06.007     Document Type: Article
Times cited : (14)

References (32)
  • 1
    • 0030907924 scopus 로고    scopus 로고
    • Signal transduction by the neurotrophin receptors
    • Kaplan D.R., Miller F.D. Signal transduction by the neurotrophin receptors. Curr. Opin. Cell Biol. 1997, 9:213-221.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 213-221
    • Kaplan, D.R.1    Miller, F.D.2
  • 2
    • 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
  • 3
    • 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
  • 4
    • 0034615946 scopus 로고    scopus 로고
    • Genuine monovalent ligands of TrkA nerve growth factor receptors reveal a novel pharmacological mechanism of action
    • Maliartchouk S., Debeir T., Beglova N., Cuello A.C., Gehring K., Saragovi H.U. Genuine monovalent ligands of TrkA nerve growth factor receptors reveal a novel pharmacological mechanism of action. J. Biol. Chem. 2000, 275:9946-9956.
    • (2000) J. Biol. Chem. , vol.275 , pp. 9946-9956
    • Maliartchouk, S.1    Debeir, T.2    Beglova, N.3    Cuello, A.C.4    Gehring, K.5    Saragovi, H.U.6
  • 5
    • 0030877884 scopus 로고    scopus 로고
    • Optimal nerve growth factor trophic signals mediated by synergy of TrkA and p75 receptor-specific ligands
    • Maliartchouk S., Saragovi H.U. Optimal nerve growth factor trophic signals mediated by synergy of TrkA and p75 receptor-specific ligands. J. Neurosci. 1997, 17:6031-6037.
    • (1997) J. Neurosci. , vol.17 , pp. 6031-6037
    • Maliartchouk, S.1    Saragovi, H.U.2
  • 7
    • 0029826905 scopus 로고    scopus 로고
    • Hormone Mimicry
    • Wells J.A. Hormone Mimicry. Science 1996, 273:449-450.
    • (1996) Science , vol.273 , pp. 449-450
    • Wells, J.A.1
  • 8
    • 0031409894 scopus 로고    scopus 로고
    • Growth factor receptors: structure, mechanism, and drug discovery
    • McInnes C., Sykes B.D. Growth factor receptors: structure, mechanism, and drug discovery. Biopolymers 1997, 43:339-366.
    • (1997) Biopolymers , vol.43 , pp. 339-366
    • McInnes, C.1    Sykes, B.D.2
  • 11
    • 36049003755 scopus 로고    scopus 로고
    • Gambogic amide, a selective agonist for TrkA receptor that possesses robust neurotrophic activity, prevents neuronal cell death
    • Jang S.W., Okada M., Sayeed I., Xiao G., Stein D., Jin P., Ye K. Gambogic amide, a selective agonist for TrkA receptor that possesses robust neurotrophic activity, prevents neuronal cell death. Proc. Natl Acad. Sci. USA 2007, 104:16329-16334.
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 16329-16334
    • Jang, S.W.1    Okada, M.2    Sayeed, I.3    Xiao, G.4    Stein, D.5    Jin, P.6    Ye, K.7
  • 13
    • 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
  • 14
    • 73949119705 scopus 로고    scopus 로고
    • An agonistic mAb directed to the TrkC receptor juxtamembrane region defines a trophic hot spot, and interactions with p75 co-receptors
    • Guillemard V., Ivanisevic L., Garcia A.G., Scholten V., Lazo O.M., Bronfman F.C., Saragovi H.U. An agonistic mAb directed to the TrkC receptor juxtamembrane region defines a trophic hot spot, and interactions with p75 co-receptors. Dev. Neurobiol. 2010, 70(3):150-164.
    • (2010) Dev. Neurobiol. , vol.70 , Issue.3 , pp. 150-164
    • Guillemard, V.1    Ivanisevic, L.2    Garcia, A.G.3    Scholten, V.4    Lazo, O.M.5    Bronfman, F.C.6    Saragovi, H.U.7
  • 16
    • 70349270689 scopus 로고    scopus 로고
    • Bivalent peptidomimetic ligands of TrkC are biased agonists and selectively induce neuritogenesis or potentiate neurotrophin-3 trophic signals
    • Chen D., Brahimi F., Angell Y., Li Y.C., Moscowicz J., Saragovi H.U., Burgess K. Bivalent peptidomimetic ligands of TrkC are biased agonists and selectively induce neuritogenesis or potentiate neurotrophin-3 trophic signals. ACS Chem. Biol. 2009, 4:769-781.
    • (2009) ACS Chem. Biol. , vol.4 , pp. 769-781
    • Chen, D.1    Brahimi, F.2    Angell, Y.3    Li, Y.C.4    Moscowicz, J.5    Saragovi, H.U.6    Burgess, K.7
  • 17
    • 34447128781 scopus 로고    scopus 로고
    • TrkA receptor "hot spots" for binding of NT-3 as a heterologous ligand
    • Ivanisevic L., Zheng W., Woo S.B., Neet K.E., Saragovi H.U. TrkA receptor "hot spots" for binding of NT-3 as a heterologous ligand. J. Biol. Chem. 2007, 282:16754-16763.
    • (2007) J. Biol. Chem. , vol.282 , pp. 16754-16763
    • Ivanisevic, L.1    Zheng, W.2    Woo, S.B.3    Neet, K.E.4    Saragovi, H.U.5
  • 18
    • 0035903101 scopus 로고    scopus 로고
    • P75 Co-receptors regulate ligand-dependent and ligand-independent Trk receptor activation, in part by altering Trk docking subdomains
    • Zaccaro M.C., Ivanisevic L., Perez P., Meakin S.O., Saragovi H.U. p75 Co-receptors regulate ligand-dependent and ligand-independent Trk receptor activation, in part by altering Trk docking subdomains. J. Biol. Chem. 2001, 276:31023-31029.
    • (2001) J. Biol. Chem. , vol.276 , pp. 31023-31029
    • Zaccaro, M.C.1    Ivanisevic, L.2    Perez, P.3    Meakin, S.O.4    Saragovi, H.U.5
  • 19
    • 0028912281 scopus 로고
    • Small Peptide Mimics of Nerve Growth Factor Bind TrkA Receptors and Affect Biological Responses
    • LeSauteur L., Wei L., Gibbs B., Saragovi H.U. Small Peptide Mimics of Nerve Growth Factor Bind TrkA Receptors and Affect Biological Responses. J. Biol. Chem. 1995, 270:6564-6569.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6564-6569
    • LeSauteur, L.1    Wei, L.2    Gibbs, B.3    Saragovi, H.U.4
  • 21
    • 0035219761 scopus 로고    scopus 로고
    • A Rigid Linker-Scaffold for Solid Phase Synthesis of Dimeric Pharmacophores
    • Pattarawarapan M., Chen J., Steffensen M., Burgess K. A Rigid Linker-Scaffold for Solid Phase Synthesis of Dimeric Pharmacophores. J. Comb. Chem. 2001, 3:102-116.
    • (2001) J. Comb. Chem. , vol.3 , pp. 102-116
    • Pattarawarapan, M.1    Chen, J.2    Steffensen, M.3    Burgess, K.4
  • 22
    • 0037179650 scopus 로고    scopus 로고
    • 10 β-Turn Peptidomimetics Leading To The First Reported Small Molecule Mimic of Neurotrophin-3
    • 10 β-Turn Peptidomimetics Leading To The First Reported Small Molecule Mimic of Neurotrophin-3. J. Med. Chem. 2002, 45:4387-4390.
    • (2002) J. Med. Chem. , vol.45 , pp. 4387-4390
    • Pattarawarapan, M.1    Zaccaro, M.C.2    Saragovi, U.3    Burgess, K.4
  • 23
    • 34447562933 scopus 로고    scopus 로고
    • Neurotrophic rationale in glaucoma: a TrkA agonist, but not NGF or a p75 antagonist, protects retinal ganglion cells in vivo
    • Shi Z., Birman E., Saragovi H.U. Neurotrophic rationale in glaucoma: a TrkA agonist, but not NGF or a p75 antagonist, protects retinal ganglion cells in vivo. Dev. Neurobiol. 2007, 67:884-894.
    • (2007) Dev. Neurobiol. , vol.67 , pp. 884-894
    • Shi, Z.1    Birman, E.2    Saragovi, H.U.3
  • 24
    • 4644297646 scopus 로고    scopus 로고
    • Long-lasting rescue of age-associated deficits in cognition and the CNS cholinergic phenotype by a partial agonist peptidomimetic ligand of TrkA
    • Bruno M.A., Clarke P.B., Seltzer A., Quirion R., Burgess K., Cuello A.C., Saragovi H.U. Long-lasting rescue of age-associated deficits in cognition and the CNS cholinergic phenotype by a partial agonist peptidomimetic ligand of TrkA. J. Neurosci. 2004, 24:8009-8018.
    • (2004) J. Neurosci. , vol.24 , pp. 8009-8018
    • Bruno, M.A.1    Clarke, P.B.2    Seltzer, A.3    Quirion, R.4    Burgess, K.5    Cuello, A.C.6    Saragovi, H.U.7
  • 25
    • 62949123326 scopus 로고    scopus 로고
    • Inhibition of p75(NTR) in glia potentiates TrkA-mediated survival of injured retinal ganglion cells
    • Lebrun-Julien F., Morquette B., Douillette A., Saragovi H.U., Di Polo A. Inhibition of p75(NTR) in glia potentiates TrkA-mediated survival of injured retinal ganglion cells. Mol. Cell. Neurosci. 2009, 40:410-420.
    • (2009) Mol. Cell. Neurosci. , vol.40 , pp. 410-420
    • Lebrun-Julien, F.1    Morquette, B.2    Douillette, A.3    Saragovi, H.U.4    Di Polo, A.5
  • 26
    • 0032725569 scopus 로고    scopus 로고
    • NAr Macrocyclizations to Give Turn-extended-turn Peptidomimetics
    • NAr Macrocyclizations to Give Turn-extended-turn Peptidomimetics. Chem. A Eur. J. 1999, 5:3261-3272.
    • (1999) Chem. A Eur. J. , vol.5 , pp. 3261-3272
    • Feng, Y.1    Burgess, K.2
  • 27
    • 40149107624 scopus 로고    scopus 로고
    • A combinatorial method for solution-phase synthesis of labeled bivalent beta-turn mimics
    • Angell Y., Chen D., Brahimi F., Saragovi H.U., Burgess K. A combinatorial method for solution-phase synthesis of labeled bivalent beta-turn mimics. J. Am. Chem. Soc. 2008, 130:556-565.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 556-565
    • Angell, Y.1    Chen, D.2    Brahimi, F.3    Saragovi, H.U.4    Burgess, K.5
  • 28
    • 0033860103 scopus 로고    scopus 로고
    • TrkA immunoglobulin-like ligand binding domains inhibit spontaneous activation of the receptor
    • Arevalo J., Conde B., Hempstead B., Chao M., 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.1    Conde, B.2    Hempstead, B.3    Chao, M.4    Martin-Zanca, D.5    Perez, P.6
  • 29
    • 0035826109 scopus 로고    scopus 로고
    • A novel mutation within the extracellular domain of TrkA causes constitutive receptor activation
    • Arevalo J., Conde B., Hempstead B., Chao M., Martin-Zanca D., Perez P. A novel mutation within the extracellular domain of TrkA causes constitutive receptor activation. Oncogene 2001, 20:1229-1234.
    • (2001) Oncogene , vol.20 , pp. 1229-1234
    • Arevalo, J.1    Conde, B.2    Hempstead, B.3    Chao, M.4    Martin-Zanca, D.5    Perez, P.6
  • 30
    • 33845306460 scopus 로고    scopus 로고
    • Transmembrane helix packing of ErbB/Neu receptor in membrane environment: a molecular dynamics study
    • Aller P., Garnier N., Genest M. Transmembrane helix packing of ErbB/Neu receptor in membrane environment: a molecular dynamics study. J. Biomol. Struct. Dyn. 2006, 24:209-228.
    • (2006) J. Biomol. Struct. Dyn. , vol.24 , pp. 209-228
    • Aller, P.1    Garnier, N.2    Genest, M.3
  • 31
    • 0031010495 scopus 로고    scopus 로고
    • Secondary dimerization between members of the epidermal growth factor receptor family
    • Gamett D.C., Pearson G., Cerione R.A., Friedberg I. Secondary dimerization between members of the epidermal growth factor receptor family. J. Biol. Chem. 1997, 272:12052-12056.
    • (1997) J. Biol. Chem. , vol.272 , pp. 12052-12056
    • Gamett, D.C.1    Pearson, G.2    Cerione, R.A.3    Friedberg, I.4
  • 32
    • 0030987181 scopus 로고    scopus 로고
    • A model for the activation of the epidermal growth factor receptor kinase involvement of an asymmetric dimer?
    • Groenen L.C., Walker F., Burgess A.W., Treutlein H.R. A model for the activation of the epidermal growth factor receptor kinase involvement of an asymmetric dimer?. Biochemistry 1997, 36:3826-3836.
    • (1997) Biochemistry , vol.36 , pp. 3826-3836
    • Groenen, L.C.1    Walker, F.2    Burgess, A.W.3    Treutlein, H.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.