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Volumn 9, Issue 15, 1999, Pages

Receptor signaling: When dimerization is not enough

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA;

EID: 0033615077     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-9822(99)80357-1     Document Type: Note
Times cited : (157)

References (25)
  • 1
    • 0028838012 scopus 로고
    • Dimerization of cell surface receptors in signal transduction
    • Heldin CH: Dimerization of cell surface receptors in signal transduction. Cell 1995, 80:213-223.
    • (1995) Cell , vol.80 , pp. 213-223
    • Heldin, C.H.1
  • 4
    • 0033548259 scopus 로고    scopus 로고
    • Crystallographic evidence for preformed dimers of erythropoietin receptor before ligand activation
    • Livnah O, Stura EA, Middleton SA, Johnson DL, Jolliffe LK, Wilson IA: Crystallographic evidence for preformed dimers of erythropoietin receptor before ligand activation. Science 1999, 283:987-990.
    • (1999) Science , vol.283 , pp. 987-990
    • Livnah, O.1    Stura, E.A.2    Middleton, S.A.3    Johnson, D.L.4    Jolliffe, L.K.5    Wilson, I.A.6
  • 5
    • 0033548048 scopus 로고    scopus 로고
    • Erythropoietin receptor activation by a ligand-induced conformation change
    • Remy I, Wilson IA, Michnick SW: Erythropoietin receptor activation by a ligand-induced conformation change. Science 1999, 283:990-993.
    • (1999) Science , vol.283 , pp. 990-993
    • Remy, I.1    Wilson, I.A.2    Michnick, S.W.3
  • 7
    • 0031842104 scopus 로고    scopus 로고
    • Activation of neu (ErbB-2) mediated by disulfide bond-induced dimerization reveals a receptor tyrosine kinase dimer interface
    • Burke CL, Stern DF: Activation of neu (ErbB-2) mediated by disulfide bond-induced dimerization reveals a receptor tyrosine kinase dimer interface. Mol Cell Biol 1998, 18:5371-5379.
    • (1998) Mol Cell Biol , vol.18 , pp. 5371-5379
    • Burke, C.L.1    Stern, D.F.2
  • 8
    • 0024505028 scopus 로고
    • A point mutation in the neu oncogene mimics ligand induction of receptor aggregation
    • Weiner DB, Liu J, Cohen JA, Williams WV, Greene MI: A point mutation in the neu oncogene mimics ligand induction of receptor aggregation. Nature 1989, 339:230-231.
    • (1989) Nature , vol.339 , pp. 230-231
    • Weiner, D.B.1    Liu, J.2    Cohen, J.A.3    Williams, W.V.4    Greene, M.I.5
  • 9
    • 0029881315 scopus 로고    scopus 로고
    • Strong hydrogen bonding interactions involving a buried glutamic acid in the transmembrane sequence of the neu/erbB-2 receptor
    • Smith SO, Smith CS, Bormann BJ: Strong hydrogen bonding interactions involving a buried glutamic acid in the transmembrane sequence of the neu/erbB-2 receptor. Nat Struct Biol 1996, 3:252-258.
    • (1996) Nat Struct Biol , vol.3 , pp. 252-258
    • Smith, S.O.1    Smith, C.S.2    Bormann, B.J.3
  • 11
    • 0029742943 scopus 로고    scopus 로고
    • Activation of the erythropoietin (EPO) receptor by bivalent anti-EPO receptor antibodies
    • Elliott S, Lorenzini T, Yanagihara D, Chang D, Elliott G: Activation of the erythropoietin (EPO) receptor by bivalent anti-EPO receptor antibodies. J Biol Chem 1996, 271:24691-24697.
    • (1996) J Biol Chem , vol.271 , pp. 24691-24697
    • Elliott, S.1    Lorenzini, T.2    Yanagihara, D.3    Chang, D.4    Elliott, G.5
  • 12
    • 0028332086 scopus 로고
    • Activation and inhibition of erythropoietin receptor function: Role of receptor dimerization
    • Watowich SS, Hilton DJ, Lodish HF: Activation and inhibition of erythropoietin receptor function: Role of receptor dimerization. Mol Cell Biol 1994, 14:3535-3549.
    • (1994) Mol Cell Biol , vol.14 , pp. 3535-3549
    • Watowich, S.S.1    Hilton, D.J.2    Lodish, H.F.3
  • 13
    • 0031739144 scopus 로고    scopus 로고
    • Structural basis for cytokine hormone-receptor recognition and receptor activation
    • Kossiakoff AA, De Vos AM: Structural basis for cytokine hormone-receptor recognition and receptor activation. Adv Protein Chem 1998, 52:67-108.
    • (1998) Adv Protein Chem , vol.52 , pp. 67-108
    • Kossiakoff, A.A.1    De Vos, A.M.2
  • 14
    • 0028832719 scopus 로고    scopus 로고
    • Point mutations within a dimer interface homology domain of c-Mpl induce constitutive receptor activity and tumorigenicity
    • Alexander WS, Metcalf D, Dunn AR: Point mutations within a dimer interface homology domain of c-Mpl induce constitutive receptor activity and tumorigenicity. EMBO J 1995, 14:5569-5578.
    • EMBO J 1995 , vol.14 , pp. 5569-5578
    • Alexander, W.S.1    Metcalf, D.2    Dunn, A.R.3
  • 15
    • 0025274249 scopus 로고
    • A sequence motif in the transmembrane region of growth factor receptors with tyrosine kinase activity mediates dimerization
    • Sternberg MJ, Gullick WJ: A sequence motif in the transmembrane region of growth factor receptors with tyrosine kinase activity mediates dimerization. Protein Eng 1990, 3:245-248.
    • (1990) Protein Eng , vol.3 , pp. 245-248
    • Sternberg, M.J.1    Gullick, W.J.2
  • 16
    • 0028018178 scopus 로고
    • Signalling through the insulin receptor and the receptor insulin-like growth factor-I receptor
    • Van Obberghen E: Signalling through the insulin receptor and the insulin-like growth factor-I receptor. Diabetologia 1994, 37:S125-134.
    • (1994) Diabetologia , vol.37
    • Van Obberghen, E.1
  • 17
    • 0029069758 scopus 로고
    • Crystallographic evidence for dimerization of unliganded tumor necrosis factor receptor
    • Naismith JH, Devine TQ, Brandhuber BJ, Sprang SR: Crystallographic evidence for dimerization of unliganded tumor necrosis factor receptor. J Biol Chem 1995, 270:13303-13307.
    • (1995) J Biol Chem , vol.270 , pp. 13303-13307
    • Naismith, J.H.1    Devine, T.Q.2    Brandhuber, B.J.3    Sprang, S.R.4
  • 18
    • 0030589099 scopus 로고    scopus 로고
    • Structures of the extracellular domain of the type I tumor necrosis factor receptor
    • Naismith JH, Devine TQ, Kohno T, Sprang SR: Structures of the extracellular domain of the type I tumor necrosis factor receptor. Structure 1996, 4:1251-1262.
    • (1996) Structure , vol.4 , pp. 1251-1262
    • Naismith, J.H.1    Devine, T.Q.2    Kohno, T.3    Sprang, S.R.4
  • 19
    • 0033593655 scopus 로고    scopus 로고
    • Prevention of constitutive TNF receptor 1 signaling by silencer of death domains
    • Jiang Y, Woronicz JD, Liu W, Goeddel DV: Prevention of constitutive TNF receptor 1 signaling by silencer of death domains. Science 1999, 283:543-546.
    • (1999) Science , vol.283 , pp. 543-546
    • Jiang, Y.1    Woronicz, J.D.2    Liu, W.3    Goeddel, D.V.4
  • 20
    • 0029865503 scopus 로고    scopus 로고
    • Molecular mechanism of transmembrane signaling by the aspartate receptor: A model
    • Chervitz SA, Falke JJ: Molecular mechanism of transmembrane signaling by the aspartate receptor: A model. Proc Natl Acad Sci USA 1996, 93:2545-2550.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 2545-2550
    • Chervitz, S.A.1    Falke, J.J.2
  • 21
    • 0030041323 scopus 로고    scopus 로고
    • Dimerization of the extracellular domain of the erythropoietin (EPO) receptor by EPO: One high-affinity and one low-affinity interaction
    • Philo JS, Aoki KH, Arakawa T, Narhi LO, Wen J: Dimerization of the extracellular domain of the erythropoietin (EPO) receptor by EPO: One high-affinity and one low-affinity interaction. Biochemistry 1996, 35:1681-1691.
    • (1996) Biochemistry , vol.35 , pp. 1681-1691
    • Philo, J.S.1    Aoki, K.H.2    Arakawa, T.3    Narhi, L.O.4    Wen, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.