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Volumn 6, Issue 10, 2010, Pages 3274-3283

Activating the prolactin receptor: Effect of the ligand on the conformation of the extracellular domain

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EID: 77957958248     PISSN: 15499618     EISSN: 15499626     Source Type: Journal    
DOI: 10.1021/ct1003934     Document Type: Article
Times cited : (2)

References (29)
  • 1
    • 0032460226 scopus 로고    scopus 로고
    • Prolactin (PRL) and its receptor: Actions, signal transduction pathways and phenotypes observed in PRL receptor knockout mice
    • Bole-Feysot, C.; Goffin, V.; Edery, M.; Binart, N.; Kelly, P. A. Prolactin (PRL) and its receptor: Actions, signal transduction pathways and phenotypes observed in PRL receptor knockout mice Endocr. Rev. 1998, 19, 225-268
    • (1998) Endocr. Rev. , vol.19 , pp. 225-268
    • Bole-Feysot, C.1    Goffin, V.2    Edery, M.3    Binart, N.4    Kelly, P.A.5
  • 2
    • 0025162844 scopus 로고
    • Structural design and molecular evolution of a cytokine receptor superfamily
    • Bazan, J. F. Structural design and molecular evolution of a cytokine receptor superfamily Proc. Natl. Acad. Sci. U.S.A. 1990, 87, 6934-6938
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 6934-6938
    • Bazan, J.F.1
  • 3
    • 41149122296 scopus 로고    scopus 로고
    • Pregnancy-induced adaptation in the neuroendocrine control of prolactin secretion
    • Grattan, D. R.; Steyn, F. J.; Kokay, I. C.; Anderson, G. M.; Bunn, S. J. Pregnancy-induced adaptation in the neuroendocrine control of prolactin secretion J. Neuroendocrinol. 2008, 20, 497-507
    • (2008) J. Neuroendocrinol. , vol.20 , pp. 497-507
    • Grattan, D.R.1    Steyn, F.J.2    Kokay, I.C.3    Anderson, G.M.4    Bunn, S.J.5
  • 4
    • 0031958292 scopus 로고    scopus 로고
    • Prolactin receptor gene diversity: Structure and regulation
    • Hu, Z. Z.; Zhuang, L.; Dufau, M. L. Prolactin receptor gene diversity: Structure and regulation Trends Endocrinol. Metab. 1998, 9, 94-102
    • (1998) Trends Endocrinol. Metab. , vol.9 , pp. 94-102
    • Hu, Z.Z.1    Zhuang, L.2    Dufau, M.L.3
  • 5
    • 0037294370 scopus 로고    scopus 로고
    • Alternative splicing to exon 11 of human prolactin receptor gene results in multiple isoforms including a secreted prolactin-binding protein
    • Trott, J. F.; Hovey, R. C.; Koduri, S.; Vonderhaar, B. K. Alternative splicing to exon 11 of human prolactin receptor gene results in multiple isoforms including a secreted prolactin-binding protein J. Mol. Endocrinol. 2003, 30, 31-47
    • (2003) J. Mol. Endocrinol. , vol.30 , pp. 31-47
    • Trott, J.F.1    Hovey, R.C.2    Koduri, S.3    Vonderhaar, B.K.4
  • 6
    • 33751526473 scopus 로고    scopus 로고
    • Ligand-independent dimerization of the human prolactin receptor isoforms: Functional implications
    • Gadd, S. L.; Clevenger, C. V. Ligand-independent dimerization of the human prolactin receptor isoforms: Functional implications Mol. Endocrinol. 2006, 20, 2734-2746
    • (2006) Mol. Endocrinol. , vol.20 , pp. 2734-2746
    • Gadd, S.L.1    Clevenger, C.V.2
  • 7
    • 33746606004 scopus 로고    scopus 로고
    • Ligand-independent homo- and heterodimerization of human prolactin receptor variants: Inhibitory action of the short forms by heterodimerization
    • Qazi, A. M.; Tsai-Morris, C.-H.; Dufau, M. L. Ligand-independent homo- and heterodimerization of human prolactin receptor variants: Inhibitory action of the short forms by heterodimerization Mol. Endocrinol. 2006, 20, 1912-1923
    • (2006) Mol. Endocrinol. , vol.20 , pp. 1912-1923
    • Qazi, A.M.1    Tsai-Morris, C.-H.2    Dufau, M.L.3
  • 8
    • 0028032203 scopus 로고
    • The X-ray structure of a growth hormone-prolactin receptor complex
    • Somers, W.; Ultsch, M.; de Vos, A. M.; Kossiakoff, A. A. The X-ray structure of a growth hormone-prolactin receptor complex Nature 1994, 372, 478-481
    • (1994) Nature , vol.372 , pp. 478-481
    • Somers, W.1    Ultsch, M.2    De Vos, A.M.3    Kossiakoff, A.A.4
  • 11
    • 0029785849 scopus 로고    scopus 로고
    • Real-time kinetic measurements of the interactions between lactogenic hormones and prolactin-receptor extracellular domains from several species support the model of hormone-induced transient receptor dimerization
    • Gertler, A.; Grosclaude, J.; Strasburger, C. J.; Nir, S.; Djiane, J. Real-time kinetic measurements of the interactions between lactogenic hormones and prolactin-receptor extracellular domains from several species support the model of hormone-induced transient receptor dimerization J. Biol. Chem. 1996, 271, 24482-24491
    • (1996) J. Biol. Chem. , vol.271 , pp. 24482-24491
    • Gertler, A.1    Grosclaude, J.2    Strasburger, C.J.3    Nir, S.4    Djiane, J.5
  • 12
    • 0026598960 scopus 로고
    • Human growth hormone and extracellular domain of its receptor: Crystal structure of the complex
    • de Vos, A.; Ultsch, M.; Kossiakoff, A. A. Human growth hormone and extracellular domain of its receptor: Crystal structure of the complex Science 1992, 255, 306-312
    • (1992) Science , vol.255 , pp. 306-312
    • De Vos, A.1    Ultsch, M.2    Kossiakoff, A.A.3
  • 13
    • 0030831289 scopus 로고    scopus 로고
    • Direct evidence that lactogenic hormones induce homodimerization of membrane-anchored prolactin receptor in intact Nb2-11C rat lymphoma cells
    • Sakal, E.; Elberg, G.; Gertler, A. Direct evidence that lactogenic hormones induce homodimerization of membrane-anchored prolactin receptor in intact Nb2-11C rat lymphoma cells FEBS Lett. 1997, 410, 289-292
    • (1997) FEBS Lett. , vol.410 , pp. 289-292
    • Sakal, E.1    Elberg, G.2    Gertler, A.3
  • 15
    • 77951251864 scopus 로고    scopus 로고
    • Turning the growth hormone receptor on: Evidence that hormone binding induces subunit rotation
    • Poger, D.; Mark, A. E. Turning the growth hormone receptor on: Evidence that hormone binding induces subunit rotation Proteins 2010, 78, 1163-1174
    • (2010) Proteins , vol.78 , pp. 1163-1174
    • Poger, D.1    Mark, A.E.2
  • 16
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex, N.; Peitsch, M. SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling Electrophoresis 1997, 18, 2714-2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.2
  • 18
    • 77950101403 scopus 로고    scopus 로고
    • On the validation of molecular dynamics simulations of saturated and cis -monounsaturated phosphatidylcholine lipid bilayers: A comparison with experiment
    • Poger, D.; Mark, A. E. On the validation of molecular dynamics simulations of saturated and cis -monounsaturated phosphatidylcholine lipid bilayers: A comparison with experiment J. Chem. Theory Comput. 2010, 6, 325-336
    • (2010) J. Chem. Theory Comput. , vol.6 , pp. 325-336
    • Poger, D.1    Mark, A.E.2
  • 20
    • 4444282928 scopus 로고    scopus 로고
    • A biomolecular force field based on the free enthalpy of hydration and solvation: The Gromos force-field parameter sets 53a5 and 53a6
    • Oostenbrink, C.; Villa, A.; Mark, A. E.; van Gunsteren, W. F. A biomolecular force field based on the free enthalpy of hydration and solvation: The Gromos force-field parameter sets 53a5 and 53a6 J. Comput. Chem. 2004, 25, 1656-1676
    • (2004) J. Comput. Chem. , vol.25 , pp. 1656-1676
    • Oostenbrink, C.1    Villa, A.2    Mark, A.E.3    Van Gunsteren, W.F.4
  • 21
    • 77950590441 scopus 로고    scopus 로고
    • A new force field for simulating phosphatidylcholine bilayers
    • Poger, D.; van Gunsteren, W. F.; Mark, A. E. A new force field for simulating phosphatidylcholine bilayers J. Comput. Chem. 2010, 30, 117-1125
    • (2010) J. Comput. Chem. , vol.30 , pp. 117-1125
    • Poger, D.1    Van Gunsteren, W.F.2    Mark, A.E.3
  • 22
    • 0002775934 scopus 로고
    • Interaction models for water in relation to protein hydration. in
    • Reidel: Dordrecht, The Netherlands
    • Berendsen, H. J. C.; Postma, J. P. M.; van Gunsteren, W. F.; Hermans, J. Interaction models for water in relation to protein hydration. In Intermolecular Forces; Reidel: Dordrecht, The Netherlands, 1981; pp 331 - 342.
    • (1981) Intermolecular Forces , pp. 331-342
    • Berendsen, H.J.C.1    Postma, J.P.M.2    Van Gunsteren, W.F.3    Hermans, J.4
  • 24
    • 4544369164 scopus 로고
    • A generalized reaction field method for molecular dynamics simulations
    • Tironi, I. G.; Sperb, R.; Smith, P. E.; van Gunsteren, W. F. A generalized reaction field method for molecular dynamics simulations J. Chem. Phys. 1995, 102, 5451-5459
    • (1995) J. Chem. Phys. , vol.102 , pp. 5451-5459
    • Tironi, I.G.1    Sperb, R.2    Smith, P.E.3    Van Gunsteren, W.F.4
  • 26
    • 0001585978 scopus 로고    scopus 로고
    • Improving efficiency of large time-scale molecular dynamics simulations of hydrogen-rich systems
    • Feenstra, K.; Hess, B.; Berendsen, H. J. C. Improving efficiency of large time-scale molecular dynamics simulations of hydrogen-rich systems J. Comput. Chem. 1999, 20, 786-798
    • (1999) J. Comput. Chem. , vol.20 , pp. 786-798
    • Feenstra, K.1    Hess, B.2    Berendsen, H.J.C.3
  • 28
    • 0037162458 scopus 로고    scopus 로고
    • Ligand-independent growth hormone receptor dimerization occurs in the endoplasmic reticulum and is required for ubiquitin system-dependent endocytosis
    • Gent, J.; van Kerkhof, P.; Roza, M.; Bu, G.; Strous, G. J. Ligand-independent growth hormone receptor dimerization occurs in the endoplasmic reticulum and is required for ubiquitin system-dependent endocytosis Proc. Natl. Acad. Sci. U.S.A. 2002, 99, 9858-9863
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 9858-9863
    • Gent, J.1    Van Kerkhof, P.2    Roza, M.3    Bu, G.4    Strous, G.J.5
  • 29
    • 0026748268 scopus 로고
    • Preparation, purification, and determination of the biological activities of 12 N-terminus-truncated recombinant analogues of bovine placental lactogen
    • Gertler, A.; Hauser, S. D.; Sakal, E.; Vashdi, D.; Staten, N.; Freeman, J. J.; Krivi, G. G. Preparation, purification, and determination of the biological activities of 12 N-terminus-truncated recombinant analogues of bovine placental lactogen J. Biol. Chem. 1992, 267, 12655-12659
    • (1992) J. Biol. Chem. , vol.267 , pp. 12655-12659
    • Gertler, A.1    Hauser, S.D.2    Sakal, E.3    Vashdi, D.4    Staten, N.5    Freeman, J.J.6    Krivi, G.G.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.