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Volumn 45, Issue 51, 2006, Pages 15327-15337

Allosteric and orthosteric binding modes of two nonpeptide human gonadotropin-releasing hormone receptor antagonists

Author keywords

[No Author keywords available]

Indexed keywords

ALLOSTERIC TERNARY COMPLEX MODEL; ORTHOSTERIC BINDING; RADIOLABELED PEPTIDE AGONISTS; THERAPEUTICS;

EID: 33845958682     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0617097     Document Type: Article
Times cited : (10)

References (72)
  • 1
    • 0034490989 scopus 로고    scopus 로고
    • The expression, regulation and signal transduction pathways of the mammalian gonadotropin-releasing hormone receptor
    • Cheng, K. W., and Leung, P. C. (2000) The expression, regulation and signal transduction pathways of the mammalian gonadotropin-releasing hormone receptor, Can. J. Physiol. Pharmacol. 78, 1029-52.
    • (2000) Can. J. Physiol. Pharmacol , vol.78 , pp. 1029-1052
    • Cheng, K.W.1    Leung, P.C.2
  • 2
    • 0004270728 scopus 로고
    • Knobil, E. N, Jr, Ed, pp, Raven Press, New York
    • Fink, G. (1988) in The Physiology of Reproduction (Knobil, E. N., Jr., Ed.) pp 1349-77, Raven Press, New York.
    • (1988) The Physiology of Reproduction , pp. 1349-1377
    • Fink, G.1
  • 4
    • 0025294617 scopus 로고
    • 2+ mobilizing hormones: The case of gonadotropin-releasing hormone
    • 2+ mobilizing hormones: The case of gonadotropin-releasing hormone, Endocr. Rev. 11, 326-53.
    • (1990) Endocr. Rev , vol.11 , pp. 326-353
    • Naor, Z.1
  • 5
    • 0028306250 scopus 로고
    • Gonadotropin-releasing hormone and its analogs
    • Conn, P. M., and Crowley, W. F., Jr. (1994) Gonadotropin-releasing hormone and its analogs, Annu. Rev. Med. 45, 391-405.
    • (1994) Annu. Rev. Med , vol.45 , pp. 391-405
    • Conn, P.M.1    Crowley Jr., W.F.2
  • 8
    • 0026501267 scopus 로고
    • Hormone treatment of endometriosis: The estrogen threshold hypothesis
    • Barbieri, R. L. (1992) Hormone treatment of endometriosis: The estrogen threshold hypothesis, Am. J. Obstet. Gynecol. 166, 740-5.
    • (1992) Am. J. Obstet. Gynecol , vol.166 , pp. 740-745
    • Barbieri, R.L.1
  • 9
    • 0028235123 scopus 로고
    • The use of leutenizing releasing hormone agonists and antagonists in gynaecological cancers
    • Emons, G., and Schally, A. V. (1994) The use of leutenizing releasing hormone agonists and antagonists in gynaecological cancers, Hum. Reprod. 9, 1364-79.
    • (1994) Hum. Reprod , vol.9 , pp. 1364-1379
    • Emons, G.1    Schally, A.V.2
  • 10
    • 0034511980 scopus 로고    scopus 로고
    • Progress towards the development of non-peptide orally-active gonadotropin-releasing hormone (GnRH) antagonists: Therapeutic implications
    • Millar, R. P., Zhu, Y. F., Chen, C., and Struthers, R. S. (2000) Progress towards the development of non-peptide orally-active gonadotropin-releasing hormone (GnRH) antagonists: Therapeutic implications, Br. Med. Bull. 56, 761-72.
    • (2000) Br. Med. Bull , vol.56 , pp. 761-772
    • Millar, R.P.1    Zhu, Y.F.2    Chen, C.3    Struthers, R.S.4
  • 11
    • 4344637399 scopus 로고    scopus 로고
    • Role of gonadotropin-releasing hormone (GnRH) in ovarian cancer
    • Grundker, C., and Emons, G. (2003) Role of gonadotropin-releasing hormone (GnRH) in ovarian cancer, Reprod. Biol. Endocrinol. 1, 65.
    • (2003) Reprod. Biol. Endocrinol , vol.1 , pp. 65
    • Grundker, C.1    Emons, G.2
  • 12
    • 0344444706 scopus 로고    scopus 로고
    • Gonadotropin-releasing hormone antagonists
    • Herbst, K. L. (2003) Gonadotropin-releasing hormone antagonists, Curr. Opin. Pharmacol. 3, 660-6.
    • (2003) Curr. Opin. Pharmacol , vol.3 , pp. 660-666
    • Herbst, K.L.1
  • 13
    • 0035944837 scopus 로고    scopus 로고
    • Gonadotropin-releasing-hormone- receptor antagonists
    • Huirne, J. A., and Lambalk, C. B. (2001) Gonadotropin-releasing-hormone- receptor antagonists, Lancet 358, 1793-803.
    • (2001) Lancet , vol.358 , pp. 1793-1803
    • Huirne, J.A.1    Lambalk, C.B.2
  • 14
    • 77956858305 scopus 로고
    • Gonadotropin releasing hormone antagonists
    • Academic Press Inc, New York
    • Goulet, M. T. (1995) Gonadotropin releasing hormone antagonists, in Annual Reports in Medicinal Chemistry, pp 169-78, Academic Press Inc., New York.
    • (1995) Annual Reports in Medicinal Chemistry , pp. 169-178
    • Goulet, M.T.1
  • 15
    • 0035046991 scopus 로고    scopus 로고
    • The gonadotropin- releasing hormone antagonist abarelix depot versus luteinizing hormone releasing hormone agonists leuprolide or goserelin: Initial results of endocrinological and biochemical efficacies in patients with prostate cancer
    • Tomera, K., Gleason, D., Gittelman, M., Moseley, W., Zinner, N., Murdoch, M., Menon, M., Campion, M., and Garnick, M. B. (2001) The gonadotropin- releasing hormone antagonist abarelix depot versus luteinizing hormone releasing hormone agonists leuprolide or goserelin: Initial results of endocrinological and biochemical efficacies in patients with prostate cancer, J. Urol. 165, 1585-9.
    • (2001) J. Urol , vol.165 , pp. 1585-1589
    • Tomera, K.1    Gleason, D.2    Gittelman, M.3    Moseley, W.4    Zinner, N.5    Murdoch, M.6    Menon, M.7    Campion, M.8    Garnick, M.B.9
  • 16
    • 0033766116 scopus 로고    scopus 로고
    • Abarelix Depot, a GnRH antagonist, v LHRH superagonists in prostate cancer: Differential effects on follicle-stimulating hormone. Abarelix Depot study group
    • Garnick, M. B., and Campion, M. (2000) Abarelix Depot, a GnRH antagonist, v LHRH superagonists in prostate cancer: Differential effects on follicle-stimulating hormone. Abarelix Depot study group, Mol. Urol. 4, 275-7.
    • (2000) Mol. Urol , vol.4 , pp. 275-277
    • Garnick, M.B.1    Campion, M.2
  • 17
    • 0029865119 scopus 로고    scopus 로고
    • Down-regulation of pituitary receptors for luteinizing hormone-releasing hormone (LH-RH) in rats by LH-RH antagonist Cetrorelix
    • Halmos, G., Schally, A. V., Pinski, J., Vadillo-Buenfil, M., and Groot, K. (1996) Down-regulation of pituitary receptors for luteinizing hormone-releasing hormone (LH-RH) in rats by LH-RH antagonist Cetrorelix, Proc. Natl. Acad. Sci. U.S.A. 93, 2398-402.
    • (1996) Proc. Natl. Acad. Sci. U.S.A , vol.93 , pp. 2398-2402
    • Halmos, G.1    Schally, A.V.2    Pinski, J.3    Vadillo-Buenfil, M.4    Groot, K.5
  • 19
    • 5644242134 scopus 로고    scopus 로고
    • Non-Peptidic GnRH Receptor Antagonists
    • Armer, R. E., and Smelt, K. H. (2004) Non-Peptidic GnRH Receptor Antagonists, Curr. Med. Chem. 11, 3017-28.
    • (2004) Curr. Med. Chem , vol.11 , pp. 3017-3028
    • Armer, R.E.1    Smelt, K.H.2
  • 20
    • 33748510561 scopus 로고    scopus 로고
    • Nonpeptide Gonadotropin Releasing Hormone Antagonists
    • Zhu, Y. F., Chen, C., and Struthers, R. S. (2004) Nonpeptide Gonadotropin Releasing Hormone Antagonists, Annu. Rep. Med. Chem. 39, 99-110.
    • (2004) Annu. Rep. Med. Chem , vol.39 , pp. 99-110
    • Zhu, Y.F.1    Chen, C.2    Struthers, R.S.3
  • 21
    • 31544438603 scopus 로고    scopus 로고
    • Overlapping, nonidentical binding sites of different classes of nonpeptide antagonists for the human gonadotropin-releasing hormone receptor
    • Betz, S. F., Reinhart, G. J., Lio, F. M., Chen, C., and Struthers, R. S. (2006) Overlapping, nonidentical binding sites of different classes of nonpeptide antagonists for the human gonadotropin-releasing hormone receptor, J. Med. Chem. 49, 637-47.
    • (2006) J. Med. Chem , vol.49 , pp. 637-647
    • Betz, S.F.1    Reinhart, G.J.2    Lio, F.M.3    Chen, C.4    Struthers, R.S.5
  • 22
    • 33750132372 scopus 로고    scopus 로고
    • Determination of the Binding Mode of Thienopyrimidinedione Antagonists to the Human Gonadotropin Releasing Hormone Receptor Using SAR, Site-Directed Mutagenesis, and Homology Modeling
    • in press
    • Betz, S. F., Lio, F. M., Gao, Y., Reinhart, G. J., Guo, Z., Mesleh, M. F., Zhu, Y. F., and Struthers, R. S. (2006) Determination of the Binding Mode of Thienopyrimidinedione Antagonists to the Human Gonadotropin Releasing Hormone Receptor Using SAR, Site-Directed Mutagenesis, and Homology Modeling, J. Med. Chem. (in press).
    • (2006) J. Med. Chem
    • Betz, S.F.1    Lio, F.M.2    Gao, Y.3    Reinhart, G.J.4    Guo, Z.5    Mesleh, M.F.6    Zhu, Y.F.7    Struthers, R.S.8
  • 23
    • 0036258990 scopus 로고    scopus 로고
    • G protein-coupled receptor allosterism and complexing
    • Christopoulos, A., and Kenakin, T. (2002) G protein-coupled receptor allosterism and complexing, Pharmacol. Rev. 54, 323-74.
    • (2002) Pharmacol. Rev , vol.54 , pp. 323-374
    • Christopoulos, A.1    Kenakin, T.2
  • 25
    • 0029126526 scopus 로고
    • Detection, quantitation, and verification of allosteric interactions of agents with labeled and unlabeled ligands at G protein-coupled receptors: Interactions of strychnine and acetylcholine at muscarinic receptors
    • Lazareno, S., and Birdsall, N. J. (1995) Detection, quantitation, and verification of allosteric interactions of agents with labeled and unlabeled ligands at G protein-coupled receptors: Interactions of strychnine and acetylcholine at muscarinic receptors, Mol. Pharmacol. 48, 362-78.
    • (1995) Mol. Pharmacol , vol.48 , pp. 362-378
    • Lazareno, S.1    Birdsall, N.J.2
  • 26
    • 8744219619 scopus 로고    scopus 로고
    • G protein-coupled receptor allosterism: The promise and the problem(s)
    • Christopoulos, A., May, L. T., Avlani, V. A., and Sexton, P. M. (2004) G protein-coupled receptor allosterism: The promise and the problem(s), Biochem. Soc. Trans. 32, 873-7.
    • (2004) Biochem. Soc. Trans , vol.32 , pp. 873-877
    • Christopoulos, A.1    May, L.T.2    Avlani, V.A.3    Sexton, P.M.4
  • 27
    • 0025603686 scopus 로고
    • Allosteric enhancement of adenosine Al receptor binding and function by 2-amino-3-benzoylthiophenes
    • Bruns, R. F., and Fergus, J. H. (1990) Allosteric enhancement of adenosine Al receptor binding and function by 2-amino-3-benzoylthiophenes, Mol. Pharmacol. 38, 939-49.
    • (1990) Mol. Pharmacol , vol.38 , pp. 939-949
    • Bruns, R.F.1    Fergus, J.H.2
  • 28
    • 0033539111 scopus 로고    scopus 로고
    • 1 receptor. Synthesis and biological evaluation of novel 2-amino-3-benzoylthiophenes as allosteric enhancers of agonist binding
    • 1 receptor. Synthesis and biological evaluation of novel 2-amino-3-benzoylthiophenes as allosteric enhancers of agonist binding, J. Med. Chem. 42, 3629-35.
    • (1999) J. Med. Chem , vol.42 , pp. 3629-3635
    • van der Klein, P.A.1    Kourounakis, A.P.2    IJzerman, A.P.3
  • 30
    • 3142576214 scopus 로고    scopus 로고
    • 2-Amino-3-benzoylthiophene allosteric enhancers of Al adenosine agonist binding: New 3, 4-, and 5-modifications
    • Lutjens, H., Zickgraf, A., Figler, H., Linden, J., Olsson, R. A., and Scammells, P. J. (2003) 2-Amino-3-benzoylthiophene allosteric enhancers of Al adenosine agonist binding: New 3, 4-, and 5-modifications, J. Med. Chem. 46, 1870-7.
    • (2003) J. Med. Chem , vol.46 , pp. 1870-1877
    • Lutjens, H.1    Zickgraf, A.2    Figler, H.3    Linden, J.4    Olsson, R.A.5    Scammells, P.J.6
  • 33
    • 0036232127 scopus 로고    scopus 로고
    • Allosteric modulation of muscarinic receptor signaling: Alcuronium-induced conversion of pilocarpine from an agonist into an antagonist
    • Zahn, K., Eckstein, N., Trankle, C., Sadee, W., and Mohr, K. (2002) Allosteric modulation of muscarinic receptor signaling: Alcuronium-induced conversion of pilocarpine from an agonist into an antagonist, J. Pharmacol. Exp. Ther. 301, 720-8.
    • (2002) J. Pharmacol. Exp. Ther , vol.301 , pp. 720-728
    • Zahn, K.1    Eckstein, N.2    Trankle, C.3    Sadee, W.4    Mohr, K.5
  • 34
    • 1342323325 scopus 로고    scopus 로고
    • Application of a kinetic model to the apparently complex behavior of negative and positive allosteric modulators of muscarinic acetylcholine receptors
    • Avlani, V., May, L. T., Sexton, P. M., and Christopoulos, A. (2004) Application of a kinetic model to the apparently complex behavior of negative and positive allosteric modulators of muscarinic acetylcholine receptors, J. Pharmacol. Exp. Ther. 308, 1062-72.
    • (2004) J. Pharmacol. Exp. Ther , vol.308 , pp. 1062-1072
    • Avlani, V.1    May, L.T.2    Sexton, P.M.3    Christopoulos, A.4
  • 35
    • 11844253226 scopus 로고    scopus 로고
    • Regulation of M2 muscarinic acetylcholine receptor expression and signaling by prolonged exposure to allosteric modulators
    • May, L. T., Lin, Y., Sexton, P. M., and Christopoulos, A. (2005) Regulation of M2 muscarinic acetylcholine receptor expression and signaling by prolonged exposure to allosteric modulators, J. Pharmacol. Exp. Ther. 312, 382-90.
    • (2005) J. Pharmacol. Exp. Ther , vol.312 , pp. 382-390
    • May, L.T.1    Lin, Y.2    Sexton, P.M.3    Christopoulos, A.4
  • 38
    • 0035818605 scopus 로고    scopus 로고
    • Positive allosteric modulators of metabotropic glutamate 1 receptor: Characterization, mechanism of action, and binding site
    • Knoflach, F., Mutel, V., Jolidon, S., Kew, J. N., Malherbe, P., Vieira, E., Wichmann, J., and Kemp, J. A. (2001) Positive allosteric modulators of metabotropic glutamate 1 receptor: Characterization, mechanism of action, and binding site, Proc. Natl. Acad. Sci. U.S.A. 98, 13402-7.
    • (2001) Proc. Natl. Acad. Sci. U.S.A , vol.98 , pp. 13402-13407
    • Knoflach, F.1    Mutel, V.2    Jolidon, S.3    Kew, J.N.4    Malherbe, P.5    Vieira, E.6    Wichmann, J.7    Kemp, J.A.8
  • 39
    • 0142090782 scopus 로고    scopus 로고
    • Maj, M., Bruno, V., Dragic, Z., Yamamoto, R., Battaglia, G., Inderbitzin, W., Stoehr, N., Stein, T., Gasparini, F., Vranesic, I., Kuhn, R., Nicoletti, F., and Flor, P. J. (2003) (-)-PHCCC, a positive allosteric modulator of mGluR4: Characterization, mechanism of action, and neuroprotection, Neuropharmacology 45, 895-906.
    • Maj, M., Bruno, V., Dragic, Z., Yamamoto, R., Battaglia, G., Inderbitzin, W., Stoehr, N., Stein, T., Gasparini, F., Vranesic, I., Kuhn, R., Nicoletti, F., and Flor, P. J. (2003) (-)-PHCCC, a positive allosteric modulator of mGluR4: Characterization, mechanism of action, and neuroprotection, Neuropharmacology 45, 895-906.
  • 41
    • 27844482134 scopus 로고    scopus 로고
    • A close structural analog of 2-methyl-6- (phenylethynyl)-pyridine acts as a neutral allosteric site ligand on metabotropic glutamate receptor subtype 5 and blocks the effects of multiple allosteric modulators
    • Rodriguez, A. L., Nong, Y., Sekaran, N. K., Alagille, D., Tamagnan, G. D., and Conn, P. J. (2005) A close structural analog of 2-methyl-6- (phenylethynyl)-pyridine acts as a neutral allosteric site ligand on metabotropic glutamate receptor subtype 5 and blocks the effects of multiple allosteric modulators, Mol. Pharmacol. 68, 1793-802.
    • (2005) Mol. Pharmacol , vol.68 , pp. 1793-1802
    • Rodriguez, A.L.1    Nong, Y.2    Sekaran, N.K.3    Alagille, D.4    Tamagnan, G.D.5    Conn, P.J.6
  • 43
    • 0037334023 scopus 로고    scopus 로고
    • Mechanism of corticotropin-releasing factor type I receptor regulation by nonpeptide antagonists
    • Hoare, S. R., Sullivan, S. K., Ling, N., Crowe, P. D., and Grigoriadis, D. E. (2003) Mechanism of corticotropin-releasing factor type I receptor regulation by nonpeptide antagonists, Mol. Pharmacol. 63, 151-65.
    • (2003) Mol. Pharmacol , vol.63 , pp. 151-165
    • Hoare, S.R.1    Sullivan, S.K.2    Ling, N.3    Crowe, P.D.4    Grigoriadis, D.E.5
  • 44
    • 15744391870 scopus 로고    scopus 로고
    • The CCR5 receptor-based mechanism of action of 873140, a potent allosteric noncompetitive HIV entry inhibitor
    • Watson, C., Jenkinson, S., Kazmierski, W., and Kenakin, T. (2005) The CCR5 receptor-based mechanism of action of 873140, a potent allosteric noncompetitive HIV entry inhibitor, Mol. Pharmacol. 67, 1268-82.
    • (2005) Mol. Pharmacol , vol.67 , pp. 1268-1282
    • Watson, C.1    Jenkinson, S.2    Kazmierski, W.3    Kenakin, T.4
  • 45
    • 0033028258 scopus 로고    scopus 로고
    • CPCCOEt, a noncompetitive metabotropic glutamate receptor 1 antagonist, inhibits receptor signaling without affecting glutamate binding
    • Litschig, S., Gasparini, F., Rueegg, D., Stoehr, N., Flor, P. J., Vranesic, I., Prezeau, L., Pin, J. P., Thomsen, C. P., and Kuhn, R. (1999) CPCCOEt, a noncompetitive metabotropic glutamate receptor 1 antagonist, inhibits receptor signaling without affecting glutamate binding, Mol. Pharmacol. 55, 453-61.
    • (1999) Mol. Pharmacol , vol.55 , pp. 453-461
    • Litschig, S.1    Gasparini, F.2    Rueegg, D.3    Stoehr, N.4    Flor, P.J.5    Vranesic, I.6    Prezeau, L.7    Pin, J.P.8    Thomsen, C.P.9    Kuhn, R.10
  • 46
    • 0034721795 scopus 로고    scopus 로고
    • The non-competitive antagonists 2-methyl-6-(phenylethynyl)pyridine and 7-hydroxyiminocyclopropan[b] criromen-1a-carboxylic acid ethyl ester interact with overlapping binding pockets in the transmembrane region of group I metabotropic glutamate receptors
    • Pagano, A., Ruegg, D., Litschig, S., Stoehr, N., Stierlin, C., Heinrich, M., Floersheim, P., Prezeau, L., Carroll, F., Pin, J. P., Cambria, A., Vranesic, I., Flor, P. J., Gasparini, F., and Kuhn, R. (2000) The non-competitive antagonists 2-methyl-6-(phenylethynyl)pyridine and 7-hydroxyiminocyclopropan[b] criromen-1a-carboxylic acid ethyl ester interact with overlapping binding pockets in the transmembrane region of group I metabotropic glutamate receptors, J. Biol. Chem. 275, 33750-8.
    • (2000) J. Biol. Chem , vol.275 , pp. 33750-33758
    • Pagano, A.1    Ruegg, D.2    Litschig, S.3    Stoehr, N.4    Stierlin, C.5    Heinrich, M.6    Floersheim, P.7    Prezeau, L.8    Carroll, F.9    Pin, J.P.10    Cambria, A.11    Vranesic, I.12    Flor, P.J.13    Gasparini, F.14    Kuhn, R.15
  • 47
    • 0036232127 scopus 로고    scopus 로고
    • Allosteric modulation of muscarinic receptor signaling: Alcuronium-induced conversion of pilocarpine from an agonist into an antagonist
    • Zahn, K., Eckstein, N., Trankle, C., Sadee, W., and Mohr, K. (2005) Allosteric modulation of muscarinic receptor signaling: Alcuronium-induced conversion of pilocarpine from an agonist into an antagonist, J. Pharmacol. Exp. Ther. 301, 720-8.
    • (2005) J. Pharmacol. Exp. Ther , vol.301 , pp. 720-728
    • Zahn, K.1    Eckstein, N.2    Trankle, C.3    Sadee, W.4    Mohr, K.5
  • 52
    • 10444219551 scopus 로고    scopus 로고
    • Tucci, F. C., Zhu, Y. F., Struthers, R. S., Guo, Z., Gross, T. D., Rowbottom, M. W., Acevedo, O., Gao, Y., Saunders, J., Xie, Q., Reinhart, G. J., Liu, X. J., Ling, N., Bonneville, A. K., Chen, T., Bozigian, H., and Chen, C. (2005) 3-[(2R)-Amino-2-phenylethyl]-1-(2,6-difluorobenzyl)-5-(2-fluoro-3- methoxyphenyl)-6-methylpyrimidin-2,4-dione (NBI 42902) as a potent and orally active antagonist of the human gonadotropin-releasing hormone receptor. Design, synthesis, and in vitro and in vivo characterization, J. Med. Chem. 48, 1169-78.
    • Tucci, F. C., Zhu, Y. F., Struthers, R. S., Guo, Z., Gross, T. D., Rowbottom, M. W., Acevedo, O., Gao, Y., Saunders, J., Xie, Q., Reinhart, G. J., Liu, X. J., Ling, N., Bonneville, A. K., Chen, T., Bozigian, H., and Chen, C. (2005) 3-[(2R)-Amino-2-phenylethyl]-1-(2,6-difluorobenzyl)-5-(2-fluoro-3- methoxyphenyl)-6-methylpyrimidin-2,4-dione (NBI 42902) as a potent and orally active antagonist of the human gonadotropin-releasing hormone receptor. Design, synthesis, and in vitro and in vivo characterization, J. Med. Chem. 48, 1169-78.
  • 54
    • 33748074796 scopus 로고    scopus 로고
    • Kinetics of Nonpeptide Antagonist Binding to the Human Gonadotropin Releasing Hormone Receptor: Implications for Structure-Activity Relationships and Insurmountable Antagonism
    • in press
    • Sullivan, S. K., Hoare, S. R. J., Fleck, B. F., Zhu, Y. F., Heise, C. E., Struthers, R. S., and Crowe, P. D. (2006) Kinetics of Nonpeptide Antagonist Binding to the Human Gonadotropin Releasing Hormone Receptor: Implications for Structure-Activity Relationships and Insurmountable Antagonism, Biochem. Pharmacol. (in press).
    • (2006) Biochem. Pharmacol
    • Sullivan, S.K.1    Hoare, S.R.J.2    Fleck, B.F.3    Zhu, Y.F.4    Heise, C.E.5    Struthers, R.S.6    Crowe, P.D.7
  • 55
    • 33749547640 scopus 로고    scopus 로고
    • Suppression of Serum Luteinizing Hormone in Postmenopausal Women by an Orally Administered Nonpeptide Antagonist of the Gonadotropin-Releasing Hormone Receptor (NBI-42902)
    • in press
    • Struthers, R. S., Chen, T., Campbell, B., Jimenez, R., Pan, H., Yen, S. C., and Bozigian, H. (2006) Suppression of Serum Luteinizing Hormone in Postmenopausal Women by an Orally Administered Nonpeptide Antagonist of the Gonadotropin-Releasing Hormone Receptor (NBI-42902), J. Clin. Endocrinol. Metab. (in press).
    • (2006) J. Clin. Endocrinol. Metab
    • Struthers, R.S.1    Chen, T.2    Campbell, B.3    Jimenez, R.4    Pan, H.5    Yen, S.C.6    Bozigian, H.7
  • 56
    • 77957055780 scopus 로고
    • Integrated methods for the construction of three dimensional models and computational probing of structure-function relations in G-protein coupled receptors
    • Ballasteros, J., and Weinstein, H. (1995) Integrated methods for the construction of three dimensional models and computational probing of structure-function relations in G-protein coupled receptors, Methods Neurosci. 25, 366-428.
    • (1995) Methods Neurosci , vol.25 , pp. 366-428
    • Ballasteros, J.1    Weinstein, H.2
  • 58
    • 0031764251 scopus 로고    scopus 로고
    • A high affinity gonadotropin-releasing hormone (GnRH) tracer, radioiodinated at position 6, facilitates analysis of mutant GnRH receptors
    • Flanagan, C. A., Fromme, B. J., Davidson, J. S., and Millar, R. P. (1998) A high affinity gonadotropin-releasing hormone (GnRH) tracer, radioiodinated at position 6, facilitates analysis of mutant GnRH receptors, Endocrinology 139, 4115-9.
    • (1998) Endocrinology , vol.139 , pp. 4115-4119
    • Flanagan, C.A.1    Fromme, B.J.2    Davidson, J.S.3    Millar, R.P.4
  • 59
    • 4544377876 scopus 로고    scopus 로고
    • Species selectivity of nonpeptide antagonists of the gonadotropin-releasing hormone receptor is determined by residues in extracellular loops II and III and the amino terminus
    • Reinhart, G. J., Xie, Q., Liu, X. J., Zhu, Y. F., Fan, J., Chen, C., and Struthers, R. S. (2004) Species selectivity of nonpeptide antagonists of the gonadotropin-releasing hormone receptor is determined by residues in extracellular loops II and III and the amino terminus, J. Biol. Chem. 279, 34115-22.
    • (2004) J. Biol. Chem , vol.279 , pp. 34115-34122
    • Reinhart, G.J.1    Xie, Q.2    Liu, X.J.3    Zhu, Y.F.4    Fan, J.5    Chen, C.6    Struthers, R.S.7
  • 60
    • 0031785874 scopus 로고    scopus 로고
    • A single amino acid substitution in transmembrane helix VI results in overexpression of the human GnRH receptor
    • Myburgh, D. B., Pawson, A. J., Davidson, J. S., Flanagan, C. A., Millar, R. P., and Hapgood, J. P. (1998) A single amino acid substitution in transmembrane helix VI results in overexpression of the human GnRH receptor, Eur. J. Endocrinol. 139, 438-47.
    • (1998) Eur. J. Endocrinol , vol.139 , pp. 438-447
    • Myburgh, D.B.1    Pawson, A.J.2    Davidson, J.S.3    Flanagan, C.A.4    Millar, R.P.5    Hapgood, J.P.6
  • 61
    • 16544378561 scopus 로고    scopus 로고
    • A miniaturized column chromatography method for measuring receptor-mediated inositol phosphate accumulation
    • Benjamin, E. R., Haftl, S. L., Xanthos, D. N., Crumley, G., Hachicha, M., and Valenzano, K. J. (2004) A miniaturized column chromatography method for measuring receptor-mediated inositol phosphate accumulation, J. Biomol. Screening 9, 343-53.
    • (2004) J. Biomol. Screening , vol.9 , pp. 343-353
    • Benjamin, E.R.1    Haftl, S.L.2    Xanthos, D.N.3    Crumley, G.4    Hachicha, M.5    Valenzano, K.J.6
  • 62
    • 5544242529 scopus 로고    scopus 로고
    • MMFF VI. MMFF94s Option for Energy Minimization Studies
    • Halgren, T. A. (1999) MMFF VI. MMFF94s Option for Energy Minimization Studies, J. Comput. Chem. 20, 720-9.
    • (1999) J. Comput. Chem , vol.20 , pp. 720-729
    • Halgren, T.A.1
  • 63
    • 0001242234 scopus 로고    scopus 로고
    • MMFF VII. Characterization of MMFF94, MMFF94s, and Other Widely Available Force Fields for Conformational Energies and for Intermolecular-Interaction Energies and Geometries
    • Halgren, T. A. (1999) MMFF VII. Characterization of MMFF94, MMFF94s, and Other Widely Available Force Fields for Conformational Energies and for Intermolecular-Interaction Energies and Geometries, J. Comput. Chem. 20, 730-48.
    • (1999) J. Comput. Chem , vol.20 , pp. 730-748
    • Halgren, T.A.1
  • 64
    • 23844481788 scopus 로고    scopus 로고
    • Mutations remote from the human gonadotropin-releasing hormone (GnRH) receptor binding sites specifically increase binding affinity for GnRH II, but not GnRH I: Evidence for ligand-selective receptor active conformations
    • Lu, Z. L., Gallagher, R., Sellar, R., Coetsee, M., and Millar, R. R. (2005) Mutations remote from the human gonadotropin-releasing hormone (GnRH) receptor binding sites specifically increase binding affinity for GnRH II, but not GnRH I: Evidence for ligand-selective receptor active conformations, J. Biol. Chem. 280, 29796-803.
    • (2005) J. Biol. Chem , vol.280 , pp. 29796-29803
    • Lu, Z.L.1    Gallagher, R.2    Sellar, R.3    Coetsee, M.4    Millar, R.R.5
  • 66
    • 0028100755 scopus 로고
    • Glutamate 301 of the mouse gonadotropin-releasing hormone receptor confers specificity for arginine 8 of mammalian gonadotropin-releasing hormone
    • Flanagan, C. A., Becker, I. I., Davidson, J. S., Wakefield, I. K., Zhou, W., Sealfon, S. C., and Millar, R. P. (1994) Glutamate 301 of the mouse gonadotropin-releasing hormone receptor confers specificity for arginine 8 of mammalian gonadotropin-releasing hormone, J. Biol. Chem. 269, 22636-41.
    • (1994) J. Biol. Chem , vol.269 , pp. 22636-22641
    • Flanagan, C.A.1    Becker, I.I.2    Davidson, J.S.3    Wakefield, I.K.4    Zhou, W.5    Sealfon, S.C.6    Millar, R.P.7
  • 67
    • 0034747357 scopus 로고    scopus 로고
    • Role of aspartate 7.32 (302) of the human gonadotropin-releasing hormone receptor in stabilizing a high affinity ligand conformation
    • Fromme, B. J., Katz, A. A., Roeske, R. W., Millar, R. P., and Flanagan, C. A. (2001) Role of aspartate 7.32 (302) of the human gonadotropin-releasing hormone receptor in stabilizing a high affinity ligand conformation, Mol. Pharmacol. 60, 1280-7.
    • (2001) Mol. Pharmacol , vol.60 , pp. 1280-1287
    • Fromme, B.J.1    Katz, A.A.2    Roeske, R.W.3    Millar, R.P.4    Flanagan, C.A.5
  • 69
    • 0033669603 scopus 로고    scopus 로고
    • Modeling the functional effects of allosteric modulators at pharmacological receptors: An extension of the two-state model of receptor activation
    • Hall, D. A. (2000) Modeling the functional effects of allosteric modulators at pharmacological receptors: An extension of the two-state model of receptor activation, Mol. Pharmacol. 58, 1412-23.
    • (2000) Mol. Pharmacol , vol.58 , pp. 1412-1423
    • Hall, D.A.1
  • 70
    • 9944263528 scopus 로고    scopus 로고
    • Searching for new allosteric sites in enzymes
    • Hardy, J. A., and Wells, J. A. (2004) Searching for new allosteric sites in enzymes, Curr. Opin. Struct. Biol. 14, 706-15.
    • (2004) Curr. Opin. Struct. Biol , vol.14 , pp. 706-715
    • Hardy, J.A.1    Wells, J.A.2
  • 71
    • 0031866950 scopus 로고    scopus 로고
    • On the unique binding and activating properties of xanomeline at the M1 muscarinic acetylcholine receptor
    • Christopoulos, A., Pierce, T. L., Sorman, J. L., and El-Fakahany, E. E. (1998) On the unique binding and activating properties of xanomeline at the M1 muscarinic acetylcholine receptor, Mol. Pharmacol. 53, 1120-30.
    • (1998) Mol. Pharmacol , vol.53 , pp. 1120-1130
    • Christopoulos, A.1    Pierce, T.L.2    Sorman, J.L.3    El-Fakahany, E.E.4


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