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Volumn 79, Issue 11, 2010, Pages 1610-1615

The effect of stereochemistry on the thermodynamic characteristics of the binding of fenoterol stereoisomers to the β2-adrenoceptor

Author keywords

Binding mechanisms; Binding thermodynamics; Chirality; Enantiomers; Enantiospecific binding; Thermodynamic agonist antagonist discrimination

Indexed keywords

BETA 2 ADRENERGIC RECEPTOR; COMPLEMENTARY DNA; FENOTEROL; ISOPRENALINE; PROPRANOLOL;

EID: 77950078520     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcp.2010.01.035     Document Type: Article
Times cited : (26)

References (16)
  • 1
    • 0018607313 scopus 로고
    • Fundamental difference between the molecular interactions of agonists and antagonists with the β-adrenergic receptor
    • Weiland G.A., Minneman K.P., Molinoff P.B. Fundamental difference between the molecular interactions of agonists and antagonists with the β-adrenergic receptor. Nature 1979, 281:114-117.
    • (1979) Nature , vol.281 , pp. 114-117
    • Weiland, G.A.1    Minneman, K.P.2    Molinoff, P.B.3
  • 2
    • 0022621697 scopus 로고
    • Thermodynamic properties of agonist interactions with the beta adrenergic receptor-coupled adenylate cyclase system. I. High-and low-affinity states of agonist binding to membrane-bound beta adrenergic receptors
    • Contreras M.L., Wolfe B.B., Molinoff P.B. Thermodynamic properties of agonist interactions with the beta adrenergic receptor-coupled adenylate cyclase system. I. High-and low-affinity states of agonist binding to membrane-bound beta adrenergic receptors. J Pharm Exp Ther 1986, 237:154-164.
    • (1986) J Pharm Exp Ther , vol.237 , pp. 154-164
    • Contreras, M.L.1    Wolfe, B.B.2    Molinoff, P.B.3
  • 3
    • 0025100420 scopus 로고
    • On the fundamental difference in the thermodynamics of agonist and antagonist interactions with β-adrenergic receptors and the mechanism of entropy-driven binding
    • Miklavc A., Kocjan D., Mavri J., Koller J., Hadzi D. On the fundamental difference in the thermodynamics of agonist and antagonist interactions with β-adrenergic receptors and the mechanism of entropy-driven binding. Biochem Pharm 1990, 40:663-669.
    • (1990) Biochem Pharm , vol.40 , pp. 663-669
    • Miklavc, A.1    Kocjan, D.2    Mavri, J.3    Koller, J.4    Hadzi, D.5
  • 4
    • 0034571319 scopus 로고    scopus 로고
    • Can thermodynamic measurements of receptor binding yield information on drug affinity and efficacy?
    • Borea P.A., Dalpiaz A., Varani K., Gilli P., Gilli G. Can thermodynamic measurements of receptor binding yield information on drug affinity and efficacy?. Biochem Pharm 2000, 60:1549-1556.
    • (2000) Biochem Pharm , vol.60 , pp. 1549-1556
    • Borea, P.A.1    Dalpiaz, A.2    Varani, K.3    Gilli, P.4    Gilli, G.5
  • 12
    • 0034996884 scopus 로고    scopus 로고
    • Functional differences between full and partial agonists: evidence for ligand-specific receptor conformations
    • Seifert R., Wenzel-Seifert K., Gether U., Kobilka B.K. Functional differences between full and partial agonists: evidence for ligand-specific receptor conformations. J Pharmacol Exp Ther 2001, 297:1218-1226.
    • (2001) J Pharmacol Exp Ther , vol.297 , pp. 1218-1226
    • Seifert, R.1    Wenzel-Seifert, K.2    Gether, U.3    Kobilka, B.K.4
  • 14
    • 77951227614 scopus 로고    scopus 로고
    • 2 adrenoceptor model yield theoretical affinity values in function with experimental values for R-ligands, but not for S-antagonists
    • [published online 11 July]
    • 2 adrenoceptor model yield theoretical affinity values in function with experimental values for R-ligands, but not for S-antagonists. J Mol Model 2009, [published online 11 July]. 10.1007/s00894-009-0563-5.
    • (2009) J Mol Model
    • Soriano-Ursúa, M.A.1    Trujillo-Ferrara, J.G.2    Alvarez-Cedillo, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.