메뉴 건너뛰기




Volumn 54, Issue 4, 1998, Pages 616-622

Identification of a key amino acid of the β2-adrenergic receptor for high affinity binding of salmeterol

Author keywords

[No Author keywords available]

Indexed keywords

BETA 2 ADRENERGIC RECEPTOR; BETAXOLOL; OXYGEN; SALMETEROL; SALMETEROL DERIVATIVE; TYROSINE; UNCLASSIFIED DRUG;

EID: 0031752778     PISSN: 0026895X     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (42)

References (25)
  • 2
    • 0023084134 scopus 로고
    • Use of eukaryotic expression technology in the functional analysis of cloned genes
    • Cullen BR (1987) Use of eukaryotic expression technology in the functional analysis of cloned genes. Methods Enzymol 152:684-704.
    • (1987) Methods Enzymol , vol.152 , pp. 684-704
    • Cullen, B.R.1
  • 9
    • 0029002258 scopus 로고
    • Salmeterol
    • Johnson M (1995) Salmeterol. Med Res Rev 15:225-257.
    • (1995) Med Res Rev , vol.15 , pp. 225-257
    • Johnson, M.1
  • 13
    • 0024991898 scopus 로고
    • pEF-BOS, a powerful mammalian expression vector
    • Mizushima S and Nagata S (1990) pEF-BOS, a powerful mammalian expression vector. Nucleic Acids Res 18:5322.
    • (1990) Nucleic Acids Res , vol.18 , pp. 5322
    • Mizushima, S.1    Nagata, S.2
  • 14
    • 0030922145 scopus 로고    scopus 로고
    • Interactions between conserved residues in transmembrane helices 1, 2, and 7 of the thyrotropin-releasing hormone receptor
    • Perlman JH, Colson A-O, Wang W, Bence K, Osman R, and Gershengorn MC (1997) Interactions between conserved residues in transmembrane helices 1, 2, and 7 of the thyrotropin-releasing hormone receptor. J Biol Chem 272:11937-11942.
    • (1997) J Biol Chem , vol.272 , pp. 11937-11942
    • Perlman, J.H.1    Colson, A.-O.2    Wang, W.3    Bence, K.4    Osman, R.5    Gershengorn, M.C.6
  • 15
    • 0028043957 scopus 로고
    • Mutations along transmembrane segment II of the NK-1 receptor affect substance P competition with non-peptide antagonists but not substance P binding
    • Rosenkilde MM, Cahir M, Gether U, Hjorth SA, and Schwartz TW (1994) Mutations along transmembrane segment II of the NK-1 receptor affect substance P competition with non-peptide antagonists but not substance P binding. J Biol Chem 269:28160-28164.
    • (1994) J Biol Chem , vol.269 , pp. 28160-28164
    • Rosenkilde, M.M.1    Cahir, M.2    Gether, U.3    Hjorth, S.A.4    Schwartz, T.W.5
  • 17
    • 0026548156 scopus 로고
    • In vitro mutagenesis and search for structure-function relationships among G protein-coupled receptors
    • Savarese TM and Fraser CM (1992) In vitro mutagenesis and search for structure-function relationships among G protein-coupled receptors. Biochem J 283:1-19.
    • (1992) Biochem J , vol.283 , pp. 1-19
    • Savarese, T.M.1    Fraser, C.M.2
  • 18
    • 0029898348 scopus 로고    scopus 로고
    • Is there a 'lock' for all agonist 'keys' in 7TM receptors?
    • Schwartz TW and Rosenkilde MM (1996) Is there a 'lock' for all agonist 'keys' in 7TM receptors? Trends Pharmacol Sci 17:213-216.
    • (1996) Trends Pharmacol Sci , vol.17 , pp. 213-216
    • Schwartz, T.W.1    Rosenkilde, M.M.2
  • 20
    • 0024344941 scopus 로고
    • Identification of two serine residues involved in agonist activation of the β-adrenergic receptor
    • Strader CD, Candelore MR, Hill WS, Sigal IS, and Dixon RAF (1989) Identification of two serine residues involved in agonist activation of the β-adrenergic receptor. J Biol Chem 264:13572-13578.
    • (1989) J Biol Chem , vol.264 , pp. 13572-13578
    • Strader, C.D.1    Candelore, M.R.2    Hill, W.S.3    Sigal, I.S.4    Dixon, R.A.F.5
  • 23
    • 0023740863 scopus 로고
    • Conserved aspartic acid residues 79 and 113 of the β-adrenergic receptor have different roles in receptor function
    • Strader CD, Sigal IS, Candelore MR, Hill WS, and Dixon RAF (1988) Conserved aspartic acid residues 79 and 113 of the β-adrenergic receptor have different roles in receptor function. J Biol Chem 263:10267-10271.
    • (1988) J Biol Chem , vol.263 , pp. 10267-10271
    • Strader, C.D.1    Sigal, I.S.2    Candelore, M.R.3    Hill, W.S.4    Dixon, R.A.F.5
  • 24
    • 0023941859 scopus 로고
    • The catecholamine binding site of the β-adrenergic receptor is formed by juxtaposed membrane-spanning domains
    • Wong SK-F, Slaughter C, Ruoho AE, and Ross EM (1988) The catecholamine binding site of the β-adrenergic receptor is formed by juxtaposed membrane-spanning domains. J Biol Chem 263:7925-7928.
    • (1988) J Biol Chem , vol.263 , pp. 7925-7928
    • Wong, S.K.-F.1    Slaughter, C.2    Ruoho, A.E.3    Ross, E.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.