PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 30131371-4 2018 We showed that an alanine mutant of the highly conserved residue tyrosine 219 (Y219A) in transmembrane domain five of the beta2-adrenergic receptor (beta2AR) was incapable of beta-arrestin recruitment, receptor internalization, and beta-arrestin-mediated activation of extracellular signal-regulated kinase (ERK), whereas it retained the ability to signal through G protein. Alanine 18-25 adrenoceptor beta 2 Homo sapiens 122-147 32436653-5 2020 METHODS AND RESULTS: Non-conserved amino acids within the beta1 ECII loop (compared with the amino acids constituting the ECII loop of the beta2 -adrenoceptor) were one by one replaced with alanine; potential intra-loop disulfide bridges were probed by cysteine-serine exchanges. Alanine 190-197 adrenoceptor beta 2 Homo sapiens 139-158 29520682-0 2018 Deuteration and selective labeling of alanine methyl groups of beta2-adrenergic receptor expressed in a baculovirus-insect cell expression system. Alanine 38-45 adrenoceptor beta 2 Homo sapiens 63-88 18983266-7 2009 A beta2AR construct with these two residues mutated to alanine, beta2AR RK/AA (R333A/K348A), was generated. Alanine 55-62 adrenoceptor beta 2 Homo sapiens 2-9 18983266-7 2009 A beta2AR construct with these two residues mutated to alanine, beta2AR RK/AA (R333A/K348A), was generated. Alanine 55-62 adrenoceptor beta 2 Homo sapiens 64-71 16920721-4 2006 Here we demonstrated that overexpression of GRK2 mutated at the clathrin-binding motif with alanine (GRK2-5A) results in inhibition of phosphorylation and internalization of the beta2-adrenergic receptor (beta2AR). Alanine 92-99 adrenoceptor beta 2 Homo sapiens 178-203 16920721-4 2006 Here we demonstrated that overexpression of GRK2 mutated at the clathrin-binding motif with alanine (GRK2-5A) results in inhibition of phosphorylation and internalization of the beta2-adrenergic receptor (beta2AR). Alanine 92-99 adrenoceptor beta 2 Homo sapiens 205-212 10510435-5 1999 The EC50 value for cyclic AMP generation in response to (-)-isoprenaline was increased, by about 120 fold, for each alanine-substituted beta2-AR mutant. Alanine 116-123 adrenoceptor beta 2 Homo sapiens 136-144 15492118-7 2005 Biochemical studies confirmed that B2AR/B2AR-ala homomeric complexes form more readily than DOR/B2AR heteromers in expression-matched cell clones and support the hypothesis that B2AR/B2AR-ala complexes are not disrupted by agonist. Alanine 45-48 adrenoceptor beta 2 Homo sapiens 35-39 15492118-7 2005 Biochemical studies confirmed that B2AR/B2AR-ala homomeric complexes form more readily than DOR/B2AR heteromers in expression-matched cell clones and support the hypothesis that B2AR/B2AR-ala complexes are not disrupted by agonist. Alanine 45-48 adrenoceptor beta 2 Homo sapiens 40-44 15492118-7 2005 Biochemical studies confirmed that B2AR/B2AR-ala homomeric complexes form more readily than DOR/B2AR heteromers in expression-matched cell clones and support the hypothesis that B2AR/B2AR-ala complexes are not disrupted by agonist. Alanine 45-48 adrenoceptor beta 2 Homo sapiens 40-44 15492118-7 2005 Biochemical studies confirmed that B2AR/B2AR-ala homomeric complexes form more readily than DOR/B2AR heteromers in expression-matched cell clones and support the hypothesis that B2AR/B2AR-ala complexes are not disrupted by agonist. Alanine 45-48 adrenoceptor beta 2 Homo sapiens 40-44 12460637-4 2002 Homology of the translated protein with the human beta(2)-adrenoceptor was 88% with Ala at position 16 and Glu at position 27. Alanine 84-87 adrenoceptor beta 2 Homo sapiens 50-70 10531390-3 1999 Alanine-substituted mutants of TM7 of the beta(2)AR showed that Tyr(308,) located at the top of TM7, mainly contributed to beta(2) selectivity. Alanine 0-7 adrenoceptor beta 2 Homo sapiens 42-51 15492118-7 2005 Biochemical studies confirmed that B2AR/B2AR-ala homomeric complexes form more readily than DOR/B2AR heteromers in expression-matched cell clones and support the hypothesis that B2AR/B2AR-ala complexes are not disrupted by agonist. Alanine 45-48 adrenoceptor beta 2 Homo sapiens 40-44 15492118-7 2005 Biochemical studies confirmed that B2AR/B2AR-ala homomeric complexes form more readily than DOR/B2AR heteromers in expression-matched cell clones and support the hypothesis that B2AR/B2AR-ala complexes are not disrupted by agonist. Alanine 188-191 adrenoceptor beta 2 Homo sapiens 35-39 15492118-7 2005 Biochemical studies confirmed that B2AR/B2AR-ala homomeric complexes form more readily than DOR/B2AR heteromers in expression-matched cell clones and support the hypothesis that B2AR/B2AR-ala complexes are not disrupted by agonist. Alanine 188-191 adrenoceptor beta 2 Homo sapiens 40-44 15492118-7 2005 Biochemical studies confirmed that B2AR/B2AR-ala homomeric complexes form more readily than DOR/B2AR heteromers in expression-matched cell clones and support the hypothesis that B2AR/B2AR-ala complexes are not disrupted by agonist. Alanine 188-191 adrenoceptor beta 2 Homo sapiens 40-44 15492118-7 2005 Biochemical studies confirmed that B2AR/B2AR-ala homomeric complexes form more readily than DOR/B2AR heteromers in expression-matched cell clones and support the hypothesis that B2AR/B2AR-ala complexes are not disrupted by agonist. Alanine 188-191 adrenoceptor beta 2 Homo sapiens 40-44 15492118-7 2005 Biochemical studies confirmed that B2AR/B2AR-ala homomeric complexes form more readily than DOR/B2AR heteromers in expression-matched cell clones and support the hypothesis that B2AR/B2AR-ala complexes are not disrupted by agonist. Alanine 188-191 adrenoceptor beta 2 Homo sapiens 40-44 11993999-2 2002 Here the equivalent residue, Phe(282), in the beta(2)-AR was evaluated by mutation to glycine, asparagine, alanine, or leucine. Alanine 107-114 adrenoceptor beta 2 Homo sapiens 46-56 11146000-3 2001 Mutation of this site (Ala(345,346)beta(2)AR) significantly reduced the rate and extent of the rapid desensitization promoted by sustained treatment with the agonist isoproterenol. Alanine 23-26 adrenoceptor beta 2 Homo sapiens 35-44 11146000-6 2001 However, despite its phosphorylated state, Ala(261,262)beta ARK(-)beta(2)AR did not undergo rapid desensitization upon agonist treatment, indicating that phosphorylation of Ser(345,346) alone is not sufficient to promote desensitization. Alanine 43-46 adrenoceptor beta 2 Homo sapiens 66-75 9560162-6 1998 Mutation of the final residue of the beta2-adrenergic receptor from leucine to alanine abolishes the receptor"s interaction with NHERF and also markedly alters beta2-adrenergic receptor regulation of NHE3 in cells without altering receptor-mediated activation of adenylyl cyclase. Alanine 79-86 adrenoceptor beta 2 Homo sapiens 37-62 9585128-3 1998 Alanine-substituted beta2AR mutants showed that tyrosine at position 308 in TMD7 played an important role in binding of beta2 selective agonists with high affinity. Alanine 0-7 adrenoceptor beta 2 Homo sapiens 20-27 9443940-12 1998 To determine the specific amino acid which confers this high affinity binding of TA-2005 to the beta 2AR, an alanine-scanning mutagenesis approach was employed. Alanine 109-116 adrenoceptor beta 2 Homo sapiens 96-104 7559596-3 1995 Mutation of tyrosine residue 326 to an alanine resulted in a beta 2AR mutant (beta 2AR-Y326A) that was defective in its ability to sequester and was less well coupled to adenylyl cyclase than the wild-type beta 2AR. Alanine 39-46 adrenoceptor beta 2 Homo sapiens 61-69 7559596-3 1995 Mutation of tyrosine residue 326 to an alanine resulted in a beta 2AR mutant (beta 2AR-Y326A) that was defective in its ability to sequester and was less well coupled to adenylyl cyclase than the wild-type beta 2AR. Alanine 39-46 adrenoceptor beta 2 Homo sapiens 78-86 7559596-3 1995 Mutation of tyrosine residue 326 to an alanine resulted in a beta 2AR mutant (beta 2AR-Y326A) that was defective in its ability to sequester and was less well coupled to adenylyl cyclase than the wild-type beta 2AR. Alanine 39-46 adrenoceptor beta 2 Homo sapiens 78-86 8120019-10 1994 In the beta 2 adrenoceptor, alanine substitution of the i2 residue Phe-139, equivalent to Leu-131 in Hm1, also resulted in impaired coupling to adenylyl cyclase and sequestration, indicating a general role for this conserved i2 loop residue in both processes. Alanine 28-35 adrenoceptor beta 2 Homo sapiens 7-26 7507928-2 1994 The potential role of this conserved aromatic amino acid residue in the cellular processes of sequestration (a rapid internalization of the surface receptor) and down-regulation (a slower loss of total cellular receptors) associated with agonist-mediated desensitization of the beta 2-adrenergic receptor was assessed by replacing tyrosine residue 326 with an alanine residue (beta 2AR-Y326A). Alanine 360-367 adrenoceptor beta 2 Homo sapiens 278-304