PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 16432212-2 2006 We report that dynamin, which interacts with NO synthase, is S-nitrosylated at a single cysteine residue (C607) after stimulation of the beta(2) adrenergic receptor. Cysteine 88-96 adrenoceptor beta 2 Homo sapiens 137-164 17451656-5 2007 Based on these results, we propose that agonist-dependent ROS formation is needed for beta2AR signal transduction, perhaps through stabilization of active receptor conformers by redox-mediated modification of receptor and/or Galpha proteins cysteine residues. Cysteine 241-249 adrenoceptor beta 2 Homo sapiens 86-93 12167654-4 2002 In the beta(2) adrenergic receptor, mutation of Cys(6.47) to Thr, which in an alpha-helix has a different rotamer distribution from Cys and Ser, produced a constitutively active receptor, whereas the Ser mutant was similar to wild-type receptor. Cysteine 48-51 adrenoceptor beta 2 Homo sapiens 7-34 12519093-4 2003 The Cys/Cys (CC) genotype of the alpha(1A)-AR R492C polymorphism was associated with a longer ECG PR interval before and during the adrenaline infusions. Cysteine 4-7 adrenoceptor beta 2 Homo sapiens 43-45 12519093-4 2003 The Cys/Cys (CC) genotype of the alpha(1A)-AR R492C polymorphism was associated with a longer ECG PR interval before and during the adrenaline infusions. Cysteine 8-11 adrenoceptor beta 2 Homo sapiens 43-45 12167654-4 2002 In the beta(2) adrenergic receptor, mutation of Cys(6.47) to Thr, which in an alpha-helix has a different rotamer distribution from Cys and Ser, produced a constitutively active receptor, whereas the Ser mutant was similar to wild-type receptor. Cysteine 132-135 adrenoceptor beta 2 Homo sapiens 7-34 11395517-5 2001 The beta(2)-AR contains a valine in this position (V(3.36); position number 117) and a cysteine in the preceding position (Cys(116)) and was not inactivated by PB (10 microm, 30 min) (inactivation 26%). Cysteine 87-95 adrenoceptor beta 2 Homo sapiens 4-14 11395517-5 2001 The beta(2)-AR contains a valine in this position (V(3.36); position number 117) and a cysteine in the preceding position (Cys(116)) and was not inactivated by PB (10 microm, 30 min) (inactivation 26%). Cysteine 123-126 adrenoceptor beta 2 Homo sapiens 4-14 10323412-10 1999 The exchange at -47 may alter the expression level of the beta2-adrenergic receptor gene, because the nucleotide substitution at -47 results in a Cys-->Arg exchange at the C terminal of the leader peptide. Cysteine 146-149 adrenoceptor beta 2 Homo sapiens 58-83 10908293-2 2000 In the beta(2)-adrenergic receptor the agonist binding site has previously been structurally and functionally exchanged with an activating metal-ion site located between AspIII:08-or a His residue introduced at this position in transmembrane domain (TM)-III-and a Cys residue substituted for AsnVII:06 in TM-VII. Cysteine 264-267 adrenoceptor beta 2 Homo sapiens 7-34 11353823-2 2001 To monitor directly the formation of the active state of a prototypical GPCR, we devised a method to site specifically attach fluorescein to an endogenous cysteine (Cys-265) at the cytoplasmic end of transmembrane 6 (TM6) of the beta(2) adrenergic receptor (beta(2)AR), adjacent to the G-protein-coupling domain. Cysteine 155-163 adrenoceptor beta 2 Homo sapiens 229-256 11353823-2 2001 To monitor directly the formation of the active state of a prototypical GPCR, we devised a method to site specifically attach fluorescein to an endogenous cysteine (Cys-265) at the cytoplasmic end of transmembrane 6 (TM6) of the beta(2) adrenergic receptor (beta(2)AR), adjacent to the G-protein-coupling domain. Cysteine 155-163 adrenoceptor beta 2 Homo sapiens 258-267 11353823-2 2001 To monitor directly the formation of the active state of a prototypical GPCR, we devised a method to site specifically attach fluorescein to an endogenous cysteine (Cys-265) at the cytoplasmic end of transmembrane 6 (TM6) of the beta(2) adrenergic receptor (beta(2)AR), adjacent to the G-protein-coupling domain. Cysteine 165-168 adrenoceptor beta 2 Homo sapiens 229-256 11353823-2 2001 To monitor directly the formation of the active state of a prototypical GPCR, we devised a method to site specifically attach fluorescein to an endogenous cysteine (Cys-265) at the cytoplasmic end of transmembrane 6 (TM6) of the beta(2) adrenergic receptor (beta(2)AR), adjacent to the G-protein-coupling domain. Cysteine 165-168 adrenoceptor beta 2 Homo sapiens 258-267 11118431-2 2001 In the background of a mutant beta(2) adrenergic receptor, with a minimal number of endogenous cysteine residues, new cysteines were introduced in positions 269(6.31), 270(6.32), 271(6.33), and 272(6.34) at the cytoplasmic side of transmembrane segment (TM) 6. Cysteine 95-103 adrenoceptor beta 2 Homo sapiens 30-57 11118431-2 2001 In the background of a mutant beta(2) adrenergic receptor, with a minimal number of endogenous cysteine residues, new cysteines were introduced in positions 269(6.31), 270(6.32), 271(6.33), and 272(6.34) at the cytoplasmic side of transmembrane segment (TM) 6. Cysteine 118-127 adrenoceptor beta 2 Homo sapiens 30-57 9835617-8 1998 In human airway smooth muscle cells that natively express beta2AR, receptor expression was approximately twofold higher in those bearing the Cys versus the Arg polymorphism, confirming the phenotype in a relevant cell type. Cysteine 141-144 adrenoceptor beta 2 Homo sapiens 58-65 8702933-0 1996 Palmitoylated cysteine 341 modulates phosphorylation of the beta2-adrenergic receptor by the cAMP-dependent protein kinase. Cysteine 14-22 adrenoceptor beta 2 Homo sapiens 60-85 9585127-1 1998 The environmentally sensitive and cysteine reactive fluorescent probe, IANBD, was used to monitor ligand-induced structural changes in the beta2 adrenergic receptor (beta2AR) by fluorescent spectroscopy. Cysteine 34-42 adrenoceptor beta 2 Homo sapiens 139-164 9585127-1 1998 The environmentally sensitive and cysteine reactive fluorescent probe, IANBD, was used to monitor ligand-induced structural changes in the beta2 adrenergic receptor (beta2AR) by fluorescent spectroscopy. Cysteine 34-42 adrenoceptor beta 2 Homo sapiens 166-173 8702933-1 1996 We previously showed that substitution of a glycine residue for the palmitoylated cysteine 341 of the human beta2-adrenergic receptor (Gly341beta2AR), increases the basal level of the receptor phosphorylation and reduces its ability to functionally interact with Gs. Cysteine 82-90 adrenoceptor beta 2 Homo sapiens 108-133 8702933-7 1996 Taken together, the data demonstrate that palmitoylation of cysteine 341 controls the phosphorylation state of the PKA site located in the carboxyl tail of the beta2AR and by doing so modulates the responsiveness of the receptor. Cysteine 60-68 adrenoceptor beta 2 Homo sapiens 160-167 7776964-3 1995 In the case of the beta 2-adrenergic receptor, it was also reported that mutation of the palmitoylated cysteine to glycine greatly diminished the ability of this receptor to interact with and activate Gs. Cysteine 103-111 adrenoceptor beta 2 Homo sapiens 19-45 7499324-3 1995 Purified human beta 2 adrenergic receptor was covalently labeled with the cysteine-reactive, fluorescent probe N,N"-dimethyl-N-(iodoacetyl)-N"-(7-nitrobenz-2-oxa-1,3-diazol-4- yl)ethylenediamine (IANBD). Cysteine 74-82 adrenoceptor beta 2 Homo sapiens 15-41 7972030-2 1994 This cysteine is known to be palmitoylated in rhodopsin, the beta 2-adrenergic receptor (beta 2AR) and the alpha 2A-adrenergic receptor (alpha 2AAR). Cysteine 5-13 adrenoceptor beta 2 Homo sapiens 61-87 7972030-2 1994 This cysteine is known to be palmitoylated in rhodopsin, the beta 2-adrenergic receptor (beta 2AR) and the alpha 2A-adrenergic receptor (alpha 2AAR). Cysteine 5-13 adrenoceptor beta 2 Homo sapiens 89-97 7972030-3 1994 For the beta 2AR, this cysteine has been shown to be important for stimulatory G protein (Gs) coupling and agonist-promoted desensitization. Cysteine 23-31 adrenoceptor beta 2 Homo sapiens 8-16 2159799-4 1990 Through site-directed mutagenesis, we indeed were able to identify four cysteines which are critical for normal ligand binding affinities and for the proper expression of functional beta AR at the cell surface. Cysteine 72-81 adrenoceptor beta 2 Homo sapiens 182-189 8381352-4 1993 Here we report that substitution of the palmitoylated cysteine by a glycine (Gly341 beta 2 AR) using site directed mutagenesis leads to a receptor being highly phosphorylated and largely uncoupled from Gs. Cysteine 54-62 adrenoceptor beta 2 Homo sapiens 84-93 2556136-0 1989 Substitution of an extracellular cysteine in the beta 2-adrenergic receptor enhances agonist-promoted phosphorylation and receptor desensitization. Cysteine 33-41 adrenoceptor beta 2 Homo sapiens 49-75 2159799-0 1990 Role of extracellular disulfide-bonded cysteines in the ligand binding function of the beta 2-adrenergic receptor. Cysteine 39-48 adrenoceptor beta 2 Homo sapiens 87-113 2542304-10 1989 These data implicate one of the conserved transmembrane cysteine residues in the human beta 2-adrenergic receptor in receptor activation by agonists and also suggest that conserved cysteine residues in an extracellular domain of the receptor may be involved in ligand binding. Cysteine 56-64 adrenoceptor beta 2 Homo sapiens 87-113 2542304-10 1989 These data implicate one of the conserved transmembrane cysteine residues in the human beta 2-adrenergic receptor in receptor activation by agonists and also suggest that conserved cysteine residues in an extracellular domain of the receptor may be involved in ligand binding. Cysteine 181-189 adrenoceptor beta 2 Homo sapiens 87-113 30953343-3 2019 The beta2 -adrenergic receptor was labeled with TMS groups at two cysteines located at the cytoplasmic ends of helices VI and VII. Cysteine 66-75 adrenoceptor beta 2 Homo sapiens 4-30 2540197-2 1989 We report that a cysteine residue in the human beta 2-adrenergic receptor (beta 2AR) is covalently modified by thioesterification with palmitic acid. Cysteine 17-25 adrenoceptor beta 2 Homo sapiens 47-73 2540197-2 1989 We report that a cysteine residue in the human beta 2-adrenergic receptor (beta 2AR) is covalently modified by thioesterification with palmitic acid. Cysteine 17-25 adrenoceptor beta 2 Homo sapiens 75-83 32076070-0 2020 Cysteine redox state regulates human beta2-adrenergic receptor binding and function. Cysteine 0-8 adrenoceptor beta 2 Homo sapiens 37-62 23721409-2 2013 When a small label was incorporated on the cytosolic interface of transmembrane helix 6 (Cys-265), (19)F NMR spectra of the beta2 adrenergic receptor (beta2AR) reconstituted in maltose/neopentyl glycol detergent micelles revealed two distinct inactive states, an activation intermediate state en route to activation, and, in the presence of a G protein mimic, a predominant active state. Cysteine 89-92 adrenoceptor beta 2 Homo sapiens 124-149 27481942-1 2016 We report here that a population of human beta2-adrenergic receptors (beta2AR), a canonical G protein-coupled receptor, traffics along a previously undescribed intracellular itinerary via the Golgi complex that is associated with the sequential S-palmitoylation and depalmitoylation of a previously undescribed site of modification, Cys-265 within the third intracellular loop. Cysteine 333-336 adrenoceptor beta 2 Homo sapiens 42-68 27481942-1 2016 We report here that a population of human beta2-adrenergic receptors (beta2AR), a canonical G protein-coupled receptor, traffics along a previously undescribed intracellular itinerary via the Golgi complex that is associated with the sequential S-palmitoylation and depalmitoylation of a previously undescribed site of modification, Cys-265 within the third intracellular loop. Cysteine 333-336 adrenoceptor beta 2 Homo sapiens 70-77 27481942-6 2016 In addition, beta2AR S-palmitoylated at Cys-265 are selectively preserved under a sustained adrenergic stimulation, which results in the down-regulation and degradation of betaAR. Cysteine 40-43 adrenoceptor beta 2 Homo sapiens 13-20 27481942-7 2016 Cys-265 is not conserved in beta1AR, and S-palmitoylation of Cys-265 may thus be associated with functional differences between beta2AR and beta1AR, including relative resistance of beta2AR to down-regulation in multiple pathophysiologies. Cysteine 61-64 adrenoceptor beta 2 Homo sapiens 128-135 27481942-7 2016 Cys-265 is not conserved in beta1AR, and S-palmitoylation of Cys-265 may thus be associated with functional differences between beta2AR and beta1AR, including relative resistance of beta2AR to down-regulation in multiple pathophysiologies. Cysteine 61-64 adrenoceptor beta 2 Homo sapiens 182-189 23721409-2 2013 When a small label was incorporated on the cytosolic interface of transmembrane helix 6 (Cys-265), (19)F NMR spectra of the beta2 adrenergic receptor (beta2AR) reconstituted in maltose/neopentyl glycol detergent micelles revealed two distinct inactive states, an activation intermediate state en route to activation, and, in the presence of a G protein mimic, a predominant active state. Cysteine 89-92 adrenoceptor beta 2 Homo sapiens 151-158 22526864-1 2012 PURPOSE: Tauhat beta2-adrenergic receptor (beta2AR) haplotypes may play a key role in clinical response to beta2-agonists and haplotype Cys-19Gly16Gln27 (CysGlyGln) is reported to be associated with desensitization of beta2AR to beta-agonists in lymphocytes isolated from patients with asthma and septic shock. Cysteine 136-139 adrenoceptor beta 2 Homo sapiens 43-50 22893704-3 2012 Upon tagging Cys-265 of beta(2)AR with a trifluoromethyl probe, (19)F NMR was used to assess conformations and possible equilibria between states. Cysteine 13-16 adrenoceptor beta 2 Homo sapiens 24-33 22526864-1 2012 PURPOSE: Tauhat beta2-adrenergic receptor (beta2AR) haplotypes may play a key role in clinical response to beta2-agonists and haplotype Cys-19Gly16Gln27 (CysGlyGln) is reported to be associated with desensitization of beta2AR to beta-agonists in lymphocytes isolated from patients with asthma and septic shock. Cysteine 136-139 adrenoceptor beta 2 Homo sapiens 218-225 19422376-4 2009 With respect to beta(2)-AR, the Cys-19 variant is associated with greater beta(2)-AR expression than the Arg-19 variant; Gly16-beta(2)-AR are more susceptible, whereas Glu27-beta(2)-AR are almost resistant to agonist-promoted down-regulation; Thr164-beta(2)-AR are three to four times more responsive to agonist-evoked stimulation than Ile164-beta(2)-AR. Cysteine 32-35 adrenoceptor beta 2 Homo sapiens 74-84 22912718-3 2012 Here, we demonstrate that in cardiomyocytes, palmitoylation of beta(2)AR, the covalent acylation of cysteine residue 341, plays a critical role in shaping subcellular cAMP-PKA activities in cardiomyocytes via regulating beta(2)AR association with arrestin/PDE4D. Cysteine 100-108 adrenoceptor beta 2 Homo sapiens 63-72 22912718-3 2012 Here, we demonstrate that in cardiomyocytes, palmitoylation of beta(2)AR, the covalent acylation of cysteine residue 341, plays a critical role in shaping subcellular cAMP-PKA activities in cardiomyocytes via regulating beta(2)AR association with arrestin/PDE4D. Cysteine 100-108 adrenoceptor beta 2 Homo sapiens 220-229 22912718-4 2012 Replacing cysteine 341 on beta(2)AR with alanine (C341A) leads to an impaired binding to beta arrestin 2. Cysteine 10-18 adrenoceptor beta 2 Homo sapiens 26-35 19422376-4 2009 With respect to beta(2)-AR, the Cys-19 variant is associated with greater beta(2)-AR expression than the Arg-19 variant; Gly16-beta(2)-AR are more susceptible, whereas Glu27-beta(2)-AR are almost resistant to agonist-promoted down-regulation; Thr164-beta(2)-AR are three to four times more responsive to agonist-evoked stimulation than Ile164-beta(2)-AR. Cysteine 32-35 adrenoceptor beta 2 Homo sapiens 74-84 19422376-4 2009 With respect to beta(2)-AR, the Cys-19 variant is associated with greater beta(2)-AR expression than the Arg-19 variant; Gly16-beta(2)-AR are more susceptible, whereas Glu27-beta(2)-AR are almost resistant to agonist-promoted down-regulation; Thr164-beta(2)-AR are three to four times more responsive to agonist-evoked stimulation than Ile164-beta(2)-AR. Cysteine 32-35 adrenoceptor beta 2 Homo sapiens 74-84 19422376-4 2009 With respect to beta(2)-AR, the Cys-19 variant is associated with greater beta(2)-AR expression than the Arg-19 variant; Gly16-beta(2)-AR are more susceptible, whereas Glu27-beta(2)-AR are almost resistant to agonist-promoted down-regulation; Thr164-beta(2)-AR are three to four times more responsive to agonist-evoked stimulation than Ile164-beta(2)-AR. Cysteine 32-35 adrenoceptor beta 2 Homo sapiens 74-84 19422376-4 2009 With respect to beta(2)-AR, the Cys-19 variant is associated with greater beta(2)-AR expression than the Arg-19 variant; Gly16-beta(2)-AR are more susceptible, whereas Glu27-beta(2)-AR are almost resistant to agonist-promoted down-regulation; Thr164-beta(2)-AR are three to four times more responsive to agonist-evoked stimulation than Ile164-beta(2)-AR. Cysteine 32-35 adrenoceptor beta 2 Homo sapiens 74-84