| + |
EGLN3 | up-regulates quantity by stabilization 
hydroxylation
|
ADRB2 |
0.323 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262006 |
Pro382 |
KLLCEDLpGTEDFVG |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 19584355 |
We further show that the interaction of pVHL with beta(2)AR is dependent on proline hydroxylation (proline-382 and -395) and that the dioxygenase EGLN3 interacts directly with the beta(2)AR to serve as an endogenous beta(2)AR prolyl hydroxylase. Under hypoxic conditions, receptor hydroxylation and subsequent ubiquitylation decrease dramatically, thus attenuating receptor degradation and down-regulation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262007 |
Pro395 |
VGHQGTVpSDNIDSQ |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 19584355 |
We further show that the interaction of pVHL with beta(2)AR is dependent on proline hydroxylation (proline-382 and -395) and that the dioxygenase EGLN3 interacts directly with the beta(2)AR to serve as an endogenous beta(2)AR prolyl hydroxylase. Under hypoxic conditions, receptor hydroxylation and subsequent ubiquitylation decrease dramatically, thus attenuating receptor degradation and down-regulation. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKCD | down-regulates activity 
phosphorylation
|
ADRB2 |
0.358 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248854 |
Ser261 |
TGHGLRRsSKFCLKE |
in vitro |
|
| pmid |
sentence |
| 1848190 |
We investigate the role of the beta 2-adrenergic receptor phosphorylation by protein kinase C in this regulatory process. Mutation of the serine-261, -262, -344 and -345 of the beta 2-adrenergic receptor prevented the phorbol-ester-induced phosphorylation of the receptor. This mutation also abolished the phorbol-ester-induced decrease in high-affinity agonist binding and potency of the beta 2-adrenergic receptor. We suggest that protein kinase C mediated phosphorylation of the receptor promotes its functional uncoupling. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248855 |
Ser262 |
GHGLRRSsKFCLKEH |
in vitro |
|
| pmid |
sentence |
| 1848190 |
We investigate the role of the beta 2-adrenergic receptor phosphorylation by protein kinase C in this regulatory process. Mutation of the serine-261, -262, -344 and -345 of the beta 2-adrenergic receptor prevented the phorbol-ester-induced phosphorylation of the receptor. This mutation also abolished the phorbol-ester-induced decrease in high-affinity agonist binding and potency of the beta 2-adrenergic receptor. We suggest that protein kinase C mediated phosphorylation of the receptor promotes its functional uncoupling. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248857 |
Ser345 |
ELLCLRRsSLKAYGN |
in vitro |
|
| pmid |
sentence |
| 1848190 |
We investigate the role of the beta 2-adrenergic receptor phosphorylation by protein kinase C in this regulatory process. Mutation of the serine-261, -262, -344 and -345 of the beta 2-adrenergic receptor prevented the phorbol-ester-induced phosphorylation of the receptor. This mutation also abolished the phorbol-ester-induced decrease in high-affinity agonist binding and potency of the beta 2-adrenergic receptor. We suggest that protein kinase C mediated phosphorylation of the receptor promotes its functional uncoupling. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248856 |
Ser346 |
LLCLRRSsLKAYGNG |
in vitro |
|
| pmid |
sentence |
| 1848190 |
We investigate the role of the beta 2-adrenergic receptor phosphorylation by protein kinase C in this regulatory process. Mutation of the serine-261, -262, -344 and -345 of the beta 2-adrenergic receptor prevented the phorbol-ester-induced phosphorylation of the receptor. This mutation also abolished the phorbol-ester-induced decrease in high-affinity agonist binding and potency of the beta 2-adrenergic receptor. We suggest that protein kinase C mediated phosphorylation of the receptor promotes its functional uncoupling. |
|
| Publications: |
4 |
Organism: |
In Vitro |
| + |
AKT | down-regulates
phosphorylation
|
ADRB2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-114466 |
Ser345 |
ELLCLRRsSLKAYGN |
Homo sapiens |
|
| pmid |
sentence |
| 11809767 |
Akt mediates sequestration of the beta(2)-adrenergic receptor in response to insulin. Phosphorylation studies of the c-terminal cytoplasmic domain of the beta(2)-adrenergic receptor by akt in vitro identified ser(345) and ser(346) within a consensus motif for akt phosphorylation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-114470 |
Ser346 |
LLCLRRSsLKAYGNG |
Homo sapiens |
|
| pmid |
sentence |
| 11809767 |
Akt mediates sequestration of the beta(2)-adrenergic receptor in response to insulin. Phosphorylation studies of the c-terminal cytoplasmic domain of the beta(2)-adrenergic receptor by akt in vitro identified ser(345) and ser(346) within a consensus motif for akt phosphorylation. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
AKT1 | down-regulates
phosphorylation
|
ADRB2 |
0.362 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252469 |
Ser345 |
ELLCLRRsSLKAYGN |
Homo sapiens |
|
| pmid |
sentence |
| 11809767 |
Akt mediates sequestration of the beta(2)-adrenergic receptor in response to insulin. Phosphorylation studies of the c-terminal cytoplasmic domain of the beta(2)-adrenergic receptor by akt in vitro identified ser(345) and ser(346) within a consensus motif for akt phosphorylation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252470 |
Ser346 |
LLCLRRSsLKAYGNG |
Homo sapiens |
|
| pmid |
sentence |
| 11809767 |
Akt mediates sequestration of the beta(2)-adrenergic receptor in response to insulin. Phosphorylation studies of the c-terminal cytoplasmic domain of the beta(2)-adrenergic receptor by akt in vitro identified ser(345) and ser(346) within a consensus motif for akt phosphorylation. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
GRK5 |
phosphorylation
|
ADRB2 |
0.682 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251195 |
Ser396 |
GHQGTVPsDNIDSQG |
in vitro |
|
| pmid |
sentence |
| 8662852 |
we report the identification of the sites of GRK2- and GRK5-mediated beta2AR phosphorylation. six are phosphorylated by GRK5 (Thr-384, Thr-393, Ser-396, Ser-401, Ser-407, and Ser-411). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251196 |
Ser401 |
VPSDNIDsQGRNCST |
in vitro |
|
| pmid |
sentence |
| 8662852 |
we report the identification of the sites of GRK2- and GRK5-mediated beta2AR phosphorylation. six are phosphorylated by GRK5 (Thr-384, Thr-393, Ser-396, Ser-401, Ser-407, and Ser-411). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251197 |
Ser407 |
DSQGRNCsTNDSLL |
in vitro |
|
| pmid |
sentence |
| 8662852 |
we report the identification of the sites of GRK2- and GRK5-mediated beta2AR phosphorylation. six are phosphorylated by GRK5 (Thr-384, Thr-393, Ser-396, Ser-401, Ser-407, and Ser-411). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251198 |
Ser411 |
RNCSTNDsLL |
in vitro |
|
| pmid |
sentence |
| 8662852 |
we report the identification of the sites of GRK2- and GRK5-mediated beta2AR phosphorylation. six are phosphorylated by GRK5 (Thr-384, Thr-393, Ser-396, Ser-401, Ser-407, and Ser-411). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251199 |
Thr384 |
LCEDLPGtEDFVGHQ |
in vitro |
|
| pmid |
sentence |
| 8662852 |
we report the identification of the sites of GRK2- and GRK5-mediated beta2AR phosphorylation. six are phosphorylated by GRK5 (Thr-384, Thr-393, Ser-396, Ser-401, Ser-407, and Ser-411). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251200 |
Thr393 |
DFVGHQGtVPSDNID |
in vitro |
|
| pmid |
sentence |
| 8662852 |
we report the identification of the sites of GRK2- and GRK5-mediated beta2AR phosphorylation. six are phosphorylated by GRK5 (Thr-384, Thr-393, Ser-396, Ser-401, Ser-407, and Ser-411). |
|
| Publications: |
6 |
Organism: |
In Vitro |
| + |
INSR | down-regulates activity
phosphorylation
|
ADRB2 |
0.385 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251299 |
Tyr132 |
CVIAVDRyFAITSPF |
Cricetulus griseus |
CHO Cell |
| pmid |
sentence |
| 8557631 |
Insulin (10 nM)-stimulated rIR-catalyzed phosphorylation of β2-adrenergic receptor peptides was found prominently in peptides L339 (Tyr350 and Tyr354), T362 (Tyr364), and to a lesser extent peptides Y132 (Tyr132 and Tyr141), and I135 (Tyr141). G-protein-linked receptors and intrinsic tyrosine-kinase growth receptors represent two prominent modalities in cell signaling. Cross-regulation among members of both receptor superfamilies has been reported, including the counter-regulatory effects of insulin on β-adrenergic catecholamine action. Cells stimulated by insulin show loss of function and increased phosphotyrosine content of β2-adrenergic receptors. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251300 |
Tyr141 |
AITSPFKyQSLLTKN |
Cricetulus griseus |
CHO Cell |
| pmid |
sentence |
| 8557631 |
Insulin (10 nM)-stimulated rIR-catalyzed phosphorylation of β2-adrenergic receptor peptides was found prominently in peptides L339 (Tyr350 and Tyr354), T362 (Tyr364), and to a lesser extent peptides Y132 (Tyr132 and Tyr141), and I135 (Tyr141). G-protein-linked receptors and intrinsic tyrosine-kinase growth receptors represent two prominent modalities in cell signaling. Cross-regulation among members of both receptor superfamilies has been reported, including the counter-regulatory effects of insulin on β-adrenergic catecholamine action. Cells stimulated by insulin show loss of function and increased phosphotyrosine content of β2-adrenergic receptors. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251301 |
Tyr350 |
RRSSLKAyGNGYSSN |
Cricetulus griseus |
CHO Cell |
| pmid |
sentence |
| 8557631 |
Insulin (10 nM)-stimulated rIR-catalyzed phosphorylation of β2-adrenergic receptor peptides was found prominently in peptides L339 (Tyr350 and Tyr354), T362 (Tyr364), and to a lesser extent peptides Y132 (Tyr132 and Tyr141), and I135 (Tyr141). G-protein-linked receptors and intrinsic tyrosine-kinase growth receptors represent two prominent modalities in cell signaling. Cross-regulation among members of both receptor superfamilies has been reported, including the counter-regulatory effects of insulin on β-adrenergic catecholamine action. Cells stimulated by insulin show loss of function and increased phosphotyrosine content of β2-adrenergic receptors. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251302 |
Tyr354 |
LKAYGNGySSNGNTG |
Cricetulus griseus |
CHO Cell |
| pmid |
sentence |
| 8557631 |
Insulin (10 nM)-stimulated rIR-catalyzed phosphorylation of β2-adrenergic receptor peptides was found prominently in peptides L339 (Tyr350 and Tyr354), T362 (Tyr364), and to a lesser extent peptides Y132 (Tyr132 and Tyr141), and I135 (Tyr141). G-protein-linked receptors and intrinsic tyrosine-kinase growth receptors represent two prominent modalities in cell signaling. Cross-regulation among members of both receptor superfamilies has been reported, including the counter-regulatory effects of insulin on β-adrenergic catecholamine action. Cells stimulated by insulin show loss of function and increased phosphotyrosine content of β2-adrenergic receptors. |
|
| Publications: |
4 |
Organism: |
Cricetulus Griseus |
| + |
olodaterol | up-regulates activity
chemical activation
|
ADRB2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257834 |
|
|
in vitro |
|
| pmid |
sentence |
| 20371707 |
In vitro, olodaterol showed a potent, nearly full agonistic response at the hbeta(2)-AR (EC(50) = 0.1 nM; intrinsic activity = 88% compared with isoprenaline) and a significant selectivity profile (241- and 2299-fold [corrected] against the hbeta(1)- and hbeta(3)-ARs, respectively). |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
terbutaline | up-regulates activity
chemical activation
|
ADRB2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257872 |
|
|
Cricetulus longicaudatus |
|
| pmid |
sentence |
| 20590599 |
Of the agonists studied here, there was a general trend that those with highest intrinsic efficacy were so across all three receptor subtypes (i.e. at the top of Tables 3–5, e.g. fenoterol, terbutaline, metaproterenol and adrenaline) |
|
| Publications: |
1 |
Organism: |
Cricetulus Longicaudatus |
| + |
SLC9A3R1 | up-regulates activity
binding
|
ADRB2 |
0.581 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262598 |
|
|
in vitro |
|
| pmid |
sentence |
| 9671706 |
The Na+/H+ exchanger regulatory factor (NHERF) binds to the tail of the beta2-adrenergic receptor and plays a role in adrenergic regulation of Na+/H+ exchange. NHERF contains two PDZ domains, the first of which is required for its interaction with the beta2 receptor. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
ADRB2 | up-regulates activity
binding
|
GNA14 |
0.318 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257192 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 31160049 |
Here we systematically quantified ligand-induced interactions between 148 GPCRs and all 11 unique G alpha subunit C-termini. For each receptor, we probed chimeric G alpha subunit activation via a transforming growth factor-alpha (TGF alpha) shedding response in HEK293 cells lacking endogenous Gq/11- and G12/13- signaling. | We defined positive coupling if any member of the subfamily scored LogRAi ≥ -1 and negative coupling if all of the members scored LogRAi < -1 (Figure 3A-B). ROC analysis gives AUC = 0.78 (Figure S4A) when considering high-confidence known coupling data and suggested a threshold of LogRAi ≥ -1.0 for defining true couplings. | The score associated to this interaction has a LogRAi ≥ -1.0. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ADRB2 | up-regulates activity
binding
|
GNAQ |
0.342 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257081 |
|
|
Homo sapiens |
HEK-293A Cell |
| pmid |
sentence |
| 31160049 |
Here we systematically quantified ligand-induced interactions between 148 GPCRs and all 11 unique G alpha subunit C-termini. For each receptor, we probed chimeric G alpha subunit activation via a transforming growth factor-alpha (TGF alpha) shedding response in HEK293 cells lacking endogenous Gq/11- and G12/13- signaling. | We defined positive coupling if any member of the subfamily scored LogRAi ≥ -1 and negative coupling if all of the members scored LogRAi < -1 (Figure 3A-B). ROC analysis gives AUC = 0.78 (Figure S4A) when considering high-confidence known coupling data and suggested a threshold of LogRAi ≥ -1.0 for defining true couplings. | The score associated to this interaction has a LogRAi ≥ -1.0. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
isoprenaline | up-regulates activity
chemical activation
|
ADRB2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258576 |
|
|
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 8982677 |
K i values of the agonists for [~25I]iodocyanopindolol binding to the COS-7 cell membranes are shown in Table 1. In the membranes expressing one of the 13-adrenoceptor subtypes, both isoproterenol and T-0509 caused monophasic dis- placement of [~25I]iodocyanopindolol, suggesting a single binding site of the agonists. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
metaproterenol | up-regulates activity
chemical activation
|
ADRB2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257814 |
|
|
in vitro |
|
| pmid |
sentence |
| 19168263 |
Synthesis, pharmacological and in silico evaluation of 1-(4-di-hydroxy-3,5-dioxa-4-borabicyclo[4.4.0]deca-7,9,11-trien-9-yl)-2-(tert-butylamino)ethanol, a compound designed to act as a β2 adrenoceptor agonist | After that, in vitro assays were carried out and the Kd value obtained for BR-AEA was compared with reported in vitro data for salbutamol and other well-known ligands. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257875 |
|
|
Cricetulus longicaudatus |
CHO-K1 Cell |
| pmid |
sentence |
| 20590599 |
Of the agonists studied here, there was a general trend that those with highest intrinsic efficacy were so across all three receptor subtypes (i.e. at the top of Tables 3–5, e.g. fenoterol, terbutaline, metaproterenol and adrenaline) |
|
| Publications: |
2 |
Organism: |
In Vitro, Cricetulus Longicaudatus |
| + |
propranolol | down-regulates activity
chemical inhibition
|
ADRB2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258334 |
|
|
Cricetulus longicaudatus |
|
| pmid |
sentence |
| 10079020 |
Similarly, the binding affinities of ICI 118–551, CGP 20712A, propranolol, bupranolol and CGP 12177 for human β1-, β2- and β3-adrenoceptors correlate with their affinities at human β1- (P=0.04), β2- (P=0.01) |
|
| Publications: |
1 |
Organism: |
Cricetulus Longicaudatus |
| + |
ADRB2 | up-regulates activity
binding
|
GNAS |
0.646 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256149 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14500986 |
We have found that signaling via the erythrocyte beta2-adrenergic receptor and heterotrimeric guanine nucleotide-binding protein (Galphas) regulated the entry of the human malaria parasite Plasmodium falciparum. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256809 |
|
|
Homo sapiens |
HEK-293A Cell |
| pmid |
sentence |
| 31160049 |
Here we systematically quantified ligand-induced interactions between 148 GPCRs and all 11 unique G alpha subunit C-termini. For each receptor, we probed chimeric G alpha subunit activation via a transforming growth factor-alpha (TGF alpha) shedding response in HEK293 cells lacking endogenous Gq/11- and G12/13- signaling. | We defined positive coupling if any member of the subfamily scored LogRAi ≥ -1 and negative coupling if all of the members scored LogRAi < -1 (Figure 3A-B). ROC analysis gives AUC = 0.78 (Figure S4A) when considering high-confidence known coupling data and suggested a threshold of LogRAi ≥ -1.0 for defining true couplings. | The score associated to this interaction has a LogRAi ≥ -1.0. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
(R)-salbutamol | up-regulates activity
chemical activation
|
ADRB2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257865 |
|
|
Cricetulus longicaudatus |
|
| pmid |
sentence |
| 20590599 |
Denopamine is the most selective ligand for β1-receptors, with regard to intrinsic activity and efficacy, and clenbuterol, procaterol, zinterol, AZ 40140d and salbutamol are more selective for the β2-adrenoceptor than the β1-adrenoceptor based on intrinsic activity and efficacy. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258326 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22182578 |
Salbutamol is a well-known β2 adrenoceptor (β2AR) partial agonist. | In order to gain insight, we carried out binding and functional assays for BCSDs in HEK-293T cells transfected with the human β2AR (hβ2AR). The transfected hβ2AR showed similar affinity for BCSDs and salbutamol |
|
| Publications: |
2 |
Organism: |
Cricetulus Longicaudatus, Homo Sapiens |
| + |
procaterol | up-regulates activity
chemical activation
|
ADRB2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257863 |
|
|
Cricetulus longicaudatus |
CHO-K1 Cell |
| pmid |
sentence |
| 20590599 |
Denopamine is the most selective ligand for β1-receptors, with regard to intrinsic activity and efficacy, and clenbuterol, procaterol, zinterol, AZ 40140d and salbutamol are more selective for the β2-adrenoceptor than the β1-adrenoceptor based on intrinsic activity and efficacy. |
|
| Publications: |
1 |
Organism: |
Cricetulus Longicaudatus |
| + |
Cy3-bifunctional dye zwitterion | up-regulates activity
chemical activation
|
ADRB2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257858 |
|
|
Cricetulus longicaudatus |
CHO-K1 Cell |
| pmid |
sentence |
| 20590599 |
Denopamine is the most selective ligand for β1-receptors, with regard to intrinsic activity and efficacy, and clenbuterol, procaterol, zinterol, AZ 40140d and salbutamol are more selective for the β2-adrenoceptor than the β1-adrenoceptor based on intrinsic activity and efficacy. |
|
| Publications: |
1 |
Organism: |
Cricetulus Longicaudatus |
| + |
8-hydroxy-5-[1-hydroxy-2-(propan-2-ylamino)butyl]-1H-quinolin-2-one | up-regulates activity
chemical activation
|
ADRB2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257857 |
|
|
Cricetulus longicaudatus |
|
| pmid |
sentence |
| 20590599 |
Denopamine is the most selective ligand for β1-receptors, with regard to intrinsic activity and efficacy, and clenbuterol, procaterol, zinterol, AZ 40140d and salbutamol are more selective for the β2-adrenoceptor than the β1-adrenoceptor based on intrinsic activity and efficacy. |
|
| Publications: |
1 |
Organism: |
Cricetulus Longicaudatus |
| + |
vilanterol | up-regulates activity
chemical activation
|
ADRB2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257843 |
|
|
Cricetulus longicaudatus |
|
| pmid |
sentence |
| 20462258 |
A series of saligenin β2 adrenoceptor agonist antedrugs having high clearance were prepared by reacting a protected saligenin oxazolidinone with protected hydroxyethoxyalkoxyalkyl bromides, followed by removal of the hydroxy-protecting group, alkylation, and final deprotection. The compounds were screened for β2, β1, and β3 agonist activity in CHO cells. | Compound 13f had high potency, selectivity, fast onset, and long duration of action in vitro and was found to have long duration in vivo |
|
| Publications: |
1 |
Organism: |
Cricetulus Longicaudatus |
| + |
2-(hydroxymethyl)-4-(1-hydroxy-2-{[6-(4-phenylbutoxy)hexyl]amino}ethyl)phenol | up-regulates activity
chemical activation
|
ADRB2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257852 |
|
|
Cricetulus longicaudatus |
|
| pmid |
sentence |
| 20590599 |
The affinity measurements (log KD values of −5.73, −9.26 and −6.33 for β1, β2 and β3, respectively), show that salmeterol has high affinity for the β2-adrenoceptor. |
|
| Publications: |
1 |
Organism: |
Cricetulus Longicaudatus |
| + |
clenbuterol | up-regulates activity
chemical activation
|
ADRB2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257861 |
|
|
Cricetulus longicaudatus |
CHO-K1 Cell |
| pmid |
sentence |
| 20590599 |
Denopamine is the most selective ligand for β1-receptors, with regard to intrinsic activity and efficacy, and clenbuterol, procaterol, zinterol, AZ 40140d and salbutamol are more selective for the β2-adrenoceptor than the β1-adrenoceptor based on intrinsic activity and efficacy. |
|
| Publications: |
1 |
Organism: |
Cricetulus Longicaudatus |
| + |
ARRB2 | down-regulates activity
binding
|
ADRB2 |
0.713 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256501 |
|
|
in vitro |
|
| pmid |
sentence |
| 2163110 |
The protein, termed beta-arrestin, was expressed and partially purified. It inhibited the signaling function of beta ARK-phosphorylated beta-adrenergic receptors by more than 75 percent, but not that of rhodopsin. It is proposed that beta-arrestin in concert with beta ARK effects homologous desensitization of beta-adrenergic receptors |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
arformoterol | up-regulates activity
chemical activation
|
ADRB2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257882 |
|
|
in vitro |
|
| pmid |
sentence |
| 20655218 |
Table 1. Human β2- and β1-adrenoceptor binding and calculated log D7.4 values for formoterol, indacaterol, salmeterol, S1319 and the representative library members 11–41 |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
ADRB2 | up-regulates activity
binding
|
GNAL |
0.412 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256952 |
|
|
Homo sapiens |
HEK-293A Cell |
| pmid |
sentence |
| 31160049 |
Here we systematically quantified ligand-induced interactions between 148 GPCRs and all 11 unique G alpha subunit C-termini. For each receptor, we probed chimeric G alpha subunit activation via a transforming growth factor-alpha (TGF alpha) shedding response in HEK293 cells lacking endogenous Gq/11- and G12/13- signaling. | We defined positive coupling if any member of the subfamily scored LogRAi ≥ -1 and negative coupling if all of the members scored LogRAi < -1 (Figure 3A-B). ROC analysis gives AUC = 0.78 (Figure S4A) when considering high-confidence known coupling data and suggested a threshold of LogRAi ≥ -1.0 for defining true couplings. | The score associated to this interaction has a LogRAi ≥ -1.0. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
(R)-adrenaline | up-regulates
chemical activation
|
ADRB2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-198501 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22863277 |
In contrast, stimulation of gs-coupled receptors by glucagon or epinephrine activates lats1/2 kinase activity, thereby inhibiting yap function. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
N-[2-hydroxy-5-(1-hydroxy-2-{[1-(4-methoxyphenyl)propan-2-yl]amino}ethyl)phenyl]formamide | up-regulates activity
chemical activation
|
ADRB2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257853 |
|
|
Cricetulus longicaudatus |
CHO-K1 Cell |
| pmid |
sentence |
| 20590599 |
Thus, overall, salmeterol is a highly selective β2-adrenoceptor agonist because of its higher β2-affinity and not because of higher β2-intrinsic efficacy. A similar reasoning can be applied to formoterol, although this agonist has higher intrinsic efficacy at all three receptors (rank 6, 8 and 5 at β1, β2 and β3). |
|
| Publications: |
1 |
Organism: |
Cricetulus Longicaudatus |
| + |
albuterol sulfate | up-regulates
chemical activation
|
ADRB2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-206682 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
L-isoprenaline | up-regulates activity
chemical activation
|
ADRB2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257457 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 31160049 |
Here we systematically quantified ligand-induced interactions between 148 GPCRs and all 11 unique G alpha subunit C-termini. For each receptor, we probed chimeric G alpha subunit activation via a transforming growth factor-alpha (TGF alpha) shedding response in HEK293 cells lacking endogenous Gq/11- and G12/13- signaling. | We defined positive coupling if any member of the subfamily scored LogRAi ≥ -1 and negative coupling if all of the members scored LogRAi < -1 (Figure 3A-B). ROC analysis gives AUC = 0.78 (Figure S4A) when considering high-confidence known coupling data and suggested a threshold of LogRAi ≥ -1.0 for defining true couplings. | The score associated to this interaction has a LogRAi ≥ -1.0. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
atenolol | down-regulates activity
chemical inhibition
|
ADRB2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258335 |
|
|
Cricetulus longicaudatus |
CHO Cell |
| pmid |
sentence |
| 10079020 |
In our CHO cells transfected with the human β1- and β2-adrenoceptors, the binding affinities of atenolol, metoprolol, betaxolol and practolol correlate with previously published β1- (P=0.03) and β2-adrenoceptor (P=0.03) binding affinities in human lung tissue |
|
| Publications: |
1 |
Organism: |
Cricetulus Longicaudatus |
| + |
adrenaline | up-regulates activity
chemical activation
|
ADRB2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257878 |
|
|
Cricetulus longicaudatus |
CHO-K1 Cell |
| pmid |
sentence |
| 20590599 |
Of the agonists studied here, there was a general trend that those with highest intrinsic efficacy were so across all three receptor subtypes (i.e. at the top of Tables 3–5, e.g. fenoterol, terbutaline, metaproterenol and adrenaline) |
|
| Publications: |
1 |
Organism: |
Cricetulus Longicaudatus |
| + |
fenoterol | up-regulates activity
chemical activation
|
ADRB2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257869 |
|
|
Cricetulus longicaudatus |
CHO-K1 Cell |
| pmid |
sentence |
| 20590599 |
Finally, comparisons of the rank order of ligands for the three different receptors provide information about relative intrinsic efficacies. Fenoterol is a full and efficacious agonist at the β1-adrenoceptor, ranking third out of the agonists studied. It was also a full agonist at the β2- and β3-adrenoceptors with the highest intrinsic efficacy (i.e. top of Tables 4 and and5,5, rank 1). |
|
| Publications: |
1 |
Organism: |
Cricetulus Longicaudatus |
3.0
ADRB2
- 
- 