| + |
acetylcholine | up-regulates activity 
chemical activation
|
CHRNA7 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253984 |
|
|
|
|
| pmid |
sentence |
| 27167578 |
Here, we demonstrate a role for α7 nAChR/G protein interaction in the activation of the small (monomeric) RhoA GTPase leading to cytoskeletal changes during neurite growth. Treatment of PC12 cells with the α7 nAChR agonist choline or PNU-282987 was associated with an increase in RhoA activity and an inhibition in neurite growth. |
|
| Publications: |
1 |
| + |
acetylcholine | up-regulates activity
chemical activation
|
Neuronal nicotinic acetylcholine receptor complex, 3xalpha4-2xbeta2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280881 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 25460185 |
Neuronal nicotinic acetylcholine receptors (nAChRs) are a heterogeneous family of pentameric ligand-gated cation channels that are expressed throughout the brain and involved in a wide range of physiological and pathophysiological processes. The nAChR subtypes share a common basic structure, but their biophysical and pharmacological properties depend on their subunit composition, which is therefore central to understanding their function in the nervous system and discovering new subtype selective drugs.The variety of subtypes in the mammalian nervous system, is mainly due to the diversity of the possible combinations of the eleven neuronal subunits (all but α8) expressed in this animal class. nAChR subtypes can be divided into two main classes: 1) αBgtx-sensitive subtypes which can be homomeric or heteromeric, and are made up of the α7, α9 and α10 subunits; and 2) αBtgx-insensitive receptors, which are heteromeric combinations of α2–6 and β2–4 subunits that bind nicotine with high affinity but not αBgtx (Fig. 1B) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
acetylcholine | up-regulates activity
chemical activation
|
Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha5-beta2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280882 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 25460185 |
Neuronal nicotinic acetylcholine receptors (nAChRs) are a heterogeneous family of pentameric ligand-gated cation channels that are expressed throughout the brain and involved in a wide range of physiological and pathophysiological processes. The nAChR subtypes share a common basic structure, but their biophysical and pharmacological properties depend on their subunit composition, which is therefore central to understanding their function in the nervous system and discovering new subtype selective drugs.The variety of subtypes in the mammalian nervous system, is mainly due to the diversity of the possible combinations of the eleven neuronal subunits (all but α8) expressed in this animal class. nAChR subtypes can be divided into two main classes: 1) αBgtx-sensitive subtypes which can be homomeric or heteromeric, and are made up of the α7, α9 and α10 subunits; and 2) αBtgx-insensitive receptors, which are heteromeric combinations of α2–6 and β2–4 subunits that bind nicotine with high affinity but not αBgtx (Fig. 1B) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
acetylcholine | up-regulates activity
chemical activation
|
Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha5-beta4 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280883 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 25460185 |
Neuronal nicotinic acetylcholine receptors (nAChRs) are a heterogeneous family of pentameric ligand-gated cation channels that are expressed throughout the brain and involved in a wide range of physiological and pathophysiological processes. The nAChR subtypes share a common basic structure, but their biophysical and pharmacological properties depend on their subunit composition, which is therefore central to understanding their function in the nervous system and discovering new subtype selective drugs.The variety of subtypes in the mammalian nervous system, is mainly due to the diversity of the possible combinations of the eleven neuronal subunits (all but α8) expressed in this animal class. nAChR subtypes can be divided into two main classes: 1) αBgtx-sensitive subtypes which can be homomeric or heteromeric, and are made up of the α7, α9 and α10 subunits; and 2) αBtgx-insensitive receptors, which are heteromeric combinations of α2–6 and β2–4 subunits that bind nicotine with high affinity but not αBgtx (Fig. 1B) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
acetylcholine | up-regulates activity
chemical activation
|
Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha6-beta4 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280884 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 25460185 |
Neuronal nicotinic acetylcholine receptors (nAChRs) are a heterogeneous family of pentameric ligand-gated cation channels that are expressed throughout the brain and involved in a wide range of physiological and pathophysiological processes. The nAChR subtypes share a common basic structure, but their biophysical and pharmacological properties depend on their subunit composition, which is therefore central to understanding their function in the nervous system and discovering new subtype selective drugs.The variety of subtypes in the mammalian nervous system, is mainly due to the diversity of the possible combinations of the eleven neuronal subunits (all but α8) expressed in this animal class. nAChR subtypes can be divided into two main classes: 1) αBgtx-sensitive subtypes which can be homomeric or heteromeric, and are made up of the α7, α9 and α10 subunits; and 2) αBtgx-insensitive receptors, which are heteromeric combinations of α2–6 and β2–4 subunits that bind nicotine with high affinity but not αBgtx (Fig. 1B) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
acetylcholine | up-regulates activity
chemical activation
|
Neuronal nicotinic acetylcholine receptor complex, alpha4-alpha5-beta2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280885 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 25460185 |
Neuronal nicotinic acetylcholine receptors (nAChRs) are a heterogeneous family of pentameric ligand-gated cation channels that are expressed throughout the brain and involved in a wide range of physiological and pathophysiological processes. The nAChR subtypes share a common basic structure, but their biophysical and pharmacological properties depend on their subunit composition, which is therefore central to understanding their function in the nervous system and discovering new subtype selective drugs.The variety of subtypes in the mammalian nervous system, is mainly due to the diversity of the possible combinations of the eleven neuronal subunits (all but α8) expressed in this animal class. nAChR subtypes can be divided into two main classes: 1) αBgtx-sensitive subtypes which can be homomeric or heteromeric, and are made up of the α7, α9 and α10 subunits; and 2) αBtgx-insensitive receptors, which are heteromeric combinations of α2–6 and β2–4 subunits that bind nicotine with high affinity but not αBgtx (Fig. 1B) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
acetylcholine | up-regulates activity
chemical activation
|
Neuronal nicotinic acetylcholine receptor complex, alpha7-beta2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280886 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 25460185 |
Neuronal nicotinic acetylcholine receptors (nAChRs) are a heterogeneous family of pentameric ligand-gated cation channels that are expressed throughout the brain and involved in a wide range of physiological and pathophysiological processes. The nAChR subtypes share a common basic structure, but their biophysical and pharmacological properties depend on their subunit composition, which is therefore central to understanding their function in the nervous system and discovering new subtype selective drugs.The variety of subtypes in the mammalian nervous system, is mainly due to the diversity of the possible combinations of the eleven neuronal subunits (all but α8) expressed in this animal class. nAChR subtypes can be divided into two main classes: 1) αBgtx-sensitive subtypes which can be homomeric or heteromeric, and are made up of the α7, α9 and α10 subunits; and 2) αBtgx-insensitive receptors, which are heteromeric combinations of α2–6 and β2–4 subunits that bind nicotine with high affinity but not αBgtx (Fig. 1B) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
acetylcholine | up-regulates activity
chemical activation
|
Muscle-type nicotinic acetylcholine receptor complex, alpha1-beta1-delta-epsilon |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280887 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15701510 |
The nicotinic ACh receptor is a member of the pentameric “Cys-loop” superfamily of transmitter-gated ion channels, which includes neuronal ACh receptors, GABAA receptors, 5-HT3 receptors and glycine receptors.1, 2, 3, 4, 5 The channel is found in high concentrations at the nerve–muscle synapse, where it mediates fast chemical transmission of electrical signals in response to ACh released from the nerve terminal into the synaptic cleft. It is a large (290 kDa) glyco-protein, assembled from a ring of homologous subunits (α, γ, α, β, δ) and divided into three domains |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle |
| + |
acetylcholine | up-regulates activity
chemical activation
|
Muscle-type nicotinic acetylcholine receptor complex, alpha1-beta1-delta-gamma |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280907 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15701510 |
The nicotinic ACh receptor is a member of the pentameric “Cys-loop” superfamily of transmitter-gated ion channels, which includes neuronal ACh receptors, GABAA receptors, 5-HT3 receptors and glycine receptors.1, 2, 3, 4, 5 The channel is found in high concentrations at the nerve–muscle synapse, where it mediates fast chemical transmission of electrical signals in response to ACh released from the nerve terminal into the synaptic cleft. It is a large (290 kDa) glyco-protein, assembled from a ring of homologous subunits (α, γ, α, β, δ) and divided into three domains |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle |
| + |
acetylcholine | up-regulates activity
chemical activation
|
Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha6-beta2-beta3 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280913 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 25460185 |
Neuronal nicotinic acetylcholine receptors (nAChRs) are a heterogeneous family of pentameric ligand-gated cation channels that are expressed throughout the brain and involved in a wide range of physiological and pathophysiological processes. The nAChR subtypes share a common basic structure, but their biophysical and pharmacological properties depend on their subunit composition, which is therefore central to understanding their function in the nervous system and discovering new subtype selective drugs.The variety of subtypes in the mammalian nervous system, is mainly due to the diversity of the possible combinations of the eleven neuronal subunits (all but α8) expressed in this animal class. nAChR subtypes can be divided into two main classes: 1) αBgtx-sensitive subtypes which can be homomeric or heteromeric, and are made up of the α7, α9 and α10 subunits; and 2) αBtgx-insensitive receptors, which are heteromeric combinations of α2–6 and β2–4 subunits that bind nicotine with high affinity but not αBgtx (Fig. 1B) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
acetylcholine | up-regulates activity
chemical activation
|
CHRM4 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257471 |
|
|
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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258633 |
|
|
Cricetulus griseus |
CHO Cell |
| pmid |
sentence |
| 9224827 |
We investigated whether the allosteric modulators can also increase the affinity of receptors for their agonists. Twelve agonists and five allosteric modulators were tested in experiments on membranes of CHO cells that had been stably transfected with genes for the M1-M4 receptor subtypes. Affinities of agonists for the M1–M4 receptor subtypes were determined according to the ability of the agonist to inhibit [3H]NMS binding in the presence of 0.5 mM GTP; in this way, the low affinity binding of agonists was measured.The computed pKi and nH values are summarized in Table 2. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens, Cricetulus Griseus |
| + |
acetylcholine | up-regulates activity
chemical activation
|
CHRM3 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257470 |
|
|
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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258632 |
|
|
Cricetulus griseus |
CHO Cell |
| pmid |
sentence |
| 9224827 |
We investigated whether the allosteric modulators can also increase the affinity of receptors for their agonists. Twelve agonists and five allosteric modulators were tested in experiments on membranes of CHO cells that had been stably transfected with genes for the M1-M4 receptor subtypes. Affinities of agonists for the M1–M4 receptor subtypes were determined according to the ability of the agonist to inhibit [3H]NMS binding in the presence of 0.5 mM GTP; in this way, the low affinity binding of agonists was measured.The computed pKi and nH values are summarized in Table 2. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens, Cricetulus Griseus |
| + |
acetylcholine | up-regulates activity
chemical activation
|
CHRM5 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257472 |
|
|
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 |
| + |
acetylcholine | up-regulates activity
chemical activation
|
CHRM2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258631 |
|
|
Cricetulus griseus |
CHO Cell |
| pmid |
sentence |
| 9224827 |
We investigated whether the allosteric modulators can also increase the affinity of receptors for their agonists. Twelve agonists and five allosteric modulators were tested in experiments on membranes of CHO cells that had been stably transfected with genes for the M1-M4 receptor subtypes. Affinities of agonists for the M1–M4 receptor subtypes were determined according to the ability of the agonist to inhibit [3H]NMS binding in the presence of 0.5 mM GTP; in this way, the low affinity binding of agonists was measured.The computed pKi and nH values are summarized in Table 2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257469 |
|
|
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: |
Cricetulus Griseus, Homo Sapiens |
| + |
acetylcholine | up-regulates activity
chemical activation
|
CHRM1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257468 |
|
|
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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258630 |
|
|
Cricetulus griseus |
CHO Cell |
| pmid |
sentence |
| 9224827 |
We investigated whether the allosteric modulators can also increase the affinity of receptors for their agonists. Twelve agonists and five allosteric modulators were tested in experiments on membranes of CHO cells that had been stably transfected with genes for the M1-M4 receptor subtypes. Affinities of agonists for the M1–M4 receptor subtypes were determined according to the ability of the agonist to inhibit [3H]NMS binding in the presence of 0.5 mM GTP; in this way, the low affinity binding of agonists was measured.The computed pKi and nH values are summarized in Table 2. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens, Cricetulus Griseus |
| + |
BCHE | down-regulates quantity 
chemical modification
|
acetylcholine |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253982 |
|
|
|
|
| pmid |
sentence |
| 15841900 |
The other subgroup, butyrylcholinesterase (BuChE) (or acyl- choline acyl-hydrolase, EC 3.1.1.8) also known as plasma, serum, benzoyl, false, butyryl, nonspecific, or type II ChE. BuChE exists in plasma and has more than eleven isoenzy- me variants. BuChE is also present in liver, smooth muscle, intestines, pancreas, heart and white matter of brain |It hydrolyzes butyrylcholine 4 times more rapidly than acetylcholine. |
|
| Publications: |
1 |
| + |
ACHE | down-regulates quantity
chemical modification
|
acetylcholine |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253983 |
|
|
|
|
| pmid |
sentence |
| 15841900 |
Acetylcholinesterase (AChE) is one of the most crucial enzymes for nerve response and function. AChE catalyzes the hydrolysis of acylcholine esters with a relative specificity for acetylcholine.|The intracellular effects of acetylcholine are mediated by the activation of nicotinic and muscarinic acetylcholine receptors (AChRs). AChE terminates transmission of neuronal impulses by rapid hydrolysis of acetylcholine. |
|
| Publications: |
1 |
| + |
acetylcholine | up-regulates activity
chemical activation
|
CHRNB3 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264258 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28901280 |
Neuronal nicotinic acetylcholine receptors (nAChRs) belong to a super-family of Cysloop ligand-gated ion channels that respond to endogenous acetylcholine (ACh) or other cholinergic ligands. These receptors are also the targets of drugs such as nicotine (the main addictive agent delivered by cigarette smoke) and are involved in a variety of physiological and pathophysiological processes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Central Nervous System |
4.0
acetylcholine