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a(MESH:Bungarotoxins)

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Entity

Name
Bungarotoxins
Namespace
mesh
Namespace Version
20181007
Namespace URL
https://raw.githubusercontent.com/pharmacome/terminology/8ccfed235e418e4c8aa576f9a5ef0f838e794c7f/external/mesh-names.belns

Appears in Networks 4

Nicotinic acetylcholine receptor signalling: roles in Alzheimer's disease and amyloid neuroprotection. v1.0.0

The Nicotinic Acetylcholine Receptor: The Founding Father of the Pentameric Ligand-gated Ion Channel Superfamily v1.0.1

Role of the nicotinic acetylcholine receptor in Alzheimer's disease pathology and treatment v1.0.1

NACHO Mediates Nicotinic Acetylcholine Receptor Function throughout the Brain v1.0.0

In-Edges 16

complex(a(MESH:Bungarotoxins), p(HGNC:CHRNA5)) hasComponent a(MESH:Bungarotoxins) View Subject | View Object

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complex(a(CHEBI:"amyloid-beta polypeptide 42"), p(HGNC:CHRNA7)) decreases act(a(MESH:Bungarotoxins)) View Subject | View Object

However, it has been shown that Abeta1–42 binds with high affinity to alpha7 nAChRs in several different neuronal tissues (Wang et al., 2000a) and displaces alpha-bungarotoxin binding (Wang et al., 2000a,b) and, rather than inhibiting receptor internalization, alpha-bungarotoxin enhances internalization of heterologously expressed nAChRs (Kumari et al., 2008). PubMed:19293145

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complex(a(MESH:Bungarotoxins), p(HGNC:CHRNA7)) hasComponent a(MESH:Bungarotoxins) View Subject | View Object

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complex(a(MESH:Bungarotoxins), p(HGNCGENEFAMILY:"Cholinergic receptors nicotinic subunits")) hasComponent a(MESH:Bungarotoxins) View Subject | View Object

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complex(a(MESH:Bungarotoxins), p(HGNC:CHRNA6)) hasComponent a(MESH:Bungarotoxins) View Subject | View Object

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complex(a(MESH:Bungarotoxins), p(HGNC:CHRNA9)) hasComponent a(MESH:Bungarotoxins) View Subject | View Object

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complex(a(MESH:Bungarotoxins), p(HGNC:CHRND)) hasComponent a(MESH:Bungarotoxins) View Subject | View Object

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complex(a(MESH:Bungarotoxins), p(HGNC:CHRNA4)) hasComponent a(MESH:Bungarotoxins) View Subject | View Object

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complex(a(MESH:Bungarotoxins), p(HGNC:CHRNG)) hasComponent a(MESH:Bungarotoxins) View Subject | View Object

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complex(a(MESH:Bungarotoxins), p(HGNC:CHRNA1)) hasComponent a(MESH:Bungarotoxins) View Subject | View Object

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complex(a(MESH:Bungarotoxins), p(HGNC:CHRNA10)) hasComponent a(MESH:Bungarotoxins) View Subject | View Object

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complex(a(MESH:Bungarotoxins), p(HGNC:CHRNA2)) hasComponent a(MESH:Bungarotoxins) View Subject | View Object

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complex(a(MESH:Bungarotoxins), p(HGNC:CHRNA3)) hasComponent a(MESH:Bungarotoxins) View Subject | View Object

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complex(a(GO:membrane), a(MESH:Bungarotoxins)) hasComponent a(MESH:Bungarotoxins) View Subject | View Object

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complex(a(MESH:"alpha7 Nicotinic Acetylcholine Receptor"), a(MESH:Bungarotoxins)) hasComponent a(MESH:Bungarotoxins) View Subject | View Object

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complex(a(MESH:Bungarotoxins), p(FPLX:CHRN)) hasComponent a(MESH:Bungarotoxins) View Subject | View Object

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Out-Edges 8

a(MESH:Bungarotoxins) decreases bp(GO:"neuromuscular synaptic transmission") View Subject | View Object

Third, Chen-Yuan Lee, a Taiwanese pharmacologist, had found that a snake venom toxin, 􏰂-bungarotoxin (􏰂-BGT), spe- cifically blocks in vivo neuromuscular transmission in high ver- tebrates at the postsynaptic level without interacting with AChE PubMed:23038257

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a(MESH:Bungarotoxins) decreases act(a(CHEBI:"amyloid-beta")) View Subject | View Object

It is noteworthy that this internalization was blocked by alpha-bungarotoxin, which may indicate that alpha-bungarotoxin either inhibits binding of Abeta to the alpha7 receptor (and therefore that Abeta toxicity results from binding of Abeta to alpha7 nAChRs) or directly inhibits alpha7 nAChR internalization. PubMed:19293145

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a(MESH:Bungarotoxins) decreases complex(a(CHEBI:"amyloid-beta"), p(HGNC:CHRNA7)) View Subject | View Object

It is noteworthy that this internalization was blocked by alpha-bungarotoxin, which may indicate that alpha-bungarotoxin either inhibits binding of Abeta to the alpha7 receptor (and therefore that Abeta toxicity results from binding of Abeta to alpha7 nAChRs) or directly inhibits alpha7 nAChR internalization. PubMed:19293145

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act(a(MESH:Bungarotoxins)) decreases p(HGNC:MAPT, pmod(Ph)) View Subject | View Object

It is also noteworthy that Abeta-induced tau protein phosphorylation in PC12 cells is inhibited not only by alpha7 agonists, as would be predicted from the role of alpha7 nAChRs in neuroprotection, but also by alpha-bungarotoxin (Hu et al., 2008), as might be predicted if the competition by alpha-bungarotoxin for the Abeta site blocked a direct action of Abeta on nAChRs. It is therefore possible that the toxicity of Abeta is mediated, at least in part, through a direct physical interaction between Abeta and nAChRs. PubMed:19293145

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Annotations
Experimental Factor Ontology (EFO)
PC12

a(MESH:Bungarotoxins) decreases act(a(MESH:"Electric Organ")) View Subject | View Object

alpha􏰂-BGT blocked the electroplaque’s electrical response in vivo and the microsac’s ion flux response to nicotinic agonists in vitro; alpha􏰂-BGT also blocked the binding of radioactive decamethonium to the detergent extract PubMed:23038257

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a(MESH:Bungarotoxins) decreases act(a(CHEBI:decamethonium)) View Subject | View Object

alpha􏰂-BGT blocked the electroplaque’s electrical response in vivo and the microsac’s ion flux response to nicotinic agonists in vitro; alpha􏰂-BGT also blocked the binding of radioactive decamethonium to the detergent extract PubMed:23038257

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a(MESH:Bungarotoxins) decreases complex(a(CHEBI:"amyloid-beta"), a(MESH:"alpha7 Nicotinic Acetylcholine Receptor")) View Subject | View Object

Subsequently, competition studies performed by incubating alpha7 nAChRs with Abeta and alpha-Bungarotoxin showed that the application of alpha-Bungarotoxin is able to decrease the amount of Abeta bound to alpha7 nAChRs, suggesting that both molecules compete for the same ligand binding domain (Wang et al., 2000b) PubMed:25514383

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a(MESH:Bungarotoxins) decreases complex(a(CHEBI:epibatidine), a(MESH:"alpha7 Nicotinic Acetylcholine Receptor")) View Subject | View Object

Strikingly, we found that alpha-bungarotoxin did not completely displace [3H]epibatidine binding to alpha7 receptors with NACHO (Figure 3B) PubMed:28445721

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About

BEL Commons is developed and maintained in an academic capacity by Charles Tapley Hoyt and Daniel Domingo-Fernández at the Fraunhofer SCAI Department of Bioinformatics with support from the IMI project, AETIONOMY. It is built on top of PyBEL, an open source project. Please feel free to contact us here to give us feedback or report any issues. Also, see our Publishing Notes and Data Protection information.

If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.