Sandbox Reserved 1095: Difference between revisions

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=== Interaction with other GPCRs ===

It has been discovered that AT1Rs were also able to bind with other GPCRs to form homo- or heterodimers. Those interactions can modify the sensitivity of the receptor, which leads to different physiological and pathological conditions than the GPCR monomer <ref ~~name="Zhang2015"~~ /><ref name="Takanobu2017"> [https://doi.org/10.1016/j.phrs.2017.06.013 Takezako T, Unal H, Karnik SS, Node K. Current topics in angiotensin II type 1 receptor research: Focus on inverse agonism, receptor dimerization and biased agonism. Pharmacol Res. 2017;123:40–50. doi:10.1016/j.phrs.2017.06.013] </ref>. The most known heterodimers including AT1 receptor are with [[Beta-2 adrenergic receptor]], [https://en.wikipedia.org/wiki/Apelin_receptor the apelin receptor] ([[5vbl]]), and AT2 receptor. Those interactions could be facilitated by several transmembrane domains.

It has been discovered that AT1Rs were also able to bind with other GPCRs to form homo- or heterodimers. Those interactions can modify the sensitivity of the receptor, which leads to different physiological and pathological conditions than the GPCR monomer <ref>PMID: 26420482 </ref><ref name="Takanobu2017"> [https://doi.org/10.1016/j.phrs.2017.06.013 Takezako T, Unal H, Karnik SS, Node K. Current topics in angiotensin II type 1 receptor research: Focus on inverse agonism, receptor dimerization and biased agonism. Pharmacol Res. 2017;123:40–50. doi:10.1016/j.phrs.2017.06.013] </ref>. The most known heterodimers including AT1 receptor are with [[Beta-2 adrenergic receptor]], [https://en.wikipedia.org/wiki/Apelin_receptor the apelin receptor] ([[5vbl]]), and AT2 receptor. Those interactions could be facilitated by several transmembrane domains.

The oligomeric complexes' formation complicate the understanding of AT1R pharmacology.

Sandbox Reserved 1095: Difference between revisions

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 === Interaction with other GPCRs ===
-It has been discovered that AT1Rs were also able to bind with other GPCRs to form homo- or heterodimers. Those interactions can modify the sensitivity of the receptor, which leads to different physiological and pathological conditions than the GPCR monomer <ref name="Zhang2015" /><ref name="Takanobu2017"> [https://doi.org/10.1016/j.phrs.2017.06.013 Takezako T, Unal H, Karnik SS, Node K. Current topics in angiotensin II type 1 receptor research: Focus on inverse agonism, receptor dimerization and biased agonism. Pharmacol Res. 2017;123:40–50. doi:10.1016/j.phrs.2017.06.013] </ref>. The most known heterodimers including AT1 receptor are with [[Beta-2 adrenergic receptor]], [https://en.wikipedia.org/wiki/Apelin_receptor the apelin receptor] ([[5vbl]]), and AT2 receptor. Those interactions could be facilitated by several transmembrane domains.
+It has been discovered that AT1Rs were also able to bind with other GPCRs to form homo- or heterodimers. Those interactions can modify the sensitivity of the receptor, which leads to different physiological and pathological conditions than the GPCR monomer <ref>PMID: 26420482 </ref><ref name="Takanobu2017"> [https://doi.org/10.1016/j.phrs.2017.06.013 Takezako T, Unal H, Karnik SS, Node K. Current topics in angiotensin II type 1 receptor research: Focus on inverse agonism, receptor dimerization and biased agonism. Pharmacol Res. 2017;123:40–50. doi:10.1016/j.phrs.2017.06.013] </ref>. The most known heterodimers including AT1 receptor are with [[Beta-2 adrenergic receptor]], [https://en.wikipedia.org/wiki/Apelin_receptor the apelin receptor] ([[5vbl]]), and AT2 receptor. Those interactions could be facilitated by several transmembrane domains.
 The oligomeric complexes' formation complicate the understanding of AT1R pharmacology.