Matches in Nanopublications for { ?s ?p "The insulin receptor and some of its substrates are also subject to serine/threonine phosphorylation. Data from some experimental models suggest that this might represent a mechanism by which signaling is terminated, or perhaps attenuated in states of insulin resistance. Numerous in vitro studies have shown that the tyrosine kinase activity of the receptor decreases as a consequence of serine/threonine phosphorylation. This might occur via feedback \"retrophosphorylation\" events in which the receptor or IRS proteins are serine phosphorylated by GSK3 or mTOR, both of which are activated downstream of IRS phosphorylation." ?g. }
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- _5 value "The insulin receptor and some of its substrates are also subject to serine/threonine phosphorylation. Data from some experimental models suggest that this might represent a mechanism by which signaling is terminated, or perhaps attenuated in states of insulin resistance. Numerous in vitro studies have shown that the tyrosine kinase activity of the receptor decreases as a consequence of serine/threonine phosphorylation. This might occur via feedback \"retrophosphorylation\" events in which the receptor or IRS proteins are serine phosphorylated by GSK3 or mTOR, both of which are activated downstream of IRS phosphorylation." provenance.
- _5 value "The insulin receptor and some of its substrates are also subject to serine/threonine phosphorylation. Data from some experimental models suggest that this might represent a mechanism by which signaling is terminated, or perhaps attenuated in states of insulin resistance. Numerous in vitro studies have shown that the tyrosine kinase activity of the receptor decreases as a consequence of serine/threonine phosphorylation. This might occur via feedback \"retrophosphorylation\" events in which the receptor or IRS proteins are serine phosphorylated by GSK3 or mTOR, both of which are activated downstream of IRS phosphorylation." provenance.
- _5 value "The insulin receptor and some of its substrates are also subject to serine/threonine phosphorylation. Data from some experimental models suggest that this might represent a mechanism by which signaling is terminated, or perhaps attenuated in states of insulin resistance. Numerous in vitro studies have shown that the tyrosine kinase activity of the receptor decreases as a consequence of serine/threonine phosphorylation. This might occur via feedback \"retrophosphorylation\" events in which the receptor or IRS proteins are serine phosphorylated by GSK3 or mTOR, both of which are activated downstream of IRS phosphorylation." provenance.
- _5 value "The insulin receptor and some of its substrates are also subject to serine/threonine phosphorylation. Data from some experimental models suggest that this might represent a mechanism by which signaling is terminated, or perhaps attenuated in states of insulin resistance. Numerous in vitro studies have shown that the tyrosine kinase activity of the receptor decreases as a consequence of serine/threonine phosphorylation. This might occur via feedback \"retrophosphorylation\" events in which the receptor or IRS proteins are serine phosphorylated by GSK3 or mTOR, both of which are activated downstream of IRS phosphorylation." provenance.