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Last Updated: 3 years ago

Possible Interaction: Insulin and Serine

drug:

Insulin

supplement:

Serine

Research Papers that Mention the Interaction

Activation of N-terminal C-Jun kinase is known to be associated with unfolded protein response activation, and has been shown to participate in the inhibition of insulin action by stimulating serine phosphorylation of the insulin receptor substrate 1, an event that attenuates insulin signaling. '
Trends in Endocrinology & Metabolism  •  2007  |  View Paper
Insulin inhibits GSK3 by promoting phosphorylation of a serine residue (Ser-21 in GSK3alpha, Ser-9 in GSK3beta), thereby relieving GSK3 inhibition of glycogen synthesis in muscle.
The Biochemical journal  •  2005  |  View Paper
Incubating adipocytes with insulin decreased the electrophoretic mobility and stimulated the phosphorylation of both Ser and Thr residues in lipin.
Proceedings of the National Academy of Sciences of the United States of America  •  2002  |  View Paper
Serine phosphorylation of insulin receptor substrate-1 (IRS-1) inhibits insulin signal transduction in a variety of cell backgrounds, which might contribute to peripheral insulin resistance.
The Journal of Biological Chemistry  •  2002  |  View Paper
Insulin induced serine phosphorylation of Akt, through the phosphatidylinositol (PI) 3-kinase pathway.
The Journal of Biological Chemistry  •  2001  |  View Paper
Phosphoamino acid analysis of the pp50 demonstrated that insulin increased phosphorylation, mainly of threonine and moderately of serine , whereas pp50 did not contain phosphotyrosine.
Endocrinology  •  1994  |  View Paper
Both insulins decreased the plasma levels of branched-chain amino acids, tyrosine, phenylalanine, methionine, serine and histidine similarly.
Hormone and metabolic research = Hormon- und Stoffwechselforschung = Hormones et metabolisme  •  1984  |  View Paper
We found that treatment of the normal human liver cell LO2 with 1000 nM insulin for 48 h reduced glucose uptake and increased serine phosphorylation of insulin receptor substrate-1, indicating a reduction in insulin receptor signaling.
Molecular and Cellular Endocrinology  •  2020  |  View Paper
Insulin increased PKB Ser⁴⁷³ , PKB Thr³⁰⁸, and GSK-3β Ser⁹ phosphorylation in skeletal muscles; coinfusion of adrenaline did not influence insulin-stimulated PKB and GSK-3 phosphorylation.
Metabolism: clinical and experimental  •  2011  |  View Paper
Initial in vitro stimulation of muscle tissue with insulin resulted in a substantial and selectively decreased Akt-2 expression and insulin-stimulated phosphorylation on the serine residue.
Endocrine practice : official journal of the American College of Endocrinology and the American Association of Clinical Endocrinologists  •  2007  |  View Paper
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