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The insulin conjugated to the NG (NG-In) is protected by protease degradation and able to bind to insulin receptor (IR), as demonstrated by immunofluorescence measurements showing colocalization of NG-InFITC with IR.
They bind to insulin receptors, attack the stomach lining of insects, bind to human intestinal lining, and they seemingly cause leptin resistance.
Adult worms of S. japonicum possess insulin receptors that can specifically bind to insulin, indicating that the parasite can utilize host insulin for development and growth by sharing the same pathway as mammalian cells in regulating glucose uptake.
Overall, our findings demonstrate that S. japonicum possesses insulin receptors that can specifically bind to insulin, indicating that the parasite can utilize host insulin for development and growth by sharing the same pathway as mammalian cells for the control of cell differentiation and proliferation.
Alternatively, HS might bind to insulin and sequester the inhibitor, or both effects could play a role.
SH2B1β is reported to bind to insulin receptor substrate (IRS) proteins and promote their tyrosyl phosphorylation in response to insulin and leptin (11, 12).
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A synthetic peptide corresponding to the serine phosphorylation domain of insulin-like growth factor-binding protein-3 (that does not bind to insulin-like growth factors) also mimicked these differential actions.
IGFBPs are reported to bind to insulin-like growth factors (IGFs), which prevents binding between IGFs and their cognate receptors, thereby inhibiting the activities of IGFs [ 9, 12, 58- 61].
These proteins bind to insulin-like growth factors (IGFs) I and II and are found in the plasma in the form of glycosylated and non-glycosylated forms [ 45- 48].
More than 95% of IGF-2 in the circulation is bound to insulin like growth factor binding proteins (IGFBP) that have high affinity for both IGF-1 and IGF-2 [ 11].
When blood-glucose levels are high, the sugar binds to insulin and activates it, allowing the insulin to stimulate cells to absorb the excess sugar.
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