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PDGFRβ dependence on NRP-1 walsolsignificantant, so NRP-1 must regulate PDGFRβ-dependent smooth muscle cell migration, proliferation and differentiation during vessel-wall maturation and repair.
To further demonstrate that PDGF ligand stimulation induces NRP-1 to associate with PDGFRs, we examined the cellular distribution of NRP-1 and phosphorylated PDGFRs by immunofluorescence microscopy.
We first evaluated the distribution of NRP-1 and p-PDGFRs during MSC network assembly by determining the immunolocalization of NRP-1 and PDGFRα-Tyr or PDGFRβ-Tyr.
Food and fodder provision remained the same for NRP-1.
Treatment with hVEGF165 did not change the inhibition in NRP-1 silencing MDA-MB-231 cells, but enhanced the aggressiveness of NRP-1 over-expressing MCF-7 cells.
Neuropilin-1 (NRP-1) is a co-receptor of VEGFR165 and molecules interfering with VEGF165 binding to NRP-1 seem to be promising candidates as new angiogenesis modulators.
Moreover, 786-O cells express VEGF and neuropilin-1 (NRP-1) rather than VEGFR-2.
The response of sediment retention was negligible with respect to NRP-1 (+/− 0).
One of these compounds (56) demonstrated inhibition of VEGF-A165 binding to NRP-1 (IC50 = 39 μM) and specificity for NRP-1 over VEGF-R2.
To argue the involvement of NRP-1, MDA-MB-231 breast cancer cells were used, strongly over-expressing NRP-1 receptor.
Nanoplatforms confer photosensitivity to cells and demonstrate a molecular affinity to NRP-1.
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com