The abstract presents PRMTs as enzymes mediating protein arginine methylation and regulating tumor angiogenesis pathways including VEGFR-2 signaling.
First-pass extracted concept
protein arginine methyltransferases
Candidate: concept label1 source documents5 linked claims
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PRMTs
Extracted Explainers
What the tool is doing
What problem it solves
Evidence Snippets
Supporting Sources
Linked Claims
Inhibiting PRMT5 suppresses VEGF-induced vessel sprouting and impairs HIF-1α stability and VEGFR-2 phosphorylation in experimental models.
Quoted textsource-backed
For example, inhibiting PRMT5 suppresses VEGF-induced vessel sprouting in experimental models while impairing hypoxia-inducible factor 1-alpha (HIF-1α) stability and VEGFR-2 phosphorylation.
PRMT1 and PRMT4 influence VEGF isoform expression, leading to increased angiogenesis.
Quoted textsource-backed
PRMT1 and PRMT4 similarly influence VEGF isoform expression, leading to increased angiogenesis.
PRMT1, PRMT4, and PRMT5 activate distinct stages of angiogenesis.
Quoted textsource-backed
PRMT1, PRMT4, and PRMT5 activate distinct stages of angiogenesis.
PRMTs regulate tumor angiogenesis pathways including VEGFR-2 signaling.
Quoted textsource-backed
PRMTs regulate various tumor angiogenesis pathways, including vascular endothelial growth factor receptor-2 (VEGFR-2) signaling.
Targeting PRMTs in experimental models suppresses angiogenesis and reduces cancer progression.
Quoted textsource-backed
Targeting PRMTs in experimental models results in suppressed angiogenesis and reduced cancer progression.