Publications by authors named "Brunie H Felding"

Article Synopsis
  • VEGF-A is a crucial factor in cancer growth through angiogenesis, and its primary isoform, VEGF165, is a significant target for cancer therapies due to its effectiveness in stimulating blood vessel formation.
  • The heparin-binding domain (HBD) of VEGF165 is essential for its mitogenic activity, as its removal greatly reduces the factor's ability to promote cell division and growth.
  • Research indicates that the binding sites of the HBD for integrin αvβ3 and the KDR receptor overlap, suggesting that competition between these binding sites can influence VEGF165 signaling and its role in cancer growth.
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VEGF-A is a key cytokine in tumor angiogenesis and a major therapeutic target for cancer. VEGF165 is the predominant isoform and is the most potent angiogenesis stimulant. VEGFR2/KDR domains 2 and 3 (D2D3) bind to the N-terminal domain (NTD, residues 1-110) of VEGF165.

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CD40L is a member of the TNF superfamily that participates in immune cell activation. It binds to and signals through several integrins, including αvβ3 and α5β1, which bind to the trimeric interface of CD40L. We previously showed that several integrin ligands can bind to the allosteric site (site 2), which is distinct from the classical ligand-binding site (site 1), raising the question of if CD40L activates integrins.

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Employing live cells as therapeutics is a direction of future drug discovery. An easy and robust method to modify the surfaces of cells directly to incorporate novel functionalities is highly desirable. However, genetic methods for cell-surface engineering are laborious and limited by low efficiency for primary cell modification.

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