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Our approach involves coating of synthetic scaffolds with tailor-made, cyclic RGD-peptides, which bind to specific integrin receptors on the cell surface.
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Arginine-glycine-aspartic (RGD) containing peptides that bind to specific integrins have been widely utilized to provide ligand-mediated targeting capabilities to small molecules, peptides, proteins, and antibodies, as well as to drug/imaging agent-containing nanomedicines, with the final aim of maximizing their therapeutic index.
Targeting tumor angiogenesis for drug delivery has been identified as a promising approach for three main reasons: (i) angiogenesis is a common and genetically stable characteristic of most solid tumors; (ii) the tumor vasculature is readily accessible from the bloodstream; (iii) neovasculature can be targeted by RGD-containing peptides that bind to specific integrins.
Integrins bind to specific components of the extracellular matrix (ECM) or to respective cellular counter-receptors (Hynes, 2002).
The use of synthetic peptide toolkits to probe for receptor-binding specificity indicates that the DDRs bind to specific amino acid consensus sequences on fibrillar collagen that are distinct from integrin-binding motifs [ 10– 10].
Cells bind to specific amino acid sequences of these molecules through membrane receptors (e.g., integrins).
Binding of specific integrin adhesion receptors to this protein modulates the activity of focal adhesion kinase (FAK) and the intracellular signaling cascades of osteoblast- and myoblast-like cells [ 13, 14].
Cells bind to the ECM via specific integrin receptors and this binding can directly affect cell function.
The specific alpha or beta chains that constitute the integrin receptor determine the repertoire of ECM proteins to which a specific integrin may bind.
It is known that endothelial cells bind to platelets through integrin αvβ3 and CD40 [31].
Fmp has been shown to efficiently bind to integrin β1 in several studies.
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