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The superfamily of integrins includes several transmembrane cell adhesion proteins that bind to extracellular matrix, cell surface and soluble ligands.
We identified 36 genes with a pattern of high expression in xenograft samples that encoded proteins involved in extracellular matrix, cell surface receptors and transcription factors.
Genes that were restored towards wild-type levels were enriched for gene ontology terms associated with the extracellular matrix, cell surface, plasma membrane and integrin-mediated signalling, suggesting that specific cellular pathways respond to the restoration of dystrophin (Supplementary Material, Fig. S9A).
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Matrix metalloproteinases are zinc-dependent endopeptidases, which degrade various extracellular matrix and cell surface proteins.
Matrix metalloproteinases (MMPs) remodel the pericellular environment by regulating the cleavage of extracellular matrix proteins, cell surface components, neurotransmitter receptors, and growth factors.
In contrast, genes expressed in xenograft samples encoded proteins involved in extracellular matrix, cell adhesion, cell surface receptors transcription and translation.
Many of the genes expressed in xenograft samples encoded for proteins involved in extracellular matrix, cell adhesion, cell surface receptors transcription and translation and suggest increased interactions with an in vivo stromal environment, including the development of a 3-dimensional matrix.
Nearly all of these factors bind to heparan sulfate, a glycosaminoglycan present in extracellular matrix and cell surface proteoglycans.
Lpl binds to heparin, suggesting that it might associate with heparan sulfate that is covalently attached to extracellular matrix or cell surface proteoglycans [16], [17].
While heparin sulphate proteoglycans reportedly mediate the interaction of Cyr61 with the matrix and cell surface, the role of other extracellular associated proteins has not been revealed.
Of note, GAGs have been proposed to store as well as activate growth factors in the extracellular matrix and cell surface.
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