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Matches in SemOpenAlex for { <https://semopenalex.org/work/W1979650146> ?p ?o ?g. }

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• W1979650146 startingPage "1853" @default.
• W1979650146 abstract "The cell adhesion molecule, N-cadherin plays a pivotal role in many biological and disease processes. Drugs that modulate N-cadherin function should therefore be useful therapeutic agents. We have used phage display technology to identify amino acid sequences capable of binding to N-cadherin. All of these sequences harbor a Trp residue in the second position from the N-terminus. A synthetic linear peptide containing one of these sequences, H-SWTLYTPSGQSK-NH2 was found to bind a chimeric protein composed of the N-cadherin ectodomain fused to the immunoglobulin G1 Fc fragment with an affinity (KD) of 10.7 μM, as determined by surface plasmon resonance. It also blocked the aggregation of beads coated with this chimeric protein. Furthermore, this peptide disrupted adhesion and tube formation by N-cadherin-expressing human umbilical vein endothelial cells in vitro. These observations suggest that N-cadherin antagonists have the potential of serving as anti-angiogenic agents. The peptide, H-SWTLYTPSGQSK-NH2 should prove useful for studies designed to evaluate N-cadherin function in various biological processes." @default.
• W1979650146 created "2016-06-24" @default.
• W1979650146 creator A5007582883 @default.
• W1979650146 creator A5031354093 @default.
• W1979650146 date "2008-11-01" @default.
• W1979650146 modified "2023-09-26" @default.
• W1979650146 title "Identification of a novel N-cadherin antagonist" @default.
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• W1979650146 doi "https://doi.org/10.1016/j.peptides.2008.06.025" @default.
• W1979650146 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/18655820" @default.
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