Most of the compounds have physiologically active properties, and their biological properties are often attributed to the heteroatoms contained in their molecules, and most of these heteroatoms also appear in cyclic structures. A Journal, Article, Research Support, Non-U.S. Gov’t, ChemMedChem called Selective Targeting of the TPX2 Site of Importin-α Using Fragment-Based Ligand Design, Author is Holvey, Rhian S.; Valkov, Eugene; Neal, David; Stewart, Murray; Abell, Chris, which mentions a compound: 217192-22-8, SMILESS is OCC1=CC=C(C2=CC=NC=C2)C=C1, Molecular C12H11NO, Related Products of 217192-22-8.
Protein-protein interactions are difficult therapeutic targets, and inhibiting pathol. relevant interactions without disrupting other essential ones presents an addnl. challenge. Herein the authors report how this might be achieved for the potential anticancer target, the TPX2-importin-α interaction. Importin-α is a nuclear transport protein that regulates the spindle assembly protein TPX2. It has two binding sites-major and minor-to which partners bind. Most nuclear transport cargoes use the major site, whereas TPX2 binds principally to the minor site. Fragment-based approaches were used to identify small mols. that bind importin-α, and crystallog. studies identified a lead series that was observed to bind specifically to the minor site, representing the first ligands specific for this site. Structure-guided synthesis informed the elaboration of these fragments to explore the source of ligand selectivity between the minor and major sites. These ligands are starting points for the development of inhibitors of this protein-protein interaction.
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Reference:
Quinoxaline – Wikipedia,
Quinoxaline | C8H6N2 | ChemSpider