Cargando…
En route to photoaffinity labeling of the bacterial lectin FimH
Mannose-specific adhesion of Escherichia coli bacteria to cell surfaces, the cause of various infections, is mediated by a fimbrial lectin, called FimH. X-ray studies have revealed a carbohydrate recognition domain (CRD) on FimH that can complex α-D-mannosides. However, as the precise nature of the...
Autores principales: | Lindhorst, Thisbe K, Märten, Michaela, Fuchs, Andreas, Knight, Stefan D |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
Beilstein-Institut
2010
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2956469/ https://www.ncbi.nlm.nih.gov/pubmed/20978617 http://dx.doi.org/10.3762/bjoc.6.91 |
Ejemplares similares
-
Diazirine-functionalized mannosides for photoaffinity labeling: trouble with FimH
por: Beiroth, Femke, et al.
Publicado: (2018) -
Synthesis and testing of the first azobenzene mannobioside as photoswitchable ligand for the bacterial lectin FimH
por: Chandrasekaran, Vijayanand, et al.
Publicado: (2013) -
Are D-manno-configured Amadori products ligands of the bacterial lectin FimH?
por: Gloe, Tobias-Elias, et al.
Publicado: (2015) -
A bivalent glycopeptide to target two putative carbohydrate binding sites on FimH
por: Lindhorst, Thisbe K, et al.
Publicado: (2010) -
Catch-bond mechanism of the bacterial adhesin FimH
por: Sauer, Maximilian M., et al.
Publicado: (2016)