% IMPORTANT: The following is UTF-8 encoded. This means that in the presence % of non-ASCII characters, it will not work with BibTeX 0.99 or older. % Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or % “biber”. @ARTICLE{StencelBaerenwald:202141, author = {Stencel-Baerenwald, Jennifer E and Reiss, Kerstin and Reiter, Dirk M and Stehle, Thilo and Dermody, Terence S}, title = {{T}he sweet spot: defining virus-sialic acid interactions}, journal = {Nature reviews / Microbiology}, volume = {12}, number = {11}, issn = {1740-1534}, address = {Basingstoke}, publisher = {Nature Publ. Group}, reportid = {FZJ-2015-04430}, pages = {739 - 749}, year = {2014}, abstract = {Viral infections are initiated by attachment of the virus to host cell surface receptors, including sialic acid-containing glycans. It is now possible to rapidly identify specific glycan receptors using glycan array screening, to define atomic-level structures of virus-glycan complexes and to alter the glycan-binding site to determine the function of glycan engagement in viral disease. This Review highlights general principles of virus-glycan interactions and provides specific examples of sialic acid binding by viruses with stalk-like attachment proteins, including influenza virus, reovirus, adenovirus and rotavirus. Understanding virus-glycan interactions is essential to combating viral infections and designing improved viral vectors for therapeutic applications.}, keywords = {Polysaccharides (NLM Chemicals) / Receptors, Cell Surface (NLM Chemicals) / Receptors, Virus (NLM Chemicals) / N-Acetylneuraminic Acid (NLM Chemicals)}, cin = {ICS-6}, ddc = {570}, cid = {I:(DE-Juel1)ICS-6-20110106}, pnm = {452 - Structural Biology (POF2-452)}, pid = {G:(DE-HGF)POF2-452}, typ = {PUB:(DE-HGF)16 / PUB:(DE-HGF)36}, pubmed = {pmid:25263223}, UT = {WOS:000343916900008}, doi = {10.1038/nrmicro3346}, url = {https://juser.fz-juelich.de/record/202141}, }