| pubmed-article:12616627 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12616627 | lifeskim:mentions | umls-concept:C0003451 | lld:lifeskim |
| pubmed-article:12616627 | lifeskim:mentions | umls-concept:C0071583 | lld:lifeskim |
| pubmed-article:12616627 | pubmed:issue | 2-3 | lld:pubmed |
| pubmed-article:12616627 | pubmed:dateCreated | 2003-3-4 | lld:pubmed |
| pubmed-article:12616627 | pubmed:abstractText | Tetraantennary peptides [glycine(n)-NHCH(2)](4)C can form stable noncovalent structures by self-assembly through intermolecular hydrogen bonding. The oligopeptide chains assemble as polyglycine II to yield submicron-sized, flat, one-molecule-thick sheets. Attachment of alpha-N-acetylneuraminic acid (Neu5Acalpha) to the terminal glycine residues gives rise to water-soluble assembled glycopeptides that are able to bind influenza virus multivalently and inhibit adhesion of the virus to cells 10(3)-fold more effectively than a monomeric glycoside of Neu5Acalpha. Another antiviral strategy based on virus-promoted assembly of the glycopeptides was also demonstrated. Consequently, the self-assembly principle offers new perspectives on the design of multivalent antivirals. | lld:pubmed |
| pubmed-article:12616627 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12616627 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12616627 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12616627 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12616627 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12616627 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12616627 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12616627 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12616627 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12616627 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:12616627 | pubmed:issn | 1439-4227 | lld:pubmed |
| pubmed-article:12616627 | pubmed:author | pubmed-author:BovinNicolai... | lld:pubmed |
| pubmed-article:12616627 | pubmed:author | pubmed-author:TuzikovAlexan... | lld:pubmed |
| pubmed-article:12616627 | pubmed:author | pubmed-author:ChinarevAlexa... | lld:pubmed |
| pubmed-article:12616627 | pubmed:author | pubmed-author:GambaryanAlex... | lld:pubmed |
| pubmed-article:12616627 | pubmed:author | pubmed-author:OleinikovVlad... | lld:pubmed |
| pubmed-article:12616627 | pubmed:author | pubmed-author:KlinovDmitry... | lld:pubmed |
| pubmed-article:12616627 | pubmed:author | pubmed-author:MatskoNadezhd... | lld:pubmed |
| pubmed-article:12616627 | pubmed:author | pubmed-author:KadykovVasily... | lld:pubmed |
| pubmed-article:12616627 | pubmed:author | pubmed-author:ErmishovMikha... | lld:pubmed |
| pubmed-article:12616627 | pubmed:author | pubmed-author:DeminIl'ya... | lld:pubmed |
| pubmed-article:12616627 | pubmed:author | pubmed-author:DeminVictor... | lld:pubmed |
| pubmed-article:12616627 | pubmed:author | pubmed-author:RyePhil DPD | lld:pubmed |
| pubmed-article:12616627 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12616627 | pubmed:day | 3 | lld:pubmed |
| pubmed-article:12616627 | pubmed:volume | 4 | lld:pubmed |
| pubmed-article:12616627 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12616627 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12616627 | pubmed:pagination | 147-54 | lld:pubmed |
| pubmed-article:12616627 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:12616627 | pubmed:meshHeading | pubmed-meshheading:12616627... | lld:pubmed |
| pubmed-article:12616627 | pubmed:meshHeading | pubmed-meshheading:12616627... | lld:pubmed |
| pubmed-article:12616627 | pubmed:meshHeading | pubmed-meshheading:12616627... | lld:pubmed |
| pubmed-article:12616627 | pubmed:meshHeading | pubmed-meshheading:12616627... | lld:pubmed |
| pubmed-article:12616627 | pubmed:meshHeading | pubmed-meshheading:12616627... | lld:pubmed |
| pubmed-article:12616627 | pubmed:meshHeading | pubmed-meshheading:12616627... | lld:pubmed |
| pubmed-article:12616627 | pubmed:meshHeading | pubmed-meshheading:12616627... | lld:pubmed |
| pubmed-article:12616627 | pubmed:meshHeading | pubmed-meshheading:12616627... | lld:pubmed |
| pubmed-article:12616627 | pubmed:meshHeading | pubmed-meshheading:12616627... | lld:pubmed |
| pubmed-article:12616627 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12616627 | pubmed:articleTitle | Polyglycine II nanosheets: supramolecular antivirals? | lld:pubmed |
| pubmed-article:12616627 | pubmed:affiliation | Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, ul. Miklukho-Maklaya 16/10, Moscow V-437, 117997, Russia. | lld:pubmed |
| pubmed-article:12616627 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12616627 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
