| pubmed-article:18316741 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18316741 | lifeskim:mentions | umls-concept:C0019682 | lld:lifeskim |
| pubmed-article:18316741 | lifeskim:mentions | umls-concept:C0019699 | lld:lifeskim |
| pubmed-article:18316741 | lifeskim:mentions | umls-concept:C0042232 | lld:lifeskim |
| pubmed-article:18316741 | lifeskim:mentions | umls-concept:C1522570 | lld:lifeskim |
| pubmed-article:18316741 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:18316741 | lifeskim:mentions | umls-concept:C1521797 | lld:lifeskim |
| pubmed-article:18316741 | lifeskim:mentions | umls-concept:C1136254 | lld:lifeskim |
| pubmed-article:18316741 | lifeskim:mentions | umls-concept:C0033268 | lld:lifeskim |
| pubmed-article:18316741 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:18316741 | pubmed:dateCreated | 2008-3-12 | lld:pubmed |
| pubmed-article:18316741 | pubmed:abstractText | A series of small-molecule microbicides has been developed for vaginal delivery to prevent heterosexual HIV transmission, but results from human clinical trials have been disappointing. Protein-based microbicides, such as HIV-specific monoclonal antibodies, have been considered as an alternative approach. Despite their promising safety profile and efficacy, the major drawback of such molecules is the economy of large-scale production in mammalian cells, the current system of choice. Here, we show that an alternative biomanufacturing platform is now available for one of the most promising anti-HIV antibodies (2G12). Our data show that the HIV-neutralization capability of the antibody is equal to or superior to that of the same antibody produced in CHO cells. We conclude that this protein production system may provide a means to achieve microbicide ingredient manufacture at costs that would allow product introduction and manufacture in the developing world. | lld:pubmed |
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| pubmed-article:18316741 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18316741 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18316741 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18316741 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:18316741 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18316741 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:18316741 | pubmed:issn | 1091-6490 | lld:pubmed |
| pubmed-article:18316741 | pubmed:author | pubmed-author:SackMarkusM | lld:pubmed |
| pubmed-article:18316741 | pubmed:author | pubmed-author:StieglerGabri... | lld:pubmed |
| pubmed-article:18316741 | pubmed:author | pubmed-author:ChristouPaulP | lld:pubmed |
| pubmed-article:18316741 | pubmed:author | pubmed-author:CapellTeresaT | lld:pubmed |
| pubmed-article:18316741 | pubmed:author | pubmed-author:StögerEvaE | lld:pubmed |
| pubmed-article:18316741 | pubmed:author | pubmed-author:RademacherTho... | lld:pubmed |
| pubmed-article:18316741 | pubmed:author | pubmed-author:AltmannFritzF | lld:pubmed |
| pubmed-article:18316741 | pubmed:author | pubmed-author:PlatisDimitri... | lld:pubmed |
| pubmed-article:18316741 | pubmed:author | pubmed-author:MaJulianJ | lld:pubmed |
| pubmed-article:18316741 | pubmed:author | pubmed-author:StadlmannJoha... | lld:pubmed |
| pubmed-article:18316741 | pubmed:author | pubmed-author:RamessarKoree... | lld:pubmed |
| pubmed-article:18316741 | pubmed:author | pubmed-author:LabrouNikosN | lld:pubmed |
| pubmed-article:18316741 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18316741 | pubmed:day | 11 | lld:pubmed |
| pubmed-article:18316741 | pubmed:volume | 105 | lld:pubmed |
| pubmed-article:18316741 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18316741 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18316741 | pubmed:pagination | 3727-32 | lld:pubmed |
| pubmed-article:18316741 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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