| pubmed-article:8797855 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8797855 | lifeskim:mentions | umls-concept:C0206679 | lld:lifeskim |
| pubmed-article:8797855 | lifeskim:mentions | umls-concept:C2608085 | lld:lifeskim |
| pubmed-article:8797855 | lifeskim:mentions | umls-concept:C1824884 | lld:lifeskim |
| pubmed-article:8797855 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:8797855 | lifeskim:mentions | umls-concept:C1883254 | lld:lifeskim |
| pubmed-article:8797855 | lifeskim:mentions | umls-concept:C0597731 | lld:lifeskim |
| pubmed-article:8797855 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:8797855 | lifeskim:mentions | umls-concept:C0243071 | lld:lifeskim |
| pubmed-article:8797855 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:8797855 | pubmed:dateCreated | 1996-11-4 | lld:pubmed |
| pubmed-article:8797855 | pubmed:abstractText | The interaction between mAb A16 and glycoprotein D (gD) of herpes simplex virus type 1 was analyzed by studying the kinetics of binding with a surface-plasmon-resonance biosensor. mAb A16 belongs to group VII antibodies, which recognize residues 11-19 of gD. In a previous study, three critical residues, Asp13, Arg16 and Phe17, of this epitope were identified by screening a phage display library that contained a random 15-amino-acid insert with the antibody. The contribution to binding of these residues in the motif DXXRF was further analyzed by an amino-acid-replacement study of the epitope gD-(9-19)-peptide and of a gD-(9-19)-peptide mimotope, previously obtained by screening the phage display library. Amino acid residues of the motif were replaced by a neutral amino acid residue, an amino acid residue with opposite charge and a corresponding D-amino acid residue. Kinetic parameters of peptide analogues were determined with a surface plasmon-resonance biosensor. The kinetic parameters of the peptide analogues were compared with the kinetic parameters of the interaction between mAb A16 and the epitope gD-(9-19)-peptide. The minimal size of the gD epitope for mAb A16 was also determined in this study. The kinetic constants of the resulting gD-(11-17)-peptide were found to be similar to those of entire gD. The kinetic analysis precisely defined the epitope on gD for mAb A16 to residues 11-17, identified Arg16 as an essential residue and suggested that Asp13 and Phe17 are mainly involved in stabilization of the secondary structure of the peptide. | lld:pubmed |
| pubmed-article:8797855 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8797855 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8797855 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8797855 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8797855 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8797855 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8797855 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:8797855 | pubmed:issn | 0014-2956 | lld:pubmed |
| pubmed-article:8797855 | pubmed:author | pubmed-author:WellingG WGW | lld:pubmed |
| pubmed-article:8797855 | pubmed:author | pubmed-author:SchefferA JAJ | lld:pubmed |
| pubmed-article:8797855 | pubmed:author | pubmed-author:Welling-Weste... | lld:pubmed |
| pubmed-article:8797855 | pubmed:author | pubmed-author:FeijlbriefMM | lld:pubmed |
| pubmed-article:8797855 | pubmed:author | pubmed-author:SchellekensG... | lld:pubmed |
| pubmed-article:8797855 | pubmed:author | pubmed-author:DamhofR ARA | lld:pubmed |
| pubmed-article:8797855 | pubmed:author | pubmed-author:KoedijkD GDG | lld:pubmed |
| pubmed-article:8797855 | pubmed:author | pubmed-author:LasonderEE | lld:pubmed |
| pubmed-article:8797855 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8797855 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:8797855 | pubmed:volume | 240 | lld:pubmed |
| pubmed-article:8797855 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8797855 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8797855 | pubmed:pagination | 209-14 | lld:pubmed |
| pubmed-article:8797855 | pubmed:dateRevised | 2007-7-23 | lld:pubmed |
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| pubmed-article:8797855 | pubmed:meshHeading | pubmed-meshheading:8797855-... | lld:pubmed |
| pubmed-article:8797855 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8797855 | pubmed:articleTitle | Kinetic analysis of synthetic analogues of linear-epitope peptides of glycoprotein D of herpes simplex virus type 1 by surface plasmon resonance. | lld:pubmed |
| pubmed-article:8797855 | pubmed:affiliation | Department of Medical Microbiology, University of Groningen, The Netherlands. | lld:pubmed |
| pubmed-article:8797855 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8797855 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:8797855 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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