Výsledky vyhledávání - "J B, Burritt"

Epitope identification for human neutrophil flavocytochrome b monoclonals 48 and 449

Autor: J B, Burritt, G N, Fritel, I, Dahan, E, Pick, D, Roos, A J, Jesaitis

Publikováno v: European journal of haematology. 65(6)

Flavocytochrome b558 (Cyt b) is important in generating superoxide and other toxic oxygen species involved in inflammation and host defense. Monoclonal antibodies (mAbs) 48 and 449 bind the gp91Phox and p22phox subunits of Cyt b, respectively, and ha

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::d625db6fa62f4f623126698c949edbbe
https://pubmed.ncbi.nlm.nih.gov/11168498

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Phage display epitope mapping of human neutrophil flavocytochrome b558. Identification of two juxtaposed extracellular domains

Autor: J B, Burritt, F R, DeLeo, C L, McDonald, J R, Prigge, M C, Dinauer, M, Nakamura, W M, Nauseef, A J, Jesaitis

Publikováno v: The Journal of biological chemistry. 276(3)

Despite extensive experimental and clinical evidence demonstrating the critical role of flavocytochrome b558 (Cyt b) in the NADPH-dependent oxidase, there is a paucity of direct structural data defining its topology in the phagocyte membrane. Unlike

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::540fa67d2d75f3e9b30f9b4025732b15
https://pubmed.ncbi.nlm.nih.gov/11027685

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Peptide ligands that bind IgM antibodies and block interaction with antigen

Autor: P M, Glee, S H, Pincus, D K, McNamer, M J, Smith, J B, Burritt, J E, Cutler

Publikováno v: Journal of immunology (Baltimore, Md. : 1950). 163(2)

We have selected a peptide-display phage library on IgM Abs and identified a panel of phage-expressing peptides that bind to IgM Abs in general, but not to Abs of other classes. A synthetic peptide corresponding to one of the displayed peptide sequen

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::a5ffab23482419906a277943e18b4ff3
https://pubmed.ncbi.nlm.nih.gov/10395676

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Cell-specific peptide binding by human neutrophils

Autor: L, Mazzucchelli, J B, Burritt, A J, Jesaitis, A, Nusrat, T W, Liang, A T, Gewirtz, F J, Schnell, C A, Parkos

Publikováno v: Blood. 93(5)

Analysis of peptide binding to human neutrophils (PMN) using phage display techniques has revealed cell-specific motifs reactive with the PMN surface. Phage libraries displaying either linear 9-mer or cyclic 10-mer and 6-mer peptides were incubated w

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::6470981cfdfab743ee2d0018e42b9bdf
https://pubmed.ncbi.nlm.nih.gov/10029604

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Antibody imprint of a membrane protein surface. Phagocyte flavocytochrome b

Autor: J B, Burritt, S C, Busse, D, Gizachew, D W, Siemsen, M T, Quinn, C W, Bond, E A, Dratz, A J, Jesaitis

Publikováno v: The Journal of biological chemistry. 273(38)

Structural features of the integral membrane protein flavocytochrome b (Cyt b) were discovered using an antibody "imprint" of the Cyt b surface. Amino acid sequences were selected from a random nonapeptide phage-display library by their affinity for

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::f2eafa6a4d3b7f70acbf2a7499bb3b28
https://pubmed.ncbi.nlm.nih.gov/9733789

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Peptides that mimic the group B streptococcal type III capsular polysaccharide antigen

Autor: S H, Pincus, M J, Smith, H J, Jennings, J B, Burritt, P M, Glee

Publikováno v: Journal of immunology (Baltimore, Md. : 1950). 160(1)

Microbial polysaccharides are notably poor immunogens. We have developed an alternate route for the production of Abs to important carbohydrate epitopes. mAb S9, a protective mAb against the type III capsular polysaccharide of group B streptococci (G

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::a5f958dfc10beeefb47f251c272050f5
https://pubmed.ncbi.nlm.nih.gov/9551983

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