3 research outputs found

    The FLY phage mimics the VTVTNVFLYNRPLN peptide.

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    <p>(a) Binding of FLY phage and fd-tet to immobilized CK18 and to (b) LLC-MK<sub>2</sub> cells. (c) Binding of FLY phage to CK18 in the presence of increasing concentrations of VTVTNVFLYNRPLN synthetic peptide (FLY, black squares) or the alanine mutagenized version VTVTNVFAYNRPLN synthetic peptide (FAY, open triangles). Results are show as percentage of binding relative to FLY phage in the absence of peptides. Shown are standard error of the mean (SEM) of two biological replicates performed in triplicate.</p

    FLY phage binding to organ-derived endothelial cells.

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    <p>Binding of FLY phage to bone marrow, bladder, heart or lung-derived endothelial cells; fd-tet and FAY phage were used as control. Phage binding was normalized to endothelial cell DNA, quantified using ribosomal RNA specific probes. The error bars are standard error of the mean (SEM) of experiments performed in triplicate. Where indicated, * denotes P<0.05.</p

    FLY phage interaction with intermediate filament proteins.

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    <p>Phage binding to immobilized cytokeratin-8 (CK8), -18 (CK18) and -20 (CK20), and to vimentin. The FAY and fd-tet phage were used as control. Shown are SEM of experiments performed in triplicate. Where indicated, * denotes P<0.05.</p
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