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We therefore hypothesized that a proteomic biomarker panel consisting of multiple serum proteins assessed simultaneously would enhance the diagnostic accuracy for VTE compared to D-dimer.
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Highly specific and sensitive assays for serum-based protein biomarkers of lung cancer progression based on selective reaction monitoring (SRM) mass spectrometry are entering the clinic [ 33] and chip-based ELISA platforms have been described that can simultaneously measure multiple serum protein biomarkers from tiny samples of peripheral blood [ 34].
We developed a model incorporating physiologic concentrations of multiple VEGF-binding serum proteins, sFlt-1, sKDR, and α2-M.
Our competition model suggested that competitive interactions between multiple VEGF-binding serum proteins (sFlt-1, sKDR, and α2-M) could increase VEGF release rates.
Modeling results suggest a potential mechanism whereby competition between VEGF and multiple VEGF-binding serum proteins including sFlt-1, soluble kinase insert domain receptor (sKDR), and α2-macroglobulin (α2-M) likely influenced VEGF release from microspheres.
The plasma sample was depleted of top six abundant serum proteins using a multiple-affinity MARS column (Agilent Technologies, Palo Alto, CA, USA) [ 12], and precipitated with trichloroacetic acid.
Multiple logistic regression analysis was used to examine the inter-relationships between serum proteins, biliary obstruction, patient age and cancer likelihood.
Secondary antibodies were designed for multiple labelling with minimal cross-reactivity with human, bovine, horse, rabbit/mouse and swine serum proteins.
Serum proteins adsorbed on CNPs attenuated the inherent cytotoxicity of CNPs, and the extent of toxicity attenuation increased with increasing amounts of serum proteins adsorbed on CNPs.
Protein adsorption assay shows that the a-C film can covalently bind more serum proteins than a-C H film.
The possible reasons responsible for the considerable influence of serum proteins on cytotoxicity were indicated.
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