ArticleFrontiers in immunology2024
Exopeptidase combination enhances the degradation of isotopically labelled gluten immunogenic peptides in humans.
Article in Frontiers in immunology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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2 citing papers in PubMed.
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9 authors.
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Abstract
Introduction: Celiac disease is a common autoimmune-like enteropathy caused by an aberrant response to incompletely digested dietary gluten. Gluten immunogenic peptides including the immunodominant 33-mer are thought to be resistant to proteolytic digestion by human gastrointestinal peptidases. We developed a novel enzyme therapy approach to support gluten peptide digestion using a combination of two tandem-acting exopeptidases, AMYNOPEP, that complement the intrinsic enzymatic activity of intestinal brush border enterocytes. Methods: We evaluated the effects of AMYNOPEP supplementation on 33-mer degradation Results: AMYNOPEP achieved rapid, complete amino-to-carboxyl terminal degradation of the 33-mer Conclusions: AMYNOPEP achieved complete degradation of the 33-mer into single amino acids and dipeptides
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