ArticleJournal of the American Chemical Society2015
Engineering of Kuma030: A Gliadin Peptidase That Rapidly Degrades Immunogenic Gliadin Peptides in Gastric Conditions.
Article in Journal of the American Chemical Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
48 citing papers in PubMed, 117 citations in OpenAlex.
- Evaluating Responses to Gluten Challenge: A Randomized, Double-Blind, 2-Dose Gluten Challenge Trial.Gastroenterology · 2021Trial
- Latiglutenase Improves Symptoms in Seropositive Celiac Disease Patients While on a Gluten-Free Diet.Digestive diseases and sciences · 2017Trial
- Proteases in intestinal health and disease.Nature reviews. Gastroenterology & hepatology · 2026Review
- Gluten Proteins: Beneficial Factors and Toxic Triggers in Human Health.Foods (Basel, Switzerland) · 2025Review
- Is There a Future Without Gluten Restrictions for Celiac Patients? Update on Current Treatments.Nutrients · 2025Review
- Computational Screening and Experimental Evaluation of Wheat Proteases for Use in the Enzymatic Therapy of Gluten-Related Disorders.Pharmaceuticals (Basel, Switzerland) · 2025Article
- New Therapeutic Challenges in Pediatric Gastroenterology: A Narrative Review.Healthcare (Basel, Switzerland) · 2025Review
- Review Article: Novel Enzyme Therapy Design for Gluten Peptide Digestion Through Exopeptidase Supplementation.Alimentary pharmacology & therapeutics · 2025Review
- Celiac Disease-Narrative Review on Progress in Celiac Disease.Foods (Basel, Switzerland) · 2025Review
- Advances in understanding and managing celiac disease: Pathophysiology and treatment strategies.World journal of gastroenterology · 2024Article
- Emerging Chemical, Biochemical, and Non-Thermal Physical Treatments in the Production of Hypoallergenic Plant Protein Ingredients.Foods (Basel, Switzerland) · 2024Review
- New Insights on Genes, Gluten, and Immunopathogenesis of Celiac Disease.Gastroenterology · 2024Review
- Specificity Enhancement of Glutenase Bga1903 toward Celiac Disease-Eliciting Pro-Immunogenic Peptides via Active-Site Modification.International journal of molecular sciences · 2023Article
- Article
- Celiac disease: mechanisms and emerging therapeutics.Trends in pharmacological sciences · 2023Review
- Bromelain-loaded nanocomposites decrease inflammatory and cytotoxicity effects of gliadin on Caco-2 cells and peripheral blood mononuclear cells of celiac patients.Scientific reports · 2023Article
- Fighting Celiac Disease: Improvement of pH Stability of Cathepsin L In Vitro by Computational Design.International journal of molecular sciences · 2023Article
- Data-driven enzyme engineering to identify function-enhancing enzymes.Protein engineering, design & selection : PEDS · 2023Review
- New Developments in Celiac Disease Treatment.International journal of molecular sciences · 2023Review
- A Comprehensive Review of the Neurological Manifestations of Celiac Disease and Its Treatment.Diseases (Basel, Switzerland) · 2022Review
Corrections and comments
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Authors and funding
10 authors at 6 institutions in 2 countries.
Funding
Abstract
Celiac disease is characterized by intestinal inflammation triggered by gliadin, a component of dietary gluten. Oral administration of proteases that can rapidly degrade gliadin in the gastric compartment has been proposed as a treatment for celiac disease; however, no protease has been shown to specifically reduce the immunogenic gliadin content, in gastric conditions, to below the threshold shown to be toxic for celiac patients. Here, we used the Rosetta Molecular Modeling Suite to redesign the active site of the acid-active gliadin endopeptidase KumaMax. The resulting protease, Kuma030, specifically recognizes tripeptide sequences that are found throughout the immunogenic regions of gliadin, as well as in homologous proteins in barley and rye. Indeed, treatment of gliadin with Kuma030 eliminates the ability of gliadin to stimulate a T cell response. Kuma030 is capable of degrading >99% of the immunogenic gliadin fraction in laboratory-simulated gastric digestions within physiologically relevant time frames, to a level below the toxic threshold for celiac patients, suggesting great potential for this enzyme as an oral therapeutic for celiac disease.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.