ArticleJournal of enzyme inhibition and medicinal chemistry2017
Allosteric inhibition of carnosinase (CN1) by inducing a conformational shift.
Article in Journal of enzyme inhibition and medicinal chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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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
10 citing papers in PubMed, 25 citations in OpenAlex.
- Carnosine Dipeptidase(Cndp): An emerging therapeutic target for metabolic diseases and cancers.Genes & diseases · 2026Review
- Serum carnosinase 1, an early indicator for incident microalbuminuria in type 1 diabetes.Journal of diabetes and metabolic disorders · 2024Article
- State of the Art in the Development of Human Serum Carnosinase Inhibitors.Molecules (Basel, Switzerland) · 2024Review
- The Therapeutic Potential of Novel Carnosine Formulations: Perspectives for Drug Development.Pharmaceuticals (Basel, Switzerland) · 2023Review
- Anserine and Carnosine Induce HSP70-Dependent HAntioxidants (Basel, Switzerland) · 2022Article
- Longitudinal proteomics study of serum changes after allogeneic HSCT reveals potential markers of metabolic complications related to aGvHD.Scientific reports · 2022Article
- Natural and Synthetic Agents Targeting Reactive Carbonyl Species against Metabolic Syndrome.Molecules (Basel, Switzerland) · 2022Review
- Dexamethasone-Induced Perturbations in Tissue Metabolomics Revealed by Chemical Isotope Labeling LC-MS analysis.Metabolites · 2020Article
- Therapeutic potential of carbonyl-scavenging carnosine derivative in metabolic disorders.The Journal of clinical investigation · 2018Article
- Carnosinase, diabetes mellitus and the potential relevance of carnosinase deficiency.Journal of inherited metabolic disease · 2018Review
Corrections and comments
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Authors and funding
13 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In humans, low serum carnosinase (CN1) activity protects patients with type 2 diabetes from diabetic nephropathy. We now characterized the interaction of thiol-containing compounds with CN1 cysteine residue at position 102, which is important for CN1 activity. Reduced glutathione (GSH), N-acetylcysteine and cysteine (3.2 ± 0.4, 2.0 ± 0.3, 1.6 ± 0.2 µmol/mg/h/mM; p < .05) lowered dose-dependently recombinant CN1 (rCN1) efficiency (5.2 ± 0.2 µmol/mg/h/mM) and normalized increased CN1 activity renal tissue samples of diabetic mice. Inhibition was allosteric. Substitution of rCN1 cysteine residues at position 102 (Mut1
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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.