ReviewInternational journal of molecular sciences2020
Regulation of the Proteolytic Activity of Cysteine Cathepsins by Oxidants.
Review in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 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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Who cites it
23 citing papers in PubMed, 37 citations in OpenAlex.
- Ageing alters cysteine oxidation-regulated redox signalling in skeletal muscle: Integrative omics and AI-based structural predictions.Experimental physiology · 2026Article
- Cathepsin L as a Driver of Tumour Invasion and a Novel Therapeutic Target in Ovarian Cancer.Cancers · 2026Review
- Therapeutic Potential of Cysteine and Its Derivatives in Dermatology.Molecules (Basel, Switzerland) · 2026Review
- Metabolic dysfunction-associated steatohepatitis reduces hepatic HRedox biology · 2025Article
- Chemical structure drives developmental toxicity of alkyl-substituted naphthalenes in zebrafish.Environment international · 2025Article
- The Capacities of the Probiotic StrainsBiomolecules · 2025Article
- Causal association between cathepsins and asthma: a Mendelian randomization study.Scientific reports · 2025Article
- Association between serum cystatin C and chronic lung disease in middle-aged and elderly Chinese: a CHARLS cross-sectional study.Scientific reports · 2025Article
- Gold Nanoparticles as a Platform for Delivery of Immunogenic Peptides to THP-1 Derived Macrophages: Insights into Nanotoxicity.Vaccines · 2025Article
- A quantitative proteomic approach to evaluate the efficacy of carnosine in a murine model of chronic obstructive pulmonary disease (COPD).Redox biology · 2024Article
- Analysis of Differential Gene Expression under Acute Lead or Mercury Exposure in Larval Zebrafish Using RNA-Seq.Animals : an open access journal from MDPI · 2024Article
- Neutrophil-Derived Proteases in Lung Inflammation: Old Players and New Prospects.International journal of molecular sciences · 2024Review
- The Intricate Balance between Life and Death: ROS, Cathepsins, and Their Interplay in Cell Death and Autophagy.International journal of molecular sciences · 2024Review
- Unveiling Cathepsin B inhibition with repurposed drugs for anticancer and anti-Alzheimer's drug discovery.PloS one · 2024Article
- The Role of Cysteine Protease Cathepsins B, H, C, and X/Z in Neurodegenerative Diseases and Cancer.International journal of molecular sciences · 2023Review
- Isolation of Nocuolin A and Synthesis of New Oxadiazine Derivatives. Design, Synthesis, Molecular Docking, Apoptotic Evaluation, and Cathepsin B Inhibition.Marine drugs · 2023Article
- Cleavage of Occludin by Cigarette Smoke-Elicited Cathepsin S Increases Permeability of Lung Epithelial Cells.Antioxidants (Basel, Switzerland) · 2022Article
- Insights into the Mechanisms ofAntioxidants (Basel, Switzerland) · 2022Article
- Intracellular Protein S-Nitrosylation-A Cells Response to Extracellular S100B and RAGE Receptor.Biomolecules · 2022Article
- Can thiol-based redox systems be utilized as parts for synthetic biology applications?Redox report : communications in free radical research · 2021Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Besides their primary involvement in the recycling and degradation of proteins in endo-lysosomal compartments and also in specialized biological functions, cysteine cathepsins are pivotal proteolytic contributors of various deleterious diseases. While the molecular mechanisms of regulation via their natural inhibitors have been exhaustively studied, less is currently known about how their enzymatic activity is modulated during the redox imbalance associated with oxidative stress and their exposure resistance to oxidants. More specifically, there is only patchy information on the regulation of lung cysteine cathepsins, while the respiratory system is directly exposed to countless exogenous oxidants contained in dust, tobacco, combustion fumes, and industrial or domestic particles. Papain-like enzymes (clan CA, family C1, subfamily C1A) encompass a conserved catalytic thiolate-imidazolium pair (Cys25-His159) in their active site. Although the sulfhydryl group (with a low acidic pKa) is a potent nucleophile highly susceptible to chemical modifications, some cysteine cathepsins reveal an unanticipated resistance to oxidative stress. Besides an introductory chapter and peculiar attention to lung cysteine cathepsins, the purpose of this review is to afford a concise update of the current knowledge on molecular mechanisms associated with the regulation of cysteine cathepsins by redox balance and by oxidants (e.g., Michael acceptors, reactive oxygen, and nitrogen species).
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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.