ReviewInternational journal of molecular sciences2021
Mechanisms Applied by Protein Inhibitors to Inhibit Cysteine Proteases.
Review in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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.
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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
19 citing papers in PubMed.
- Article
- The design and synthesis of cysteine protease inhibitors containing isoxazole bearing warheads against Leishmania donovani.Naunyn-Schmiedeberg's archives of pharmacology · 2026Article
- Extracellular matrix and proteolysis: mechanisms driving irreversible changes and shaping cell behavior.The FEBS journal · 2026Review
- Integrated biochemical, histological, and transcriptomic analyses reveal dose-dependent effects of sodium alginate on the physiology of Meretrix meretrix.Scientific reports · 2026Article
- Structure-Based Insights into Stefin-Mediated Targeting of Fowlerpain-1: Towards Novel Therapeutics forPharmaceuticals (Basel, Switzerland) · 2025Article
- Evaluating the Cytotoxic Potential of 3-(2-(3,4 dimethoxyphenyl)-2-oxoethylidene) indolin-2-one) (RAJI) on Triple Negative Breast Cancer Cells.Asian Pacific journal of cancer prevention : APJCP · 2025Article
- Complete stranded RNA profiling during early mouse gonad development.NAR molecular medicine · 2025Article
- Emerging trends in the cystatin C sensing technologies: towards better chronic kidney disease management.RSC advances · 2025Review
- Trichocystatin-2 fromFrontiers in parasitology · 2025Article
- Cystatin from Austrelaps superbus snake venom as a model for identifying potential inhibitors of Trypanosoma cruzi cruzain.The journal of venomous animals and toxins including tropical diseases · 2025Article
- Recovery of Proteases and Protease Inhibitors fromCurrent protein & peptide science · 2025Article
- Coordination chemistry suggests that independently observed benefits of metformin and ZnBiometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2024Article
- Is cholesterol both the lock and key to abnormal transmembrane signals in Autism Spectrum Disorder?Lipids in health and disease · 2024Article
- The Power of Molecular Dynamics Simulations and Their Applications to Discover Cysteine Protease Inhibitors.Mini reviews in medicinal chemistry · 2024Review
- The Role of Cysteine Protease Cathepsins B, H, C, and X/Z in Neurodegenerative Diseases and Cancer.International journal of molecular sciences · 2023Review
- Proteomic data and structure analysis combined reveal interplay of structural rigidity and flexibility on selectivity of cysteine cathepsins.Communications biology · 2023Article
- Proteases and Their Potential Role as Biomarkers and Drug Targets in Dry Eye Disease and Ocular Surface Dysfunction.International journal of molecular sciences · 2022Review
- A Review: Natural and Synthetic Compounds TargetingMembranes · 2022Review
- Review
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Protein inhibitors of proteases are an important tool of nature to regulate and control proteolysis in living organisms under physiological and pathological conditions. In this review, we analyzed the mechanisms of inhibition of cysteine proteases on the basis of structural information and compiled kinetic data. The gathered structural data indicate that the protein fold is not a major obstacle for the evolution of a protease inhibitor. It appears that nature can convert almost any starting fold into an inhibitor of a protease. In addition, there appears to be no general rule governing the inhibitory mechanism. The structural data make it clear that the "lock and key" mechanism is a historical concept with limited validity. However, the analysis suggests that the shape of the active site cleft of proteases imposes some restraints. When the S1 binding site is shaped as a pocket buried in the structure of protease, inhibitors can apply substrate-like binding mechanisms. In contrast, when the S1 binding site is in part exposed to solvent, the substrate-like inhibition cannot be employed. It appears that all proteases, with the exception of papain-like proteases, belong to the first group of proteases. Finally, we show a number of examples and provide hints on how to engineer protein inhibitors.
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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.