ArticleCell chemical biology2016
Bifunctional Probes of Cathepsin Protease Activity and pH Reveal Alterations in Endolysosomal pH during Bacterial Infection.
Article in Cell chemical biology, 2016. 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, 51 citations in OpenAlex.
- Time-resolved simultaneous imaging of mitochondrial reactive oxygen species and lysosomal permeabilization to determine organelle-centred cell death.Redox report : communications in free radical research · 2026Article
- Understanding the Potential of Antibody-Drug Conjugates Functionalized Engineered Exosomes in Hepatocellular Carcinoma Therapy: A Comprehensive Narrative Review.Health science reports · 2026Article
- SARS-CoV-2 enhances lysosomal exocytosis and deacidifies lysosomes to facilitate viral release.mLife · 2026Article
- It's a Trap!-Potential of Cathepsins in NET Formation.International journal of molecular sciences · 2025Review
- The Role of Oxidative Stress in the Antifungal Activity of Two Mollusk Fractions on Resistant Fungal Strains.International journal of molecular sciences · 2025Article
- Novel Peptide-Based Fluorescent Probe for Simultaneous Sensing of Chymotrypsin and Hydrogen Peroxide.ACS omega · 2024Article
- Distinct Cleavage Properties of Cathepsin B Compared to Cysteine Cathepsins Enable the Design and Validation of a Specific Substrate for Cathepsin B over a Broad pH Range.Biochemistry · 2023Article
- Bi-functional particles for real-time phagosome acidification and proteolysis multiplex assay in macrophages.Frontiers in immunology · 2023Article
- Two Tags in One Probe: Combining Fluorescence- and Biotin-based Detection of the Trypanosomal Cysteine Protease Rhodesain.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- Catalytic Antibodies in Bipolar Disorder: Serum IgGs Hydrolyze Myelin Basic Protein.International journal of molecular sciences · 2022Article
- Review
- Real-Time Simultaneous Imaging of Acidification and Proteolysis in Single Phagosomes Using Bifunctional Janus-Particle Probes.Angewandte Chemie (International ed. in English) · 2021Article
- Universal Access to Protease Chemiluminescent Probes through Solid-Phase Synthesis.Bioconjugate chemistry · 2021Article
- Molecular probes for selective detection of cysteine cathepsins.Organic & biomolecular chemistry · 2021Review
- Differential Neuropeptidomes of Dense Core Secretory Vesicles (DCSV) Produced at Intravesicular and Extracellular pH Conditions by Proteolytic Processing.ACS chemical neuroscience · 2021Article
- Identification of highly selective covalent inhibitors by phage display.Nature biotechnology · 2021Article
- Article
- Review
- Cathepsins in Bacteria-Macrophage Interaction: Defenders or Victims of Circumstance?Frontiers in cellular and infection microbiology · 2020Review
- Coxiella burnetii Type 4B Secretion System-dependent manipulation of endolysosomal maturation is required for bacterial growth.PLoS pathogens · 2019Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Cysteine cathepsins are lysosomal proteases involved in regulation of both normal cellular processes and disease. Biochemical studies with peptide substrates indicate that cathepsins have optimal activity at acidic pH and highly attenuated activity at neutral pH. In contrast, there is mounting evidence that cathepsins have biological roles in environments that have non-acidic pH. To further define the specific pH environments where cathepsins act, we designed bifunctional activity-based probes (ABPs) that allow simultaneous analysis of cathepsin protease activity and pH. We use these probes to analyze the steady-state environment of cathepsin activity in macrophages and to measure dynamic changes in activity and pH upon stimulation. We show that Salmonella typhimurium induces a change in lysosomal pH that ultimately impairs cathepsin activity in both infected cells and a fraction of bystander cells, highlighting a mechanism by which Salmonella can simultaneously flourish within host cells and alter the behavior of nearby uninfected cells.
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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.