ReviewBiochimie2010
Prokaryote-derived protein inhibitors of peptidases: A sketchy occurrence and mostly unknown function.
Review in Biochimie, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
27 citing papers in PubMed, 54 citations in OpenAlex.
- Interspecies regulation of virulence through gingipain inhibition by a Tannerella forsythia serpin.EMBO reports · 2026Article
- Discovery of protease inhibitors from bacteria as novel adjuvants for oral vaccine formulations.Frontiers in immunology · 2025Article
- NMR structure of emfourin, a novel protein metalloprotease inhibitor: Insights into the mechanism of action.The Journal of biological chemistry · 2023Article
- A unique network of attack, defence and competence on the outer membrane of the periodontitis pathogenChemical science · 2023Article
- Fungal Proteases as Emerging Biocatalysts to Meet the Current Challenges and Recent Developments in Biomedical Therapies: An Updated Review.Journal of fungi (Basel, Switzerland) · 2022Review
- A disordered region retains the full protease inhibitor activity and the capacity to induce CD8Computational and structural biotechnology journal · 2022Article
- Genome analysis provides insights into the biocontrol ability of Mitsuaria sp. strain TWR114.Archives of microbiology · 2021Article
- A Comprehensive Phylogenetic Analysis of the Serpin Superfamily.Molecular biology and evolution · 2021Article
- Gut Serpinome: Emerging Evidence in IBD.International journal of molecular sciences · 2021Review
- A malaria parasite subtilisin propeptide-like protein is a potent inhibitor of the egress protease SUB1.The Biochemical journal · 2020Article
- Characterization of ecotin homologs from Campylobacter rectus and Campylobacter showae.PloS one · 2020Article
- Proteolytic processing and activation of gingipain zymogens secreted by T9SS of Porphyromonas gingivalis.Biochimie · 2019Article
- Article
- Potential Anticoagulant Activity of Trypsin Inhibitor Purified from an Isolated Marine Bacterium Oceanimonas Sp. BPMS22 and its Kinetics.Marine biotechnology (New York, N.Y.) · 2018Article
- Proteolytic systems of archaea: slicing, dicing, and mincing in the extreme.Emerging topics in life sciences · 2018Article
- Article
- A structure-derived snap-trap mechanism of a multispecific serpin from the dysbiotic human oral microbiome.The Journal of biological chemistry · 2017Article
- A novel subtilase inhibitor in plants shows structural and functional similarities to protease propeptides.The Journal of biological chemistry · 2017Article
- Article
- Screen of Non-annotated Small Secreted Proteins of Pseudomonas syringae Reveals a Virulence Factor That Inhibits Tomato Immune Proteases.PLoS pathogens · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 3 institutions in 3 countries.
Funding
Abstract
In metazoan organisms protein inhibitors of peptidases are important factors essential for regulation of proteolytic activity. In vertebrates genes encoding peptidase inhibitors constitute up to 1% of genes reflecting a need for tight and specific control of proteolysis especially in extracellular body fluids. In stark contrast unicellular organisms, both prokaryotic and eukaryotic consistently contain only few, if any, genes coding for putative peptidase inhibitors. This may seem perplexing in the light of the fact that these organisms produce large numbers of proteases of different catalytic classes with the genes constituting up to 6% of the total gene count with the average being about 3%. Apparently, however, a unicellular life-style is fully compatible with other mechanisms of regulation of proteolysis and does not require protein inhibitors to control their intracellular and extracellular proteolytic activity. So in prokaryotes occurrence of genes encoding different types of peptidase inhibitors is infrequent and often scattered among phylogenetically distinct orders or even phyla of microbiota. Genes encoding proteins homologous to alpha-2-macroglobulin (family I39), serine carboxypeptidase Y inhibitor (family I51), alpha-1-peptidase inhibitor (family I4) and ecotin (family I11) are the most frequently represented in Bacteria. Although several of these gene products were shown to possess inhibitory activity, with an exception of ecotin and staphostatins, the biological function of microbial inhibitors is unclear. In this review we present distribution of protein inhibitors from different families among prokaryotes, describe their mode of action and hypothesize on their role in microbial physiology and interactions with hosts and environment.
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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.