ArticleApplied and environmental microbiology2012
Degradation of the twin-arginine translocation substrate YwbN by extracytoplasmic proteases of Bacillus subtilis.
Article in Applied and environmental microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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
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Who cites it
5 citing papers in PubMed, 13 citations in OpenAlex.
- Whole-genome sequencing and assessment of a novel protein- and gossypol-degrading Bacillus subtilis strain isolated from intestinal digesta of Tibetan Pigs.BMC microbiology · 2024Article
- Transport of Folded Proteins by the Tat System.The protein journal · 2019Review
- The Twin-Arginine Pathway for Protein Secretion.EcoSal Plus · 2019Review
- Degradation of extracytoplasmic catalysts for protein folding in Bacillus subtilis.Applied and environmental microbiology · 2014Article
- Bacillus subtilis: from soil bacterium to super-secreting cell factory.Microbial cell factories · 2013Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial twin-arginine translocases can export fully folded proteins from the cytoplasm. Such proteins are usually resistant to proteolysis. Here we show that multiple extracellular proteases degrade the B. subtilis Tat substrate YwbN. This suggests either that secreted YwbN is not fully folded or that folded YwbN exposes protease cleavage sites.
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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.