ReviewApplied microbiology and biotechnology2009
Applications of thiol-disulfide oxidoreductases for optimized in vivo production of functionally active proteins in Bacillus.
Review in Applied microbiology and biotechnology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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
6 citing papers in PubMed, 18 citations in OpenAlex.
- Toward Antibody Production in Genome-MinimizedACS synthetic biology · 2025Article
- From the outer space to the inner cell: deconvoluting the complexity ofMicrobiology spectrum · 2024Article
- Disulfide Bonds of Proteins Displayed on Spores of Bacillus subtilis Can Occur Spontaneously.Current microbiology · 2015Article
- Molecular engineering of secretory machinery components for high-level secretion of proteins in Bacillus species.Journal of industrial microbiology & biotechnology · 2014Review
- Bacillus subtilis: from soil bacterium to super-secreting cell factory.Microbial cell factories · 2013Article
- Cloning and Expression of Randomly Mutated Bacillus subtilis α-Amylase Genes in HB101.Biotechnology research international · 2011Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacillus subtilis is a well-established cellular factory for proteins and fine chemicals. In particular, the direct secretion of proteinaceous products into the growth medium greatly facilitates their downstream processing, which is an important advantage of B. subtilis over other biotechnological production hosts, such as Escherichia coli. The application spectrum of B. subtilis is, however, often confined to proteins from Bacillus or closely related species. One of the major reasons for this (current) limitation is the inefficient formation of disulfide bonds, which are found in many, especially eukaryotic, proteins. Future exploitation of B. subtilis to fulfill the ever-growing demand for pharmaceutical and other high-value proteins will therefore depend on overcoming this particular hurdle. Recently, promising advances in this area have been achieved, which focus attention on the need to modulate the cellular levels and activity of thiol-disulfide oxidoreductases (TDORs). These TDORs are enzymes that control the cleavage or formation of disulfide bonds. This review will discuss readily applicable approaches for TDOR modulation and aims to provide leads for further improvement of the Bacillus cell factory for production of disulfide bond-containing proteins.
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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.