ReviewNature biotechnology2004
Recombinant protein folding and misfolding in Escherichia coli.
Review in Nature biotechnology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 476 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
476 citing papers in PubMed, 1,436 citations in OpenAlex.
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- Production of isotope-labeled nanobody KN035 inMagnetic resonance letters · 2026Article
- From gene to enzyme: Microbial engineering of bovine chymosin for efficient cheese coagulation.World journal of microbiology & biotechnology · 2026Article
- Recombinant expression of natural Arabidopsis PRLIP1 variants reveals temperature-dependent differences in fluorescence and functional protein recovery in Escherichia coli.World journal of microbiology & biotechnology · 2026Article
- Application of the YebF secretion pathway inRSC chemical biology · 2026Article
- Achieving protease substrate-specific inhibition by mAb dual functional selections.Protein science : a publication of the Protein Society · 2026Article
- Efficient in vivo removal of solubility tag to improve the bacterial production of soluble, bioactive human IGF-1.World journal of microbiology & biotechnology · 2026Article
- Effects of heterologous expression of glycolysis enzymes on product formation inMetabolic engineering communications · 2026Article
- Structure-Guided Design and in Vivo Validation of a VP4-Derived Subunit Vaccine Candidate against Bovine Rotavirus.Molecular biotechnology · 2026Article
- Integrated chaperone engineering and process optimization enable enhanced production of ChCODH-II A559W in Escherichia coli.World journal of microbiology & biotechnology · 2026Article
- Natural diversity-guided catalytic-core chimerism engineers a rapid and inhibitor-tolerant reverse transcriptase.Journal of biological engineering · 2026Article
- A Novel Recombinant MAGE-B10-HSP110 Fusion Protein Enhances Innate and Adaptive Immune Responses in Mice: A Potential Vaccine Candidate for Canine Mammary Tumors.Animals : an open access journal from MDPI · 2026Article
- Recombinant Protein Nanoparticles for Dual-Stage Inhibition of SARS-CoV‑2 Infection.ACS nanoscience Au · 2026Article
- A proteome optimal allocation model for elucidating effects of temperature on bacterial growth.NPJ systems biology and applications · 2026Article
416 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The past 20 years have seen enormous progress in the understanding of the mechanisms used by the enteric bacterium Escherichia coli to promote protein folding, support protein translocation and handle protein misfolding. Insights from these studies have been exploited to tackle the problems of inclusion body formation, proteolytic degradation and disulfide bond generation that have long impeded the production of complex heterologous proteins in a properly folded and biologically active form. The application of this information to industrial processes, together with emerging strategies for creating designer folding modulators and performing glycosylation all but guarantee that E. coli will remain an important host for the production of both commodity and high value added proteins.
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What OpenQuestion holds
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.