Evidence map›Paper›PMID 19442264›Full record

ArticleMicrobial cell factories2009

Strategies for successful recombinant expression of disulfide bond-dependent proteins in Escherichia coli.

Ario de Marco

Open access · goldAbstract read
In one paragraph

Article in Microbial cell factories, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 152 papers.

0numbers the graph read from it
0cells of the map it votes in
152citing papers in PubMed
10.9field-weighted citation impact, top 1% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

152 citing papers in PubMed, 359 citations in OpenAlex.

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  3. A Simple Method to Produce Recombinant Mammalian Serum Albumins inInternational journal of molecular sciences · 2026
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  8. A biosensor toolbox for monitoring recombinant protein production inFrontiers in bioengineering and biotechnology · 2026
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  10. Monomeric and Oligomeric Decorsins of the Asian Medicinal LeechInternational journal of molecular sciences · 2025
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  15. Papain expression in theApplied and environmental microbiology · 2025
    Article
  16. Article
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  19. Article
  20. Review

92 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

1 author.

Ario de MarcoCogentech, IFOM-IEO Campus for Oncogenomic, via Adamello, 16 - 20139, Milano, Italy. ario.demarco@ifom-ieo-campus.it.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bacteria are simple and cost effective hosts for producing recombinant proteins. However, their physiological features may limit their use for obtaining in native form proteins of some specific structural classes, such as for instance polypeptides that undergo extensive post-translational modifications. To some extent, also the production of proteins that depending on disulfide bridges for their stability has been considered difficult in E. coli.Both eukaryotic and prokaryotic organisms keep their cytoplasm reduced and, consequently, disulfide bond formation is impaired in this subcellular compartment. Disulfide bridges can stabilize protein structure and are often present in high abundance in secreted proteins. In eukaryotic cells such bonds are formed in the oxidizing environment of endoplasmic reticulum during the export process. Bacteria do not possess a similar specialized subcellular compartment, but they have both export systems and enzymatic activities aimed at the formation and at the quality control of disulfide bonds in the oxidizing periplasm.This article reviews the available strategies for exploiting the physiological mechanisms of bactera to produce properly folded disulfide-bonded proteins.

Identifiers

PMID19442264
PMCPMC2689190
OpenAlexW2166726458

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.