Evidence map›Paper›PMID 27581654›Full record

ReviewOpen biology2016

High-throughput recombinant protein expression in Escherichia coli: current status and future perspectives.

Baolei Jia, Che Ok Jeon

Abstract readReview
In one paragraph

Review in Open biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 129 papers.

0numbers the graph read from it
0cells of the map it votes in
129citing papers in PubMed
–field-weighted citation impact
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

129 citing papers in PubMed.

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  8. Production of Novel Thermostable Esterases fromInternational journal of molecular sciences · 2026
    Article
  9. Article
  10. A novel recombinant oligogalacturonide lyase fromFrontiers in bioengineering and biotechnology · 2026
    Article
  11. Article
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69 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

2 authors.

Baolei JiaDepartment of Life Science, Chung-Ang University, Seoul 06974, Republic of Korea baoleijia@cau.ac.kr.ORCID 0000-0001-6434-5604
Che Ok JeonDepartment of Life Science, Chung-Ang University, Seoul 06974, Republic of Korea cojeon@cau.ac.kr.ORCID 0000-0003-1665-2399

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ease of genetic manipulation, low cost, rapid growth and number of previous studies have made Escherichia coli one of the most widely used microorganism species for producing recombinant proteins. In this post-genomic era, challenges remain to rapidly express and purify large numbers of proteins for academic and commercial purposes in a high-throughput manner. In this review, we describe several state-of-the-art approaches that are suitable for the cloning, expression and purification, conducted in parallel, of numerous molecules, and we discuss recent progress related to soluble protein expression, mRNA folding, fusion tags, post-translational modification and production of membrane proteins. Moreover, we address the ongoing efforts to overcome various challenges faced in protein expression in E. coli, which could lead to an improvement of the current system from trial and error to a predictable and rational design.

Indexed as

Cloning, MolecularEscherichia coliGene ExpressionProtein EngineeringProtein Processing, Post-TranslationalRecombinant ProteinsRNA FoldingRNA, MessengerRecombinant ProteinsRNA, Messenger5′UTR and N-terminal codonsEscherichia colifusion taghigh-throughputmembrane proteinrecombinant protein expression

Identifiers

PMID27581654
PMCPMC5008019

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.