Evidence map›Paper›PMID 36109777›Full record

ReviewMicrobial cell factories2022

Strategies for efficient production of recombinant proteins in Escherichia coli: alleviating the host burden and enhancing protein activity.

Zi-Xu Zhang, Fang-Tong Nong, Yu-Zhou Wang, Chun-Xiao Yan, Yang Gu, Ping Song, Xiao-Man Sun

Open access · goldAbstract readReview
In one paragraph

Review in Microbial cell factories, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing papers in PubMed
9.4field-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

70 citing papers in PubMed, 108 citations in OpenAlex.

  1. Article
  2. UnconditionalSynthetic and systems biotechnology · 2026
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  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
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  11. A Simple Method to Produce Recombinant Mammalian Serum Albumins inInternational journal of molecular sciences · 2026
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Bio-Inspired and Protein-Based Elastomeric Materials.Polymer science & technology (Washington, D.C.) · 2026
    Review

10 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

7 authors at 1 institution in 1 country.

Zi-Xu Zhang *School of Food Science and Pharmaceutical Engineering, Nanjing Normal University, Xuelin Road, Qixia District, Nanjing, People's Republic of China.
Fang-Tong Nong *School of Food Science and Pharmaceutical Engineering, Nanjing Normal University, Xuelin Road, Qixia District, Nanjing, People's Republic of China.
Yu-Zhou WangSchool of Food Science and Pharmaceutical Engineering, Nanjing Normal University, Xuelin Road, Qixia District, Nanjing, People's Republic of China.
Chun-Xiao YanSchool of Food Science and Pharmaceutical Engineering, Nanjing Normal University, Xuelin Road, Qixia District, Nanjing, People's Republic of China.
Yang GuSchool of Food Science and Pharmaceutical Engineering, Nanjing Normal University, Xuelin Road, Qixia District, Nanjing, People's Republic of China.
Ping SongSchool of Food Science and Pharmaceutical Engineering, Nanjing Normal University, Xuelin Road, Qixia District, Nanjing, People's Republic of China. songping@njnu.edu.cn.
Xiao-Man SunSchool of Food Science and Pharmaceutical Engineering, Nanjing Normal University, Xuelin Road, Qixia District, Nanjing, People's Republic of China. xiaomansun@njnu.edu.cn.
Nanjing Normal University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Escherichia coli, one of the most efficient expression hosts for recombinant proteins (RPs), is widely used in chemical, medical, food and other industries. However, conventional expression strains are unable to effectively express proteins with complex structures or toxicity. The key to solving this problem is to alleviate the host burden associated with protein overproduction and to enhance the ability to accurately fold and modify RPs at high expression levels. Here, we summarize the recently developed optimization strategies for the high-level production of RPs from the two aspects of host burden and protein activity. The aim is to maximize the ability of researchers to quickly select an appropriate optimization strategy for improving the production of RPs.

Indexed as

Escherichia coliRecombinant ProteinsRecombinant ProteinsEscherichia coliHost burdenInclusion bodiesPost-translational modificationRecombinant protein

Identifiers

PMID36109777
PMCPMC9479345
OpenAlexW4296036875

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.