Evidence map›Paper›PMID 31918694›Full record

ArticleBMC biotechnology2020

Intein-mediated recombinant expression of monomeric B22Asp desB30 insulin.

Minmin Zhang, Yunlong Zhang, Bingnan Wu, Yanhao Peng, Altaf Ahmed Simair, Geoffery W Siegel, Changrui Lu, Ting Chen

Abstract read
In one paragraph

Article in BMC biotechnology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

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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

3 citing papers in PubMed.

  1. Article
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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

8 authors.

Minmin ZhangKey Laboratory of Science and Technology of Eco-Textiles, Ministry of Education, College of Chemistry, Chemical Engineering and Biotechnology, Donghua University, 2999 North Ren Min Rd, Shanghai, 201620, China.
Yunlong ZhangKey Laboratory of Science and Technology of Eco-Textiles, Ministry of Education, College of Chemistry, Chemical Engineering and Biotechnology, Donghua University, 2999 North Ren Min Rd, Shanghai, 201620, China.
Bingnan WuKey Laboratory of Science and Technology of Eco-Textiles, Ministry of Education, College of Chemistry, Chemical Engineering and Biotechnology, Donghua University, 2999 North Ren Min Rd, Shanghai, 201620, China.
Yanhao PengKey Laboratory of Science and Technology of Eco-Textiles, Ministry of Education, College of Chemistry, Chemical Engineering and Biotechnology, Donghua University, 2999 North Ren Min Rd, Shanghai, 201620, China.
Altaf Ahmed SimairKey Laboratory of Science and Technology of Eco-Textiles, Ministry of Education, College of Chemistry, Chemical Engineering and Biotechnology, Donghua University, 2999 North Ren Min Rd, Shanghai, 201620, China.
Geoffery W SiegelDepartment of Orthopaedic Surgery, Musculoskeletal Oncology Division, University of Michigan Medical School, Ann Arbor, MI, 10, USA.
Changrui LuKey Laboratory of Science and Technology of Eco-Textiles, Ministry of Education, College of Chemistry, Chemical Engineering and Biotechnology, Donghua University, 2999 North Ren Min Rd, Shanghai, 201620, China. crlu@dhu.edu.cn.
Ting ChenKey Laboratory of Science and Technology of Eco-Textiles, Ministry of Education, College of Chemistry, Chemical Engineering and Biotechnology, Donghua University, 2999 North Ren Min Rd, Shanghai, 201620, China. chenting@dhu.edu.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundInsulin controls hyperglycemia caused by diabetes, and virtually all treatments require exogenous insulin. However, the product's extensive post-translational modifications have hindered the manufacture of recombinant insulin.

resultHere we report a novel production method for a monomeric B22Asp desB30 insulin analog (B22D desB30 insulin). Its precursor, DPIP, is fused to an N-terminal chitin-binding domain and intein self-cleavage tag. The fusion protein is expressed and purified from E. coli and immobilized on chitin resins. DPIP is then released using an optimized pH shift and converted to mature insulin via trypsin digest. The resulting product appears monomeric, > 90% pure and devoid of any exogenous enzyme.

conclusionThus, biologically active insulin analog can be efficiently produced in bacteria and potentially applicable in the treatment of human diabetes.

Indexed as

Escherichia coliInsulinInteinsProinsulinProtein EngineeringProtein MultimerizationProtein SplicingRecombinant Fusion ProteinsInsulinProinsulinRecombinant Fusion ProteinsB22D desB30 insulinInteinOptimizationSelf-cleavage

Identifiers

PMID31918694
PMCPMC6953245

What OpenQuestion holds

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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.