Evidence map›Paper›PMID 38963110›Full record

ArticleProtein and peptide letters2024

Comparing the Soluble Form of Recombinant Human Insulin-like Growth Factor-1 (rhIGF-1) in

Sara Hemmati, Parvaneh Maghami, Javad Ranjbari, Maryam Tabarzad

Abstract readComparative Study
PubMed Publisher
In one paragraph

Article in Protein and peptide letters, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

4 authors.

Sara HemmatiDepartment of Biology, Science and Research Branch, Islamic Azad University, Tehran, Iran.
Parvaneh MaghamiDepartment of Biology, Science and Research Branch, Islamic Azad University, Tehran, Iran.
Javad RanjbariDepartment of Medical Biotechnology, School of Advanced Technologies in Medicine, Shahid Beheshti University of Medical Sciences, Tehran, Iran.ORCID 0000-0001-7025-1479
Maryam TabarzadProtein Technology Research Center, Shahid Beheshti University of Medical Sciences, Tehran, Iran.ORCID 0000-0001-9923-0639

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

introductionInsulin-like growth factor-1 (IGF-1) is a single-chain polypeptide with various physiological functions.

objectivesIn this study, bacterial thioredoxin (Trx) was studied as a fused and non-fused protein to convert the insoluble form of recombinant human IGF-1 (rhIGF-1) to its soluble form in E. coli.

methodsThe rhIGF-1 was expressed in the

resultsResults showed that Trx in both the fused and non-fused forms had a positive effect on the production of the soluble form of rhIGF-1. A significant increase in ALP activity in hASCs after rhIGF-1 treatment was observed, confirming protein bioactivity.

conclusionIt was strongly suggested that the overproduction of Trx could increase the solubility of co-expressed recombinant proteins by changing the redox state in

Indexed as

Escherichia coliInsulin-Like Growth Factor IRecombinant Fusion ProteinsSolubilityThioredoxinsAdipose TissueCell DifferentiationHumansInsulin-Like PeptidesRecombinant ProteinsStem CellsIGF1 protein, humanInsulin-Like Growth Factor IInsulin-Like PeptidesRecombinant Fusion ProteinsRecombinant ProteinsThioredoxinsalkaline phosphatasebioactivity.Escherichia coliInsulin-like growth factor Iosteogenesisthioredoxin

Identifiers

PMID38963110

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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.