Evidence map›Paper›PMID 38847260›Full record

ArticleProtein and peptide letters2024

Study on Cloning and Expression of TNF-α Variants in

Gülşah Akçadağ, Demet Cansaran-Duman, Emine Sümer Aras, Haluk Ataoğlu

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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. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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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

2 citing papers in PubMed.

  1. Article
  2. The miR-146a/Human mutation · 2026
    Article
4 · The record

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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.

Gülşah AkçadağDepartment of Biology, Science Faculty, Ankara University, Tandogan, Ankara, Turkey.
Demet Cansaran-DumanBiotechnology Institute, Keçiören, Ankara University, 06135, Ankara, Turkey.
Emine Sümer ArasDepartment of Biology, Science Faculty, Ankara University, Tandogan, Ankara, Turkey.
Haluk AtaoğluMatriks Biotechnology Industry and Trade Ltd. Co., Gazi Teknopark, Ankara, Turkey.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundTNF-α is a proinflammatory cytokine and plays a role in cell proliferation, differentiation, survival, and death pathways. When administered at high doses, it may cause damage to the tumor vasculature, thereby increasing the permeability of the blood vessels. Therefore, monitoring the dose and the response of the TNF-α molecule is essential for patients' health.

objectivesThis study aimed to clone, express, and purify the active form of the TNF-α protein, which can interact with various anti-TNF-α inhibitors with high efficiency.

methodsRecombinant DNA technology was used to clone three different versions of codon-optimized human TNF-α sequences to

resultsUnder native condition (25°C), interaction between sTNF-α and anti-TNF-α antibody was 3,970, compared to positive control. The interaction was 0,587, whereas it was 0,535 for TNF- α and anti-TNF-α antibodies under denaturing conditions (37°C). F7 of sTNF-α (920 μg/mL) had the same/higher binding efficiency to adalimumab, etanercept, and infliximab, compared to commercial TNF-α.

conclusionThis study was the first to analyze binding efficiency of homemade sTNF-α protein against three major TNF-α inhibitors (adalimumab, etanercept, and infliximab) in a single study. The high binding efficiency of sTNF-α with adalimumab, etanercept, and infliximab, evidenced in this study supports the feasibility of its use in therapeutic applications, contributing to more sustainable, cost-effective, and independent healthcare system.

Indexed as

Cloning, MolecularEscherichia coliTumor Necrosis Factor-alphaAdalimumabHumansRecombinant ProteinsAdalimumabRecombinant ProteinsTumor Necrosis Factor-alphaadalimumabE. coliELISA.etanerceptinfliximabTumor necrosis factor-α

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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.