ArticleFrontiers in microbiology2020
Structure-Function Relationship of Inclusion Bodies of a Multimeric Protein.
Article in Frontiers in microbiology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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.
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.
Who cites it
13 citing papers in PubMed, 33 citations in OpenAlex.
- The effect of monomers number in peptides on Escherichia coli strain productivity and inclusion bodies-associated target protein accumulation.Folia microbiologica · 2026Article
- Catalytically active inclusion bodies of Bacillus clausii laccase protein recombinantly produced in E. coli for dye decolorization.Microbial cell factories · 2026Article
- The Missing Link: Connecting Cultivation Conditions and Refolding Performance via Inclusion Body Biophysical Properties.Biotechnology and bioengineering · 2025Article
- DNA shuffling to improve crude-water interfacial activity in biosurfactants with OmpA protein ofPeerJ · 2024Article
- Antibody preparation and age-dependent distribution of TLR8 in Bactrian camel spleens.BMC veterinary research · 2023Article
- Liquid-Liquid Phase Separation and Protective Protein Aggregates in Bacteria.Molecules (Basel, Switzerland) · 2023Review
- Expression and Characterization of Monomeric Recombinant Isocitrate Dehydrogenases fromInternational journal of molecular sciences · 2022Article
- Methodological advances and strategies for high resolution structure determination of cellular protein aggregates.The Journal of biological chemistry · 2022Review
- The pre-induction temperature affects recombinant HuGM-CSF aggregation in thermoinducible Escherichia coli.Applied microbiology and biotechnology · 2022Article
- Thermostable adenosine 5'-monophosphate phosphorylase from Thermococcus kodakarensis forms catalytically active inclusion bodies.Scientific reports · 2021Article
- Studies on the Structure and Properties of Membrane Phospholipase AMolecules (Basel, Switzerland) · 2021Article
- Challenges Associated With the Formation of Recombinant Protein Inclusion Bodies inFrontiers in bioengineering and biotechnology · 2021Review
- Functional and structural evaluation of the antileukaemic enzyme L-asparaginase II expressed at low temperature by different Escherichia coli strains.Biotechnology letters · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
High level expression of recombinant proteins in bacteria often results in their aggregation into inclusion bodies. Formation of inclusion bodies poses a major bottleneck in high-throughput recovery of recombinant protein. These aggregates have amyloid-like nature and can retain biological activity. Here, effect of expression temperature on the quality of
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.