ArticleFrontiers in microbiology2021
Molecular Attributes Associated With Refolding of Inclusion Body Proteins Using the Freeze-Thaw Method.
Article in Frontiers in microbiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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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.
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Who cites it
4 citing papers in PubMed, 17 citations in OpenAlex.
- Recovery of mouse growth hormone from E. coli inclusion bodies using a mild solubilisation and repeated freeze-thaw approach.Molecular biology reports · 2025Article
- Growth hormone receptor agonists and antagonists: From protein expression and purification to long-acting formulations.Protein science : a publication of the Protein Society · 2023Review
- Current state of molecular and metabolic strategies for the improvement of L-asparaginase expression in heterologous systems.Frontiers in pharmacology · 2023Review
- Protein Extraction and Purification by Differential Solubilization.Methods in molecular biology (Clifton, N.J.) · 2023Article
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Understanding the structure-function of inclusion bodies (IBs) in the last two decades has led to the development of several mild solubilization buffers for the improved recovery of bioactive proteins. The recently developed freeze-thaw-based inclusion body protein solubilization method has received a great deal of attention due to its simplicity and cost-effectiveness. The present report investigates the reproducibility, efficiency, and plausible mechanism of the freeze-thaw-based IB solubilization. The percentage recovery of functionally active protein species of human growth hormone (hGH) and L-asparaginase from their IBs in
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