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Article

Evaluating the ability of different chaperones in improving soluble expression of a triple-mutated human interferon gamma in Escherichia coli.

Journal of bioscience and bioengineering - 1 Sept 2024

Yasamut Umpa, Thongheang Kanyarat, Weechan Anuwat, Sornsuwan Kanokporn, Juntit On-Anong, Tayapiwatana Chatchai

Abstract excerpt

Human interferon gamma (hIFN-γ) plays a pivotal role as a soluble cytokine with diverse functions in both innate and adaptive immunity. In a previous investigation, we pinpointed three critical amino acid residues, i.e., threonine (T) 27, phenylalanine (F) 29, and leucine (L) 30, on the IFN-γ structure, which are integral to the epitope recognized by anti-IFN-γ autoantibodies. It is crucial to impede the...

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Identifiers

PMID: 38969548
DOI: 10.1016/j.jbiosc.2024.06.005

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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