ReviewProtein science : a publication of the Protein Society2015
Production of recombinant proteins in Mycobacterium smegmatis for structural and functional studies.
Review in Protein science : a publication of the Protein Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 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.
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.
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Who cites it
33 citing papers in PubMed, 48 citations in OpenAlex.
- AscF in the mycobacterial CIII-CIV supercomplex lacks metal and nucleotide binding but links malate oxidation to respiration.FEBS letters · 2026Article
- His-Tag-Aptamer-Liposome-Conjugates as a Multipurpose Tool for Recombinant Protein Screening and Protein-Based Bioassays.Analytical chemistry · 2026Article
- Recombinant proteins expressed in Mycolicibacterium smegmatis enhance antibody-based detection of bovine tuberculosis.Veterinary research · 2026Article
- Synthesis of an Adjuvant-Free Single Polypeptide-Based Tuberculosis Subunit Vaccine that Elicits In Vivo Immunogenicity in Rats.Molecular biotechnology · 2026Article
- Cloning, expression, purification, and characterization of glutamate decarboxylase (Rv3432c) from Mycobacterium tuberculosis.International microbiology : the official journal of the Spanish Society for Microbiology · 2025Article
- Molecular Cloning, Optimization of Expression and Functional Characterization of the Global Transcriptional Regulator MosR (Rv0348) of Mycobacterium tuberculosis.Applied biochemistry and biotechnology · 2025Article
- RecombinantVaccines · 2025Review
- Mycobacterium tuberculosis Rv1048c affects the biological characteristics of recombinant Mycobacterium smegmatis.Scientific reports · 2024Article
- A high-throughput target-based screening approach for the identification and assessment ofMicrobiology spectrum · 2024Article
- Lactiplantibacillus plantarum as a novel platform for production and purification of integral membrane proteins using RseP as the benchmark.Scientific reports · 2023Article
- Review
- Identification and characterization of a novel lytic peptidoglycan transglycosylase (MltC) in Shigella dysenteriae.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2023Article
- Coordination Properties of the Zinc Domains of BigR4 and SmtB Proteins in Nickel Systems─Designation of Key Donors.Inorganic chemistry · 2022Article
- Investigating a putative transcriptional regulatory protein encoded by Rv1719 gene of Mycobacterium tuberculosis.The protein journal · 2022Article
- LysX2 is a Mycobacterium tuberculosis membrane protein with an extracytoplasmic MprF-like domain.BMC microbiology · 2022Article
- Mycobacterium tuberculosis Rv0790c inhibits the cellular autophagy at its early stage and facilitates mycobacterial survival.Frontiers in cellular and infection microbiology · 2022Article
- Towards Reverse Vaccinology for Bovine TB: High Throughput Expression of Full Length RecombinantFrontiers in molecular biosciences · 2022Article
- Regulation of Ribosomal Protein Synthesis in Mycobacteria: The Autogenous Control ofInternational journal of molecular sciences · 2021Article
- Label-Free Comparative Proteomics of Differentially ExpressedPathogens (Basel, Switzerland) · 2021Article
- Effect of Protein O-Mannosyltransferase (MSMEG_5447) onFrontiers in microbiology · 2021Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
Protein production using recombinant DNA technology has a fundamental impact on our understanding of biology through providing proteins for structural and functional studies. Escherichia coli (E. coli) has been traditionally used as the default expression host to over-express and purify proteins from many different organisms. E. coli does, however, have known shortcomings for obtaining soluble, properly folded proteins suitable for downstream studies. These shortcomings are even more pronounced for the mycobacterial pathogen Mycobacterium tuberculosis, the bacterium that causes tuberculosis, with typically only one third of proteins expressed in E. coli produced as soluble proteins. Mycobacterium smegmatis (M. smegmatis) is a closely related and non-pathogenic species that has been successfully used as an expression host for production of proteins from various mycobacterial species. In this review, we describe the early attempts to produce mycobacterial proteins in alternative expression hosts and then focus on available expression systems in M. smegmatis. The advantages of using M. smegmatis as an expression host, its application in structural biology and some practical aspects of protein production are also discussed. M. smegmatis provides an effective expression platform for enhanced understanding of mycobacterial biology and pathogenesis and for developing novel and better therapeutics and diagnostics.
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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.