Evidence map›Paper›PMID 42376770›Full record

ArticleCurrent protocols2026

Recombinant Protein Expression in Rhodococcus species.

Michael Akintubosun, Melanie A Higgins

Abstract read
In one paragraph

Article in Current protocols, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

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

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Article
4 · The record

Corrections and comments

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

2 authors.

Michael AkintubosunDepartment of Biological Sciences, The University of Alabama, Tuscaloosa, Alabama.
Melanie A HigginsDepartment of Biological Sciences, The University of Alabama, Tuscaloosa, Alabama.ORCID https://orcid.org/0000-0003-1485-1378

Funding

Investigating biosynthetic enzymes to enhance natural product discoveryR35GM151137 · NIGMS · UNIVERSITY OF ALABAMA IN TUSCALOOSA · PI Melanie Ann Higgins · 2023 to 2026
$1.4M
NIGMS NIH HHS R35 GM151137NIGMS NIH HHS R35GM151137
6 · The paper itself

Abstract

Producing recombinant bacterial proteins is essential for elucidating their structure and function, making efficient overexpression systems a key requirement. Escherichia coli is widely used for this purpose, particularly for bacterial proteins, but certain targets remain challenging to express or obtain as soluble protein. A recently developed Rhodococcus expression system has successfully produced proteins that were poorly expressed or not expressed in E. coli, highlighting the value of standardized protocols for this alternative host. Here, we present detailed methods for cloning into Rhodococcus expression vectors, transforming electrocompetent Rhodococcus cells, and performing protein expression and purification in this system. We also outline strategies to improve yields and provide troubleshooting guidance. These protocols are designed to equip protein scientists across disciplines with a robust alternative for bacterial protein production. © 2026 The Author(s). Current Protocols published by Wiley Periodicals LLC. Basic Protocol 1: Cloning into a Rhodococcus expression vector Basic Protocol 2: Generation of electrocompetent Rhodococcus cells Basic Protocol 3: Transformation into a Rhodococcus host Basic Protocol 4: Recombinant protein production and purification using the Rhodococcus system.

Indexed as

Bacterial ProteinsCloning, MolecularRecombinant ProteinsRhodococcusEscherichia coliGenetic VectorsBacterial ProteinsRecombinant Proteinsalternative expression hostbacterial transformationcloningrecombinant protein expressionRhodococcus

Identifiers

PMID42376770
PMCPMC13316812

What OpenQuestion holds

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LicenceCC BY-NC
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Registered trials

None linked

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.