ArticleMicrobiology (Reading, England)2019
Engineering the PduT shell protein to modify the permeability of the 1,2-propanediol microcompartment of
Article in Microbiology (Reading, England), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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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
9 citing papers in PubMed, 23 citations in OpenAlex.
- Review
- Delay-facilitated self-assembly in compartmentalized systems.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Quantitative Measurement of Molecular Permeability to a Synthetic Bacterial Microcompartment Shell System.ACS synthetic biology · 2025Article
- Electrochemical cofactor recycling of bacterial microcompartments.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- A method for targeting a specified segment of DNA to a bacterial microorganelle.Nucleic acids research · 2022Article
- Pore structure controls stability and molecular flux in engineered protein cages.Science advances · 2022Article
- A comprehensive review on microbial production of 1,2-propanediol: micro-organisms, metabolic pathways, and metabolic engineering.Biotechnology for biofuels · 2021Review
- Introducing noncanonical amino acids for studying and engineering bacterial microcompartments.Current opinion in microbiology · 2021Review
- Prokaryotic Organelles: Bacterial Microcompartments inEcoSal Plus · 2020Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 2 countries.
Funding
Abstract
Bacterial microcompartments (MCPs) are protein-based organelles that consist of metabolic enzymes encapsulated within a protein shell. The function of MCPs is to optimize metabolic pathways by increasing reaction rates and sequestering toxic pathway intermediates. A substantial amount of effort has been directed toward engineering synthetic MCPs as intracellular nanoreactors for the improved production of renewable chemicals. A key challenge in this area is engineering protein shells that allow the entry of desired substrates. In this study, we used site-directed mutagenesis of the PduT shell protein to remove its central iron-sulfur cluster and create openings (pores) in the shell of the Pdu MCP that have varied chemical properties. Subsequently,
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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.