ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences2015
A combined kinetic push and thermodynamic pull as driving forces for outer membrane protein sorting and folding in bacteria.
Review in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 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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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
32 citing papers in PubMed, 46 citations in OpenAlex.
- Autoproteolytic mechanism of CdiA toxin release reconstitutedJournal of bacteriology · 2024Article
- Targeting BamA, the essential component of theHeliyon · 2024Article
- β-Barrel Assembly Machinery (BAM) Complex as Novel Antibacterial Drug Target.Molecules (Basel, Switzerland) · 2023Review
- Chaperones Skp and SurA dynamically expand unfolded OmpX and synergistically disassemble oligomeric aggregates.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Reconstitution of Bam Complex-Mediated Assembly of a Trimeric Porin into Proteoliposomes.mBio · 2021Article
- Article
- Comparison of Single and Multiple Turnovers of SecYEG in Escherichia coli.Journal of bacteriology · 2020Article
- Inter-domain dynamics in the chaperone SurA and multi-site binding to its outer membrane protein clients.Nature communications · 2020Article
- Reversible folding energetics of Yersinia Ail barrel reveals a hyperfluorescent intermediate.Biochimica et biophysica acta. Biomembranes · 2020Article
- Outer Membrane Protein Insertion by the β-barrel Assembly Machine.EcoSal Plus · 2019Review
- Folded Synthetic Peptides and Other Molecules Targeting Outer Membrane Protein Complexes in Gram-Negative Bacteria.Frontiers in chemistry · 2019Review
- The Escherichia coli β-Barrel Assembly Machinery Is Sensitized to Perturbations under High Membrane Fluidity.Journal of bacteriology · 2019Article
- Monoclonal antibody targeting the β-barrel assembly machine ofProceedings of the National Academy of Sciences of the United States of America · 2018Article
- The Bam complex catalyzes efficient insertion of bacterial outer membrane proteins into membrane vesicles of variable lipid composition.The Journal of biological chemistry · 2018Article
- Outer membrane protein folding from an energy landscape perspective.BMC biology · 2017Review
- Transmembrane β-barrels: Evolution, folding and energetics.Biochimica et biophysica acta. Biomembranes · 2017Review
- Selective pressure for rapid membrane integration constrains the sequence of bacterial outer membrane proteins.Molecular microbiology · 2017Article
- Effects of Periplasmic Chaperones and Membrane Thickness on BamA-Catalyzed Outer-Membrane Protein Folding.Journal of molecular biology · 2017Article
- Structural basis for substrate selection by the translocation and assembly module of the β-barrel assembly machinery.Molecular microbiology · 2017Article
- Outer Membrane Biogenesis.Annual review of microbiology · 2017Review
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
In vitro folding studies of outer membrane beta-barrels have been invaluable in revealing the lipid effects on folding rates and efficiencies as well as folding free energies. Here, the biophysical results are summarized, and these kinetic and thermodynamic findings are considered in terms of the requirements for folding in the context of the cellular environment. Because the periplasm lacks an external energy source the only driving forces for sorting and folding available within this compartment are binding or folding free energies and their associated rates. These values define functions for periplasmic chaperones and suggest a biophysical mechanism for the BAM complex.
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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.