ArticleThe Journal of biological chemistry2017
Energetics of side-chain partitioning of β-signal residues in unassisted folding of a transmembrane β-barrel protein.
Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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.
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
10 citing papers in PubMed.
- Mitochondrial Transmembrane β-Barrels: Deducing Thermodynamic Regulators of Folding and Stability.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Engineering a HyperstableJournal of the American Chemical Society · 2022Article
- GeTFEP: A general transfer free energy profile of transmembrane proteins.Protein science : a publication of the Protein Society · 2020Article
- Hydrophobic Characteristic Is Energetically Preferred for Cysteine in a Model Membrane Protein.Biophysical journal · 2019Article
- Outer Membrane Protein Insertion by the β-barrel Assembly Machine.EcoSal Plus · 2019Review
- Salvaging the Thermodynamic Destabilization of Interface Histidine in Transmembrane β-Barrels.Biochemistry · 2018Article
- Article
- Position-Specific contribution of interface tryptophans on membrane protein energetics.Biochimica et biophysica acta. Biomembranes · 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
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
The free energy of water-to-interface amino acid partitioning is a major contributing factor in membrane protein folding and stability. The interface residues at the C terminus of transmembrane β-barrels form the β-signal motif required for assisted β-barrel assembly
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Registered trials
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