ArticleAngewandte Chemie (International ed. in English)2014
Control of the conductance of engineered protein nanopores through concerted loop motions.
Article in Angewandte Chemie (International ed. in English), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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.
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.
Who cites it
21 citing papers in PubMed.
- Engineering Linker-Enhanced OmpG Nanopores for Rapid Single-Molecule Protease Detection.Sensors (Basel, Switzerland) · 2025Article
- Barrel expansion of outer membrane protein G nanopore through β-hairpin duplication.Protein science : a publication of the Protein Society · 2025Article
- Gating of β-Barrel Protein Pores, Porins, and Channels: An Old Problem with New Facets.International journal of molecular sciences · 2023Review
- An Engineered OmpG Nanopore with Displayed Peptide Motifs for Single-Molecule Multiplex Protein Detection.Angewandte Chemie (International ed. in English) · 2023Article
- Fast slow folding of an outer membrane porin.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Modifying the pH sensitivity of OmpG nanopore for improved detection at acidic pH.Biophysical journal · 2022Article
- Recent advances in integrated solid-state nanopore sensors.Lab on a chip · 2021Review
- Correlation of membrane protein conformational and functional dynamics.Nature communications · 2021Article
- A pH-independent quiet OmpG pore with enhanced electrostatic repulsion among the extracellular loops.Biochimica et biophysica acta. Biomembranes · 2021Article
- Single molecule observation of hard-soft-acid-base (HSAB) interaction in engineeredChemical science · 2019Article
- Quiet Outer Membrane Protein G (OmpG) Nanopore for Biosensing.ACS sensors · 2019Article
- Engineering of protein nanopores for sequencing, chemical or protein sensing and disease diagnosis.Current opinion in biotechnology · 2018Review
- Mechanism of OmpG pH-Dependent Gating from Loop Ensemble and Single Channel Studies.Journal of the American Chemical Society · 2018Article
- Aberrantly Large Single-Channel Conductance of Polyhistidine Arm-Containing Protein Nanopores.Biochemistry · 2017Article
- Engineering a Novel Porin OmpGF Via Strand Replacement from Computational Analysis of Sequence Motif.Biochimica et biophysica acta. Biomembranes · 2017Article
- Tuning the selectivity and sensitivity of an OmpG nanopore sensor by adjusting ligand tether length.ACS sensors · 2016Article
- Global redesign of a native β-barrel scaffold.Biochimica et biophysica acta · 2016Article
- Selective Detection of Protein Homologues in Serum Using an OmpG Nanopore.Analytical chemistry · 2015Article
- Electrostatic Interactions between OmpG Nanopore and Analyte Protein Surface Can Distinguish between Glycosylated Isoforms.The journal of physical chemistry. B · 2015Article
- Quasithermodynamic contributions to the fluctuations of a protein nanopore.ACS chemical biology · 2015Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
Protein nanopores have attracted much interest for nucleic acid sequencing, chemical sensing, and protein folding at the single molecule level. The outer membrane protein OmpG from E. coli stands out because it forms a nanopore from a single polypeptide chain. This property allows the separate engineering of each of the seven extracellular loops that control access to the pore. The longest of these loops, loop 6, has been recognized as the main gating loop that closes the pore at low pH values and opens it at high pH values. A method was devised to pin each of the loops to the embedding membrane and measure the single-pore conductances of the resulting constructs. The electrophysiological and complementary NMR measurements show that the pinning of individual loops alters the structure and dynamics of neighboring and distant loops in a correlated fashion. Pinning loop 6 generates a constitutively open pore and patterns of concerted loop motions control access to the OmpG nanopore.
Indexed as
Identifiers
What OpenQuestion holds
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.