ArticlePeerJ2018
NMR structure of the C-terminal domain of TonB protein from
Article in PeerJ, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 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
13 citing papers in PubMed.
- Gromacs MetaDump: a tool for extracting GROMACS simulation metadata.Journal of cheminformatics · 2025Article
- Molecular Dynamics of the Intrinsically Disordered Protein COR15A─A Force Field Validation on Structure and Dynamics.Journal of chemical theory and computation · 2025Article
- Quality Evaluation Based Simulation Selection (QEBSS) for analysis of conformational ensembles and dynamics of multidomain proteins.Communications chemistry · 2025Article
- Article
- The 100-protein NMR spectra dataset: A resource for biomolecular NMR data analysis.Scientific data · 2024Article
- The Name Is Barrel, β-Barrel.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Energization of Outer Membrane Transport by the ExbB ExbD Molecular Motor.Journal of bacteriology · 2023Review
- An Organ System-Based Synopsis ofVirulence · 2021Review
- The Effect ofFrontiers in microbiology · 2021Article
- Structure and Stoichiometry of the Ton Molecular Motor.International journal of molecular sciences · 2020Review
- NMR Structure and Dynamics of TonB Investigated by Scar-Less Segmental Isotopic Labeling Using a Salt-Inducible Split Intein.Frontiers in chemistry · 2020Article
- A TonB-dependent receptor constitutes the outer membrane transport system for a lignin-derived aromatic compound.Communications biology · 2019Article
- Rotational Dynamics of Proteins from Spin Relaxation Times and Molecular Dynamics Simulations.The journal of physical chemistry. B · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The TonB protein plays an essential role in the energy transduction system to drive active transport across the outer membrane (OM) using the proton-motive force of the cytoplasmic membrane of Gram-negative bacteria. The C-terminal domain (CTD) of TonB protein is known to interact with the conserved TonB box motif of TonB-dependent OM transporters, which likely induces structural changes in the OM transporters. Several distinct conformations of differently dissected CTDs of
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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.