ArticleFrontiers in molecular biosciences2014
Efficient and stable reconstitution of the ABC transporter BmrA for solid-state NMR studies.
Article in Frontiers in molecular biosciences, 2014. 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
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
13 citing papers in PubMed, 29 citations in OpenAlex.
- An in vitro set-up to study Pdr5-mediated substrate translocation.Protein science : a publication of the Protein Society · 2024Article
- 3D-Printable centrifugal devices for biomolecular solid state NMR rotors.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2023Article
- Solid-State NMR Reveals Asymmetric ATP Hydrolysis in the Multidrug ABC Transporter BmrA.Journal of the American Chemical Society · 2022Article
- Backbone NMR assignment of the nucleotide binding domain of the Bacillus subtilis ABC multidrug transporter BmrA in the post-hydrolysis state.Biomolecular NMR assignments · 2022Article
- Extensively sparseJournal of biomolecular NMR · 2021Article
- ATP Analogues for Structural Investigations: Case Studies of a DnaB Helicase and an ABC Transporter.Molecules (Basel, Switzerland) · 2020Review
- Proton-Detected Solid-State NMR of the Cell-Free Synthesized α-Helical Transmembrane Protein NS4B from Hepatitis C Virus.Chembiochem : a European journal of chemical biology · 2020Article
- Flexible-to-rigid transition is central for substrate transport in the ABC transporter BmrA fromCommunications biology · 2019Article
- Selective labeling and unlabeling strategies in protein solid-state NMR spectroscopy.Journal of biomolecular NMR · 2018Review
- Gradient reconstitution of membrane proteins for solid-state NMR studies.Journal of biomolecular NMR · 2017Article
- On the use of ultracentrifugal devices for routine sample preparation in biomolecular magic-angle-spinning NMR.Journal of biomolecular NMR · 2017Article
- Cell-free expression, purification, and membrane reconstitution for NMR studies of the nonstructural protein 4B from hepatitis C virus.Journal of biomolecular NMR · 2016Article
- The ABC exporter MsbA probed by solid state NMR – challenges and opportunities.Biological chemistry · 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
9 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We present solid-state NMR sample preparation and first 2D spectra of the Bacillus subtilis ATP-binding cassette (ABC) transporter BmrA, a membrane protein involved in multidrug resistance. The homodimeric 130-kDa protein is a challenge for structural characterization due to its membrane-bound nature, size, inherent flexibility and insolubility. We show that reconstitution of this protein in lipids from Bacillus subtilis at a lipid-protein ratio of 0.5 w/w allows for optimal protein insertion in lipid membranes with respect to two central NMR requirements, high signal-to-noise in the spectra and sample stability over a time period of months. The obtained spectra point to a well-folded protein and a highly homogenous preparation, as witnessed by the narrow resonance lines and the signal dispersion typical for the expected secondary structure distribution of BmrA. This opens the way for studies of the different conformational states of the transporter in the export cycle, as well as on interactions with substrates, via chemical-shift fingerprints and sequential resonance assignments.
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.