ArticleNature protocols2014
In-cell ¹³C NMR spectroscopy for the study of intrinsically disordered proteins.
Article in Nature protocols, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 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
23 citing papers in PubMed, 57 citations in OpenAlex.
- Going high-throughput: Dynamic conformations and interactionsMagnetic resonance letters · 2027Review
- Toward a unified framework for determining conformational ensembles of disordered proteins.Nature methods · 2026Review
- OptimizedInternational journal of molecular sciences · 2025Article
- From molecular descriptions to cellular functions of intrinsically disordered protein regions.Biophysics reviews · 2024Review
- Combined H-N Cross-Polarization and Carbonyl Detection NMR Spectroscopy Allow to Record High-Resolution, High-Sensitivity Spectra of Alpha-Synuclein in Bacterial Cells.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Radio Signals from Live Cells: The Coming of Age of In-Cell Solution NMR.Chemical reviews · 2022Review
- Review
- Spotlight on the Ballet of Proteins: The Structural Dynamic Properties of Proteins Illuminated by Solution NMR.International journal of molecular sciences · 2020Review
- NMR Characterization of Surface Receptor Protein Interactions in Live Cells Using Methylcellulose Hydrogels.Angewandte Chemie (International ed. in English) · 2020Article
- Emerging solution NMR methods to illuminate the structural and dynamic properties of proteins.Current opinion in structural biology · 2019Review
- Residue-specific identification of phase separation hot spots of Alzheimer's-related protein tau.Chemical science · 2019Article
- Taking Simultaneous Snapshots of Intrinsically Disordered Proteins in Action.Biophysical journal · 2019Article
- Article
- Interaction proteomics by using in-cell NMR spectroscopy.Journal of proteomics · 2019Review
- Improved sensitivity and resolution of in-cell NMR spectra.Methods in enzymology · 2019Article
- MobiDB 3.0: more annotations for intrinsic disorder, conformational diversity and interactions in proteins.Nucleic acids research · 2018Article
- NMR of Macromolecular Assemblies and Machines at 1 GHz and Beyond: New Transformative Opportunities for Molecular Structural Biology.Methods in molecular biology (Clifton, N.J.) · 2018Review
- The PROSECCO server for chemical shift predictions in ordered and disordered proteins.Journal of biomolecular NMR · 2017Article
- Determining rotational dynamics of the guanidino group of arginine side chains in proteins by carbon-detected NMR.Chemical communications (Cambridge, England) · 2017Article
- Cancer/Testis Antigens: "Smart" Biomarkers for Diagnosis and Prognosis of Prostate and Other Cancers.International journal of molecular sciences · 2017Review
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 at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A large number of proteins carry out their function in highly flexible and disordered states, lacking a well-defined 3D structure. These proteins, referred to as intrinsically disordered proteins (IDPs), are now in the spotlight of modern structural biology. Nuclear magnetic resonance (NMR) spectroscopy represents a unique tool for accessing atomic resolution information on IDPs in complex environments as whole cells, provided that the methods are optimized to their peculiar properties and to the characteristics of in-cell experiments. We describe procedures for the preparation of in-cell NMR samples, as well as for the setup of NMR experiments and their application to in-cell studies, using human α-synuclein overexpressed in Escherichia coli as an example. The expressed protein is labeled with (13)C and (15)N stable isotopes to enable the direct recording of (13)C-detected NMR experiments optimized for the properties of IDPs. The entire procedure covers 24 h, including cell transformation, cell growth overnight, setup of the spectrometer and NMR experiment recording.
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.