ArticleNature communications2019
Characterising side chains in large proteins by protonless
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 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
15 citing papers in PubMed.
- A combined NMR and deep neural network approach for enhancing the spectral resolution of aromatic side chains in proteins.Science advances · 2024Article
- Solution-state methyl NMR spectroscopy of large non-deuterated proteins enabled by deep neural networks.Nature communications · 2024Article
- Paramagnetic NMR to study iron sulfur proteins:Journal of biomolecular NMR · 2023Article
- The design of functional proteins using tensorized energy calculations.Cell reports methods · 2023Article
- Studying micro to millisecond protein dynamics using simple amideJournal of biomolecular NMR · 2023Article
- A rationally designed synthetic antimicrobial peptide against Pseudomonas-associated corneal keratitis: Structure-function correlation.Biophysical chemistry · 2022Article
- Review
- Large Chaperone Complexes Through the Lens of Nuclear Magnetic Resonance Spectroscopy.Annual review of biophysics · 2022Review
- Observation of Arginine Side-Chain Motions Coupled to the Global Conformational Exchange Process in Deubiquitinase A.ACS omega · 2022Article
- nightshift: A Python program for plotting simulated NMR spectra from assigned chemical shifts from the Biological Magnetic Resonance Data Bank.Protein science : a publication of the Protein Society · 2022Article
- 15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the µs-ms Timescale.Journal of visualized experiments : JoVE · 2021Article
- A CEST NMR experiment to obtain glycineJournal of biomolecular NMR · 2020Article
- Racemic phosphorothioate as a tool for NMR investigations of protein-DNA complexes.Journal of biomolecular NMR · 2020Article
- Multiquantum Chemical Exchange Saturation Transfer NMR to Quantify Symmetrical Exchange: Application to Rotational Dynamics of the Guanidinium Group in Arginine Side Chains.The journal of physical chemistry letters · 2020Article
- Intra-residue methyl-methyl correlations for valine and leucine residues in large proteins from a 3D-HMBC-HMQC experiment.Journal of biomolecular NMR · 2019Article
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
Side chains cover protein surfaces and are fundamental to processes as diverse as substrate recognition, protein folding and enzyme catalysis. However, characterisation of side-chain motions has so far been restricted to small proteins and methyl-bearing side chains. Here we present a class of methods, based on
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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.