ArticleJournal of biomolecular NMR2017
A
Article in Journal of biomolecular NMR, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 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
14 citing papers in PubMed.
- At the core of the interaction: Probing charged side chains in flexible protein regions with simultaneous nuclear magnetic resonance experiments.Protein science : a publication of the Protein Society · 2026Article
- Synthesis of SelectivelyChemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Guanidinium and amide CEST mapping of human brain by high spectral resolution CEST at 3 T.Magnetic resonance in medicine · 2023Article
- Review
- Isotope Effects on Chemical Shifts in the Study of Hydrogen Bonds in Small Molecules.Molecules (Basel, Switzerland) · 2022Review
- 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
- Nucleotide Binding Modes in a Motor Protein Revealed byChembiochem : a European journal of chemical biology · 2020Article
- More than Proton Detection-New Avenues for NMR Spectroscopy of RNA.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020Review
- NovelAngewandte Chemie (International ed. in English) · 2019Article
- Dynamic ion pair behavior stabilizes single α-helices in proteins.The Journal of biological chemistry · 2019Article
- The pKProtein science : a publication of the Protein Society · 2019Article
- Arginine Side-Chain Hydrogen Exchange: Quantifying Arginine Side-Chain Interactions in Solution.Chemphyschem : a European journal of chemical physics and physical chemistry · 2019Article
- Measuring the signs of the methylJournal of biomolecular NMR · 2018Article
- Article
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
Arginine side-chains are often key for enzyme catalysis, protein-ligand and protein-protein interactions. The importance of arginine stems from the ability of the terminal guanidinium group to form many key interactions, such as hydrogen bonds and salt bridges, as well as its perpetual positive charge. We present here an arginine
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.