Synthesis of Selectively

Darja I Rohden, Giorgia Toscano, Paul Schanda, Roman J Lichtenecker

Abstract read

In one paragraph

Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it

0cells of the map it votes in

1citing papers in PubMed

–field-weighted citation impact

1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

Bumps on the Road: The Way to Clean Relaxation Dispersion Magic-Angle Spinning NMR.Journal of the American Chemical Society · 2025
Article

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors.

Darja I RohdenFaculty of Chemistry, Institute of Organic Chemistry, University of Vienna, Währinger Str. 38, Vienna, 1090, Austria.

Giorgia ToscanoFaculty of Chemistry, Institute of Organic Chemistry, University of Vienna, Währinger Str. 38, Vienna, 1090, Austria.ORCID https://orcid.org/0000-0002-9712-5031

Paul SchandaInstitute of Science and Technology Austria, Am Campus 1, Klosterneuburg, 3400, Austria.ORCID https://orcid.org/0000-0002-9350-7606

Roman J LichteneckerFaculty of Chemistry, Institute of Organic Chemistry, University of Vienna, Währinger Str. 38, Vienna, 1090, Austria.ORCID https://orcid.org/0000-0003-2168-5216

Funding

Austrian Science Fund I5812-B

6 · The paper itself

Abstract

The charged arginine side chain is unique in determining many innate properties of proteins, contributing to stability and interaction surfaces, and directing allosteric regulation and enzymatic catalysis. NMR experiments can be used to reveal these processes at the molecular level, but it often requires selective insertion of carbon-13, nitrogen-15, and deuterium at defined atomic positions. We introduce a method to endow arginine residues with defined isotope patterns, combining synthetic organic chemistry and cell-based protein overexpression. The resulting proteins feature NMR active spin systems with optimized relaxation pathways leading to simplified NMR spectra with a sensitive response to changes in the chemical environment of the nuclei observed.

Indexed as

ArginineProteinsCarbon IsotopesDeuteriumMagnetic Resonance SpectroscopyNitrogen IsotopesNuclear Magnetic Resonance, BiomolecularProtein ConformationArginineCarbon-13Carbon IsotopesDeuteriumNitrogen-15Nitrogen IsotopesProteinsarginine labelingprotein interaction studiesprotein NMR spectroscopystable isotope labeling

Identifiers

PMID40080421

DOI10.1002/chem.202500408

PMCPMC12043044

What OpenQuestion holds

Textmetadata

LicenceCC BY

Read underepoch 390

Registered trials

None linked

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.