Detecting and Characterizing Interactions of Metabolites with Proteins by Saturation Transfer Difference Nuclear Magnetic Resonance (STD NMR) Spectroscopy.

Ruslan Nedielkov, Heiko M Möller

Abstract read

In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it

0cells of the map it votes in

0citing papers in PubMed

1.0field-weighted citation impact, top 24% of its field

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

0 citing papers in PubMed, 2 citations in OpenAlex.

No citing paper in PubMed yet.

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

2 authors at 1 institution in 1 country.

Ruslan NedielkovUniversity of Potsdam, Institute for Chemistry, Potsdam, Germany. ruslan.nedielkov@uni-potsdam.de.

Heiko M MöllerUniversity of Potsdam, Institute for Chemistry, Potsdam, Germany.

University of Potsdam · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Saturation transfer difference (STD) nuclear magnetic resonance (NMR) spectroscopy is an established technique for detecting and characterizing the binding of small molecules, such as metabolites, to biological macromolecules like proteins and nucleic acids. STD NMR allows detection of binding in complex mixtures of potential ligands, which is often used for library screening in the pharmaceutical industry but may also be beneficial for binding studies with metabolite mixtures. The nature of the ligand is normally restricted to small molecules in terms of NMR spectroscopy, and the size of the macromolecule on the other side should be larger than 10-15 kDa. This technique is especially applicable to detecting binders of intermediate to low affinity with the dissociation constant (K

Indexed as

Biological ProductsNucleic AcidsVibrio choleraeComplex MixturesLigandsMagnetic Resonance SpectroscopyNADNuclear Magnetic Resonance, BiomolecularOxidoreductasesProtein BindingProteinsUbiquinoneBiological ProductsComplex MixturesLigandsNADNucleic AcidsOxidoreductasesProteinsUbiquinoneEpitope mappingLigand-based NMRNa+-transporting NADH:ubiquinone oxidoreductase (Na+-NQR)Nuclear magnetic resonance (NMR)Protein-metabolite interactionsSaturation transfer difference (STD)Ubiquinone-1

Identifiers

PMID36178624

DOI10.1016/j.jmr.2009.11.015

OpenAlexW4298086897

What OpenQuestion holds

Textmetadata

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Registered trials

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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.