ArticleRNA (New York, N.Y.)2026
Integrated NMR/MD investigation reveals differences after reweighting in conformational ensembles of the GAAG and GCAA tetraloops.
David Leopold, Andreas Oxenfarth, F Emil Thomasen, Felix Kümmerer, Robbin Schnieders, György Pinter, Anna Wacker, Hendrik R A Jonker, Boris Fürtig, Christian Richter and 2 more
Abstract read
In one paragraphArticle in RNA (New York, N.Y.), 2026. 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
–field-weighted citation impact
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 registryThe 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 literatureWho cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
4 · The recordCorrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
5 · Who and what moneyAuthors and funding
12 authors.
David LeopoldInstitute for Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance (BMRZ), Goethe University Frankfurt am Main, Frankfurt/Main 60438, Germany.ORCID http://orcid.org/0000-0003-3250-3043 Andreas OxenfarthInstitute for Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance (BMRZ), Goethe University Frankfurt am Main, Frankfurt/Main 60438, Germany.ORCID http://orcid.org/0000-0001-6859-6849 F Emil ThomasenStructural Biology and NMR Laboratory, Linderstrøm-Lang Centre for Protein Science, Department of Biology, University of Copenhagen, Copenhagen N DK-2200, Denmark.ORCID http://orcid.org/0000-0002-2096-4873 Felix KümmererStructural Biology and NMR Laboratory, Linderstrøm-Lang Centre for Protein Science, Department of Biology, University of Copenhagen, Copenhagen N DK-2200, Denmark.ORCID http://orcid.org/0000-0002-4697-4658 Robbin SchniedersInstitute for Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance (BMRZ), Goethe University Frankfurt am Main, Frankfurt/Main 60438, Germany.
György PinterInstitute for Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance (BMRZ), Goethe University Frankfurt am Main, Frankfurt/Main 60438, Germany.ORCID http://orcid.org/0000-0001-6769-7277 Anna WackerInstitute for Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance (BMRZ), Goethe University Frankfurt am Main, Frankfurt/Main 60438, Germany.ORCID http://orcid.org/0000-0001-5892-5661 Hendrik R A JonkerInstitute for Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance (BMRZ), Goethe University Frankfurt am Main, Frankfurt/Main 60438, Germany.ORCID http://orcid.org/0000-0002-5582-3931 Boris FürtigInstitute for Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance (BMRZ), Goethe University Frankfurt am Main, Frankfurt/Main 60438, Germany.ORCID http://orcid.org/0000-0001-6443-7656 Christian RichterInstitute for Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance (BMRZ), Goethe University Frankfurt am Main, Frankfurt/Main 60438, Germany.ORCID http://orcid.org/0000-0002-5420-2826 Kresten Lindorff-LarsenStructural Biology and NMR Laboratory, Linderstrøm-Lang Centre for Protein Science, Department of Biology, University of Copenhagen, Copenhagen N DK-2200, Denmark lindorff@bio.ku.dk schwalbe@nmr.uni-frankfurt.de.ORCID http://orcid.org/0000-0002-4750-6039 Harald SchwalbeInstitute for Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance (BMRZ), Goethe University Frankfurt am Main, Frankfurt/Main 60438, Germany lindorff@bio.ku.dk schwalbe@nmr.uni-frankfurt.de.ORCID http://orcid.org/0000-0001-5693-7909 Funding
No grant is acknowledged in the PubMed record.
6 · The paper itselfAbstract
While the GNRA tetraloops are an extensively studied and common RNA motif, their dynamic NMR structures in solution integrating state-of-the-art NMR parameters such as residual dipolar couplings (RDC) and cross correlated relaxation rates (CCR) have previously not been determined. Given their dominant occurrence among tetraloops in the PDB and the advance of experimentally reweighted MD simulations, the present work aims at investigating the entire conformational space of two known tetraloop sequences by an extensive NMR investigation of NOEs,
Indexed as
Molecular Dynamics SimulationNucleic Acid ConformationRNAAlgorithmsBayes TheoremMagnetic Resonance SpectroscopyNuclear Magnetic Resonance, BiomolecularRNABayesian/maximum entropy reweightingmolecular dynamicsnuclear magnetic resonancesRNAtetraloop
Identifiers
PMID42215280
PMCPMC13374517
What Socratic holds
Textmetadata
LicenceCC BY
Read underepoch 390