Evidence map›Paper›PMID 39340154›Full record

ArticleBiophysical journal2024

On the use of dioxane as reference for determination of the hydrodynamic radius by NMR spectroscopy.

Emil E Tranchant, Francesco Pesce, Nina L Jacobsen, Catarina B Fernandes, Birthe B Kragelund, Kresten Lindorff-Larsen

Abstract read
In one paragraph

Article in Biophysical journal, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. 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

6 authors.

Emil E TranchantStructural Biology and NMR Laboratory, The Linderstrøm-Lang Centre for Protein Science, University of Copenhagen, Copenhagen, Denmark; REPIN, Department of Biology, University of Copenhagen, Copenhagen, Denmark.
Francesco PesceStructural Biology and NMR Laboratory, The Linderstrøm-Lang Centre for Protein Science, University of Copenhagen, Copenhagen, Denmark.
Nina L JacobsenStructural Biology and NMR Laboratory, The Linderstrøm-Lang Centre for Protein Science, University of Copenhagen, Copenhagen, Denmark; REPIN, Department of Biology, University of Copenhagen, Copenhagen, Denmark.
Catarina B FernandesStructural Biology and NMR Laboratory, The Linderstrøm-Lang Centre for Protein Science, University of Copenhagen, Copenhagen, Denmark; REPIN, Department of Biology, University of Copenhagen, Copenhagen, Denmark.
Birthe B KragelundStructural Biology and NMR Laboratory, The Linderstrøm-Lang Centre for Protein Science, University of Copenhagen, Copenhagen, Denmark; REPIN, Department of Biology, University of Copenhagen, Copenhagen, Denmark. Electronic address: bbk@bio.ku.dk.
Kresten Lindorff-LarsenStructural Biology and NMR Laboratory, The Linderstrøm-Lang Centre for Protein Science, University of Copenhagen, Copenhagen, Denmark. Electronic address: lindorff@bio.ku.dk.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Measuring the compaction of a protein or complex is key to our understanding of the interactions within and between biomolecules. Experimentally, protein compaction is often probed either by estimating the radius of gyration (R

Indexed as

DioxanesHydrodynamicsDiffusionMagnetic Resonance SpectroscopyReference StandardsScattering, Small AngleX-Ray Diffraction1,4-dioxaneDioxanes

Identifiers

PMID39340154
PMCPMC11560309

What OpenQuestion holds

Textmetadata
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.