Evidence map›Paper›PMID 39103163›Full record

ArticleJournal of the American Chemical Society2024

Proton Transfer Kinetics in Histidine Side Chains Determined by pH-Dependent Multi-Nuclear NMR Relaxation.

Heiner N Raum, Kristofer Modig, Mikael Akke, Ulrich Weininger

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Transition State Analysis of SAMHD1 from PrimaryJournal of the American Chemical Society · 2025
    Article
  10. Review
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.

Heiner N RaumInstitute of Physics, Biophysics, Martin-Luther-University Halle-Wittenberg, Halle (Saale) D-06120, Germany.
Kristofer ModigDivision of Biophysical Chemistry, Center for Molecular Protein Science, Department of Chemistry, Lund University, P.O. Box 124, Lund SE-22100, Sweden.
Mikael AkkeDivision of Biophysical Chemistry, Center for Molecular Protein Science, Department of Chemistry, Lund University, P.O. Box 124, Lund SE-22100, Sweden.ORCID 0000-0002-2395-825X
Ulrich WeiningerInstitute of Physics, Biophysics, Martin-Luther-University Halle-Wittenberg, Halle (Saale) D-06120, Germany.ORCID 0000-0003-0841-8332

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Histidine is a key amino-acid residue in proteins with unique properties engendered by its imidazole side chain that can exist in three different states: two different neutral tautomeric forms and a protonated, positively charged one with a p

Indexed as

HistidineProtonsHydrogen-Ion ConcentrationKineticsNuclear Magnetic Resonance, BiomolecularHistidineProtons

Identifiers

PMID39103163
PMCPMC11328173

What OpenQuestion holds

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LicenceCC BY-NC-ND
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.