Evidence map›Paper›PMID 30229369›Full record

ArticleJournal of biomolecular NMR2018

Conformational exchange of aromatic side chains by

Heiner N Raum, Matthias Dreydoppel, Ulrich Weininger

Abstract read
In one paragraph

Article in Journal of biomolecular NMR, 2018. 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. Article
  3. Article
  4. Article
  5. Article
  6. Journal of biomolecular NMR · 2021
    Article
  7. Article
  8. Article
  9. Modulating Enzyme FunctionFrontiers in molecular biosciences · 2021
    Article
  10. Site-selectiveJournal of biomolecular NMR · 2019
    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

3 authors.

Heiner N RaumInstitute of Physics, Biophysics, Martin-Luther-University Halle-Wittenberg, 06120, Halle (Saale), Germany.
Matthias DreydoppelInstitute of Physics, Biophysics, Martin-Luther-University Halle-Wittenberg, 06120, Halle (Saale), Germany.
Ulrich WeiningerInstitute of Physics, Biophysics, Martin-Luther-University Halle-Wittenberg, 06120, Halle (Saale), Germany. ulrich.weininger@physik.uni-halle.de.ORCID http://orcid.org/0000-0003-0841-8332

Funding

Deutsche Forschungsgemeinschaft WE 5587/1-1
6 · The paper itself

Abstract

Aromatic side chains are attractive probes of protein dynamics on the millisecond time scale, because they are often key residues in enzyme active sites and protein binding sites. Further they allow to study specific processes, like histidine tautomerization and ring flips. Till now such processes have been studied by aromatic

Indexed as

Amino Acids, AromaticBacterial ProteinsKineticsNuclear Magnetic Resonance, BiomolecularProtein FoldingProteinsAmino Acids, AromaticBacterial Proteinscold-shock protein CspB, BacteriaProteinsAromatic side chainsConformational exchangeProtein dynamicsStrong couplings

Identifiers

PMID30229369
PMCPMC6209042

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.