Evidence map›Paper›PMID 29314603›Full record

ReviewChemphyschem : a European journal of chemical physics and physical chemistry2018

Investigating Protein-Ligand Interactions by Solution Nuclear Magnetic Resonance Spectroscopy.

Walter Becker, Krishna Chaitanya Bhattiprolu, Nina Gubensäk, Klaus Zangger

Abstract readReview
In one paragraph

Review in Chemphyschem : a European journal of chemical physics and physical chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing 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

63 citing papers in PubMed.

  1. InNMR: DirectAnalytical chemistry · 2026
    Article
  2. Article
  3. Special Issue "Application of NMR Spectroscopy in Biomolecules".International journal of molecular sciences · 2026
    Article
  4. Article
  5. Immunoproteomics: The Evolution from Classical Methods to Emerging Techniques.Methods in molecular biology (Clifton, N.J.) · 2026
    Review
  6. Article
  7. Formulation insights into competitive binding of NJournal of pharmaceutical and biomedical analysis · 2025
    Article
  8. Article
  9. Article
  10. Article
  11. Investigation of structural and dynamic properties of the Butyrophilin BTN3A1/BTN2A1 cytoplasmic complex byFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Article
  12. Synthesis of aChembiochem : a European journal of chemical biology · 2025
    Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

3 more citing papers are in PubMed but not listed here.

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.

Walter BeckerInstitute of Chemistry, University of Graz, Heinrichstrasse 28, A-8010, Graz, Austria.
Krishna Chaitanya BhattiproluInstitute of Chemistry, University of Graz, Heinrichstrasse 28, A-8010, Graz, Austria.
Nina GubensäkInstitute of Chemistry, University of Graz, Heinrichstrasse 28, A-8010, Graz, Austria.
Klaus ZanggerInstitute of Chemistry, University of Graz, Heinrichstrasse 28, A-8010, Graz, Austria.ORCID 0000-0003-1682-1594

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein-ligand interactions are of fundamental importance in almost all processes in living organisms. The ligands comprise small molecules, drugs or biological macromolecules and their interaction strength varies over several orders of magnitude. Solution NMR spectroscopy offers a large repertoire of techniques to study such complexes. Here, we give an overview of the different NMR approaches available. The information they provide ranges from the simple information about the presence of binding or epitope mapping to the complete 3 D structure of the complex. NMR spectroscopy is particularly useful for the study of weak interactions and for the screening of binding ligands with atomic resolution.

Indexed as

LigandsAnimalsNuclear Magnetic Resonance, BiomolecularProtein BindingProteinsLigandsProteinschemical shift mappingnuclear magnetic resonancenuclear Overhauser effectprotein-ligand interactionssaturation-transfer difference

Identifiers

PMID29314603
PMCPMC5915746

What OpenQuestion holds

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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.