Evidence map›Paper›PMID 42737465›Full record

ReviewInternational journal of molecular sciences2026

NMR Studies on Protein-Ligand Interactions.

Haiqin Yao, Ning Xu

Abstract readReview
In one paragraph

Review in International journal of molecular sciences, 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
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

2 authors.

Haiqin YaoSchool of Life Sciences, Tsinghua University, Beijing 100084, China.
Ning XuTechnology Center for Protein Sciences, Tsinghua University, Beijing 100084, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein-ligand interactions are fundamental to physiological processes and drug discovery. Based on the types of information on protein-ligand interactions provided by nuclear magnetic resonance (NMR) experiments, these NMR experiments can be categorized into three distinct classes: (i) molecular-level qualitative binding detection, (ii) residue-level mapping of binding interfaces, and (iii) atomic-level structure determination and conformational dynamics of protein-ligand complexes. This hierarchy enables a workflow that accelerates the progression from initial binding identification to structural and dynamic characterization. In this review, we discuss how these experiments characterize molecular recognition. Notably, the term "ligand" in this article refers exclusively to small molecules.

Indexed as

Nuclear Magnetic Resonance, BiomolecularProteinsBinding SitesHumansLigandsMagnetic Resonance SpectroscopyModels, MolecularProtein BindingProtein ConformationLigandsProteinsconformational dynamicsinterface mappingNMR screeningprotein–ligand interactionssolution structures

Identifiers

PMID42737465
PMCPMC13566631

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.