ArticleScientific reports2026
Atomistic insights into the magnetic-field modulation of the [Formula: see text] adenosine receptor.
Article in Scientific reports, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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.
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.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pulsed electromagnetic fields (PEMFs) are increasingly used in clinical settings for the treatment of inflammatory and degenerative conditions. Among their molecular targets, [Formula: see text] adenosine receptors ([Formula: see text]) show increased receptor density on the cell membrane upon PEMF exposure, yet the underlying physical mechanism remains uncertain. In this study, atomistic molecular dynamics simulations were used to investigate how an external static magnetic field, used as a simplified representation of the quasi-static magnetic component of PEMF exposure, influences the structure and electrostatics of the [Formula: see text]. Our simulations revealed that the field predominantly affects the receptor's extracellular region, resulting in a transition from a closed to a more open conformation of the ligand-entry region. This structural rearrangement was accompanied by widening and increased hydration of the extracellular entrance, indicating enhanced accessibility of the orthosteric binding site. At residue level, Glu169, Ala265, and Pro266 exhibited pronounced dipole reorientation, indicating localized electrostatic adaptation consistent with the structural response. Together, these findings provide an atomistic insight into how magnetic perturbations can influence [Formula: see text] extracellular dynamics and offer a mechanistic framework compatible with experimental observations of altered [Formula: see text] function under PEMF exposure.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.