Evidence map›Paper›PMID 37217486›Full record

ArticleNature communications2023

Nonthermal acceleration of protein hydration by sub-terahertz irradiation.

Jun-Ichi Sugiyama, Yuji Tokunaga, Mafumi Hishida, Masahito Tanaka, Koh Takeuchi, Daisuke Satoh, Masahiko Imashimizu

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
3.9field-weighted citation impact, top 6% of its field
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

14 citing papers in PubMed, 30 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Changes in Water Dynamics by Osmolytes Regulate Enzyme Activity.The journal of physical chemistry. B · 2026
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Advances in Terahertz Biophysics and Chemistry.Research (Washington, D.C.) · 2025
    Review
  12. Review
  13. Article
  14. 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

7 authors at 3 institutions in 1 country.

Jun-Ichi Sugiyama *Nanomaterials Research Institute, National Institute of Advanced Industrial Science and Technology, Tsukuba, 305-8565, Japan.ORCID 0000-0001-5477-2637
Yuji Tokunaga *Graduate School of Pharmaceutical Sciences, The University of Tokyo, Hongo, Bunkyo, Tokyo, 113-0033, Japan.ORCID 0000-0002-8774-9780
Mafumi Hishida *Department of Chemistry, Faculty of Pure and Applied Sciences, University of Tsukuba, Tsukuba, Ibaraki, 305-8571, Japan.
Masahito TanakaResearch Institute for Measurement and Analytical Instrumentation, National Institute of Advanced Industrial Science and Technology, Tsukuba, 305-8568, Japan.ORCID 0000-0003-3869-0919
Koh TakeuchiGraduate School of Pharmaceutical Sciences, The University of Tokyo, Hongo, Bunkyo, Tokyo, 113-0033, Japan.ORCID 0000-0002-6227-4627
Daisuke SatohResearch Institute for Measurement and Analytical Instrumentation, National Institute of Advanced Industrial Science and Technology, Tsukuba, 305-8568, Japan.ORCID 0000-0003-4120-8062
Masahiko ImashimizuCellular and Molecular Biotechnology Research Institute, National Institute of Advanced Industrial Science and Technology, Tsukuba, 305-8565, Japan. m.imashimizu@aist.go.jp.ORCID 0000-0003-4891-5034
National Institute of Advanced Industrial Science and Technology · JPThe University of Tokyo · JPUniversity of Tsukuba · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The collective intermolecular dynamics of protein and water molecules, which overlap in the sub-terahertz (THz) frequency region, are relevant for expressing protein functions but remain largely unknown. This study used dielectric relaxation (DR) measurements to investigate how externally applied sub-THz electromagnetic fields perturb the rapid collective dynamics and influence the considerably slower chemical processes in protein-water systems. We analyzed an aqueous lysozyme solution, whose hydration is not thermally equilibrated. By detecting time-lapse differences in microwave DR, we demonstrated that sub-THz irradiation gradually decreases the dielectric permittivity of the lysozyme solution by reducing the orientational polarization of water molecules. Comprehensive analysis combining THz and nuclear magnetic resonance spectroscopies suggested that the gradual decrease in the dielectric permittivity is not induced by heating but is due to a slow shift toward the hydrophobic hydration structure in lysozyme. Our findings can be used to investigate hydration-mediated protein functions based on sub-THz irradiation.

Indexed as

MuramidaseProteinsChemical PhenomenaWaterMuramidaseProteinsWater

Identifiers

PMID37217486
PMCPMC10203368
OpenAlexW4377291777

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.