Evidence map›Paper›PMID 36937586›Full record

ArticleChemical science2023

Hysteresis behavior in the unfolding/refolding processes of a protein trapped in metallo-cages.

Takahiro Nakama, Anouk Rossen, Risa Ebihara, Maho Yagi-Utsumi, Daishi Fujita, Koichi Kato, Sota Sato, Makoto Fujita

Open access · diamondAbstract read
In one paragraph

Article in Chemical science, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

4 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Article
  3. Enzyme Immobilization in Porous Crystals via Cage Encapsulation.Angewandte Chemie (International ed. in English) · 2025
    Article
  4. 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

8 authors at 4 institutions in 1 country.

Takahiro NakamaDepartment of Applied Chemistry, Graduate School of Engineering, The University of Tokyo 7-3-1 Hongo Bunkyo-ku Tokyo 113-8656 Japan mfujita@appchem.t.u-tokyo.ac.jp.ORCID https://orcid.org/0000-0002-1023-7090
Anouk RossenDepartment of Applied Chemistry, Graduate School of Engineering, The University of Tokyo 7-3-1 Hongo Bunkyo-ku Tokyo 113-8656 Japan mfujita@appchem.t.u-tokyo.ac.jp.ORCID https://orcid.org/0000-0002-8896-3068
Risa EbiharaDepartment of Applied Chemistry, Graduate School of Engineering, The University of Tokyo 7-3-1 Hongo Bunkyo-ku Tokyo 113-8656 Japan mfujita@appchem.t.u-tokyo.ac.jp.ORCID https://orcid.org/0000-0002-3499-6921
Maho Yagi-UtsumiInstitute for Molecular Science (IMS) 5-1 Higashiyama, Myodaiji Okazaki Aichi 444-8787 Japan.ORCID https://orcid.org/0000-0001-8144-740X
Daishi FujitaInstitute for Integrated Cell-Material Sciences (iCeMS), Institute for Advanced Study, Kyoto University Yoshida, Sakyo-ku Kyoto 606-8501 Japan.ORCID https://orcid.org/0000-0001-5726-0645
Koichi KatoInstitute for Molecular Science (IMS) 5-1 Higashiyama, Myodaiji Okazaki Aichi 444-8787 Japan.ORCID https://orcid.org/0000-0001-7187-9612
Sota SatoDepartment of Applied Chemistry, Graduate School of Engineering, The University of Tokyo 7-3-1 Hongo Bunkyo-ku Tokyo 113-8656 Japan mfujita@appchem.t.u-tokyo.ac.jp.ORCID https://orcid.org/0000-0002-7395-2112
Makoto FujitaDepartment of Applied Chemistry, Graduate School of Engineering, The University of Tokyo 7-3-1 Hongo Bunkyo-ku Tokyo 113-8656 Japan mfujita@appchem.t.u-tokyo.ac.jp.ORCID https://orcid.org/0000-0001-6105-7340
The University of Tokyo · JPNational Institutes of Natural Sciences · JPInstitute for Molecular Science · JPKyoto University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Confinement of molecules in a synthetic host can physically isolate even their unstable temporary structures, which has potential for application to protein transient structure analysis. Here we report the NMR snapshot observation of protein unfolding and refolding processes by confining a target protein in a self-assembled coordination cage. With increasing acetonitrile content in CD

Identifiers

PMID36937586
PMCPMC10016334
OpenAlexW4321505866

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.