Evidence map›Paper›PMID 37695902›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2023

Visualization of

Natsumi Hoshino, Takashi Kanadome, Tomomi Takasugi, Mizuho Itoh, Ryosuke Kaneko, Yukiko U Inoue, Takayoshi Inoue, Takahiro Hirabayashi, Masahiko Watanabe, Tomoki Matsuda and 3 more

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Review
  6. Article
  7. 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

13 authors.

Natsumi Hoshino *KOKORO-Biology Group, Graduate School of Frontier Biosciences, Osaka University, Suita, Osaka 565-0871, Japan.ORCID 0000-0002-2039-9755
Takashi Kanadome *Department of Biomolecular Science and Engineering, SANKEN, Osaka University, Ibaraki, Osaka 567-0047, Japan.
Tomomi TakasugiKOKORO-Biology Group, Graduate School of Frontier Biosciences, Osaka University, Suita, Osaka 565-0871, Japan.ORCID 0009-0000-8663-6373
Mizuho ItohKOKORO-Biology Group, Graduate School of Frontier Biosciences, Osaka University, Suita, Osaka 565-0871, Japan.
Ryosuke KanekoKOKORO-Biology Group, Graduate School of Frontier Biosciences, Osaka University, Suita, Osaka 565-0871, Japan.
Yukiko U InoueDepartment of Biochemistry and Cellular Biology, National Institute of Neuroscience, National Center of Neurology and Psychiatry, Tokyo 187-8501, Japan.ORCID 0000-0002-4105-9127
Takayoshi InoueDepartment of Biochemistry and Cellular Biology, National Institute of Neuroscience, National Center of Neurology and Psychiatry, Tokyo 187-8501, Japan.ORCID 0000-0001-7155-2150
Takahiro HirabayashiKOKORO-Biology Group, Graduate School of Frontier Biosciences, Osaka University, Suita, Osaka 565-0871, Japan.ORCID 0000-0002-1688-4029
Masahiko WatanabeDepartment of Anatomy, Faculty of Medicine, Hokkaido University, Sapporo, Hokkaido 060-8638, Japan.ORCID 0000-0001-5037-7138
Tomoki MatsudaDepartment of Biomolecular Science and Engineering, SANKEN, Osaka University, Ibaraki, Osaka 567-0047, Japan.
Takeharu NagaiDepartment of Biomolecular Science and Engineering, SANKEN, Osaka University, Ibaraki, Osaka 567-0047, Japan.ORCID 0000-0003-2650-9895
Etsuko TarusawaKOKORO-Biology Group, Graduate School of Frontier Biosciences, Osaka University, Suita, Osaka 565-0871, Japan.
Takeshi YagiKOKORO-Biology Group, Graduate School of Frontier Biosciences, Osaka University, Suita, Osaka 565-0871, Japan.

Funding

Epigenomic Regulation of a Large, Neuron-specific Chromatin DomainR01MH117790 · NIMH · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI AKBARIAN, SCHAHRAM · 2018 to 2022
$2.1M
NIMH NIH HHS R01 MH117790
6 · The paper itself

Abstract

Clustered protocadherin (Pcdh) functions as a cell recognition molecule through the homophilic interaction in the central nervous system. However, its interactions have not yet been visualized in neurons. We previously reported PcdhγB2-Förster resonance energy transfer (FRET) probes to be applicable only to cell lines. Herein, we designed γB2-FRET probes by fusing FRET donor and acceptor fluorescent proteins to a single γB2 molecule and succeeded in visualizing γB2 homophilic interaction in cultured hippocampal neurons. The γB2-FRET probe localized in the soma and neurites, and FRET signals, which were observed at contact sites between neurites, eliminated by ethylene glycol tetraacetic acid (EGTA) addition. Live imaging revealed that the FRET-negative γB2 signals rapidly moved along neurites and soma, whereas the FRET-positive signals remained in place. We observed that the γB2 proteins at synapses rarely interact homophilically. The γB2-FRET probe might allow us to elucidate the function of the homophilic interaction and the cell recognition mechanism.

Indexed as

NeuronsProtocadherinsCell BodyCell CommunicationNeuritesProtocadherinsclustered protocadherinFRETprotein–protein interactionself/non-self-recognitionsynapse

Identifiers

PMID37695902
PMCPMC10515168

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.