Evidence map›Paper›PMID 34782670›Full record

ArticleScientific reports2021

Development of FRET-based indicators for visualizing homophilic trans interaction of a clustered protocadherin.

Takashi Kanadome, Natsumi Hoshino, Takeharu Nagai, Tomoki Matsuda, Takeshi Yagi

Abstract read
In one paragraph

Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Review
  2. Article
  3. Visualization ofProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  4. Visualization ofiScience · 2023
    Article
  5. 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

5 authors.

Takashi Kanadome *Department of Biomolecular Science and Engineering, SANKEN (The Institute of Scientific and Industrial Research), Osaka University, 8-1 Mihogaoka, Ibaraki, 567-0047, Japan.
Natsumi Hoshino *KOKORO-Biology Group, Laboratories for Integrated Biology, Graduate School of Frontier Biosciences, Osaka University, Suita, 565-0871, Japan.
Takeharu NagaiDepartment of Biomolecular Science and Engineering, SANKEN (The Institute of Scientific and Industrial Research), Osaka University, 8-1 Mihogaoka, Ibaraki, 567-0047, Japan.
Tomoki MatsudaDepartment of Biomolecular Science and Engineering, SANKEN (The Institute of Scientific and Industrial Research), Osaka University, 8-1 Mihogaoka, Ibaraki, 567-0047, Japan. tmatsuda@sanken.osaka-u.ac.jp.
Takeshi YagiKOKORO-Biology Group, Laboratories for Integrated Biology, Graduate School of Frontier Biosciences, Osaka University, Suita, 565-0871, Japan. yagi@fbs.osaka-u.ac.jp.

Funding

Grant-in-Aid for Scientific Research on Innovative Areas "Integrated analysis and regulation of cellular diversity" No. 20H05035Grant-in-Aid for Scientific Research on Innovative Areas "Interplay of developmental clock and extracellular environment in brain formation" No. JP16H06487Grant-in-Aid for Scientific Research on Innovative Areas "Singularity biology" No. 18H05410JST CREST Program No. JPMJCR20E4JST PREST Program No. JPMJPR2045MEXT Grant-in-Aid for Scientific Research (A) from JSPS No. 18H04016
6 · The paper itself

Abstract

Clustered protocadherins (Pcdhs), which are cell adhesion molecules, play a fundamental role in self-recognition and non-self-discrimination by conferring diversity on the cell surface. Although systematic cell-based aggregation assays provide information regarding the binding properties of Pcdhs, direct visualization of Pcdh trans interactions across cells remains challenging. Here, we present Förster resonance energy transfer (FRET)-based indicators for directly visualizing Pcdh trans interactions. We developed the indicators by individually inserting FRET donor and acceptor fluorescent proteins (FPs) into the ectodomain of Pcdh molecules. They enabled successful visualization of specific trans interactions of Pcdh and revealed that the Pcdh trans interaction is highly sensitive to changes in extracellular Ca

Indexed as

Cell LineFluorescence Resonance Energy TransferHumansMolecular ImagingProtein BindingProtein Interaction Domains and MotifsProtein MultimerizationProtein TransportProtocadherinsProtocadherins

Identifiers

PMID34782670
PMCPMC8593154

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.