Evidence map›Paper›PMID 29371682›Full record

ArticleScientific reports2018

Real-time TIRF observation of vinculin recruitment to stretched α-catenin by AFM.

Koichiro Maki, Sung-Woong Han, Yoshinori Hirano, Shigenobu Yonemura, Toshio Hakoshima, Taiji Adachi

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

15 citing papers in PubMed, 30 citations in OpenAlex.

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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

6 authors at 4 institutions in 2 countries.

Koichiro MakiLaboratory of Biomechanics, Department of Biosystems Science, Institute for Frontier Life and Medical Sciences, Kyoto University, 53 Shogoin-Kawahara-cho, Sakyo, Kyoto, 606-8507, Japan.
Sung-Woong HanNational Institute for Nanomaterials Technology, Pohang University of Science and Technology, 77 Cheongam-ro, Nam-Gu, Pohang, Gyeongbuk, 790-784, Korea.
Yoshinori HiranoStructural Biology Laboratory, Graduate School of Biological Sciences, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara, 630-0192, Japan.
Shigenobu YonemuraDepartment of Cell Biology, Graduate School of Medical Science, Tokushima University, 3-18-15 Kuramoto-cho, Tokushima, Tokushima, 770-8503, Japan.
Toshio HakoshimaStructural Biology Laboratory, Graduate School of Biological Sciences, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara, 630-0192, Japan.
Taiji AdachiLaboratory of Biomechanics, Department of Biosystems Science, Institute for Frontier Life and Medical Sciences, Kyoto University, 53 Shogoin-Kawahara-cho, Sakyo, Kyoto, 606-8507, Japan. adachi@frontier.kyoto-u.ac.jp.
Kyoto University · JPNara Institute of Science and Technology · JPPohang University of Science and Technology · KRTokushima University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Adherens junctions (AJs) adaptively change their intensities in response to intercellular tension; therefore, they integrate tension generated by individual cells to drive multicellular dynamics, such as morphogenetic change in embryos. Under intercellular tension, α-catenin, which is a component protein of AJs, acts as a mechano-chemical transducer to recruit vinculin to promote actin remodeling. Although in vivo and in vitro studies have suggested that α-catenin-mediated mechanotransduction is a dynamic molecular process, which involves a conformational change of α-catenin under tension to expose a cryptic vinculin binding site, there are no suitable experimental methods to directly explore the process. Therefore, in this study, we developed a novel system by combining atomic force microscopy (AFM) and total internal reflection fluorescence (TIRF). In this system, α-catenin molecules (residues 276-634; the mechano-sensitive M

Indexed as

FluorometryMicroscopy, Atomic Forcealpha CateninAnimalsMiceProtein BindingVinculinalpha CateninVinculin

Identifiers

PMID29371682
PMCPMC5785519
OpenAlexW2804103300

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.