Evidence map›Paper›PMID 36288901›Full record

ArticleLife science alliance2023

Actin-binding domain of Rng2 sparsely bound on F-actin strongly inhibits actin movement on myosin II.

Yuuki Hayakawa, Masak Takaine, Kien Xuan Ngo, Taiga Imai, Masafumi D Yamada, Arash Badami Behjat, Kenichi Umeda, Keiko Hirose, Ayhan Yurtsever, Noriyuki Kodera and 6 more

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Life science alliance, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

9 citing papers in PubMed, 22 citations in OpenAlex.

  1. Queue Gaps Among the IQGAPs inInternational journal of molecular sciences · 2026
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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

16 authors at 5 institutions in 1 country.

Yuuki HayakawaDepartment of Physics, Faculty of Science and Engineering, Graduate School of Waseda University, Shinjuku, Japan.
Masak TakaineDepartment of Biology, Degree Programs in Life and Earth Sciences, Graduate School of Science and Technology, University of Tsukuba, Tsukuba, Japan.ORCID 0000-0002-1279-9505
Kien Xuan NgoNano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kanazawa, Japan.ORCID 0000-0002-9710-5452
Taiga ImaiDepartment of Applied Sciences, Muroran Institute of Technology, Muroran, Japan.
Masafumi D YamadaBiomedical Research Institute, National Institute of Advanced Industrial Science and Technology, Tsukuba, Japan.
Arash Badami BehjatNano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kanazawa, Japan.
Kenichi UmedaNano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kanazawa, Japan.
Keiko HiroseDepartment of Biology, Degree Programs in Life and Earth Sciences, Graduate School of Science and Technology, University of Tsukuba, Tsukuba, Japan.ORCID 0000-0003-4587-8346
Ayhan YurtseverNano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kanazawa, Japan.
Noriyuki KoderaNano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kanazawa, Japan.ORCID 0000-0003-4880-8423
Kiyotaka TokurakuDepartment of Applied Sciences, Muroran Institute of Technology, Muroran, Japan.ORCID 0000-0002-7747-4808
Osamu NumataDepartment of Biology, Degree Programs in Life and Earth Sciences, Graduate School of Science and Technology, University of Tsukuba, Tsukuba, Japan.ORCID 0000-0001-8427-0371
Takeshi FukumaNano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kanazawa, Japan.ORCID 0000-0001-8971-6002
Toshio AndoNano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kanazawa, Japan.ORCID 0000-0001-8819-154X
Kentaro NakanoDepartment of Biology, Degree Programs in Life and Earth Sciences, Graduate School of Science and Technology, University of Tsukuba, Tsukuba, Japan t-uyeda@waseda.jp knakano@biol.tsukuba.ac.jp.ORCID 0000-0001-5100-1765
Taro Qp UyedaDepartment of Physics, Faculty of Science and Engineering, Graduate School of Waseda University, Shinjuku, Japan t-uyeda@waseda.jp knakano@biol.tsukuba.ac.jp.ORCID 0000-0002-3584-9499
Kanazawa University · JPUniversity of Tsukuba · JPMuroran Institute of Technology · JPNational Institute of Advanced Industrial Science and Technology · JPWaseda University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We report a case in which sub-stoichiometric binding of an actin-binding protein has profound structural and functional consequences, providing an insight into the fundamental properties of actin regulation. Rng2 is an IQGAP contained in contractile rings in the fission yeast

Indexed as

DictyosteliumSchizosaccharomycesActin CytoskeletonActinsActomyosinAdenosine DiphosphateCytoskeletal ProteinsMicrofilament ProteinsMyosin Type IISkeletal Muscle MyosinsActinsActomyosinAdenosine DiphosphateCytoskeletal ProteinsMicrofilament ProteinsMyosin Type IISkeletal Muscle Myosins

Identifiers

PMID36288901
PMCPMC9610768
OpenAlexW4307557780

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.