Evidence map›Paper›PMID 25642645›Full record

ArticleeLife2015

Cofilin-induced unidirectional cooperative conformational changes in actin filaments revealed by high-speed atomic force microscopy.

Kien Xuan Ngo, Noriyuki Kodera, Eisaku Katayama, Toshio Ando, Taro Q P Uyeda

Open access · goldAbstract read
In one paragraph

Article in eLife, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing papers in PubMed
7.4field-weighted citation impact, top 2% 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

85 citing papers in PubMed, 170 citations in OpenAlex.

  1. Myosin II-independent contraction of actin filaments in membrane nanotubes.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  10. The Baraitser-Winter Cerebrofrontofacial Syndrome Recurrent R196H Variant in Cytoplasmic β-Actin Impairs Its Cellular Polymerization and Stability.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
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25 more citing papers are in PubMed but not listed here.

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 at 5 institutions in 1 country.

Kien Xuan NgoBiomedical Research Institute, National Institute of Advanced Industrial Science and Technology, Tsukuba, Japan.
Noriyuki KoderaDepartment of Physics and Bio-AFM Frontier Research Center, Kanazawa University, Kanazawa, Japan.
Eisaku KatayamaDepartment of Biology, Graduate School of Science, Osaka City University, Osaka, Japan.
Toshio AndoDepartment of Physics and Bio-AFM Frontier Research Center, Kanazawa University, Kanazawa, Japan.
Taro Q P UyedaBiomedical Research Institute, National Institute of Advanced Industrial Science and Technology, Tsukuba, Japan.
Japan Science and Technology Agency · JPKanazawa University · JPNational Institute of Advanced Industrial Science and Technology · JPOsaka City University · JPUniversity of Tsukuba · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

High-speed atomic force microscopy was employed to observe structural changes in actin filaments induced by cofilin binding. Consistent with previous electron and fluorescence microscopic studies, cofilin formed clusters along actin filaments, where the filaments were 2-nm thicker and the helical pitch was ~25% shorter, compared to control filaments. Interestingly, the shortened helical pitch was propagated to the neighboring bare zone on the pointed-end side of the cluster, while the pitch on the barbed-end side was similar to the control. Thus, cofilin clusters induce distinctively asymmetric conformational changes in filaments. Consistent with the idea that cofilin favors actin structures with a shorter helical pitch, cofilin clusters grew unidirectionally toward the pointed-end of the filament. Severing was often observed near the boundaries between bare zones and clusters, but not necessarily at the boundaries.

Indexed as

Actin CytoskeletonActin Depolymerizing FactorsAnimalsDictyosteliumHumansLipid BilayersMicroscopy, Atomic ForceProtein BindingProtein Structure, SecondaryRabbitsRecombinant Fusion ProteinsActin Depolymerizing FactorsLipid BilayersRecombinant Fusion Proteinsactinbiochemistrybiophysicscofilincooperative conformational changedictyosteliumhumanmyosinS. cerevisiaestructural biology

Identifiers

PMID25642645
PMCPMC4337605
OpenAlexW2167431292

What OpenQuestion holds

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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.