Evidence map›Paper›PMID 32567727›Full record

ArticleThe EMBO journal2020

Structural insights into actin filament recognition by commonly used cellular actin markers.

Archana Kumari, Shubham Kesarwani, Manjunath G Javoor, Kutti R Vinothkumar, Minhajuddin Sirajuddin

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
6.2field-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

63 citing papers in PubMed, 104 citations in OpenAlex.

  1. Article
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  9. Article
  10. Review
  11. Cryo-EM structure revealed a novel F-actin binding motif in abioRxiv : the preprint server for biology · 2025
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  13. Effect of Retinal on Dictyostelium Cells During Development.Genes to cells : devoted to molecular & cellular mechanisms · 2025
    Article
  14. Mapping the interaction surface between CaNature communications · 2025
    Article
  15. Article
  16. Structure of the F-tractin-F-actin complex.The Journal of cell biology · 2025
    Article
  17. Article
  18. Article
  19. Article
  20. Review

3 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 3 institutions in 1 country.

Archana KumariCenter for Cardiovascular Biology and Diseases, Institute for Stem Cell Science and Regenerative Medicine, Bengaluru, India.
Shubham KesarwaniCenter for Cardiovascular Biology and Diseases, Institute for Stem Cell Science and Regenerative Medicine, Bengaluru, India.
Manjunath G JavoorCenter for Cardiovascular Biology and Diseases, Institute for Stem Cell Science and Regenerative Medicine, Bengaluru, India.
Kutti R VinothkumarNational Center for Biological Sciences, TIFR, Bengaluru, India.
Minhajuddin SirajuddinCenter for Cardiovascular Biology and Diseases, Institute for Stem Cell Science and Regenerative Medicine, Bengaluru, India.ORCID 0000-0001-5742-2130
Institute for Stem Cell Biology and Regenerative Medicine · INManipal Academy of Higher Education · INNational Centre for Biological Sciences · IN

Funding

Central Imaging and Flow Facility (CIFF)Department of Biotechnology, Ministry of Science and Technology (DBT) DBT/PR12422/MED/31/287/2014Department of Biotechnology, Ministry of Science and Technology (DBT) RA-40796915460European Molecular Biology Organization (EMBO)Indo-French Centre for the Promotion of Advanced Research (IFCPAR) 5703-1NCBS-TIFR/DAEScience and Engineering Research Board (SERB) SB/S2/RJN-094/2017The Wellcome Trust DBT India Alliance (India Alliance) IA/I/14/2/501533Wellcome Trust
6 · The paper itself

Abstract

Cellular studies of filamentous actin (F-actin) processes commonly utilize fluorescent versions of toxins, peptides, and proteins that bind actin. While the choice of these markers has been largely based on availability and ease, there is a severe dearth of structural data for an informed judgment in employing suitable F-actin markers for a particular requirement. Here, we describe the electron cryomicroscopy structures of phalloidin, lifeAct, and utrophin bound to F-actin, providing a comprehensive high-resolution structural comparison of widely used actin markers and their influence towards F-actin. Our results show that phalloidin binding does not induce specific conformational change and lifeAct specifically recognizes closed D-loop conformation, i.e., ADP-Pi or ADP states of F-actin. The structural models aided designing of minimal utrophin and a shorter lifeAct, which can be utilized as F-actin marker. Together, our study provides a structural perspective, where the binding sites of utrophin and lifeAct overlap with majority of actin-binding proteins and thus offering an invaluable resource for researchers in choosing appropriate actin markers and generating new marker variants.

Indexed as

Models, MolecularActinsCryoelectron MicroscopyHumansActinsactin cytoskeletoncellular markerscryoEMlifeActphalloidin

Identifiers

PMID32567727
PMCPMC7360965
OpenAlexW3035970226

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.