Evidence map›Paper›PMID 31836290›Full record

ReviewSeminars in cell & developmental biology2020

Towards a structural understanding of the remodeling of the actin cytoskeleton.

Felipe Merino, Sabrina Pospich, Stefan Raunser

Open access · hybridAbstract readReview
In one paragraph

Review in Seminars in cell & developmental biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
4.7field-weighted citation impact, top 5% 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

58 citing papers in PubMed, 107 citations in OpenAlex.

  1. Article
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  3. SiR-XActin: A Fluorescent Probe for Imaging Actin Dynamics in Live Cells.Angewandte Chemie (International ed. in English) · 2025
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  7. Mapping the interaction surface between CaNature communications · 2025
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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

3 authors at 1 institution in 1 country.

Felipe MerinoDepartment of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Dortmund, Germany.
Sabrina PospichDepartment of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Dortmund, Germany.
Stefan RaunserDepartment of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Dortmund, Germany. Electronic address: raunser@mpi-dortmund.mpg.de.
Max Planck Institute of Molecular Physiology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Actin filaments (F-actin) are a key component of eukaryotic cells. Whether serving as a scaffold for myosin or using their polymerization to push onto cellular components, their function is always related to force generation. To control and fine-tune force production, cells have a large array of actin-binding proteins (ABPs) dedicated to control every aspect of actin polymerization, filament localization, and their overall mechanical properties. Although great advances have been made in our biochemical understanding of the remodeling of the actin cytoskeleton, the structural basis of this process is still being deciphered. In this review, we summarize our current understanding of this process. We outline how ABPs control the nucleation and disassembly, and how these processes are affected by the nucleotide state of the filaments. In addition, we highlight recent advances in the understanding of actomyosin force generation, and describe recent advances brought forward by the developments of electron cryomicroscopy.

Indexed as

Actin CytoskeletonAnimalsHumansModels, MolecularMolecular StructureActinActin-based motilityActin-binding proteinActomyosinElectron cryomicroscopyMotor proteinMyosin

Identifiers

PMID31836290
PMCPMC7221352
OpenAlexW2994817058

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.