Evidence map›Paper›PMID 37660224›Full record

ArticleCommunications biology2023

Crowding alters F-actin secondary structure and hydration.

Xiaobing Chen, Steven J Roeters, Francis Cavanna, José Alvarado, Carlos R Baiz

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

13 citing papers in PubMed, 12 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Label-Free Molecular Characterization of Protein Aggregates in Differentiated Astrocytes.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  6. Article
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  9. Disulfidptosis: A new type of cell death.Apoptosis : an international journal on programmed cell death · 2024
    Review
  10. Structural adaptability and surface activity of peptides derived from tardigrade proteins.Protein science : a publication of the Protein Society · 2024
    Article
  11. Article
  12. Silactins and Structural Diversity of Biosilica in Sponges.Biomimetics (Basel, Switzerland) · 2024
    Article
  13. Article
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 2 institutions in 3 countries.

Xiaobing ChenDepartment of Chemistry, University of Texas at Austin, Austin, TX, USA.ORCID http://orcid.org/0000-0002-6107-1713
Steven J RoetersDepartment of Chemistry, Aarhus University, Aarhus, Denmark.
Francis CavannaDepartment of Physics, University of Texas at Austin, Center for Nonlinear Dynamics, Austin, TX, USA.
José AlvaradoDepartment of Physics, University of Texas at Austin, Center for Nonlinear Dynamics, Austin, TX, USA.
Carlos R BaizDepartment of Chemistry, University of Texas at Austin, Austin, TX, USA. cbaiz@cm.utexas.edu.ORCID http://orcid.org/0000-0003-0699-8468
The University of Texas at Austin · USAarhus University · DK

Funding

Protein structure and dynamics in ultra-heterogeneous environments-RenewalR35GM133359 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI Carlos Raul Baiz · 2019 to 2026
$1.8M
NIGMS NIH HHS R35 GM133359
6 · The paper itself

Abstract

Actin, an important component of eukaryotic cell cytoskeleton, regulates cell shape and transport. The morphology and biochemical properties of actin filaments are determined by their structure and protein-protein contacts. Crowded environments can organize filaments into bundles, but less is known about how they affect F-actin structure. This study used 2D IR spectroscopy and spectral calculations to examine how crowding and bundling impact the secondary structure and local environments in filaments and weakly or strongly bundled networks. The results reveal that bundling induces changes in actin's secondary structure, leading to a decrease in β-sheet and an increase in loop conformations. Strongly bundled networks exhibit a decrease in backbone solvent exposure, with less perturbed α-helices and nearly "locked" β-sheets. Similarly, the loops become less hydrated but maintain a dynamic environment. These findings highlight the role of loop structure in actin network morphology and stability under morphology control by PEG.

Indexed as

Actin CytoskeletonActinsCell ShapeCytoskeletonProtein Structure, SecondaryActins

Identifiers

PMID37660224
PMCPMC10475093
OpenAlexW4386392547

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.