Evidence map›Paper›PMID 41806920›Full record

ArticleBiochimica et biophysica acta. Proteins and proteomics2026

Localization and functional exploration of leiomodin-2's C-terminal binding sites.

Mason D Summers, Madison Little, Robert P Young, Brayan Osegueda, Alan Palma Guillen, Garry E Smith, John R Cort, Vitold E Galkin, Alla S Kostyukova

Abstract read
In one paragraph

Article in Biochimica et biophysica acta. Proteins and proteomics, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

9 authors.

Mason D SummersVoiland School of Chemical Engineering and Bioengineering, Washington State University, Pullman, WA, United States of America.
Madison LittleVoiland School of Chemical Engineering and Bioengineering, Washington State University, Pullman, WA, United States of America.
Robert P YoungEarth and Biological Sciences Directorate, Pacific Northwest National Laboratory, Richland, WA, United States of America.
Brayan OseguedaVoiland School of Chemical Engineering and Bioengineering, Washington State University, Pullman, WA, United States of America.
Alan Palma GuillenVoiland School of Chemical Engineering and Bioengineering, Washington State University, Pullman, WA, United States of America.
Garry E SmithVoiland School of Chemical Engineering and Bioengineering, Washington State University, Pullman, WA, United States of America.
John R CortEarth and Biological Sciences Directorate, Pacific Northwest National Laboratory, Richland, WA, United States of America; Institute of Biological Chemistry, Washington State University, Pullman, WA, United States of America.
Vitold E GalkinDepartment of Biomedical and Translational Science, Macon & Joan Brock Virginia Health Sciences at Old Dominion University, Norfolk, VA, United States of America.
Alla S KostyukovaVoiland School of Chemical Engineering and Bioengineering, Washington State University, Pullman, WA, United States of America. Electronic address: alla.kostyukova@wsu.edu.

Funding

REGULATION OF THE ACTIN FILAMENT POINTED END DYNAMICS IN HEALTH AND DISEASER01GM120137 · NIGMS · WASHINGTON STATE UNIVERSITY · PI GALKIN, VITOLD, GREGORIO, CAROL C · 2017 to 2024
$4.0M
Training in Biotechnology: Emphasis in Protein ChemistryT32GM152310 · NIGMS · WASHINGTON STATE UNIVERSITY · PI Bernd Markus Lange · 2024 to 2026
$1.6M
MARC at Washington State UniversityT34GM141971 · NIGMS · WASHINGTON STATE UNIVERSITY · PI GIZERIAN, SAMANTHA, KOSTYUKOVA, ALLA S. · 2021 to 2025
$1.3M
Motivating Innovation and Research Achievement (MIRA)R25EB027606 · NIBIB · WASHINGTON STATE UNIVERSITY · PI Samantha Gizerian, Alla S. Kostyukova · 2020 to 2026
$1.2M
NIBIB NIH HHS R25 EB027606NIGMS NIH HHS R01 GM120137NIGMS NIH HHS T32 GM152310NIGMS NIH HHS T34 GM141971
6 · The paper itself

Abstract

Striated muscle contraction occurs through interactions between overlapping myosin-based thick and actin-based thin filaments within the sarcomere. For effective contraction to occur, the length of the thin filament must be maintained to ensure sufficient overlap with the thick filament. The proteins leiomodin and tropomodulin compete for binding at the pointed ends of thin filaments to regulate their length, using their homologous N-terminal actin and tropomyosin binding sites. Leiomodin also contains a region called the C-terminal extension, absent in tropomodulin. In this region, the cardiac isoform (leiomodin-2) contains additional actin-binding sites that enable it to bind along the sides of thin filaments in a Ca

Indexed as

Cytoskeletal ProteinsMicrofilament ProteinsMuscle ProteinsActin CytoskeletonActinsAnimalsBinding SitesMagnetic Resonance SpectroscopyNuclear Magnetic Resonance, BiomolecularPeptidesProtein BindingActinsCytoskeletal Proteinsleiomodin protein, mouseMicrofilament ProteinsMuscle ProteinsPeptidespolyprolineCo-sedimentation assaysLeiomodin-2Nuclear magnetic resonancePoly-proline regionProfilinThin filamentWiskott-Aldrich homology 2 domain

Identifiers

PMID41806920
PMCPMC13292838

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.