Evidence map›Paper›PMID 41533445›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2026

Multiple modes of AFM reveal distinct mechanical properties for dystrophin and utrophin not manifest by small fragments.

Cailong Hua, Joseph Vavra, Jacob Powers, Joseph M Muretta, James M Ervasti, Murti V Salapaka

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Multiple modes of AFM reveal distinct mechanical properties for dystrophin and utrophin not manifest by small fragments.Proceedings of the National Academy of Sciences of the United States of America · 2026
    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

6 authors.

Cailong HuaDepartment of Electrical and Computer Engineering, University of Minnesota - Twin Cities, Minneapolis, MN 55455.ORCID 0000-0001-8793-3548
Joseph VavraDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota - Twin Cities, Minneapolis, MN 55455.
Jacob PowersDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota - Twin Cities, Minneapolis, MN 55455.
Joseph M MurettaDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota - Twin Cities, Minneapolis, MN 55455.
James M ErvastiDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota - Twin Cities, Minneapolis, MN 55455.ORCID 0000-0001-8259-5236
Murti V SalapakaDepartment of Electrical and Computer Engineering, University of Minnesota - Twin Cities, Minneapolis, MN 55455.ORCID 0000-0002-4595-9683

Funding

CYTOSKELETAL INTERACTIONS OF DYSTROPHINR01AR042423 · NIAMS · UNIVERSITY OF WISCONSIN MADISON · PI ERVASTI, JAMES M · 1994 to 2025
$9.3M
HHS | NIH | National Institute of Arthritis and Musculoskeletal and Skin Diseases (NIAMS) 5R01AR042423NIAMS NIH HHS R01 AR042423
6 · The paper itself

Abstract

Duchenne muscular dystrophy (DMD) is a lethal muscle disease caused by the absence of the protein dystrophin. Dystrophin is hypothesized to work as a molecular shock absorber that limits myofiber membrane damage when undergoing reversible unfolding upon muscle stretching and contraction. Here, we report the mechanical characterization of single full-length dystrophin (Dys) molecules using two operational modes of atomic force microscopy; constant speed and constant force as well as Monte Carlo simulations. Furthermore, we have compared Dys with large fragments encoding the N-terminus through spectrin repeat 10 (DysN-R10), the C-terminal retinal isoform of dystrophin (Dp260), and full-length utrophin (Utr). Our comprehensive data reveal that Dys, DysN-R10, and Dp260, all show a uniform, brittle unfolding behavior, whereas Utr demonstrates more complex unfolding dominated by a stiffening spring behavior. These fundamentally different mechanical behaviors in vitro suggest different in vivo functions for Dys and Utr with implications for the potential efficacy of Utr upregulation to substitute for Dys deficiency in DMD.

Indexed as

DystrophinMicroscopy, Atomic ForceUtrophinBiomechanical PhenomenaHumansMonte Carlo MethodMuscular Dystrophy, DuchenneDystrophinUtrophinconstant speed and constant force experimentsdystrophinforce spectroscopymechanical propertiesutrophin

Identifiers

PMID41533445
PMCPMC12818407

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.