Titin's Intrinsically Disordered PEVK Domain Modulates Actin Polymerization.

Áron Gellért Altorjay, Hedvig Tordai, Ádám Zolcsák, Nikoletta Kósa, Tamás Hegedűs, Miklós Kellermayer

Abstract read

In one paragraph

Article in International journal of molecular sciences, 2025. 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

6 authors.

Áron Gellért AltorjayDepartment of Biophysics and Radiaton Biology, Semmelweis University, 1085 Budapest, Hungary.ORCID 0000-0003-0288-4658

Hedvig TordaiDepartment of Biophysics and Radiaton Biology, Semmelweis University, 1085 Budapest, Hungary.

Ádám ZolcsákDepartment of Biophysics and Radiaton Biology, Semmelweis University, 1085 Budapest, Hungary.

Nikoletta KósaDepartment of Biophysics and Radiaton Biology, Semmelweis University, 1085 Budapest, Hungary.ORCID 0009-0007-0043-377X

Tamás HegedűsDepartment of Biophysics and Radiaton Biology, Semmelweis University, 1085 Budapest, Hungary.ORCID 0000-0002-5195-749X

Miklós KellermayerDepartment of Biophysics and Radiaton Biology, Semmelweis University, 1085 Budapest, Hungary.ORCID 0000-0002-5553-6553

Funding

Hungarian National Research, Development and Innovation Office K143321 and 150826Ministry for Innovation and Technology in Hungary 2020-4.1.1.-TKP2020

6 · The paper itself

Abstract

The multi-domain muscle protein titin provides elasticity and mechanosensing functions to the sarcomere. Titin's PEVK domain is intrinsically disordered due to the presence of a large number of prolines and highly charged residues. Although PEVK does not have canonical actin-binding motifs, it has been shown to bind F-actin. Here, we explored whether the PEVK domain may also affect actin assembly. We cloned the middle, 733-residue-long segment (called PEVKII) of the full-length PEVK domain, expressed in

Indexed as

ActinsConnectinIntrinsically Disordered ProteinsAnimalsHumansMicroscopy, Atomic ForcePolymerizationProtein BindingProtein DomainsActinsConnectinIntrinsically Disordered ProteinsTTN protein, humanactin paracrystalAlphaFoldatomic force microscopyintrinsically unstructured protein domainPEVKpolymerization assaypyrene actinsupported lipid bilayertitin

Identifiers

PMID40725251

DOI10.3390/ijms26147004

PMCPMC12295887

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.