Evidence map›Paper›PMID 35720262›Full record

ArticleiScience2022

Distinct actin-tropomyosin cofilament populations drive the functional diversification of cytoskeletal myosin motor complexes.

Theresia Reindl, Sven Giese, Johannes N Greve, Patrick Y Reinke, Igor Chizhov, Sharissa L Latham, Daniel P Mulvihill, Manuel H Taft, Dietmar J Manstein

Open access · goldAbstract read
In one paragraph

Article in iScience, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
5.4field-weighted citation impact, top 3% 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

19 citing papers in PubMed, 36 citations in OpenAlex.

  1. Kidney international reports · 2026
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  13. Structure, regulation, and mechanisms of nonmuscle myosin-2.Cellular and molecular life sciences : CMLS · 2024
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Non-muscle myosin II and the plasticity of 3D cell migration.Frontiers in cell and developmental biology · 2022
    Review
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 at 2 institutions in 2 countries.

Theresia ReindlInstitute for Biophysical Chemistry, Fritz-Hartmann-Centre for Medical Research, Hannover Medical School, 30625 Hannover, Germany.
Sven GieseInstitute for Biophysical Chemistry, Fritz-Hartmann-Centre for Medical Research, Hannover Medical School, 30625 Hannover, Germany.
Johannes N GreveInstitute for Biophysical Chemistry, Fritz-Hartmann-Centre for Medical Research, Hannover Medical School, 30625 Hannover, Germany.
Patrick Y ReinkeInstitute for Biophysical Chemistry, Fritz-Hartmann-Centre for Medical Research, Hannover Medical School, 30625 Hannover, Germany.
Igor ChizhovInstitute for Biophysical Chemistry, Fritz-Hartmann-Centre for Medical Research, Hannover Medical School, 30625 Hannover, Germany.
Sharissa L LathamInstitute for Biophysical Chemistry, Fritz-Hartmann-Centre for Medical Research, Hannover Medical School, 30625 Hannover, Germany.
Daniel P MulvihillSchool of Biosciences, University of Kent, CT2 7NJ Canterbury, UK.
Manuel H TaftInstitute for Biophysical Chemistry, Fritz-Hartmann-Centre for Medical Research, Hannover Medical School, 30625 Hannover, Germany.
Dietmar J MansteinInstitute for Biophysical Chemistry, Fritz-Hartmann-Centre for Medical Research, Hannover Medical School, 30625 Hannover, Germany.
Medizinische Hochschule Hannover · DEUniversity of Kent · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The effects of N-terminal acetylation of the high molecular weight tropomyosin isoforms Tpm1.6 and Tpm2.1 and the low molecular weight isoforms Tpm1.12, Tpm3.1, and Tpm4.2 on the actin affinity and the thermal stability of actin-tropomyosin cofilaments are described. Furthermore, we show how the exchange of cytoskeletal tropomyosin isoforms and their N-terminal acetylation affects the kinetic and chemomechanical properties of cytoskeletal actin-tropomyosin-myosin complexes. Our results reveal the extent to which the different actin-tropomyosin-myosin complexes differ in their kinetic and functional properties. The maximum sliding velocity of the actin filament as well as the optimal motor density for continuous unidirectional movement, parameters that were previously considered to be unique and invariant properties of each myosin isoform, are shown to be influenced by the exchange of the tropomyosin isoform and the N-terminal acetylation of tropomyosin.

Indexed as

BiochemistryBiological sciencesBiomoleculesBiophysicsProtein

Identifiers

PMID35720262
PMCPMC9204724
OpenAlexW4282021079

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.