Evidence map›Paper›PMID 22343723›Full record

ArticleNature structural & molecular biology2012

A novel actin binding site of myosin required for effective muscle contraction.

Boglárka H Várkuti, Zhenhui Yang, Bálint Kintses, Péter Erdélyi, Irén Bárdos-Nagy, Attila L Kovács, Péter Hári, Miklós Kellermayer, Tibor Vellai, András Málnási-Csizmadia

Abstract read
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In one paragraph

Article in Nature structural & molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

43 citing papers in PubMed, 75 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Structure, regulation, and mechanisms of nonmuscle myosin-2.Cellular and molecular life sciences : CMLS · 2024
    Review
  7. Article
  8. Unconventional Myosins fromBiomolecules · 2022
    Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Actomyosin Complex.Sub-cellular biochemistry · 2022
    Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

10 authors at 2 institutions in 2 countries.

Boglárka H VárkutiDepartment of Biochemistry, Eötvös Loránd University, Budapest, Hungary.
Zhenhui Yang
Bálint Kintses
Péter Erdélyi
Irén Bárdos-Nagy
Attila L Kovács
Péter Hári
Miklós Kellermayer
Tibor Vellai
András Málnási-Csizmadia
Eötvös Loránd University · HUSemmelweis University · HU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

F-actin serves as a track for myosin's motor functions and activates its ATPase activity by several orders of magnitude, enabling actomyosin to produce effective force against load. Although actin activation is a ubiquitous property of all myosin isoforms, the molecular mechanism and physiological role of this activation are unclear. Here we describe a conserved actin-binding region of myosin named the 'activation loop', which interacts with the N-terminal segment of actin. We demonstrate by biochemical, biophysical and in vivo approaches using transgenic Caenorhabditis elegans strains that the interaction between the activation loop and actin accelerates the movement of the relay, stimulating myosin's ATPase activity. This interaction results in efficient force generation, but it is not essential for the unloaded motility. We conclude that the binding of actin to myosin's activation loop specifically increases the ratio of mechanically productive to futile myosin heads, leading to efficient muscle contraction.

Indexed as

Muscle ContractionActinsAnimalsBinding SitesCaenorhabditis elegansDictyosteliumMiceModels, MolecularMutationMyosinsProtein BindingProtein Interaction Domains and MotifsProtein Structure, QuaternaryActinsMyosins

Identifiers

PMID22343723
OpenAlexW2045464797

What OpenQuestion holds

Textmetadata
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.