Evidence map›Paper›PMID 31861842›Full record

ReviewInternational journal of molecular sciences2019

Unconventional Myosins: How Regulation Meets Function.

Natalia Fili, Christopher P Toseland

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
5.2field-weighted citation impact, top 4% 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

33 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
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  10. Review
  11. Article
  12. Review
  13. UtilizingJournal of developmental biology · 2025
    Review
  14. Article
  15. Article
  16. Review
  17. Myosin in chromosome organisation and gene expression.Biochemical Society transactions · 2023
    Review
  18. Article
  19. Uncovering the Contributions of Charge Regulation to the Stability of Single Alpha Helices.Chemphyschem : a European journal of chemical physics and physical chemistry · 2023
    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

2 authors at 1 institution in 1 country.

Natalia FiliDepartment of Oncology and Metabolism, Medical School, University of Sheffield, Sheffield S10 2RX, UK.ORCID 0000-0002-0898-0766
Christopher P ToselandDepartment of Oncology and Metabolism, Medical School, University of Sheffield, Sheffield S10 2RX, UK.ORCID 0000-0002-1641-7535
University of Sheffield · GB

Funding

Medical Research Council MR/M020606/1Medical Research Council MR/M020606/2
6 · The paper itself

Abstract

Unconventional myosins are multi-potent molecular motors that are assigned important roles in fundamental cellular processes. Depending on their mechano-enzymatic properties and structural features, myosins fulfil their roles by acting as cargo transporters along the actin cytoskeleton, molecular anchors or tension sensors. In order to perform such a wide range of roles and modes of action, myosins need to be under tight regulation in time and space. This is achieved at multiple levels through diverse regulatory mechanisms: the alternative splicing of various isoforms, the interaction with their binding partners, their phosphorylation, their applied load and the composition of their local environment, such as ions and lipids. This review summarizes our current knowledge of how unconventional myosins are regulated, how these regulatory mechanisms can adapt to the specific features of a myosin and how they can converge with each other in order to ensure the required tight control of their function.

Indexed as

Alternative SplicingProtein Interaction MapsActinsAnimalsHumansMyosinsPhospholipidsPhosphorylationProtein IsoformsProtein MultimerizationActinsMyosinsPhospholipidsProtein Isoformsalternative splicinganchorsauto-inhibitionbinding partnerscargo recognitioncargo transportersdimerizationloadlocal environmentregulationunconventional myosins

Identifiers

PMID31861842
PMCPMC6981383
OpenAlexW2995334460

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.