Evidence map›Paper›PMID 21687988›Full record

ArticleCellular and molecular life sciences : CMLS2012

Functional characterization of the human myosin-7a motor domain.

Sarah M Heissler, Dietmar J Manstein

Open access · hybridAbstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.8field-weighted citation impact, top 14% 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

27 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Functional Role of Class III Myosins in Hair Cells.Frontiers in cell and developmental biology · 2021
    Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Review
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  12. Article
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  14. Article
  15. Article
  16. Review
  17. Various Themes of Myosin Regulation.Journal of molecular biology · 2016
    Review
  18. Article
  19. Review
  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.

Sarah M HeisslerInstitut für Biophysikalische Chemie, Medizinische Hochschule Hannover, Hannover, Germany. sarah.heissler@nih.gov
Dietmar J Manstein
Medizinische Hochschule Hannover · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Myosin-7a participates in auditory and visual processes. Defects in MYO7A, the gene encoding the myosin-7a heavy chain, are causative for Usher syndrome 1B, the most frequent cause of deaf-blindness in humans. In the present study, we performed a detailed kinetic and functional characterization of the isolated human myosin-7a motor domain to elucidate the details of chemomechanical coupling and the regulation of motor function. A rate-limiting, slow ADP release step causes long lifetimes of strong actin-binding intermediates and results in a high duty ratio. Moreover, our results reveal a Mg(2+)-sensitive regulatory mechanism tuning the kinetic and mechanical properties of the myosin-7a motor domain. We obtained direct evidence that changes in the concentration of free Mg(2+) ions affect the motor properties of human myosin-7a using an in vitro motility assay system. Our results suggest that in a cellular environment, compartment-specific fluctuations in free Mg(2+) ions can mediate the conditional switching of myosin-7a between cargo moving and tension bearing modes.

Indexed as

ActinsAdenosine DiphosphateHumansMagnesiumMyosinsMyosin VIIaActinsAdenosine DiphosphateMagnesiumMYO7A protein, humanMyosinsMyosin VIIa

Identifiers

PMID21687988
PMCPMC3249170
OpenAlexW2004084261

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.