Evidence map›Paper›PMID 8449985›Full record

ArticleThe Journal of cell biology1993

Identification, characterization and cloning of myr 1, a mammalian myosin-I.

C Ruppert, R Kroschewski, M Bähler

Abstract readComparative Study
In one paragraph

Article in The Journal of cell biology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing 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

41 citing papers in PubMed.

  1. Oncogenic role and potential mechanisms of MYO1B in breast cancer.In vitro cellular & developmental biology. Animal · 2026
    Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Unconventional Myosins: How Regulation Meets Function.International journal of molecular sciences · 2019
    Review
  7. Myosin-I molecular motors at a glance.Journal of cell science · 2016
    Review
  8. Article
  9. Review
  10. Review
  11. Principles of unconventional myosin function and targeting.Annual review of cell and developmental biology · 2011
    Review
  12. Article
  13. Control of myosin-I force sensing by alternative splicing.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  14. Myosin I can act as a molecular force sensor.Science (New York, N.Y.) · 2008
    Article
  15. Article
  16. Article
  17. Article
  18. A model of stereocilia adaptation based on single molecule mechanical studies of myosin I.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2004
    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

3 authors.

C RuppertFriedrich-Miescher Laboratorium, Max-Planck-Gesellschaft, Tübingen, Germany.
R Kroschewski
M Bähler

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have identified, characterized and cloned a novel mammalian myosin-I motor-molecule, called myr 1 (myosin-I from rat). Myr 1 exists in three alternative splice forms: myr 1a, myr 1b, and myr 1c. These splice forms differ in their numbers of putative calmodulin/light chain binding sites. Myr 1a-c were selectively released by ATP, bound in a nucleotide-dependent manner to F-actin and exhibited amino acid sequences characteristic of myosin-I motor domains. In addition to the motor domain, they contained a regulatory domain with up to six putative calmodulin/light chain binding sites and a tail domain. The tail domain exhibited 47% amino acid sequence identity to the brush border myosin-I tail domain, demonstrating that myr 1 is related to the only other mammalian myosin-I motor molecule that has been characterized so far. In contrast to brush border myosin-I which is expressed in mature enterocytes, myr 1 splice forms were differentially expressed in all tested tissues. Therefore, myr 1 is the first mammalian myosin-I motor molecule with a widespread tissue distribution in neonatal and adult tissues. The myr 1a splice form was preferentially expressed in neuronal tissues. Its expression was developmentally regulated during rat forebrain ontogeny and subcellular fractionation revealed an enrichment in purified growth cone particles, data consistent with a role for myr 1a in neuronal development.

Indexed as

ActinsAdenosine TriphosphateAlternative SplicingAmino Acid SequenceAnimalsAntibodiesBase SequenceBinding SitesCalmodulinChickensCloning, MolecularDNAGene LibraryLiverMolecular Sequence DataMyosinsActinsAdenosine TriphosphateAntibodiesCalmodulinDNAMyosinsPeptides

Identifiers

PMID8449985
PMCPMC2119751

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.