Evidence map›Paper›PMID 9560409›Full record

ArticleGenetics1998

Molecular genetic dissection of mouse unconventional myosin-VA: tail region mutations.

J D Huang, V Mermall, M C Strobel, L B Russell, M S Mooseker, N G Copeland, N A Jenkins

Erratum issuedAbstract read
In one paragraph

Article in Genetics, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing 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

40 citing papers in PubMed.

  1. Myosin-5a facilitates stress granule formation by interacting with G3BP1.Cellular and molecular life sciences : CMLS · 2024
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Unconventional Myosins: How Regulation Meets Function.International journal of molecular sciences · 2019
    Review
  7. Review
  8. Article
  9. Article
  10. Structural basis of myosin V Rab GTPase-dependent cargo recognition.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  11. Article
  12. Article
  13. Functions of class V myosins in neurons.The Journal of biological chemistry · 2013
    Review
  14. Structural basis of cargo recognitions for class V myosins.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  15. Article
  16. Full-length myosin Va exhibits altered gating during processive movement on actin.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  17. Myosin Va plays a key role in nitrergic neurotransmission by transporting nNOSα to enteric varicosity membrane.American journal of physiology. Gastrointestinal and liver physiology · 2011
    Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

7 authors.

J D HuangABL-Basic Research Program, NCI-Frederick Cancer Research and Development Center, Maryland 21702, USA.
V Mermall
M C Strobel
L B Russell
M S Mooseker
N G Copeland
N A Jenkins

Funding

Myosin Functions in the EnterocyteR01DK025387 · NIDDK · YALE UNIVERSITY · PI MOOSEKER, MARK S · 1986 to 2010
$3.6M
Myosin Functions in the EnterocyteR56DK025387 · NIDDK · YALE UNIVERSITY · PI MOOSEKER, MARK S · 2012 to 2012
$360k
CYTOSKELETAL STRUCTURE OF THE INTESTINAL BRUSH BORDERR37DK025387 · NIDDK · YALE UNIVERSITY · PI MOOSEKER, MARK S · 1992 to 1999
–
NIDDK NIH HHS DK-25387NIEHS NIH HHS 1-Y01-ES-50318-00
6 · The paper itself

Abstract

We used an RT-PCR-based sequencing approach to identify the mutations responsible for 17 viable dilute alleles, a mouse-coat-color locus encoding unconventional myosin-VA. Ten of the mutations mapped to the MyoVA tail and are reported here. These mutations represent the first extensive collection of tail mutations reported for any unconventional mammalian myosin. They identify sequences important for tail function and identify domains potentially involved in cargo binding and/or proper folding of the MyoVA tail. Our results also provide support for the notion that different myosin tail isoforms produced by alternative splicing encode important cell-type-specific functions.

Indexed as

MutagenesisMyosin Heavy ChainsMyosin Type VAnimalsBase SequenceDNAFemaleGene ExpressionIntermediate Filament ProteinsMaleMiceMice, Inbred C3HMice, Inbred C57BLMolecular Sequence DataRNA, MessengerSequence DeletionDNAIntermediate Filament ProteinsMyo5a protein, mouseMyosin Heavy ChainsMyosin Type VRNA, Messenger

Identifiers

PMID9560409
PMCPMC1460104

What OpenQuestion holds

Textmetadata
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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.