Evidence map›Paper›PMID 8022818›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1994

Identification and overlapping expression of multiple unconventional myosin genes in vertebrate cell types.

W M Bement, T Hasson, J A Wirth, R E Cheney, M S Mooseker

Erratum issuedOpen access · greenAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1994. 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 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
14.2field-weighted citation impact, top 1% 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

50 citing papers in PubMed, 159 citations in OpenAlex.

  1. Article
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  6. Article
  7. Calmodulin regulates dimerization, motility, and lipid binding of Leishmania myosin XXI.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
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  14. MARCKS and related chaperones bind to unconventional myosin V isoforms in airway epithelial cells.American journal of respiratory cell and molecular biology · 2010
    Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

W M BementDepartment of Biology, Yale University, New Haven, CT 06520-8103.
T Hasson
J A Wirth
R E Cheney
M S Mooseker
Yale University · US

Funding

Yale Liver CenterP30DK034989 · NIDDK · YALE UNIVERSITY · PI Chen Liu · 1986 to 2026
$31.1M
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
STRUCTURE AND FUNCTION OF THE RENAL EPITHELIAL CELL MEMBRANE SKELETONP01DK038979 · NIDDK · YALE UNIVERSITY · PI MORROW, JON S · 1987 to 1998
–
CYTOSKELETAL STRUCTURE OF THE INTESTINAL BRUSH BORDERR37DK025387 · NIDDK · YALE UNIVERSITY · PI MOOSEKER, MARK S · 1992 to 1999
–
NIDDK NIH HHS DK 25387NIDDK NIH HHS DK 34989NIDDK NIH HHS DK 38979
6 · The paper itself

Abstract

Myosin diversity in the human epithelial cell line Caco-2BBe, the porcine epithelial cell line LLC-PK1 (CL-4), human peripheral blood leukocytes, and human liver was analyzed. PCR amplification yielded 8-11 putative myosins (depending on the cDNA source) representing six distinct myosin classes. Analysis of clones obtained by hybridization screening demonstrated that the original PCR products correspond to bona fide myosins, based on the presence of sequences highly conserved in other myosins. RNase protection analysis confirmed mRNA expression of 11 myosins in Caco-2BBe cells. Immunoblot analysis showed that at least 6 myosin immunogens are expressed in Caco-2BBe cells. The results reveal the existence of at least 11 unconventional human myosin genes, most of which are expressed in an overlapping fashion in different cell types. The abundance of myosins suggests that the myosin I vs. myosin II paradigm is inadequate to explain actin-based cellular motility.

Indexed as

Consensus SequenceGene ExpressionAmino Acid SequenceAnimalsBase SequenceCell LineDNA PrimersEpitheliumGene LibraryHumansLeukocytesLiverMolecular Sequence DataMyosinsPolymerase Chain ReactionSequence Homology, Amino AcidDNA PrimersMyosins

Identifiers

PMID8022818
PMCPMC44240
OpenAlexW2076934291

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.