Evidence map›Paper›PMID 1429838›Full record

ArticleThe Journal of cell biology1992

An unconventional myosin heavy chain gene from Drosophila melanogaster.

K A Kellerman, K G Miller

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

53 citing papers in PubMed, 145 citations in OpenAlex.

  1. Quantifying bristle cell organization inbioRxiv : the preprint server for biology · 2025
    Article
  2. Myosin VI is expressed in developing ovarian follicles inFrontiers in cell and developmental biology · 2025
    Article
  3. Functional Characterization of theInternational journal of molecular sciences · 2022
    Article
  4. Article
  5. Diverse functions of myosin VI in spermiogenesis.Histochemistry and cell biology · 2021
    Review
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  15. Proteomics approach to study the functions of Drosophila myosin VI through identification of multiple cargo-binding proteins.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Potential roles of myosin VI in cell motility.Biochemical Society transactions · 2009
    Review
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.

K A KellermanDepartment of Biology, Washington University, St. Louis, Missouri 63130.
K G Miller
Washington University in St. Louis · US

Funding

FUNCTION OF 95F UNCONVENTIONAL MYOSIN IN DROSOPHILAR01GM043607 · NIGMS · WASHINGTON UNIVERSITY · PI MILLER, KATHRYN G · 1995 to 1997
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ACTIN-BINDING PROTEINS AND DROSOPHILA EMBRYOSR29GM043607 · NIGMS · WASHINGTON UNIVERSITY · PI MILLER, KATHRYN G · 1990 to 1994
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NIGMS NIH HHS GM43607
6 · The paper itself

Abstract

As part of a study of cytoskeletal proteins involved in Drosophila embryonic development, we have undertaken the molecular analysis of a 140-kD ATP-sensitive actin-binding protein (Miller, K. G., C. M. Field, and B. M. Alberts. 1989. J. Cell Biol. 109:2963-2975). Analysis of cDNA clones encoding this protein revealed that it represents a new class of unconventional myosin heavy chains. The amino-terminal two thirds of the protein comprises a head domain that is 29-33% identical (60-65% similar) to other myosin heads, and contains ATP-binding, actin-binding and calmodulin/myosin light chain-binding motifs. The carboxy-terminal tail has no significant similarity to other known myosin tails, but does contain a approximately 100-amino acid region that is predicted to form an alpha-helical coiled-coil. Since the unique gene that encodes this protein maps to the polytene map position 95F, we have named the new gene Drosophila 95F myosin heavy chain (95F MHC). The expression profile of the 95F MHC gene is complex. Examination of multiple cDNAs reveals that transcripts are alternatively spliced and encode at least three protein isoforms; in addition, a fourth isoform is detected on Western blots. Developmental Northern and Western blots show that transcripts and protein are present throughout the life cycle, with peak expression occurring during mid-embryogenesis and adulthood. Immunolocalization in early embryos demonstrates that the protein is primarily located in a punctate pattern throughout the peripheral cytoplasm. Most cells maintain a low level of protein expression throughout embryogenesis, but specific tissues appear to contain more protein. We speculate that the 95F MHC protein isoforms are involved in multiple dynamic processes during Drosophila development.

Indexed as

Amino Acid SequenceAnimalsBase SequenceCloning, MolecularDNADrosophila melanogasterFluorescent Antibody TechniqueIn Situ HybridizationMolecular Sequence DataMyosinsRNA, MessengerSequence Analysis, DNADNAMyosinsRNA, Messenger

Identifiers

PMID1429838
PMCPMC2289692
OpenAlexW2017017186

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.