Evidence map›Paper›PMID 8486738›Full record

ArticleThe Journal of cell biology1993

Flightin, a novel myofibrillar protein of Drosophila stretch-activated muscles.

J O Vigoreaux, J D Saide, K Valgeirsdottir, M L Pardue

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 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing 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

55 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Two Forms of Thick Filament in the Flight Muscle ofInternational journal of molecular sciences · 2024
    Article
  6. Molecular Characterization and Phylogenetic Analysis of Flightin Gene inAnimals : an open access journal from MDPI · 2024
    Article
  7. Structure of theInternational journal of molecular sciences · 2023
    Article
  8. John Squire and the myosin thick filament structure in muscle.Journal of muscle research and cell motility · 2023
    Review
  9. Structure of the Flight Muscle Thick Filament from the Bumble Bee,International journal of molecular sciences · 2022
    Article
  10. Article
  11. The Mechanisms of Thin Filament Assembly and Length Regulation in Muscles.International journal of molecular sciences · 2022
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. CryoEM structure ofLife science alliance · 2020
    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

4 authors.

J O VigoreauxDepartment of Biology, Massachusetts Institute of Technology, Cambridge 02139.
J D Saide
K Valgeirsdottir
M L Pardue

Funding

ASSEMBLY OF THE Z-BAND IN DROSOPHILA FLIGHT MUSCLER01AR038615 · NIAMS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI SAIDE, JUDITH D · 1987 to 1989
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GENE EXPRESSION IN DROSOPHILAR01GM021874 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI PARDUE, MARY-LOU · 1985 to 1994
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GENETIC STUDIES ON AN UNUSUAL RNA CODING GENE, HSR-OMEGAR21GM021874 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI PARDUE, MARY-LOU · 1997 to 1998
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NIAMS NIH HHS AR38615NIGMS NIH HHS GM21874
6 · The paper itself

Abstract

The indirect flight muscles of Drosophila are adapted for rapid oscillatory movements which depend on properties of the contractile apparatus itself. Flight muscles are stretch activated and the frequency of contraction in these muscles is independent of the rate of nerve impulses. Little is known about the molecular basis of these adaptations. We now report a novel protein that is found only in flight muscles and has, therefore, been named flightin. Although we detect only one gene (in polytene region 76D) for flightin, this protein has several isoforms (relative gel mobilities, 27-30 kD; pIs, 4.6-6.0). These isoforms appear to be created by posttranslational modifications. A subset of these isoforms is absent in newly emerged adults but appears when the adult develops the ability to fly. In intact muscles flightin is associated with the A band of the sarcomere, where evidence suggests it interacts with the myosin filaments. Computer database searches do not reveal extensive similarity to any known protein. However, the NH2-terminal 12 residues show similarity to the NH2-terminal sequence of actin, a region that interacts with myosin. These features suggest a role for flightin in the regulation of contraction, possibly by modulating actin-myosin interaction.

Indexed as

ActinsAmino Acid SequenceAnimalsBase SequenceDrosophila melanogasterDrosophila ProteinsFilaminsFlight, AnimalMolecular Sequence DataMuscle ContractionMuscle ProteinsMyosinsProtein Processing, Post-TranslationalActinsDrosophila ProteinsFilaminsfln protein, DrosophilaMuscle ProteinsMyosins

Identifiers

PMID8486738
PMCPMC2119567

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.