Evidence map›Paper›PMID 2642912›Full record

ArticleThe Journal of cell biology1989

The organization of myosin and actin in rapid frozen nerve growth cones.

P C Bridgman, M E Dailey

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
7.1field-weighted citation impact, top 2% 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

48 citing papers in PubMed, 212 citations in OpenAlex.

  1. Article
  2. Imaging Cytoskeleton Components by Electron Microscopy.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  3. Article
  4. Neurexin-1α regulates neurite growth of rat hippocampal neurons.International journal of physiology, pathophysiology and pharmacology · 2019
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Molecular motor proteins and amyotrophic lateral sclerosis.International journal of molecular sciences · 2011
    Review
  13. Phosphorylation of ezrin/radixin/moesin proteins by LRRK2 promotes the rearrangement of actin cytoskeleton in neuronal morphogenesis.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2009
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Myosin IIA drives neurite retraction.Molecular biology of the cell · 2003
    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

2 authors at 1 institution in 1 country.

P C BridgmanDepartment of Anatomy and Neurobiology, Washington University School of Medicine, St. Louis, Missouri 63110.
M E Dailey
Washington University in St. Louis · US

Funding

ULTRASTRUCTURE OF NEWLY-FORMED NERVE-MUSCLE SYNAPSES IN VITROP01NS015070 · NINDS · WASHINGTON UNIVERSITY · PI DAW, NIGEL W · 1985 to 1989
–
REGENERATION &FUNCTIONAL RECOVERY IN NEURAL TISSUEP50NS015070 · NINDS · WASHINGTON UNIVERSITY · PI DAW, NIGEL W · 1990 to 1990
–
NINDS NIH HHS NS15070
6 · The paper itself

Abstract

Rapid freezing and freeze substitution were used in conjunction with immunofluorescence, whole mount EM, and immunoelectron microscopy to study the organization of myosin and actin in growth cones of cultured rat superior cervical ganglion neurons. The general cytoplasmic organization was determined by whole mount EM; tight microfilament bundles formed the core of filopodia while a dense meshwork formed the underlying structure of lamellipodia. Although the central microtubule and organelle-rich region of the growth cone had fewer microfilaments, dense foci and bundles of microfilaments were usually observed. Anti-actin immunofluorescence and rhodamine phalloidin staining of f-actin both showed intense staining of filopodia and lamellipodia. In addition, staining of bundles and foci were observed in central regions suggesting that the majority of the microfilaments seen by whole mount EM are actin filaments. Anti-myosin immunofluorescence was brightest in the central region and usually had a punctate pattern. Although less intense, anti-myosin staining was also seen in peripheral regions; it was most prominent at the border with the central region, in portions of lamellipodia undergoing ruffling, and in spots along the shaft and at the base of filopodia. Immunoelectron microscopy of myosin using postembedment labeling with colloidal gold showed a similar distribution to that seen by immunofluorescence. Label was scattered throughout the growth cone, but present as distinct aggregates in the peripheral region mainly along the border with the central region. Less frequently, aggregates were also seen centrally and along the shaft and at the base of filopodia. This distribution is consistent with myosins involvement in the production of tension and movements of growth cone filopodia and lamellipodia that occur during active neurite elongation.

Indexed as

Actin CytoskeletonActinsAnimalsCells, CulturedCytoskeletonFluorescent Antibody TechniqueFreezingGanglia, SympatheticMicroscopy, ElectronMyosinsNeuronsPseudopodiaRatsActinsMyosins

Identifiers

PMID2642912
PMCPMC2115362
OpenAlexW2073368157

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.