Evidence map›Paper›PMID 6682423›Full record

ArticleThe Journal of cell biology1983

Three-dimensional structure of actin filaments and of an actin gel made with actin-binding protein.

R Niederman, P C Amrein, J Hartwig

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1983. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
5.4field-weighted citation impact, top 4% 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

27 citing papers in PubMed, 119 citations in OpenAlex.

  1. Myosin-5a facilitates stress granule formation by interacting with G3BP1.Cellular and molecular life sciences : CMLS · 2024
    Article
  2. A Stop-gain Variant c.220C>T (p.(Gln74*)) inThe Yale journal of biology and medicine · 2023
    Review
  3. Review
  4. Article
  5. The mechanobiome: a goldmine for cancer therapeutics.American journal of physiology. Cell physiology · 2021
    Review
  6. Review
  7. Structural basis of filamin A functions.The Journal of cell biology · 2007
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Interaction of presenilins with the filamin family of actin-binding proteins.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1998
    Article
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  15. Article
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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

3 authors at 1 institution in 1 country.

R Niederman
P C Amrein
J Hartwig
Harvard University Press · US

Funding

PHAGOCYTOSIS--PULMONARY ALVEOLAR MACROPHAGESR01HL019429 · NHLBI · MASSACHUSETTS GENERAL HOSPITAL · PI STOSSEL, THOMAS PETER · 1985 to 2015
$10.1M
PHAGOCYTOSIS: PULMONARY ALVEOLAR MACROPHAGESR37HL019429 · NHLBI · MASSACHUSETTS GENERAL HOSPITAL · PI STOSSEL, THOMAS PETER · 1989 to 1998
–
NHLBI NIH HHS HL 19429NHLBI NIH HHS HL 27971NIDCR NIH HHS DE 06540
6 · The paper itself

Abstract

Purified muscle actin and mixtures of actin and actin-binding protein were examined in the transmission electron microscope after fixation, critical point drying, and rotary shadowing. The three-dimensional structure of the protein assemblies was analyzed by a computer-assisted graphic analysis applicable to generalized filament networks. This analysis yielded information concerning the frequency of filament intersections, the filament length between these intersections, the angle at which filaments branch at these intersections, and the concentration of filaments within a defined volume. Purified actin at a concentration of 1 mg/ml assembled into a uniform mass of long filaments which overlap at random angles between 0 degrees and 90 degrees. Actin in the presence of macrophage actin-binding protein assembled into short, straight filaments, organized in a perpendicular branching network. The distance between branch points was inversely related to the molar ratio of actin-binding protein to actin. This distance was what would be predicted if actin filaments grew at right angles off of nucleation sites on the two ends of actin-binding protein dimers, and then annealed. The results suggest that actin in combination with actin-binding protein self-assembles to form a three-dimensional network resembling the peripheral cytoskeleton of motile cells.

Indexed as

Microfilament ProteinsActinsAnimalsCarrier ProteinsCytoskeletonGelsolinMicrocomputersMicroscopy, ElectronModels, StructuralMusclesRabbitsActinsbrevinCarrier ProteinsGelsolinMicrofilament Proteins

Identifiers

PMID6682423
PMCPMC2112656
OpenAlexW2038049928

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.