Evidence map›Paper›PMID 7858134›Full record

ArticleBiophysical journal1994

Formation of two-dimensional complexes of F-actin and crosslinking proteins on lipid monolayers: demonstration of unipolar alpha-actinin-F-actin crosslinking.

K A Taylor, D W Taylor

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

28 citing papers in PubMed, 77 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Crosstalk between mechanotransduction and metabolism.Nature reviews. Molecular cell biology · 2021
    Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Adducin is required for desmosomal cohesion in keratinocytes.The Journal of biological chemistry · 2014
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. The 3D structure of villin as an unusual F-Actin crosslinker.Structure (London, England : 1993) · 2008
    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.

K A TaylorDepartment of Cell Biology, Duke University Medical Center, Durham, North Carolina 27710.
D W Taylor
Duke University · US

Funding

EM STUDIES ON MUSCLER01GM030598 · NIGMS · FLORIDA STATE UNIVERSITY · PI TAYLOR, KENNETH ALLEN · 1985 to 2020
$4.9M
NIGMS NIH HHS GM30598NIGMS NIH HHS R01 GM030598
6 · The paper itself

Abstract

A method is described for forming two-dimensional (2-D) paracrystalline complexes of F-actin and bundling/gelation proteins on positively charged lipid monolayers. These arrays facilitate detailed structural studies of protein interactions with F-actin by eliminating superposition effects present in 3-D bundles. Bundles of F-actin have been produced using the glycolytic enzymes aldolase and glyceraldehyde-3-phosphate dehydrogenase, the cytoskeletal protein erythrocyte adducin as well as smooth muscle alpha-actinin from chicken gizzard. All of the 2-D bundles formed contain F-actin with a 13/6 helical structure. F-actin-aldolase bundles have an interfilament spacing of 12.6 nm and a superlattice arrangement of actin filaments that can be explained by expression of a local twofold axis in the neighborhood of the aldolase. Well ordered F-actin-alpha-actinin 2-D bundles have an interfilament spacing of 36 nm and contain crosslinks 33 nm in length angled approximately 25-35 degrees to the filament axis. Images and optical diffraction patterns of these bundles suggest that they consist of parallel, unipolar arrays of actin filaments. This observation is consistent with an actin crosslinking function at adhesion plaques where actin filaments are bound to the cell membrane with uniform polarity.

Indexed as

ActininActinsAdducinsAnimalsBiophysical PhenomenaBiophysicsCalmodulin-Binding ProteinsChickensCross-Linking ReagentsFructose-Bisphosphate AldolaseGlyceraldehyde-3-Phosphate DehydrogenasesIn Vitro TechniquesLipidsMacromolecular SubstancesMicroscopy, ElectronPolymersActininActinsAdducinsCalmodulin-Binding ProteinsCross-Linking ReagentsFructose-Bisphosphate AldolaseGlyceraldehyde-3-Phosphate DehydrogenasesLipidsMacromolecular SubstancesPolymers

Identifiers

PMID7858134
PMCPMC1225572
OpenAlexW2015535115

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.