Evidence map›Paper›PMID 15111441›Full record

ArticleBiophysical journal2004

The effect of alpha-actinin on the length distribution of F-actin.

D Biron, E Moses

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

8 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Article
  3. Altered Actin Dynamics in Cell Migration of GNE Mutant Cells.Frontiers in cell and developmental biology · 2021
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. 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.

D BironDepartment of Physics of Complex Systems, Weizmann Institute of Science, Rehovot, Israel. david.biron@weizmann.ac.il
E Moses
Weizmann Institute of Science · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Actin filament length distribution in cells is often regulated to fit specific tasks. In comparison to the well-studied regulation of the average filament length (e.g., using capping proteins), controlling the width of the distribution is less well understood. We utilize two complementary methods to measure the effect of alpha-actinin on the width of the distribution of lengths of F-actin in vitro. Analyzing transmission electron micrographs shows that crosslinking by alpha-actinin reduces the width of the length distribution of F-actin, decreasing the coefficient of variation by two- to threefold. Analysis of fluorescence data from depolymerization assays confirms this observation. We suggest a mechanistic molecular model in which a local (weak) stabilization of crosslinked monomers in the filament is the physical origin of the decrease in the variance of lengths. Although alpha-actinin is known to bind reversibly to F-actin, our model shows that even weak binding can produce this effect, and that in fact it persists throughout a wide range of binding strengths.

Indexed as

Actin CytoskeletonActininActinsAnimalsBiophysicsCytoskeletonMicrofilament ProteinsMicroscopy, Electron, TransmissionModels, StatisticalModels, TheoreticalMuscle, SkeletalProtein BindingRabbitsTime FactorsActininActinsMicrofilament Proteins

Identifiers

PMID15111441
PMCPMC1304193
OpenAlexW2037554412

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.