Evidence map›Paper›PMID 8369430›Full record

ArticleBiophysical journal1993

Affinity of alpha-actinin for actin determines the structure and mechanical properties of actin filament gels.

D H Wachsstock, W H Schwartz, T D Pollard

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 95 papers.

0numbers the graph read from it
0cells of the map it votes in
95citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

95 citing papers in PubMed, 235 citations in OpenAlex.

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  19. Calcium modulates the domain flexibility and function of an α-actinin similar to the ancestral α-actinin.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  20. Cell response to substrate rigidity is regulated by active and passive cytoskeletal stress.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article

35 more citing papers are in PubMed but not listed here.

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.

D H WachsstockDepartment of Cell Biology and Anatomy, Johns Hopkins University, Baltimore, Maryland 21205.
W H Schwartz
T D Pollard
Johns Hopkins University · US

Funding

MOLECULAR MECHANISMS OF CELLULAR MOTILITYR01GM026338 · NIGMS · YALE UNIVERSITY · PI POLLARD, THOMAS D. · 1985 to 2020
$9.8M
NIGMS NIH HHS GM-07309NIGMS NIH HHS GM-26338
6 · The paper itself

Abstract

Proteins that cross-link actin filaments can either form bundles of parallel filaments or isotropic networks of individual filaments. We have found that mixtures of actin filaments with alpha-actinin purified from either Acanthamoeba castellanii or chicken smooth muscle can form bundles or isotropic networks depending on their concentration. Low concentrations of alpha-actinin and actin filaments form networks indistinguishable in electron micrographs from gels of actin alone. Higher concentrations of alpha-actinin and actin filaments form bundles. The threshold for bundling depends on the affinity of the alpha-actinin for actin. The complex of Acanthamoeba alpha-actinin with actin filaments has a Kd of 4.7 microM and a bundling threshold of 0.1 microM; chicken smooth muscle has a Kd of 0.6 microM and a bundling threshold of 1 microM. The physical properties of isotropic networks of cross-linked actin filaments are very different from a gel of bundles: the network behaves like a solid because each actin filament is part of a single structure that encompasses all the filaments. Bundles of filaments behave more like a very viscous fluid because each bundle, while very long and stiff, can slip past other bundles. We have developed a computer model that predicts the bundling threshold based on four variables: the length of the actin filaments, the affinity of the alpha-actinin for actin, and the concentrations of actin and alpha-actinin.

Indexed as

AcanthamoebaActininActinsAnimalsBinding SitesBiomechanical PhenomenaBiophysical PhenomenaBiophysicsChickensComputer SimulationGelsIn Vitro TechniquesKineticsMicroscopy, ElectronModels, BiologicalMolecular StructureActininActinsGelsPolymers

Identifiers

PMID8369430
PMCPMC1225716
OpenAlexW2027949267

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.