Evidence map›Paper›PMID 7929556›Full record

ArticleThe Journal of cell biology1994

Purification of a cortical complex containing two unconventional actins from Acanthamoeba by affinity chromatography on profilin-agarose.

L M Machesky, S J Atkinson, C Ampe, J Vandekerckhove, T D Pollard

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 190 papers.

0numbers the graph read from it
0cells of the map it votes in
190citing papers in PubMed
5.7field-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

190 citing papers in PubMed, 495 citations in OpenAlex.

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  6. Arp2/3-mediated bidirectional actin assembly by SPIN90 dimers.Nature structural & molecular biology · 2025
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  7. Cryo-EM structure revealed a novel F-actin binding motif in abioRxiv : the preprint server for biology · 2025
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  8. Molecular mechanism of Arp2/3 complex activation by nucleation-promoting factors and an actin monomer.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  18. The WAVE complex drives the morphogenesis of the photoreceptor outer segment cilium.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  19. Article
  20. Article

130 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

5 authors at 2 institutions in 1 country.

L M MacheskyDepartment of Cell Biology and Anatomy, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.
S J Atkinson
C Ampe
J Vandekerckhove
T D Pollard
Johns Hopkins Medicine · USJohns 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-26338
6 · The paper itself

Abstract

We identified four polypeptides of 47, 44, 40, and 35 kD that bind to profilin-Sepharose and elute with high salt. When purified by conventional chromatography using an antibody to the 47-kD polypeptide, these four polypeptides copurified as a stoichiometric complex together with three additional polypeptides of 19, 18, and 13 kD that varied in their proportions to the other polypeptides. Partial protein sequences showed that the 47-kD polypeptide is a homologue of S. pombe act2 and the 44-kD polypeptide is a homologue of S. cerevisiae ACT2, both unconventional actins. The 40-kD polypeptide contains a sequence similar to the WD40 motif of the G beta subunit of a trimeric G-protein from Dictyostelium discoideum. From partial sequences, the 35-, 19-, and 18-kD polypeptides appear to be novel proteins. On gel filtration the complex of purified polypeptides cochromatograph with a Stokes' radius of 4.8 nm, a value consistent with a globular particle of 220 kD containing one copy of each polypeptide. Cell extracts also contain components of the complex that do not bind the profilin column. Affinity purified antibodies localize 47- and 18/19-kD polypeptides in the cortex and filopodia of Acanthamoeba. Antibodies to the 47-kD unconventional actin cross-react on immunoblots with polypeptides of similar size in Dictyostelium, rabbit muscle, and conventional preparations of rabbit muscle actin but do not react with actin.

Indexed as

Contractile ProteinsMicrofilament ProteinsAcanthamoebaActinsAmino Acid SequenceAnimalsAntibodies, ProtozoanChromatography, AffinityChromatography, Ion ExchangeFungal ProteinsGTP-Binding ProteinsMolecular Sequence DataMolecular WeightProfilinsProtozoan ProteinsSepharoseActinsAntibodies, ProtozoanContractile ProteinsFungal ProteinsGTP-Binding ProteinsMicrofilament ProteinsProfilinsProtozoan ProteinsSepharose

Identifiers

PMID7929556
PMCPMC2120189
OpenAlexW2118875203

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.