Evidence map›Paper›PMID 7593166›Full record

ArticleThe Journal of cell biology1995

Sequences, structural models, and cellular localization of the actin-related proteins Arp2 and Arp3 from Acanthamoeba.

J F Kelleher, S J Atkinson, T D Pollard

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
10.4field-weighted citation impact, top 1% 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

60 citing papers in PubMed, 191 citations in OpenAlex.

  1. Article
  2. Article
  3. 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
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  8. Review
  9. Article
  10. The actin seed.Nature reviews. Molecular cell biology · 2016
    Article
  11. Article
  12. Article
  13. Review
  14. Purification of native Arp2/3 complex from bovine thymus.Methods in molecular biology (Clifton, N.J.) · 2013
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. 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.

J F KelleherDepartment of Cell Biology and Anatomy, Johns Hopkins Medical School, Baltimore, Maryland 21205, USA.
S J Atkinson
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
STRUCTURE/INTERACTIONS OF ACTINS &ACTIN-BINDING PROTEINR01GM035171 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI LATTMAN, EATON E · 1985 to 1995
–
NIGMS NIH HHS GM-26338NIGMS NIH HHS GM-35171
6 · The paper itself

Abstract

We cloned and sequenced the two actin-related proteins (Arps) present in the profilin-binding complex of Acanthamoeba (Machesky, L. M., S. J. Atkinson, C. Ampe, J. Vandekerckhove, and T. D. Pollard. 1994, J. Cell Biol. 127:107-115). The sequence of Arp2 is more similar to other Arp2s than to actin, while the sequence of Arp3 is more similar to other Arp3s than to actin. Phylogenetic analysis of all known Arps demonstrates that most group into three major families, which are likely to be shared across all eukaryotic phyla. Together with conventional actins, the Arps form a larger family distinct from structurally related ATPases such as Hsp70's and sugar kinases. Atomic models of the Arps based on their sequences and the structure of actin provide some clues about function. Both Arps have atoms appropriately placed to bind ATP and divalent cation. Arp2, but not Arp3, has a conserved profilin-binding site. Neither Arp has the residues required to copolymerize with actin, but an Arp heterodimer present in the profilin-binding complex might serve as a pointed end nucleus for actin polymerization. Both Acanthamoeba Arps are soluble in cell homogenates, and both are concentrated in the cortex of Acanthamoeba. The cellular concentrations are 1.9 microM Arp2 and 5.1 microM Arp3, substoichiometric to actin (200 microM) but comparable to many actin-binding proteins.

Indexed as

Cytoskeletal ProteinsAcanthamoebaActin-Related Protein 2Actin-Related Protein 3ActinsAmino Acid SequenceAnimalsCloning, MolecularCytoskeletonModels, MolecularMolecular Sequence DataPhylogenySequence AlignmentSequence AnalysisActin-Related Protein 2Actin-Related Protein 3ActinsCytoskeletal Proteins

Identifiers

PMID7593166
PMCPMC2199984
OpenAlexW1967955638

What OpenQuestion holds

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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.