Evidence map›Paper›PMID 7518465›Full record

ArticleThe Journal of cell biology1994

Ultrastructural analysis of the dynactin complex: an actin-related protein is a component of a filament that resembles F-actin.

D A Schafer, S R Gill, J A Cooper, J E Heuser, T A Schroer

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 119 papers.

0numbers the graph read from it
0cells of the map it votes in
119citing papers in PubMed
8.0field-weighted citation impact, top 2% 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

119 citing papers in PubMed, 277 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. VezA/vezatin facilitates proper assembly of the dynactin complex in vivo.bioRxiv : the preprint server for biology · 2024
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Cargo-Mediated Activation of Cytoplasmic DyneinFrontiers in cell and developmental biology · 2020
    Review
  16. Article
  17. Nuclear movement in fungi.Seminars in cell & developmental biology · 2018
    Review
  18. Article
  19. Article
  20. Article

59 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 1 institution in 1 country.

D A SchaferDepartment of Biology, Johns Hopkins University, Baltimore, Maryland 21218.
S R Gill
J A Cooper
J E Heuser
T A Schroer
Johns Hopkins University · US

Funding

Molecular Mechanisms in Actin Assembly &Cell MotilityR01GM038542 · NIGMS · WASHINGTON UNIVERSITY · PI COOPER, JOHN A · 1989 to 2013
$7.4M
STRUCTURAL ANALYSIS OF CLATHRIN-MEDIATED ENDOCYTOSISR01GM029647 · NIGMS · WASHINGTON UNIVERSITY · PI HEUSER, JOHN EDWARD · 1985 to 2008
$4.8M
REGULATION OF CYTOPLASMIC DYNEIN-BASED VESICLE TRANSPORTR01GM044589 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI SCHROER, TRINA A · 1990 to 2012
$4.3M
Regulation of Cytoplasmic Dynein Based Vesicle TransportR56GM044589 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI SCHROER, TRINA A · 2008 to 2008
$410k
NIGMS NIH HHS GM 29647NIGMS NIH HHS GM 38542NIGMS NIH HHS GM 44589NIGMS NIH HHS R01 GM038542NIGMS NIH HHS R01 GM044589
6 · The paper itself

Abstract

The dynactin complex visualized by deepetch electron microscopy appears as a short filament 37-nm in length, which resembles F-actin, plus a thinner, laterally oriented filament that terminates in two globular heads. The locations of several of the constituent polypeptides were identified on this structure by applying antibodies to decorate the dynactin complex before processing for electron microscopy. Antibodies to the actin-related protein Arp1 (previously referred to as actin-RPV), bound at various sites along the filament, demonstrating that this protein assembles in a polymer similar to conventional actin. Antibodies to the barbed-end actin-binding protein, capping protein, bound to one end of the filament. Thus, an actin-binding protein that binds conventional actin may also bind to Arp1 to regulate its polymerization. Antibodies to the 62-kD component of the dynactin complex also bound to one end of the filament. An antibody that binds the COOH-terminal region of the 160/150-kD dynactin polypeptides bound to the globular domains at the end of the thin lateral filament, suggesting that the dynactin polypeptide comprises at least part of the sidearm structure.

Indexed as

Microfilament ProteinsMicrotubule-Associated ProteinsActin CytoskeletonActinsAmino Acid SequenceAnimalsAntibodies, MonoclonalAntibody SpecificityAntigen-Antibody ReactionsBrain ChemistryCapZ Actin Capping ProteinChick EmbryoDynactin ComplexDyneinsEpitopesIsoelectric PointActinsAntibodies, MonoclonalCapZ Actin Capping ProteincentractinDynactin ComplexDyneinsEpitopesMicrofilament ProteinsMicrotubule-Associated ProteinsMicrotubule ProteinsMuscle Proteins

Identifiers

PMID7518465
PMCPMC2200042
OpenAlexW2079164473

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.