Evidence map›Paper›PMID 30669557›Full record

ReviewInternational journal of molecular sciences2019

Arf GAPs as Regulators of the Actin Cytoskeleton-An Update.

Christine E Tanna, Louisa B Goss, Calvin G Ludwig, Pei-Wen Chen

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
3.1field-weighted citation impact, top 9% 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

37 citing papers in PubMed, 59 citations in OpenAlex.

  1. Article
  2. Liprin-α family proteins and their cellular functions.The Journal of biological chemistry · 2026
    Review
  3. Article
  4. Article
  5. Identification of Body Color-Related QTLs in Leopard Coral Grouper (Animals : an open access journal from MDPI · 2026
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Rac1 Suppression by the Focal Adhesion Protein GIT ArfGAP2 and Podocyte Protection.Journal of the American Society of Nephrology : JASN · 2025
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. 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

4 authors at 1 institution in 1 country.

Christine E TannaDepartment of Biology, Williams College, Williamstown, MA 01267, USA. cet4@williams.edu.
Louisa B GossDepartment of Biology, Williams College, Williamstown, MA 01267, USA. lbg2@williams.edu.
Calvin G LudwigDepartment of Biology, Williams College, Williamstown, MA 01267, USA. calvinludwig95@gmail.com.
Pei-Wen ChenDepartment of Biology, Williams College, Williamstown, MA 01267, USA. pc7@williams.edu.
Williams College · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Arf GTPase-activating proteins (Arf GAPs) control the activity of ADP-ribosylation factors (Arfs) by inducing GTP hydrolysis and participate in a diverse array of cellular functions both through mechanisms that are dependent on and independent of their Arf GAP activity. A number of these functions hinge on the remodeling of actin filaments. Accordingly, some of the effects exerted by Arf GAPs involve proteins known to engage in regulation of the actin dynamics and architecture, such as Rho family proteins and nonmuscle myosin 2. Circular dorsal ruffles (CDRs), podosomes, invadopodia, lamellipodia, stress fibers and focal adhesions are among the actin-based structures regulated by Arf GAPs. Arf GAPs are thus important actors in broad functions like adhesion and motility, as well as the specialized functions of bone resorption, neurite outgrowth, and pathogen internalization by immune cells. Arf GAPs, with their multiple protein-protein interactions, membrane-binding domains and sites for post-translational modification, are good candidates for linking the changes in actin to the membrane. The findings discussed depict a family of proteins with a critical role in regulating actin dynamics to enable proper cell function.

Indexed as

Actin CytoskeletonActinsADP-Ribosylation FactorsAnimalsApoptosisCell MovementFocal AdhesionsGTPase-Activating ProteinsHost-Pathogen InteractionsHumansMultigene FamilyNeuronal OutgrowthNeuronsPodosomesProtein BindingPseudopodiaActinsADP-Ribosylation FactorsGTPase-Activating Proteinsrho GTP-Binding ProteinsactinADP-ribosylation factor GTPase-activating proteinADP-ribosylation factorsARAP1ARAP2ASAP1focal adhesionGIT1/2phagocytosispodosome

Identifiers

PMID30669557
PMCPMC6358971
OpenAlexW2910527963

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.