Evidence map›Paper›PMID 27055045›Full record

ReviewCurrent opinion in hematology2016

Feisty filaments: actin dynamics in the red blood cell membrane skeleton.

David S Gokhin, Velia M Fowler

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in hematology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

25 citing papers in PubMed, 50 citations in OpenAlex.

  1. Active Force Dynamics in Red Blood Cells Under Non-Invasive Optical Tweezers.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Quantification and visualization ofNAR genomics and bioinformatics · 2024
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Cardiomyocyte mechanodynamics under conditions of actin remodelling.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2019
    Article
  18. Article
  19. Article
  20. Review
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

2 authors at 1 institution in 1 country.

David S GokhinDepartment of Cell and Molecular Biology, The Scripps Research Institute, La Jolla, California, USA.
Velia M Fowler
Scripps Research Institute · US

Funding

Capping Actin Growth in Erythroid and Nonerythroid CellsR01HL083464 · NHLBI · UNIVERSITY OF DELAWARE · PI FOWLER, VELIA M · 2006 to 2019
$7.1M
Structure and Remodeling of the Distal Segment of the Thin FilamentK99AR066534 · NIAMS · SCRIPPS RESEARCH INSTITUTE, THE · PI GOKHIN, DAVID SAMUEL · 2014 to 2015
$178k
NHLBI NIH HHS R01 HL083464NHLBI NIH HHS R01-HL083464NIAMS NIH HHS K99 AR066534NIAMS NIH HHS K99-AR066534
6 · The paper itself

Abstract

purpose of reviewThis article discusses recent advances and unsolved questions in our understanding of actin filament organization and dynamics in the red blood cell (RBC) membrane skeleton, a two-dimensional quasi-hexagonal network consisting of (α1β1)2-spectrin tetramers interconnecting short actin filament-based junctional complexes. RECENT

findingsIn contrast to the long-held view that RBC actin filaments are static structures that do not exchange subunits with the cytosol, RBC actin filaments are dynamic structures that undergo subunit exchange and turnover, as evidenced by monomer incorporation experiments with rhodamine-actin and filament disruption experiments with actin-targeting drugs. The malaria-causing parasite, Plasmodium falciparum, co-opts RBC actin dynamics to construct aberrantly branched actin filament networks. Even though RBC actin filaments are dynamic, RBC actin filament lengths are highly uniform (∼37 nm). RBC actin filament lengths are thought to be stabilized by the capping proteins, tropomodulin-1 and αβ-adducin, as well as the side-binding protein tropomyosin, present in an equimolar combination of two isoforms, TM5b (Tpm1.9) and TM5NM1 (Tpm3.1). SUMMARY: New evidence indicates that RBC actin filaments are not simply passive cytolinkers, but rather dynamic structures whose assembly and disassembly play important roles in RBC membrane function.

Indexed as

ActinsErythrocyte MembraneErythrocytesHumansPlasmodium falciparumActins

Identifiers

PMID27055045
PMCPMC4966542
OpenAlexW2329686860

What OpenQuestion holds

Textmetadata
LicenceTDM
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.