Evidence map›Paper›PMID 7612961›Full record

ArticleMolecular biology of the cell1995

Moesin, ezrin, and p205 are actin-binding proteins associated with neutrophil plasma membranes.

K Pestonjamasp, M R Amieva, C P Strassel, W M Nauseef, H Furthmayr, E J Luna

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
5.8field-weighted citation impact, top 3% 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

52 citing papers in PubMed, 171 citations in OpenAlex.

  1. On the mechanism of ezrin activation.Biophysical journal · 2026
    Article
  2. On the Mechanism of Ezrin Activation.bioRxiv : the preprint server for biology · 2025
    Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Review
  8. Small Vessel Disease-Related Dementia: An Invalid Neurovascular Coupling?International journal of molecular sciences · 2020
    Review
  9. Article
  10. Review
  11. Small GTPases and Their Role in Vascular Disease.International journal of molecular sciences · 2019
    Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  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

6 authors.

K PestonjamaspWorcester Foundation for Experimental Biology, Shrewsbury, Massachusetts 01545, USA.
M R Amieva
C P Strassel
W M Nauseef
H Furthmayr
E J Luna

Funding

CYTOSKELTON-MEMBRANE INTERACTIONSR01GM033048 · NIGMS · WORCESTER FOUNDATION FOR BIOMEDICAL RES · PI LUNA, ELIZABETH J. · 1985 to 2009
$3.3M
Human neutrophils, phospholipase A2 and S.aureus: microbial targets and responsesI01BX000513 · VA · IOWA CITY VA MEDICAL CENTER · PI NAUSEEF, WILLIAM M. · 2009 to 2017
–
MOLECULAR DETERMINANTS OF MYELOPEROXIDASE TARGETTINGP01AI028412 · NIAID · UNIVERSITY OF IOWA · PI BRITIGAN, BRADLEY E · 1989 to 1993
–
METABOLISM OF THE DERMAL MICROVASCULAR BASEMENT MEMBRANEP01AR041045 · NIAMS · STANFORD UNIVERSITY · PI HERRON, G SCOTT · 1992 to 1996
–
BLRD VA I01 BX000513NIAID NIH HHS AI28412NIAMS NIH HHS AR41045NIGMS NIH HHS GM33048NIGMS NIH HHS R01 GM033048
6 · The paper itself

Abstract

Actin-binding proteins in bovine neutrophil plasma membranes were identified using blot overlays with 125I-labeled F-actin. Along with surface-biotinylated proteins, membranes were enriched in major actin-binding polypeptides of 78, 81, and 205 kDa. Binding was specific for F-actin because G-actin did not bind. Further, unlabeled F-actin blocked the binding of 125I-labeled F-actin whereas other acidic biopolymers were relatively ineffective. Binding also was specifically inhibited by myosin subfragment 1, but not by CapZ or plasma gelsolin, suggesting that the membrane proteins, like myosin, bind along the sides of the actin filaments. The 78- and 81-kDa polypeptides were identified as moesin and ezrin, respectively, by co-migration on sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immunoprecipitation with antibodies specific for moesin and ezrin. Although not present in detectable amounts in bovine neutrophils, radixin (a third and closely related member of this gene family) also bound 125I-labeled F-actin on blot overlays. Experiments with full-length and truncated bacterial fusion proteins localized the actin-binding site in moesin to the extreme carboxy terminus, a highly conserved sequence. Immunofluorescence micrographs of permeabilized cells and cell "footprints" showed moesin co-localization with actin at the cytoplasmic surface of the plasma membrane, consistent with a role as a membrane-actin-linking protein.

Indexed as

Cytoskeletal ProteinsAmino Acid SequenceAnimalsBase SequenceBlood ProteinsCattleCytoskeletonEzrinMembrane ProteinsMiceMicrofilament ProteinsMolecular Sequence DataNeutrophilsPhosphoproteinsProteinsSequence AlignmentBlood ProteinsCytoskeletal ProteinsEzrinMembrane ProteinsMicrofilament ProteinsmoesinPhosphoproteinsProteinsradixin

Identifiers

PMID7612961
PMCPMC301185
OpenAlexW1975862854

What OpenQuestion holds

Textmetadata
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.