Evidence map›Paper›PMID 21474668›Full record

ArticleBlood2011

Regulation of membrane-cytoskeletal interactions by tyrosine phosphorylation of erythrocyte band 3.

Emanuela Ferru, Katie Giger, Antonella Pantaleo, Estela Campanella, Jesse Grey, Ken Ritchie, Rosa Vono, Francesco Turrini, Philip S Low

Open access · bronzeAbstract read
In one paragraph

Article in Blood, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 106 papers.

0numbers the graph read from it
0cells of the map it votes in
106citing papers in PubMed
8.5field-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

106 citing papers in PubMed, 195 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Main events and mechanism of human erythrocyte ageing.Expert reviews in molecular medicine · 2026
    Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Host-pathogen interactions involved in erythrocyte invasion byFrontiers in cellular and infection microbiology · 2025
    Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article

46 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

9 authors at 2 institutions in 2 countries.

Emanuela FerruDepartment of Genetics, Biology and Biochemistry, University of Turin, Turin, Italy.
Katie Giger
Antonella Pantaleo
Estela Campanella
Jesse Grey
Ken Ritchie
Rosa Vono
Francesco Turrini
Philip S Low
University of Turin · ITPurdue University West Lafayette · US

Funding

Studies of Erythrocyte Membrane StructureR01GM024417 · NIGMS · PURDUE UNIVERSITY WEST LAFAYETTE · PI LOW, PHILIP STEWART · 1985 to 2020
$5.4M
ERYTHROCYTE MEMBRANE STRUCTURER37GM024417 · NIGMS · PURDUE UNIVERSITY WEST LAFAYETTE · PI LOW, PHILIP STEWART · 1999 to 2008
$3.5M
NIGMS NIH HHS GM24417NIGMS NIH HHS R01 GM024417NIGMS NIH HHS R37 GM024417
6 · The paper itself

Abstract

The cytoplasmic domain of band 3 serves as a center of erythrocyte membrane organization and constitutes the major substrate of erythrocyte tyrosine kinases. Tyrosine phosphorylation of band 3 is induced by several physiologic stimuli, including malaria parasite invasion, cell shrinkage, normal cell aging, and oxidant stress (thalassemias, sickle cell disease, glucose-6-phosphate dehydrogenase deficiency, etc). In an effort to characterize the biologic sequelae of band 3 tyrosine phosphorylation, we looked for changes in the polypeptide's function that accompany its phosphorylation. We report that tyrosine phosphorylation promotes dissociation of band 3 from the spectrin-actin skeleton as evidenced by: (1) a decrease in ankyrin affinity in direct binding studies, (2) an increase in detergent extractability of band 3 from ghosts, (3) a rise in band 3 cross-linkability by bis-sulfosuccinimidyl-suberate, (4) significant changes in erythrocyte morphology, and (5) elevation of the rate of band 3 diffusion in intact cells. Because release of band 3 from its ankyrin and adducin linkages to the cytoskeleton can facilitate changes in multiple membrane properties, tyrosine phosphorylation of band 3 is argued to enable adaptive changes in erythrocyte biology that permit the cell to respond to the above stresses.

Indexed as

ActinsAnion Exchange Protein 1, ErythrocyteAnkyrinsCell MembraneCross-Linking ReagentsCytoskeletonErythrocyte MembraneErythrocytesHumansImmunoblottingPhosphorylationProtein BindingTyrosineVanadatesActinsAnion Exchange Protein 1, ErythrocyteAnkyrinsCross-Linking ReagentsTyrosineVanadates

Identifiers

PMID21474668
PMCPMC3112043
OpenAlexW2040534221

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.