Evidence map›Paper›PMID 15059252›Full record

ReviewGenome biology2004

The annexins.

Stephen E Moss, Reg O Morgan

Open access · bronzeAbstract readReview
In one paragraph

Review in Genome biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 224 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
224citing papers in PubMed, 2 pooled it
6.1field-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

224 citing papers in PubMed, 2 syntheses or guidelines pooled it, 478 citations in OpenAlex.

  1. Cells · 2022
    Pooled it
  2. Pooled it
  3. Review
  4. Article
  5. Article
  6. Review
  7. Comprehensive Analysis of Annexin Family fromPlants (Basel, Switzerland) · 2026
    Article
  8. Article
  9. Article
  10. Augmenting riceProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Article
  12. Article
  13. Review
  14. Annexin, a Protein for All Seasons: From Calcium Dependent Membrane Metabolism to RNA Recognition.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  15. Annexins: central regulators of plant growth and stress signaling.Acta biochimica et biophysica Sinica · 2025
    Review
  16. Article
  17. Article
  18. Review
  19. Review
  20. Review

164 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

2 authors at 2 institutions in 2 countries.

Stephen E MossDivision of Cell Biology, Institute of Ophthalmology, 11-43 Bath Street, London EC1V 9EL, UK. s.moss@ucl.ac.uk
Reg O Morgan
Institute of Ophthalmology · MXUniversidad de Oviedo · ES

Funding

Wellcome Trust
6 · The paper itself

Abstract

Annexins are traditionally thought of as calcium-dependent phospholipid-binding proteins, but recent work suggests a more complex set of functions. More than a thousand proteins of the annexin superfamily have been identified in major eukaryotic phyla, but annexins are absent from yeasts and prokaryotes. The unique annexin core domain is made up of four similar repeats approximately 70 amino acids long, each of which usually contains a characteristic 'type 2' motif for binding calcium ions. Animal and fungal annexins also have non-homologous amino-terminal domains of varying length and sequence, which are responsible for the distinct localizations and specialized functions of the proteins through post-translational modification and binding to other proteins. Annexins interact with various cell-membrane components that are involved in the structural organization of the cell, intracellular signaling by enzyme modulation and ion fluxes, growth control, and they can act as atypical calcium channels. Analysis of site-specific conservation in the core domain suggests a role for certain buried residues in the calcium-channel activity of vertebrate annexins and in the structural stability of their core domains. Evolutionarily significant differences between subfamilies are preferentially localized to accessible sites on the protein surface that determine membrane binding and interactions with cytosolic proteins.

Indexed as

AnimalsAnnexinsHumansAnnexins

Identifiers

PMID15059252
PMCPMC395778
OpenAlexW4244376495

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.