Evidence map›Paper›PMID 16683912›Full record

ReviewThe Biochemical journal2006

Calcium-dependent and -independent interactions of the S100 protein family.

Liliana Santamaria-Kisiel, Anne C Rintala-Dempsey, Gary S Shaw

Open access · bronzeAbstract readReview
In one paragraph

Review in The Biochemical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 264 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
264citing papers in PubMed, 1 pooled it
16.4field-weighted citation impact, top 1% 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

264 citing papers in PubMed, 1 synthesis or guideline pooled it, 582 citations in OpenAlex.

  1. Calprotectin (S100A8/S100A9): a key protein between inflammation and cancer.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2018
    Pooled it
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. An updated guide to hair follicle stem cell markers and changes in their expression with aging.JID innovations : skin science from molecules to population health · 2026
    Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Influence of Calcium Ions on the Membrane Binding of S100B Protein.Langmuir : the ACS journal of surfaces and colloids · 2025
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

204 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

3 authors at 1 institution in 1 country.

Liliana Santamaria-KisielDepartment of Biochemistry, The University of Western Ontario, London, Ontario, Canada, N6A 5C1.
Anne C Rintala-Dempsey
Gary S Shaw
Western University · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The S100 proteins comprise at least 25 members, forming the largest group of EF-hand signalling proteins in humans. Although the proteins are expressed in many tissues, each S100 protein has generally been shown to have a preference for expression in one particular tissue or cell type. Three-dimensional structures of several S100 family members have shown that the proteins assume a dimeric structure consisting of two EF-hand motifs per monomer. Calcium binding to these S100 proteins, with the exception of S100A10, results in an approx. 40 degrees alteration in the position of helix III, exposing a broad hydrophobic surface that enables the S100 proteins to interact with a variety of target proteins. More than 90 potential target proteins have been documented for the S100 proteins, including the cytoskeletal proteins tubulin, glial fibrillary acidic protein and F-actin, which have been identified mostly from in vitro experiments. In the last 5 years, efforts have concentrated on quantifying the protein interactions of the S100 proteins, identifying in vivo protein partners and understanding the molecular specificity for target protein interactions. Furthermore, the S100 proteins are the only EF-hand proteins that are known to form both homo- and hetero-dimers, and efforts are underway to determine the stabilities of these complexes and structural rationales for their formation and potential differences in their biological roles. This review highlights both the calcium-dependent and -independent interactions of the S100 proteins, with a focus on the structures of the complexes, differences and similarities in the strengths of the interactions, and preferences for homo- compared with hetero-dimeric S100 protein assembly.

Indexed as

Gene Expression RegulationBinding SitesCalciumCalcium-Binding ProteinsDimerizationEF Hand MotifsHumansModels, BiologicalProtein BindingProtein ConformationS100 ProteinsCalciumCalcium-Binding ProteinsS100 Proteins

Identifiers

PMID16683912
PMCPMC1462724
OpenAlexW2123404680

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.