Evidence map›Paper›PMID 23197251›Full record

ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2013

Solution structure and dynamics of human S100A14.

Ivano Bertini, Valentina Borsi, Linda Cerofolini, Soumyasri Das Gupta, Marco Fragai, Claudio Luchinat

Open access · greenAbstract read
PubMed Publisher
In one paragraph

Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.7field-weighted citation impact, top 33% 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

13 citing papers in PubMed, 22 citations in OpenAlex.

  1. Influence of Calcium Ions on the Membrane Binding of S100B Protein.Langmuir : the ACS journal of surfaces and colloids · 2025
    Article
  2. Article
  3. RAGE Inhibitors for Targeted Therapy of Cancer: A Comprehensive Review.International journal of molecular sciences · 2022
    Review
  4. Article
  5. Review
  6. Article
  7. Oncotarget · 2017
    Article
  8. Article
  9. Solving the crystal structure of human calcium-free S100Z: the siege and conquer of one of the last S100 family strongholds.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2017
    Article
  10. Human S100A5 binds CaBMC biophysics · 2017
    Article
  11. Article
  12. Article
  13. 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 at 2 institutions in 1 country.

Ivano BertiniMagnetic Resonance Center (CERM), University of Florence, Via L. Sacconi 6, 50019, Sesto Fiorentino, Italy.
Valentina BorsiMagnetic Resonance Center (CERM), University of Florence, Via L. Sacconi 6, 50019, Sesto Fiorentino, Italy.
Linda CerofoliniMagnetic Resonance Center (CERM), University of Florence, Via L. Sacconi 6, 50019, Sesto Fiorentino, Italy.
Soumyasri Das GuptaMagnetic Resonance Center (CERM), University of Florence, Via L. Sacconi 6, 50019, Sesto Fiorentino, Italy.
Marco FragaiMagnetic Resonance Center (CERM), University of Florence, Via L. Sacconi 6, 50019, Sesto Fiorentino, Italy.
Claudio LuchinatMagnetic Resonance Center (CERM), University of Florence, Via L. Sacconi 6, 50019, Sesto Fiorentino, Italy. luchinat@cerm.unifi.it.
University of Florence · ITInteruniversity Consortium for Magnetic Resonance · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human S100A14 is a member of the EF-hand calcium-binding protein family that has only recently been described in terms of its functional and pathological properties. The protein is overexpressed in a variety of tumor cells and it has been shown to trigger receptor for advanced glycation end products (RAGE)-dependent signaling in cell cultures. The solution structure of homodimeric S100A14 in the apo state has been solved at physiological temperature. It is shown that the protein does not bind calcium(II) ions and exhibits a "semi-open" conformation that thus represents the physiological structure of the S100A14. The lack of two ligands in the canonical EF-hand calcium(II)-binding site explains the negligible affinity for calcium(II) in solution, and the exposed cysteines and histidine account for the observed precipitation in the presence of zinc(II) or copper(II) ions.

Indexed as

ApoproteinsBinding SitesCalciumCalcium-Binding ProteinsCopperHumansLightModels, MolecularNuclear Magnetic Resonance, BiomolecularProtein BindingProtein Structure, QuaternaryProtein Structure, SecondaryProtein Structure, TertiaryScattering, RadiationSurface PropertiesZincApoproteinsCalciumCalcium-Binding ProteinsCopperS100A14 protein, humanZinc

Identifiers

PMID23197251
OpenAlexW1977906523

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.