Evidence map›Paper›PMID 23319127›Full record

ReviewAdvances in nutrition (Bethesda, Md.)2013

Zinc biochemistry: from a single zinc enzyme to a key element of life.

Wolfgang Maret

Registry-linked trialOpen access · bronzeAbstract readReview
In one paragraph

Review in Advances in nutrition (Bethesda, Md.), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT04975412 (Relationship of Whole Blood Zinc Levels to Acne Severity Among Filipinos 18-25 Years Old), which is not on this map. Cited by 299 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
299citing papers in PubMed, 2 pooled it
27.3field-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.

NCT04975412 completednot on this mapstarted 2017, after this paper: background citation

Relationship of Whole Blood Zinc Levels to Acne Severity Among Filipinos 18-25 Years Old: A Cross-sectional Comparative Study

TypeobservationalSponsorEast Avenue Medical Center, PhilippinesRan2017 to 2018Enrolled40ConditionsAcne VulgarisArmsWhole blood zinc level
3 · Its place in the literature

Who cites it

299 citing papers in PubMed, 2 syntheses or guidelines pooled it, 765 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Trial
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Review
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  11. Ion-Driven Regulation of CaAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  12. Article
  13. Review
  14. Article
  15. A periplasmic metallochaperone (PmcY) couples ZnAntimicrobial agents and chemotherapy · 2026
    Article
  16. Article
  17. The first and second zinc finger domains from Poly-ADP-ribose polymerase 1 (PARP1) are modified by hydrogen sulfide.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2026
    Article
  18. Article
  19. Article
  20. Review

239 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

1 author at 1 institution in 1 country.

Wolfgang MaretKing's College London, Metal Metabolism Group, Division of Diabetes and Nutritional Sciences, School of Medicine, London, United Kingdom. wolfgang.maret@kcl.ac.uk
King's College London · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The nutritional essentiality of zinc for the growth of living organisms had been recognized long before zinc biochemistry began with the discovery of zinc in carbonic anhydrase in 1939. Painstaking analytical work then demonstrated the presence of zinc as a catalytic and structural cofactor in a few hundred enzymes. In the 1980s, the field again gained momentum with the new principle of "zinc finger" proteins, in which zinc has structural functions in domains that interact with other biomolecules. Advances in structural biology and a rapid increase in the availability of gene/protein databases now made it possible to predict zinc-binding sites from metal-binding motifs detected in sequences. This procedure resulted in the definition of zinc proteomes and the remarkable estimate that the human genome encodes ∼3000 zinc proteins. More recent developments focus on the regulatory functions of zinc(II) ions in intra- and intercellular information transfer and have tantalizing implications for yet additional functions of zinc in signal transduction and cellular control. At least three dozen proteins homeostatically control the vesicular storage and subcellular distribution of zinc and the concentrations of zinc(II) ions. Novel principles emerge from quantitative investigations on how strongly zinc interacts with proteins and how it is buffered to control the remarkably low cellular and subcellular concentrations of free zinc(II) ions. It is fair to conclude that the impact of zinc for health and disease will be at least as far-reaching as that of iron.

Indexed as

Binding SitesCarbonic AnhydrasesCatalysisHomeostasisHumansKineticsProteinsProtein Structure, TertiarySignal TransductionZincZinc FingersCarbonic AnhydrasesProteinsZinc

Identifiers

PMID23319127
PMCPMC3648744
OpenAlexW2097951289

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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.