Evidence map›Paper›PMID 27117234›Full record

ArticleArchives of biochemistry and biophysics2016

The biological inorganic chemistry of zinc ions.

Artur Krężel, Wolfgang Maret

Open access · hybridAbstract read
In one paragraph

Article in Archives of biochemistry and biophysics, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 253 papers.

0numbers the graph read from it
0cells of the map it votes in
253citing papers in PubMed
37.8field-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

253 citing papers in PubMed, 734 citations in OpenAlex.

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  6. ZnbioRxiv : the preprint server for biology · 2026
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  9. Complexes of Zinc(II) Chloride withPharmaceuticals (Basel, Switzerland) · 2026
    Article
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193 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.

Artur KrężelLaboratory of Chemical Biology, Faculty of Biotechnology, University of Wroclaw, Joliot-Curie 14A, 50-383 Wroclaw, Poland. Electronic address: artur.krezel@uwr.edu.pl.
Wolfgang MaretKing's College London, Metal Metabolism Group, Division of Diabetes and Nutritional Sciences, Department of Biochemistry, Faculty of Life Sciences of Medicine, 150 Stamford Street, London, SE1 9NH, UK. Electronic address: wolfgang.maret@kcl.ac.uk.
King's College London · GBUniversity of Wrocław · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The solution and complexation chemistry of zinc ions is the basis for zinc biology. In living organisms, zinc is redox-inert and has only one valence state: Zn(II). Its coordination environment in proteins is limited by oxygen, nitrogen, and sulfur donors from the side chains of a few amino acids. In an estimated 10% of all human proteins, zinc has a catalytic or structural function and remains bound during the lifetime of the protein. However, in other proteins zinc ions bind reversibly with dissociation and association rates commensurate with the requirements in regulation, transport, transfer, sensing, signalling, and storage. In contrast to the extensive knowledge about zinc proteins, the coordination chemistry of the "mobile" zinc ions in these processes, i.e. when not bound to proteins, is virtually unexplored and the mechanisms of ligand exchange are poorly understood. Knowledge of the biological inorganic chemistry of zinc ions is essential for understanding its cellular biology and for designing complexes that deliver zinc to proteins and chelating agents that remove zinc from proteins, for detecting zinc ion species by qualitative and quantitative analysis, and for proper planning and execution of experiments involving zinc ions and nanoparticles such as zinc oxide (ZnO). In most investigations, reference is made to zinc or Zn

Indexed as

Chemistry, BioinorganicAnionsBuffersCatalysisCationsChelating AgentsHumansHydrogen-Ion ConcentrationLigandsOxidation-ReductionProteinsSignal TransductionSolubilityTemperatureZincAnionsBuffersCationsChelating AgentsLigandsProteinsZinczinczinc biochemistryzinc biophysicszinc ionszinc speciation

Identifiers

PMID27117234
PMCPMC5120989
OpenAlexW2344658806

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.