Evidence map›Paper›PMID 22380934›Full record

ArticleInorganic chemistry2012

Reaction of metal-binding ligands with the zinc proteome: zinc sensors and N,N,N',N'-tetrakis(2-pyridylmethyl)ethylenediamine.

Jeffrey W Meeusen, Andrew Nowakowski, David H Petering

Open access · greenAbstract read
In one paragraph

Article in Inorganic chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
5.0field-weighted citation impact, top 5% 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

25 citing papers in PubMed, 45 citations in OpenAlex.

  1. Chelation-Driven Dual-Interface Regulation for Long-Life Aqueous Zn-IAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  2. Review
  3. Article
  4. Review
  5. Review
  6. Article
  7. Tools and techniques for illuminating the cell biology of zinc.Biochimica et biophysica acta. Molecular cell research · 2021
    Review
  8. Article
  9. Article
  10. Article
  11. Proteomic High Affinity ZnInternational journal of molecular sciences · 2017
    Review
  12. Zinc Selectively Blocks Neurosteroid-Sensitive Extrasynaptic δGABAA Receptors in the Hippocampus.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2016
    Article
  13. Article
  14. The Critical Roles of Zinc: Beyond Impact on Myocardial Signaling.The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2015
    Review
  15. Article
  16. Review
  17. Article
  18. Review
  19. Article
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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.

Jeffrey W MeeusenDepartment of Chemistry and Biochemistry, University of Wisconsin-Milwaukee, Milwaukee, Wisconsin 53201, USA.
Andrew Nowakowski
David H Petering
University of Wisconsin–Milwaukee · US

Funding

Pilot Project ProgramP30ES004184 · NIEHS · UNIVERSITY OF WISCONSIN MILWAUKEE · PI PETERING, DAVID HAROLD · 1987 to 2015
$11.8M
Fluorescent Cellular Zinc Sensors. What Are They Imaging?R01GM085114 · NIGMS · UNIVERSITY OF WISCONSIN MILWAUKEE · PI PETERING, DAVID HAROLD · 2008 to 2011
$1.1M
NIEHS NIH HHS ES-04184NIEHS NIH HHS P30 ES004184NIGMS NIH HHS GM-85114NIGMS NIH HHS R01 GM085114
6 · The paper itself

Abstract

The commonly used Zn(2+) sensors 6-methoxy-8-p-toluenesulfonamidoquinoline (TSQ) and Zinquin have been shown to image zinc proteins as a result of the formation of sensor-zinc-protein ternary adducts not Zn(TSQ)(2) or Zn(Zinquin)(2) complexes. The powerful, cell-permeant chelating agent N,N,N',N'-tetrakis(2-pyridylmethyl)ethylenediamine (TPEN) is also used in conjunction with these and other Zn(2+) sensors to validate that the observed fluorescence enhancement seen with the sensors depends on intracellular interaction with Zn(2+). We demonstrated that the kinetics of the reaction of TPEN with cells pretreated with TSQ or Zinquin was not consistent with its reaction with Zn(TSQ)(2) or Zn(Zinquin)(2). Instead, TPEN and other chelating agents extract between 25 and 35% of the Zn(2+) bound to the proteome, including zinc(2+) from zinc metallothionein, and thereby quench some, but not all, of the sensor-zinc-protein fluorescence. Another mechanism in which TPEN exchanges with TSQ or Zinquin to form TPEN-zinc-protein adducts found support in the reactions of TPEN with Zinquin-zinc-alcohol dehydrogenase. TPEN also removed one of the two Zn(2+) ions per monomer from zinc-alcohol dehydrogenase and zinc-alkaline phosphatase, consistent with its ligand substitution reactivity with the zinc proteome.

Indexed as

ProteomeAnimalsCell LineChromatography, Ion ExchangeEthylenediaminesLigandsMetalsSwineZincEthylenediaminesLigandsMetalsN,N,N',N'-tetrakis(2-pyridylmethyl)ethylenediamineProteomeZinc

Identifiers

PMID22380934
PMCPMC3564517
OpenAlexW76703225

What OpenQuestion holds

Textmetadata
LicenceTDM
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.