Evidence map›Paper›PMID 21905645›Full record

ArticleInorganic chemistry2011

Reactions of the fluorescent sensor, Zinquin, with the zinc-proteome: adduct formation and ligand substitution.

Andrew B Nowakowski, David H Petering

Open access · greenAbstract read
In one paragraph

Article in Inorganic chemistry, 2011. 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
4.1field-weighted citation impact, top 6% 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, 50 citations in OpenAlex.

  1. ZIP1 Is a Critical DNA Damage-Responsive Zinc Transporter Induced by Bleomycin via the TNFα-NF-κB Pathway.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Proteomic High Affinity ZnInternational journal of molecular sciences · 2017
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Review
  20. 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

2 authors at 1 institution in 1 country.

Andrew B NowakowskiDepartment of Chemistry and Biochemistry, University of Wisconsin-Milwaukee, Milwaukee, Wisconsin 53201, USA.
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
Cd2+, Metallothionein and Transcriptional Control of Na+-Glucose Co-Transporter 1R01ES004026 · NIEHS · UNIVERSITY OF WISCONSIN MILWAUKEE · PI PETERING, DAVID HAROLD · 1987 to 2009
$3.4M
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-04026NIEHS NIH HHS ES-04184NIEHS NIH HHS P30 ES004184NIEHS NIH HHS R01 ES004026NIGMS NIH HHS GM-85114NIGMS NIH HHS R01 GM085114
6 · The paper itself

Abstract

Zinquin (ZQ) is a commonly used sensor for cellular Zn(2+) status. It has been assumed that it measures accessible Zn(2+) concentrations in the nanomolar range. Instead, this report shows a consistent pattern across seven mammalian cell and tissue types that ZQ reacts with micromolar concentrations of Zn(2+) bound as Zn-proteins. The predominant class of products were ZQ-Zn-protein adducts that were characterized in vivo and in vitro by a fluorescence emission spectrum centered at about 470 nm, by their migration over Sephadex G-75 as protein not low molecular weight species, by the exclusion of reaction with lipid vesicles, and by their large aggregate concentration. In addition, variable, minor formation of Zn(ZQ)(2) with a fluorescence band at about 490 nm was observed in vivo in each case. Because incubation of isolated Zn-proteome with ZQ also generated similar amounts of Zn(ZQ)(2), it was concluded that this species had formed through direct ligand substitution in which ZQ had successfully competed for protein-bound Zn(2+). Parallel studies with the model Zn-proteins, alcohol dehydrogenase (ADH), and alkaline phosphatase (AP) revealed a similar picture of reactivity: ZQ(ACID) (Zinquin acid, (2-methyl-8-p-toluenesulfonamido-6-quinolyloxy)acetate)) able to bind to one Zn(2+) and extract the other in Zn(2)-ADH, whereas it removed one Zn(2+) from Zn(2)-AP and did not bind to the other. Zinquin ethyl ester (ethyl(2-methyl-8-p-toluenesulfonamido-6-quinolyloxy)acetate); ZQ(EE)) bound to both proteins without sequestering Zn(2+) from either one. In contrast to a closely related sensor, 6-methoxy-8-p-toluenesulfonamido-quinoline (TSQ), neither ZQ(ACID) nor ZQ(EE) associated with Zn-carbonic anhydrase. A survey of reactivity of these sensors with partially fractionated Zn-proteome confirmed that ZQ and TSQ bind to distinct, overlapping subsets of the Zn-proteome.

Indexed as

Alcohol DehydrogenaseAminoquinolinesCell Line, TumorEstersFluorescent DyesHumansLigandsProtein BindingProteomeQuinolonesSpectrometry, FluorescenceTosyl CompoundsZincAlcohol DehydrogenaseAminoquinolinesEstersFluorescent DyesLigandsN-(6-methoxy-8-quinolyl)-4-toluenesulfonamideProteomeQuinolonesTosyl CompoundsZinczinquin

Identifiers

PMID21905645
PMCPMC3230276
OpenAlexW2087224117

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.