Evidence map›Paper›PMID 26210583›Full record

ArticleEnvironmental science and pollution research international2015

Molecular mechanism of copper-zinc superoxide dismutase activity change exposed to N-acetyl-L-cysteine-capped CdTe quantum dots-induced oxidative damage in mouse primary hepatocytes and nephrocytes.

Haoyu Sun, Erqian Cui, Rutao Liu

Abstract read
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In one paragraph

Article in Environmental science and pollution research international, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.0field-weighted citation impact, top 28% 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

4 citing papers in PubMed, 21 citations in OpenAlex.

  1. A Review of in vivo Toxicity of Quantum Dots in Animal Models.International journal of nanomedicine · 2023
    Review
  2. Article
  3. A biophysical probe on the binding of 2-mercaptothioazoline to bovine hemoglobin.Environmental science and pollution research international · 2019
    Article
  4. Review
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.

Haoyu SunSchool of Environmental Science and Engineering, Shandong University, Jinan, 250100, People's Republic of China.
Erqian CuiSchool of Environmental Science and Engineering, Shandong University, Jinan, 250100, People's Republic of China.
Rutao LiuSchool of Environmental Science and Engineering, Shandong University, Jinan, 250100, People's Republic of China. rutaoliu@sdu.edu.cn.
Shandong University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Quantum dots (QDs) are engineered semiconductor nanocrystals with promising application in biomedicine, which have potential toxic effect on biomacromolecules by direct interaction and indirect impact in the body. In this work, the effect of N-acetyl-L-cysteine-capped CdTe quantum dots with fluorescence emission peak at 612 nm (QDs-612) on copper-zinc superoxide dismutase (Cu/ZnSOD) at molecular and cellular level was investigated using isothermal titration calorimetry, spectroscopic techniques, cell counting kit-8, and total SOD assay. The hydrophobic interaction between Cu/ZnSOD and QDs-612 caused static fluorescence quenching of the protein, which was spontaneous with binding constant calculated to be 3.28 × 10(5) L mol(-1). The microenvironment of tyrosine residues, skeleton, and secondary structure of Cu/ZnSOD were changed with adding QDs-612. The molecular Cu/ZnSOD activity was inhibited at different concentrations of QDs-612 as well as the intracellular Cu/ZnSOD activity after 2-h exposure. Compared with the cell viability of hepatocytes and nephrocytes (decreased markedly of the initial level) with higher concentrations of QDs-612 in the absence of vitamin C, the cell viability of these two primary cells increased in the presence of vitamin C, indicating the oxidative damage induced by QDs-612. Therefore, the inhibition of Cu/ZnSOD activity in these two primary cells may be caused by the oxidative damage of massive ROS or direct interaction with QDs-612. This work establishes a new approach to investigate the biological toxicity of CdTe QDs to biomacromolecule from both molecular and cellular perspectives and obtains experimental evidence to thoroughly study the toxicity of CdTe QDs in vivo.

Indexed as

AcetylcysteineAnimalsCadmium CompoundsCells, CulturedHepatocytesKidneyMiceOxidative StressQuantum DotsSuperoxide DismutaseTelluriumAcetylcysteineCadmium Compoundscadmium tellurideSuperoxide DismutaseTelluriumCopper–zinc superoxide dismutaseHepatocytesIsothermal titration calorimetryNephrocytesOxidative damageQuantum dotsSpectroscopic techniquesToxicity

Identifiers

PMID26210583
OpenAlexW998073515

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.