Qing Cheng

2.9k total citations · 1 hit paper
58 papers, 2.1k citations indexed

About

Qing Cheng is a scholar working on Molecular Biology, Nutrition and Dietetics and Oncology. According to data from OpenAlex, Qing Cheng has authored 58 papers receiving a total of 2.1k indexed citations (citations by other indexed papers that have themselves been cited), including 41 papers in Molecular Biology, 22 papers in Nutrition and Dietetics and 8 papers in Oncology. Recurrent topics in Qing Cheng's work include Redox biology and oxidative stress (34 papers), Selenium in Biological Systems (20 papers) and Trace Elements in Health (10 papers). Qing Cheng is often cited by papers focused on Redox biology and oxidative stress (34 papers), Selenium in Biological Systems (20 papers) and Trace Elements in Health (10 papers). Qing Cheng collaborates with scholars based in Sweden, United States and Hungary. Qing Cheng's co-authors include Elias S.J. Arnér, Ylva Lindqvist, Tatyana Sandalova, Radosveta Gencheva, Péter Nagy, Edward E. Schmidt, Justin R. Prigge, Éva Dóka, Jianqiang Xu and Sharon Stone‐Elander and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Nucleic Acids Research and Journal of Biological Chemistry.

In The Last Decade

Qing Cheng

57 papers receiving 2.1k citations

Hit Papers

align trajectories

What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

The ferroptosis inducing compounds RSL3 and ML162 are not direct inhibitors of GPX4 but of TXNRD1

2023 127 citations Dorian M. Cheff, Karoline Scholzen et al. Redox Biology profile →

Peers — A (Enhanced Table)

Peers by citation overlap · career bar shows stage (early→late) cites · hero ref

Name	h						Papers	Cites
Qing Cheng Sweden	26	1.4k	492	442	284	222	58	2.1k
Margareta Berggren United States	24	1.8k 1.3×	376 0.8×	266 0.6×	284 1.0×	274 1.2×	38	2.5k
Margaret M. Briehl United States	30	1.9k 1.4×	209 0.4×	244 0.6×	237 0.8×	329 1.5×	62	2.8k
Robert J. Hondal United States	28	2.1k 1.5×	391 0.8×	1.0k 2.3×	663 2.3×	239 1.1×	67	3.6k
C. Johansson United Kingdom	22	1.8k 1.3×	347 0.7×	319 0.7×	77 0.3×	166 0.7×	33	2.4k
Stefano M. Marino United States	22	1.3k 0.9×	425 0.9×	307 0.7×	187 0.7×	161 0.7×	27	1.9k
Anna Maria Caccuri Italy	35	2.8k 2.0×	264 0.5×	143 0.3×	289 1.0×	362 1.6×	102	3.5k
Mario Lo Bello Italy	36	2.6k 1.9×	254 0.5×	170 0.4×	444 1.6×	541 2.4×	70	3.4k
W. Todd Lowther United States	34	2.7k 2.0×	649 1.3×	236 0.5×	331 1.2×	805 3.6×	63	3.7k
Christophe Glorieux Belgium	24	1.2k 0.9×	65 0.1×	218 0.5×	190 0.7×	268 1.2×	38	2.2k
Margaret E. Tome United States	26	1.1k 0.8×	122 0.2×	145 0.3×	185 0.7×	257 1.2×	59	1.8k

Countries citing papers authored by Qing Cheng

Since Specialization

Citations

This map shows the geographic impact of Qing Cheng's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by Qing Cheng with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Qing Cheng more than expected).

Fields of papers citing papers by Qing Cheng

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Qing Cheng. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by Qing Cheng. The network helps show where Qing Cheng may publish in the future.

Co-authorship network of co-authors of Qing Cheng

This figure shows the co-authorship network connecting the top 25 collaborators of Qing Cheng. A scholar is included among the top collaborators of Qing Cheng based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with Qing Cheng. Qing Cheng is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

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20 of 20 papers shown

Cheng, Qing, Aida M. Andrés, Baldomero Oliva, et al.. (2024). Ancient Loss of Catalytic Selenocysteine Spurred Convergent Adaptation in a Mammalian Oxidoreductase. Genome Biology and Evolution. 16(3).

Beusch, Christian M., Hassan Gharibi, Qing Cheng, et al.. (2023). Ultralight Ultrafast Enzymes**. Angewandte Chemie. 136(3). 1 indexed citations

Cheng, Qing, Xiaoli Ma, Jingjing Liu, et al.. (2023). Pharmacological Inhibition of the Asparaginyl Endopeptidase (AEP) in an Alzheimer’s Disease Model Improves the Survival and Efficacy of Transplanted Neural Stem Cells. International Journal of Molecular Sciences. 24(9). 7739–7739. 9 indexed citations

Schwarz, Maria, et al.. (2023). Side-by-side comparison of recombinant human glutathione peroxidases identifies overlapping substrate specificities for soluble hydroperoxides. Redox Biology. 59. 102593–102593. 32 indexed citations

Ratia, Carlos, Victoria Ballén, Yaiza Gabasa, et al.. (2023). Novel gold(III)-dithiocarbamate complex targeting bacterial thioredoxin reductase: antimicrobial activity, synergy, toxicity, and mechanistic insights. Frontiers in Microbiology. 14. 1198473–1198473. 10 indexed citations

Roveri, Antonella, Flavio Di Giacinto, Monica Rossetto, et al.. (2023). Cardiolipin drives the catalytic activity of GPX4 on membranes: Insights from the R152H mutant. Redox Biology. 64. 102806–102806. 7 indexed citations

Scholzen, Karoline, Dorian M. Cheff, Qing Cheng, et al.. (2022). Selective cellular probes for mammalian thioredoxin reductase TrxR1: Rational design of RX1, a modular 1,2-thiaselenane redox probe. Chem. 8(5). 1493–1517. 37 indexed citations

Wang, Ju, Jingjing Liu, Shanshan Wang, et al.. (2021). Pharmacological inhibition of asparaginyl endopeptidase by δ-secretase inhibitor 11 mitigates Alzheimer’s disease-related pathologies in a senescence-accelerated mouse model. Translational Neurodegeneration. 10(1). 12–12. 15 indexed citations

Sabatier, Pierre, Christian M. Beusch, Radosveta Gencheva, et al.. (2021). Comprehensive chemical proteomics analyses reveal that the new TRi-1 and TRi-2 compounds are more specific thioredoxin reductase 1 inhibitors than auranofin. Redox Biology. 48. 102184–102184. 37 indexed citations

10.

Lyu, Haining, Pavel A. Petukhov, Ajit Jadhav, et al.. (2020). Characterization of Lead Compounds Targeting the Selenoprotein Thioredoxin Glutathione Reductase for Treatment of Schistosomiasis. ACS Infectious Diseases. 6(3). 393–405. 25 indexed citations

11.

Dóka, Éva, Tomoaki Ida, Markus Dagnell, et al.. (2020). Control of protein function through oxidation and reduction of persulfidated states. Science Advances. 6(1). eaax8358–eaax8358. 153 indexed citations

12.

Dagnell, Markus, Qing Cheng, Syed Husain Mustafa Rizvi, et al.. (2019). Bicarbonate is essential for protein-tyrosine phosphatase 1B (PTP1B) oxidation and cellular signaling through EGF-triggered phosphorylation cascades. Journal of Biological Chemistry. 294(33). 12330–12338. 54 indexed citations

13.

Lyu, Haining, Giovanna Boumis, A.E. Miele, et al.. (2018). Fragment-Based Discovery of a Regulatory Site in Thioredoxin Glutathione Reductase Acting as “Doorstop” for NADPH Entry. ACS Chemical Biology. 13(8). 2190–2202. 25 indexed citations

14.

Stafford, William C., Xiaoxiao Peng, Maria Hägg Olofsson, et al.. (2018). Irreversible inhibition of cytosolic thioredoxin reductase 1 as a mechanistic basis for anticancer therapy. Science Translational Medicine. 10(428). 164 indexed citations

15.

Gencheva, Radosveta, Qing Cheng, & Elias S.J. Arnér. (2018). Efficient selenocysteine-dependent reduction of toxoflavin by mammalian thioredoxin reductase. Biochimica et Biophysica Acta (BBA) - General Subjects. 1862(11). 2511–2517. 18 indexed citations

16.

Dagnell, Markus, Paul Pace, Qing Cheng, et al.. (2017). Thioredoxin reductase 1 and NADPH directly protect protein tyrosine phosphatase 1B from inactivation during H2O2 exposure. Journal of Biological Chemistry. 292(35). 14371–14380. 39 indexed citations

17.

Wållberg, Helena, Qing Cheng, Frank Leigh Lu, et al.. (2012). HER2-Positive Tumors Imaged Within 1 Hour Using a Site-Specifically ¹¹C-Labeled Sel-Tagged Affibody Molecule. Journal of Nuclear Medicine. 53(9). 1446–1453. 25 indexed citations

18.

Rackham, Oliver, Anne-Marie J. Shearwood, Ross Thyer, et al.. (2010). Substrate and inhibitor specificities differ between human cytosolic and mitochondrial thioredoxin reductases: Implications for development of specific inhibitors. Free Radical Biology and Medicine. 50(6). 689–699. 100 indexed citations

19.

Thunberg, Sarah, Theresa Neimert-Andersson, Qing Cheng, et al.. (2009). Prolonged antigen‐exposure with carbohydrate particle based vaccination prevents allergic immune responses in sensitized mice. Allergy. 64(6). 919–926. 33 indexed citations

20.

Cheng, Qing, Tatyana Sandalova, Ylva Lindqvist, & Elias S.J. Arnér. (2008). Crystal Structure and Catalysis of the Selenoprotein Thioredoxin Reductase 1. Journal of Biological Chemistry. 284(6). 3998–4008. 169 indexed citations

Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.

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