Jing Du

581 total citations
17 papers, 431 citations indexed

About

Jing Du is a scholar working on Cell Biology, Molecular Biology and Inorganic Chemistry. According to data from OpenAlex, Jing Du has authored 17 papers receiving a total of 431 indexed citations (citations by other indexed papers that have themselves been cited), including 13 papers in Cell Biology, 12 papers in Molecular Biology and 4 papers in Inorganic Chemistry. Recurrent topics in Jing Du's work include Hemoglobin structure and function (12 papers), Heme Oxygenase-1 and Carbon Monoxide (8 papers) and Porphyrin Metabolism and Disorders (4 papers). Jing Du is often cited by papers focused on Hemoglobin structure and function (12 papers), Heme Oxygenase-1 and Carbon Monoxide (8 papers) and Porphyrin Metabolism and Disorders (4 papers). Jing Du collaborates with scholars based in United States and United Kingdom. Jing Du's co-authors include John H. Dawson, Masanori Sono, Cedric P. Owens, Celia W. Goulding, Lukasz Lebioda, Brian R. Crane, Michael V. Airola, Chunxue Wang, Roman Davydov and Jing Jin and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Clinical Investigation and Nature Communications.

In The Last Decade

Jing Du

16 papers receiving 426 citations

Peers

Jing Du

MB

CB

IC

PHYSI

MC

Andrea Coletta Italy

Vesna de Serrano United States

Terry Mincey United States

Hanna Kwon United Kingdom

Giacomo Parisi Italy

Tomoaki Uchiki United States

Taichi Shintou Japan

Susana Frago Spain

Eric S. Underbakke United States

Sanket J. Mishra United States

Andrea Coletta Italy

Jing Du

448 ×1.6

MB

86 ×0.4

CB

10 ×0.1

IC

77 ×1.9

PHYSI

23 ×0.6

MC

Citations per year, relative to Jing Du Jing Du (= 1×) peers Andrea Coletta

Countries citing papers authored by Jing Du

Since Specialization

Citations

This map shows the geographic impact of Jing Du'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 Jing Du with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Jing Du more than expected).

Fields of papers citing papers by Jing Du

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Jing Du. 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 Jing Du. The network helps show where Jing Du may publish in the future.

Co-authorship network of co-authors of Jing Du

This figure shows the co-authorship network connecting the top 25 collaborators of Jing Du. A scholar is included among the top collaborators of Jing Du 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 Jing Du. Jing Du is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

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17 of 17 papers shown

1.

Du, Jing, Pan Liu, Yalu Zhou, et al.. (2024). The mechanosensory channel PIEZO1 functions upstream of angiopoietin/TIE/FOXO1 signaling in lymphatic development. Journal of Clinical Investigation. 134(10). 9 indexed citations

2.

Thomson, Benjamin R., Pan Liu, Tuncer Onay, et al.. (2021). Cellular crosstalk regulates the aqueous humor outflow pathway and provides new targets for glaucoma therapies. Nature Communications. 12(1). 6072–6072. 52 indexed citations

3.

Sono, Masanori, et al.. (2014). Influence of heme environment structure on dioxygen affinity for the dual function Amphitrite ornata hemoglobin/dehaloperoxidase. Insights into the evolutional structure–function adaptations. Archives of Biochemistry and Biophysics. 545. 108–115. 20 indexed citations

4.

Sono, Masanori, et al.. (2014). Evidence of the Direct Involvement of the Substrate TCP Radical in Functional Switching from Oxyferrous O₂ Carrier to Ferric Peroxidase in the Dual-Function Hemoglobin/Dehaloperoxidase from Amphitrite ornata. Biochemistry. 53(30). 4956–4969. 13 indexed citations

5.

Sun, Yuhan, Abdelkrim Benabbas, Xin Ye, et al.. (2013). Investigations of Heme Ligation and Ligand Switching in Cytochromes P450 and P420. Biochemistry. 52(34). 5941–5951. 36 indexed citations

6.

Owens, Cedric P., Jing Du, John H. Dawson, & Celia W. Goulding. (2012). Characterization of Heme Ligation Properties of Rv0203, a Secreted Heme Binding Protein Involved in Mycobacterium tuberculosis Heme Uptake. Biochemistry. 51(7). 1518–1531. 57 indexed citations

7.

Du, Jing, Masanori Sono, & John H. Dawson. (2011). The H93G myoglobin cavity mutant as a versatile scaffold for modeling heme iron coordination structures in protein active sites and their characterization with magnetic circular dichroism spectroscopy. Coordination Chemistry Reviews. 255(7-8). 700–716. 45 indexed citations

8.

Sivaramakrishnan, Santhosh, Hugues Ouellet, Jing Du, et al.. (2011). A Novel Intermediate in the Reaction of Seleno CYP119 with m-Chloroperbenzoic Acid. Biochemistry. 50(14). 3014–3024. 15 indexed citations

9.

Du, Jing, Roshan Perera, & John H. Dawson. (2011). Alkylamine-Ligated H93G Myoglobin Cavity Mutant: A Model System for Endogenous Lysine and Terminal Amine Ligation in Heme Proteins such as Nitrite Reductase and Cytochrome f. Inorganic Chemistry. 50(4). 1242–1249. 15 indexed citations

10.

Du, Jing, Masanori Sono, & John H. Dawson. (2011). Ferric His93Gly myoglobin cavity mutant and its complexes with thioether and selenolate as heme protein models. Journal of Porphyrins and Phthalocyanines. 15(1). 29–38. 5 indexed citations

11.

Du, Jing, et al.. (2011). Amphitrite ornata Dehaloperoxidase (DHP): Investigations of Structural Factors That Influence the Mechanism of Halophenol Dehalogenation Using “Peroxidase-like” Myoglobin Mutants and “Myoglobin-like” DHP Mutants. Biochemistry. 50(38). 8172–8180. 38 indexed citations

12.

Davydov, Roman, Robert L. Osborne, Muralidharan Shanmugam, et al.. (2010). Probing the Oxyferrous and Catalytically Active Ferryl States of Amphitrite ornata Dehaloperoxidase by Cryoreduction and EPR/ENDOR Spectroscopy. Detection of Compound I. Journal of the American Chemical Society. 132(42). 14995–15004. 38 indexed citations

13.

Du, Jing, Masanori Sono, & John H. Dawson. (2010). Functional Switching of Amphitrite ornata Dehaloperoxidase from O₂-Binding Globin to Peroxidase Enzyme Facilitated by Halophenol Substrate and H₂O₂. Biochemistry. 49(29). 6064–6069. 37 indexed citations

14.

Airola, Michael V., Jing Du, John H. Dawson, & Brian R. Crane. (2010). Heme Binding to the Mammalian Circadian Clock Protein Period 2 Is Nonspecific. Biochemistry. 49(20). 4327–4338. 35 indexed citations

15.

Du, Jing, Masanori Sono, & John H. Dawson. (2008). The proximal and distal pockets of the H93G myoglobin cavity mutant bind identical ligands with different affinities: Quantitative analysis of imidazole and pyridine binding. 22. 123–141. 7 indexed citations

16.

Du, Jing, Masanori Sono, & John H. Dawson. (2008). The proximal and distal pockets of the H93G myoglobin cavity mutant bind identical ligands with different affinities: Quantitative analysis of imidazole and pyridine binding. Spectroscopy An International Journal. 22(2-3). 123–141. 9 indexed citations

17.

Du, Jing. (2003). Synthesis of N-Hydroxysuccinimide. Chinese Journal of Applied Chemistry.

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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