Dongdong Meng

468 total citations
21 papers, 366 citations indexed

About

Dongdong Meng is a scholar working on Molecular Biology, Biotechnology and Biomedical Engineering. According to data from OpenAlex, Dongdong Meng has authored 21 papers receiving a total of 366 indexed citations (citations by other indexed papers that have themselves been cited), including 14 papers in Molecular Biology, 11 papers in Biotechnology and 10 papers in Biomedical Engineering. Recurrent topics in Dongdong Meng's work include Enzyme Production and Characterization (11 papers), Biofuel production and bioconversion (10 papers) and Enzyme Catalysis and Immobilization (10 papers). Dongdong Meng is often cited by papers focused on Enzyme Production and Characterization (11 papers), Biofuel production and bioconversion (10 papers) and Enzyme Catalysis and Immobilization (10 papers). Dongdong Meng collaborates with scholars based in China. Dongdong Meng's co-authors include Chun You, Xinlei Wei, Fuli Li, Ming Lu, Xiaohua Chen, Zhiguang Zhu, Y.‐H. Percival Zhang, Yanhe Ma, Lushan Wang and Kang Ning and has published in prestigious journals such as Applied and Environmental Microbiology, Bioresource Technology and Biochemical Journal.

In The Last Decade

Dongdong Meng

20 papers receiving 362 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Dongdong Meng China 12 229 168 132 60 33 21 366
Petra Kornberger Germany 12 188 0.8× 109 0.6× 78 0.6× 56 0.9× 49 1.5× 15 318
Lichuang Cao China 14 308 1.3× 252 1.5× 217 1.6× 36 0.6× 51 1.5× 16 511
David Talens-Perales Spain 12 160 0.7× 90 0.5× 119 0.9× 30 0.5× 61 1.8× 21 312
Sang Kyu Shin South Korea 13 203 0.9× 145 0.9× 77 0.6× 73 1.2× 12 0.4× 16 361
Xiaojing Jia China 13 205 0.9× 236 1.4× 126 1.0× 35 0.6× 27 0.8× 24 351
Dirk Aerts Belgium 9 358 1.6× 178 1.1× 198 1.5× 79 1.3× 115 3.5× 11 486
Imrana Khushk Pakistan 12 248 1.1× 191 1.1× 212 1.6× 100 1.7× 48 1.5× 21 387
Lingtian Wu China 12 164 0.7× 116 0.7× 122 0.9× 76 1.3× 62 1.9× 19 357
Toshiba Haider India 7 263 1.1× 58 0.3× 145 1.1× 19 0.3× 38 1.2× 7 331
Willian Kopp Brazil 13 332 1.4× 190 1.1× 79 0.6× 26 0.4× 50 1.5× 19 411

Countries citing papers authored by Dongdong Meng

Since Specialization
Citations

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

Fields of papers citing papers by Dongdong Meng

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Dongdong Meng

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

All Works

20 of 20 papers shown
1.
Liu, Juanjuan, et al.. (2025). Sugar phosphatases as biocatalysts for biomanufacturing: Recent advances and applications. Biotechnology Advances. 82. 108596–108596.
2.
Liu, Juanjuan, et al.. (2024). Sustainable cellobionic acid biosynthesis from starch via artificial in vitro synthetic enzymatic biosystem. International Journal of Biological Macromolecules. 260(Pt 2). 129641–129641. 1 indexed citations
3.
Liu, Juanjuan, et al.. (2024). One-pot sustainable synthesis of glucosylglycerate from starch and glycerol through artificial in vitro enzymatic cascade. Bioresource Technology. 399. 130611–130611. 2 indexed citations
4.
Liu, Juanjuan, et al.. (2024). Enzymatic biosynthesis of D-galactose derivatives: Advances and perspectives. International Journal of Biological Macromolecules. 267(Pt 2). 131518–131518. 5 indexed citations
5.
Chen, L, et al.. (2023). Biosynthesis of Lacto-N-biose I from starch and N-acetylglucosamine via an in vitro synthetic enzymatic biosystem. Synthetic and Systems Biotechnology. 8(3). 555–562. 6 indexed citations
6.
Meng, Dongdong, Meixia Liu, Hao Su, et al.. (2023). Coenzyme Engineering of Glucose-6-phosphate Dehydrogenase on a Nicotinamide-Based Biomimic and Its Application as a Glucose Biosensor. ACS Catalysis. 13(3). 1983–1998. 14 indexed citations
7.
Meng, Dongdong, et al.. (2022). An artificial multi-enzyme cascade biocatalysis for biomanufacturing of nicotinamide mononucleotide from starch and nicotinamide in one-pot. Enzyme and Microbial Technology. 162. 110122–110122. 24 indexed citations
8.
9.
Meng, Dongdong, Xinlei Wei, Xue Bai, Wei Zhou, & Chun You. (2020). Artificial in Vitro Synthetic Enzymatic Biosystem for the One-Pot Sustainable Biomanufacturing of Glucosamine from Starch and Inorganic Ammonia. ACS Catalysis. 10(23). 13809–13819. 35 indexed citations
10.
Bai, Xue, et al.. (2019). Facile synthesis of (−)‐vibo‐quercitol from maltodextrin via an in vitro synthetic enzymatic biosystem. Biotechnology and Bioengineering. 116(10). 2710–2719. 9 indexed citations
11.
12.
13.
Meng, Dongdong, et al.. (2019). The properties of the linker in a mini-scaffoldin influence the catalytic efficiency of scaffoldin-mediated enzyme complexes. Enzyme and Microbial Technology. 133. 109460–109460. 9 indexed citations
14.
Meng, Dongdong, et al.. (2019). Enzymatic characterization of a thermostable phosphatase from Thermomicrobium roseum and its application for biosynthesis of fructose from maltodextrin. Applied Microbiology and Biotechnology. 103(15). 6129–6139. 12 indexed citations
15.
Wei, Xinlei, et al.. (2018). Conversion of d-glucose to l-lactate via pyruvate by an optimized cell-free enzymatic biosystem containing minimized reactions. Synthetic and Systems Biotechnology. 3(3). 204–210. 25 indexed citations
16.
Meng, Dongdong, Xi Liu, Sheng Dong, et al.. (2017). Structural insights into the substrate specificity of a glycoside hydrolase family 5 lichenase from Caldicellulosiruptor sp. F32. Biochemical Journal. 474(20). 3373–3389. 20 indexed citations
17.
Meng, Dongdong, Bing Wang, Xiaoqing Ma, et al.. (2016). Characterization of a thermostable endo-1,3(4)-β-glucanase from Caldicellulosiruptor sp. strain F32 and its application for yeast lysis. Applied Microbiology and Biotechnology. 100(11). 4923–4934. 20 indexed citations
18.
19.
Meng, Dongdong, Xiaohua Chen, Ming Lu, et al.. (2015). Distinct Roles for Carbohydrate-Binding Modules of Glycoside Hydrolase 10 (GH10) and GH11 Xylanases from Caldicellulosiruptor sp. Strain F32 in Thermostability and Catalytic Efficiency. Applied and Environmental Microbiology. 81(6). 2006–2014. 56 indexed citations
20.
Meng, Dongdong, et al.. (2013). An extremely thermophilic anaerobic bacterium Caldicellulosiruptor sp. F32 exhibits distinctive properties in growth and xylanases during xylan hydrolysis. Enzyme and Microbial Technology. 53(3). 194–199. 26 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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