Hai‐Meng Zhou

1.2k total citations
56 papers, 1.0k citations indexed

About

Hai‐Meng Zhou is a scholar working on Molecular Biology, Materials Chemistry and Endocrinology, Diabetes and Metabolism. According to data from OpenAlex, Hai‐Meng Zhou has authored 56 papers receiving a total of 1.0k indexed citations (citations by other indexed papers that have themselves been cited), including 45 papers in Molecular Biology, 18 papers in Materials Chemistry and 11 papers in Endocrinology, Diabetes and Metabolism. Recurrent topics in Hai‐Meng Zhou's work include Enzyme Structure and Function (18 papers), Protein Structure and Dynamics (15 papers) and Alkaline Phosphatase Research Studies (10 papers). Hai‐Meng Zhou is often cited by papers focused on Enzyme Structure and Function (18 papers), Protein Structure and Dynamics (15 papers) and Alkaline Phosphatase Research Studies (10 papers). Hai‐Meng Zhou collaborates with scholars based in China, South Korea and Russia. Hai‐Meng Zhou's co-authors include Yong‐Doo Park, Qijun Chen, Qiang Xie, Wen‐Bin Ou, Yong‐Bin Yan, Huawei He, Jun Zhang, Jia Chen, Tong Zhang and Xuechen Wang and has published in prestigious journals such as Cancer Research, Analytical Biochemistry and Scientific Reports.

In The Last Decade

Hai‐Meng Zhou

51 papers receiving 1.0k citations

Peers

Hai‐Meng Zhou

BIOTE

Nathalie Rugani France

Nham T. Nguyen Canada

Jun‐yong Choe United States

Chrislaine Martinez France

Shigeyuki Imamura Japan

D.G. Herries United Kingdom

Charlotta Filling Sweden

F. Favier France

C. L. Tsou China

Roberto Contestabile Italy

Nathalie Rugani France

Hai‐Meng Zhou

1.3k ×1.8

124 ×0.5

149 ×1.1

73 ×0.6

BIOTE

44 ×0.4

Citations per year, relative to Hai‐Meng Zhou Hai‐Meng Zhou (= 1×) peers Nathalie Rugani

Countries citing papers authored by Hai‐Meng Zhou

Since Specialization

Citations

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

Fields of papers citing papers by Hai‐Meng Zhou

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Hai‐Meng Zhou

This figure shows the co-authorship network connecting the top 25 collaborators of Hai‐Meng Zhou. A scholar is included among the top collaborators of Hai‐Meng Zhou 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 Hai‐Meng Zhou. Hai‐Meng Zhou 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

Zhou, Hai‐Meng, et al.. (2025). CLK2 Regulates the KEAP1/NRF2 and p53 Pathways to Suppress Ferroptosis in Colorectal Cancer. Cancer Research. 85(23). 4734–4750. 2 indexed citations

Liu, Huihui, Xiangjun Chen, Zhe Chen, et al.. (2016). A single residue substitution accounts for the significant difference in thermostability between two isoforms of human cytosolic creatine kinase. Scientific Reports. 6(1). 21191–21191. 5 indexed citations

Liu, Yongli, et al.. (2012). Comparison of inactivation and unfolding of calf intestinal alkaline phosphatase in guanidinium chloride solution. Tsinghua Science & Technology. 7(4). 425–429.

Xie, Qiang, Fanguo Meng, & Hai‐Meng Zhou. (2012). Low temperature induced conformation changes of aminoacylase. Tsinghua Science & Technology. 9(1). 76–80.

Lee, Jinhyuk, Sang Ho Oh, Hongjian Liu, et al.. (2012). Effects of osmolytes on human brain-type creatine kinase folding in dilute solutions and crowding systems. International Journal of Biological Macromolecules. 51(5). 845–858. 14 indexed citations

Chen, Qijun, Hai‐Meng Zhou, Jia Chen, & Xuechen Wang. (2006). A Gateway-based platform for multigene plant transformation. Plant Molecular Biology. 62(6). 927–936. 64 indexed citations

Xiang, Wei, et al.. (2006). Conformational changes and inactivation of bovine carbonic anhydrase II in 2,2,2-Trifluoroethanol solutions. Biochemistry (Moscow). 71(S1). S77–S82. 11 indexed citations

He, Huawei, Jun Zhang, Hai‐Meng Zhou, & Yong‐Bin Yan. (2005). Conformational Change in the C-Terminal Domain Is Responsible for the Initiation of Creatine Kinase Thermal Aggregation. Biophysical Journal. 89(4). 2650–2658. 74 indexed citations

Xie, Qiang, Tai L. Guo, Tingting Wang, Lu Jie, & Hai‐Meng Zhou. (2003). Aspartate-induced aminoacylase folding and forming of molten globule. The International Journal of Biochemistry & Cell Biology. 35(11). 1558–1572. 8 indexed citations

10.

Xie, Qiang, Tai L. Guo, Lu Jie, & Hai‐Meng Zhou. (2003). The guanidine like effects of arginine on aminoacylase and salt-induced molten globule state. The International Journal of Biochemistry & Cell Biology. 36(2). 296–306. 43 indexed citations

11.

Li, Sen, et al.. (2001). Aggregation of creatine kinase during refolding and chaperonin-mediated folding of creatine kinase. The International Journal of Biochemistry & Cell Biology. 33(3). 279–286. 33 indexed citations

12.

Zhu, Ying, et al.. (2000). Conformational changes and inactivation of calf intestinal alkaline phosphatase in trifluoroethanol solutions. The International Journal of Biochemistry & Cell Biology. 32(8). 887–894. 11 indexed citations

13.

Yang, Yi & Hai‐Meng Zhou. (1999). Cause of Irreversible Inactivation of Aminoacylase in Urea Solution. Tsinghua Science & Technology. 4(3). 1528–1531. 1 indexed citations

14.

Chen, Qing‐Xi, et al.. (1998). The effects of N‐thiophosphoryl amino acids on the activity of green crab (Scylla Serrata) alkaline phosphatase. IUBMB Life. 45(3). 465–473. 12 indexed citations

15.

Chen, Qing‐Xi & Hai‐Meng Zhou. (1998). An essential lysine residue of green crab (Scylla Serrata) alkaline phosphatase. IUBMB Life. 46(2). 225–231. 6 indexed citations

16.

He, Biao, Tong Zhang, & Hai‐Meng Zhou. (1997). Comparison of inactivation and conformational changes of aminoacylase during denaturation in lithium dodecylsulphate solutions. International Journal of Biological Macromolecules. 20(1). 53–62. 11 indexed citations

17.

Chen, Qing‐Xi, et al.. (1997). Unfolding and inactivation of penaeus penicillatus acid phosphatase during denaturation by guanidine hydrochloride. IUBMB Life. 42(3). 517–526. 7 indexed citations

18.

Wang, Zefeng, et al.. (1995). Aminoacylase from pig kidney contains no disulfide bonds. 38(12). 1448–1454. 2 indexed citations

19.

Zou, Xiaoming, et al.. (1995). Unfolding, conformational change of active sites and inactivation of creatine kinase in SDS solutions. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1251(2). 109–114. 31 indexed citations

20.

Wang, Hongrui, Tong Zhang, & Hai‐Meng Zhou. (1995). Comparison of inactivation and conformational changes of aminoacylase during guanidinium chloride denaturation. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1248(2). 97–106. 38 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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