Zengyi Chang

3.4k total citations
82 papers, 2.7k citations indexed

About

Zengyi Chang is a scholar working on Molecular Biology, Materials Chemistry and Genetics. According to data from OpenAlex, Zengyi Chang has authored 82 papers receiving a total of 2.7k indexed citations (citations by other indexed papers that have themselves been cited), including 70 papers in Molecular Biology, 37 papers in Materials Chemistry and 20 papers in Genetics. Recurrent topics in Zengyi Chang's work include Protein Structure and Dynamics (42 papers), Heat shock proteins research (41 papers) and Enzyme Structure and Function (37 papers). Zengyi Chang is often cited by papers focused on Protein Structure and Dynamics (42 papers), Heat shock proteins research (41 papers) and Enzyme Structure and Function (37 papers). Zengyi Chang collaborates with scholars based in China, United States and Russia. Zengyi Chang's co-authors include Xinmiao Fu, Wangwang Jiao, Florante A. Quiocho, Xuefeng Zhang, Weizhe Hong, Xi Ge, Abuduaini Abulimiti, Chong Liu, Rodney E. Kellems and Bryan C. Dickinson and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Nature Communications.

In The Last Decade

Zengyi Chang

79 papers receiving 2.7k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Zengyi Chang China 31 2.1k 777 576 264 199 82 2.7k
Ann H. West United States 25 1.9k 0.9× 406 0.5× 748 1.3× 288 1.1× 272 1.4× 67 3.0k
David A. Dougan Australia 27 2.5k 1.2× 649 0.8× 848 1.5× 498 1.9× 137 0.7× 45 2.9k
Emmanuel Courcelle France 6 2.0k 1.0× 586 0.8× 432 0.8× 212 0.8× 302 1.5× 7 3.3k
Begoña Heras Australia 28 1.5k 0.7× 399 0.5× 491 0.9× 487 1.8× 153 0.8× 90 2.5k
Svetlana E. Sedelnikova United Kingdom 32 2.1k 1.0× 708 0.9× 505 0.9× 169 0.6× 143 0.7× 109 2.9k
Joel R. Hoskins United States 32 2.9k 1.4× 833 1.1× 1.0k 1.8× 534 2.0× 125 0.6× 53 3.3k
Eilika Weber‐Ban Switzerland 31 3.0k 1.4× 691 0.9× 704 1.2× 556 2.1× 252 1.3× 62 3.6k
André Matagne Belgium 28 2.3k 1.1× 472 0.6× 274 0.5× 164 0.6× 259 1.3× 103 3.7k
Xinmiao Fu China 26 1.4k 0.7× 390 0.5× 377 0.7× 238 0.9× 94 0.5× 75 2.1k
Kürşad Turgay Germany 30 2.5k 1.2× 607 0.8× 1.4k 2.4× 275 1.0× 240 1.2× 45 3.1k

Countries citing papers authored by Zengyi Chang

Since Specialization
Citations

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

Fields of papers citing papers by Zengyi Chang

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Zengyi Chang

This figure shows the co-authorship network connecting the top 25 collaborators of Zengyi Chang. A scholar is included among the top collaborators of Zengyi Chang 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 Zengyi Chang. Zengyi Chang 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.
Ma, He, Zengyi Chang, Hongyu Sun, et al.. (2025). A novel Dual GLP-1/CCK Receptor Agonist Improves Cognitive Performance and Synaptogenesis in the 5 × FAD Alzheimer Mouse Model. Molecular Neurobiology. 62(9). 11920–11934.
2.
Wang, Yan, Rui Wang, Yang Liu, et al.. (2016). A Supercomplex Spanning the Inner and Outer Membranes Mediates the Biogenesis of β-Barrel Outer Membrane Proteins in Bacteria. Journal of Biological Chemistry. 291(32). 16720–16729. 41 indexed citations
3.
Chang, Zengyi. (2015). The discovery of Qinghaosu (artemisinin) as an effective anti-malaria drug: A unique China story. Science China Life Sciences. 59(1). 81–88. 28 indexed citations
4.
Fu, Xinmiao, Xiaodong Shi, Jiafeng Liu, et al.. (2013). Small Heat Shock Protein IbpB Acts as a Robust Chaperone in Living Cells by Hierarchically Activating Its Multi-type Substrate-binding Residues. Journal of Biological Chemistry. 288(17). 11897–11906. 30 indexed citations
5.
Liu, Chong, Kai Mao, Meng Zhang, et al.. (2007). The SH3-like Domain Switches Its Interaction Partners to Modulate the Repression Activity of Mycobacterial Iron-dependent Transcription Regulator in Response to Metal Ion Fluctuations. Journal of Biological Chemistry. 283(4). 2439–2453. 10 indexed citations
6.
7.
Feng, Yongjun, Wangwang Jiao, Xinmiao Fu, & Zengyi Chang. (2006). Stepwise disassembly and apparent nonstepwise reassembly for the oligomeric RbsD protein. Protein Science. 15(6). 1441–1448. 7 indexed citations
8.
Fu, Xinmiao & Zengyi Chang. (2006). Identification of bis-ANS binding sites in Mycobacterium tuberculosis small heat shock protein Hsp16.3: Evidences for a two-step substrate-binding mechanism. Biochemical and Biophysical Research Communications. 349(1). 167–171. 15 indexed citations
9.
Jiao, Wangwang, Pulin Li, Junrui Zhang, Hui Zhang, & Zengyi Chang. (2005). Small heat-shock proteins function in the insoluble protein complex. Biochemical and Biophysical Research Communications. 335(1). 227–231. 22 indexed citations
10.
Fu, Xinmiao, Xuefeng Zhang, & Zengyi Chang. (2005). 4,4′-Dianilino-1,1′-binaphthyl-5,5′-sulfonate, a novel molecule having chaperone-like activity. Biochemical and Biophysical Research Communications. 329(3). 1087–1093. 29 indexed citations
11.
Zhang, Hui, Xinmiao Fu, Wangwang Jiao, et al.. (2005). The association of small heat shock protein Hsp16.3 with the plasma membrane of Mycobacterium tuberculosis: Dissociation of oligomers is a prerequisite. Biochemical and Biophysical Research Communications. 330(4). 1055–1061. 24 indexed citations
12.
Chen, Xiaoyou, Xinmiao Fu, Yu Ma, & Zengyi Chang. (2005). Chaperone-Like Activity of Mycobacterium tuberculosis Hsp16.3 Does Not Require Its Intact (Native) Structures. Biochemistry (Moscow). 70(8). 913–919. 7 indexed citations
13.
Fu, Xinmiao, Hui Zhang, Xuefeng Zhang, et al.. (2004). A Dual Role for the N-terminal Region of Mycobacterium tuberculosis Hsp16.3 in Self-oligomerization and Binding Denaturing Substrate Proteins. Journal of Biological Chemistry. 280(8). 6337–6348. 64 indexed citations
14.
Zhang, Xuefeng & Zengyi Chang. (2004). Temperature Dependent Protease Activity and Structural Properties of Human HtrA2 Protease. Biochemistry (Moscow). 69(6). 687–692. 8 indexed citations
15.
Abulimiti, Abuduaini, et al.. (2003). Mycobacterium tuberculosis Hsp16.3 Nonamers are Assembled and Re-assembled via Trimer and Hexamer Intermediates. Journal of Molecular Biology. 326(4). 1013–1023. 19 indexed citations
16.
Fu, Xinmiao, et al.. (2003). Disulfide bonds convert small heat shock protein Hsp16.3 from a chaperone to a non-chaperone: implications for the evolution of cysteine in molecular chaperones. Biochemical and Biophysical Research Communications. 308(3). 627–635. 25 indexed citations
17.
Chen, Yong, Yingjie Lu, Hongwei Wang, et al.. (2003). Two-dimensional crystallization of a small heat shock protein HSP16.3 on lipid layer. Biochemical and Biophysical Research Communications. 310(2). 360–366. 6 indexed citations
18.
Chang, Zengyi, David K. Wilson, Rodney E. Kellems, & Florante A. Quiocho. (1997). Cysteine not required for catalytic activity of adenosine deaminase. Tsinghua Science & Technology. 2(1). 441–446. 1 indexed citations
19.
Chang, Zengyi, Todd P. Primm, Joanita Jakana, et al.. (1996). Mycobacterium tuberculosis 16-kDa Antigen (Hsp16.3) Functions as an Oligomeric Structure in Vitro to Suppress Thermal Aggregation. Journal of Biological Chemistry. 271(12). 7218–7223. 204 indexed citations
20.
Sharff, Andrew, David K. Wilson, Zengyi Chang, & Florante A. Quiocho. (1992). Refined 2.5Åstructure of murine adenosine deaminase at pH 6.0. Journal of Molecular Biology. 226(4). 917–921. 55 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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