Chih‐Chen Wang

1.6k total citations
30 papers, 1.1k citations indexed

About

Chih‐Chen Wang is a scholar working on Molecular Biology, Cell Biology and Surgery. According to data from OpenAlex, Chih‐Chen Wang has authored 30 papers receiving a total of 1.1k indexed citations (citations by other indexed papers that have themselves been cited), including 19 papers in Molecular Biology, 17 papers in Cell Biology and 7 papers in Surgery. Recurrent topics in Chih‐Chen Wang's work include Endoplasmic Reticulum Stress and Disease (17 papers), Heat shock proteins research (9 papers) and Pancreatic function and diabetes (7 papers). Chih‐Chen Wang is often cited by papers focused on Endoplasmic Reticulum Stress and Disease (17 papers), Heat shock proteins research (9 papers) and Pancreatic function and diabetes (7 papers). Chih‐Chen Wang collaborates with scholars based in China, Taiwan and United States. Chih‐Chen Wang's co-authors include Chen‐Lu Tsou, Lei Wang, Huimin Ke, Wang Xie, Chao Wang, Weimin Gong, Jinqi Ren, Wei Li, Wei Feng and Jiaojiao Yu and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Angewandte Chemie International Edition.

In The Last Decade

Chih‐Chen Wang

29 papers receiving 1.1k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Chih‐Chen Wang China 18 655 582 147 133 109 30 1.1k
Jun Hoseki Japan 17 898 1.4× 736 1.3× 152 1.0× 346 2.6× 75 0.7× 24 1.5k
Catherine E. Jessop United Kingdom 8 642 1.0× 652 1.1× 143 1.0× 154 1.2× 64 0.6× 8 1.1k
Tiziana Anelli Italy 19 1.0k 1.6× 1.1k 2.0× 313 2.1× 402 3.0× 137 1.3× 31 1.9k
Ramachandra K. Reddy United States 10 746 1.1× 600 1.0× 132 0.9× 254 1.9× 23 0.2× 11 1.2k
John R. Yates United States 7 936 1.4× 407 0.7× 77 0.5× 179 1.3× 43 0.4× 8 1.4k
Byoung Heon Kang South Korea 21 1.6k 2.5× 313 0.5× 171 1.2× 166 1.2× 45 0.4× 46 2.0k
Ningguo Gao United States 20 1.0k 1.5× 458 0.8× 310 2.1× 230 1.7× 47 0.4× 30 1.5k
Georg H. Lüers Germany 23 1.4k 2.2× 308 0.5× 142 1.0× 108 0.8× 28 0.3× 47 1.8k
Robert J. Boorstein United States 20 1.4k 2.2× 462 0.8× 72 0.5× 263 2.0× 38 0.3× 30 1.8k
Sandra Lobo United States 13 981 1.5× 404 0.7× 62 0.4× 106 0.8× 28 0.3× 17 1.3k

Countries citing papers authored by Chih‐Chen Wang

Since Specialization
Citations

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

Fields of papers citing papers by Chih‐Chen Wang

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Chih‐Chen Wang. 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 Chih‐Chen Wang. The network helps show where Chih‐Chen Wang may publish in the future.

Co-authorship network of co-authors of Chih‐Chen Wang

This figure shows the co-authorship network connecting the top 25 collaborators of Chih‐Chen Wang. A scholar is included among the top collaborators of Chih‐Chen Wang 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 Chih‐Chen Wang. Chih‐Chen Wang 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.
Fang, Cheng, Qianzhao Ji, Lu Wang, et al.. (2023). Reducing oxidative protein folding alleviates senescence by minimizing ER‐to‐nucleus H 2 O 2 release. EMBO Reports. 24(8). e56439–e56439. 20 indexed citations
2.
3.
Zhang, Qiao, Yini Zhang, Guozhong Huang, et al.. (2021). Two protein disulfide isomerase subgroups work synergistically in catalyzing oxidative protein folding. PLANT PHYSIOLOGY. 188(1). 241–254. 15 indexed citations
4.
Wang, Lu, Junsong Zhou, Lei Wang, Chih‐Chen Wang, & David W. Essex. (2018). The b′ domain of protein disulfide isomerase cooperates with the a and a′ domains to functionally interact with platelets. Journal of Thrombosis and Haemostasis. 17(2). 371–382. 19 indexed citations
5.
Wang, Chao, Wei Li, Jinqi Ren, et al.. (2012). Structural Insights into the Redox-Regulated Dynamic Conformations of Human Protein Disulfide Isomerase. Antioxidants and Redox Signaling. 19(1). 36–45. 171 indexed citations
6.
Li, Heng, Huimin Ke, Guoping Ren, et al.. (2009). Thermal-Induced Dissociation and Unfolding of Homodimeric DsbC Revealed by Temperature-Jump Time-Resolved Infrared Spectra. Biophysical Journal. 97(10). 2811–2819. 12 indexed citations
7.
Wang, Likun, Lei Wang, Stefano Vavassori, et al.. (2008). Crystal structure of human ERp44 shows a dynamic functional modulation by its carboxy‐terminal tail. EMBO Reports. 9(7). 642–647. 64 indexed citations
8.
Zhao, Zhen, Jianping Ye, Huimin Ma, et al.. (2004). Donor–Donor Energy‐Migration Measurements of Dimeric DsbC Labeled at Its N‐Terminal Amines with Fluorescent Probes: A Study of Protein Unfolding. Angewandte Chemie International Edition. 43(32). 4216–4219. 23 indexed citations
9.
Duan, Xuejun, Zhen Zhao, Jianping Ye, et al.. (2004). Donor–Donor Energy‐Migration Measurements of Dimeric DsbC Labeled at Its N‐Terminal Amines with Fluorescent Probes: A Study of Protein Unfolding. Angewandte Chemie. 116(32). 4312–4315. 10 indexed citations
10.
Wang, Chih‐Chen. (2002). [8] Protein disulfide isomerase as an enzyme and a chaperone in protein folding. Methods in enzymology on CD-ROM/Methods in enzymology. 348. 66–75. 14 indexed citations
11.
Liang, Yi, Jian Li, Jie Chen, & Chih‐Chen Wang. (2001). Thermodynamics of the folding of D‐glyceraldehyde‐3‐phosphate dehydrogenase assisted by protein disulfide isomerase studied by microcalorimetry. European Journal of Biochemistry. 268(15). 4183–4189. 10 indexed citations
12.
Liu, Xiaoqing & Chih‐Chen Wang. (2001). Disulfide-dependent Folding and Export of Escherichia coli DsbC. Journal of Biological Chemistry. 276(2). 1146–1151. 31 indexed citations
13.
Zhang, Sen, Jian Li, & Chih‐Chen Wang. (2001). GroEL-Assisted Dehydrogenase Folding Mediated by Coenzyme Is ATP-Independent. Biochemical and Biophysical Research Communications. 285(2). 277–282. 6 indexed citations
14.
Lin, Zong, Chih‐Chen Wang, & Chen‐Lu Tsou. (2000). High concentrations of d-glyceraldehyde-3-phosphate dehydrogenase stabilize the enzyme against denaturation by low concentrations of GuHCl. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1481(2). 283–288. 5 indexed citations
15.
Sun, Xiuxia, et al.. (2000). Contributions of protein disulfide isomerase domains to its chaperone activity. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1481(1). 45–54. 21 indexed citations
16.
Zhang, Sen, Jian Li, Chih‐Chen Wang, & Chen‐Lu Tsou. (1999). Metal regulation of metallothionein participation in redox reactions. FEBS Letters. 462(3). 383–386. 21 indexed citations
17.
Liu, Xiaoqing, Sen Zhang, Xian‐Ming Pan, & Chih‐Chen Wang. (1999). A novel method for increasing production of mature proteins in the periplasm of Escherichia coli. Protein Science. 8(10). 2085–2089. 9 indexed citations
18.
Yao, Yi Ju, et al.. (1998). Assay for enzyme activity by following the absorbance change of pH-indicators. Journal of Biochemical and Biophysical Methods. 36(2-3). 119–130. 17 indexed citations
19.
20.
Yu, Xuan‐Chuan, Chih‐Chen Wang, & Chen‐Lu Tsou. (1994). Association and dissociation of protein disulfide isomerase. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1207(1). 109–113. 21 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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