Chih-chen Wang

3.1k total citations
50 papers, 2.5k citations indexed

About

Chih-chen Wang is a scholar working on Cell Biology, Molecular Biology and Materials Chemistry. According to data from OpenAlex, Chih-chen Wang has authored 50 papers receiving a total of 2.5k indexed citations (citations by other indexed papers that have themselves been cited), including 34 papers in Cell Biology, 33 papers in Molecular Biology and 10 papers in Materials Chemistry. Recurrent topics in Chih-chen Wang's work include Endoplasmic Reticulum Stress and Disease (31 papers), Heat shock proteins research (17 papers) and Enzyme Structure and Function (8 papers). Chih-chen Wang is often cited by papers focused on Endoplasmic Reticulum Stress and Disease (31 papers), Heat shock proteins research (17 papers) and Enzyme Structure and Function (8 papers). Chih-chen Wang collaborates with scholars based in China, Taiwan and United Kingdom. Chih-chen Wang's co-authors include Lei Wang, Xi Wang, Hui Quan, Chunjuan Huang, Guoping Ren, Hui Zhou, Li Zhu, Xiuxia Sun, Chao Wang and Wang Xie and has published in prestigious journals such as Journal of Biological Chemistry, PLoS ONE and Journal of Molecular Biology.

In The Last Decade

Chih-chen Wang

50 papers receiving 2.5k 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 30 1.6k 1.3k 283 265 246 50 2.5k
Wei Feng China 32 1.8k 1.2× 1.2k 1.0× 360 1.3× 216 0.8× 138 0.6× 90 3.1k
William A. Maltese United States 36 2.7k 1.7× 1.1k 0.9× 703 2.5× 354 1.3× 272 1.1× 79 4.1k
Hisao Kondo Japan 31 2.5k 1.5× 1.8k 1.4× 478 1.7× 240 0.9× 91 0.4× 73 3.5k
Huanchen Wang United States 35 2.7k 1.7× 680 0.5× 591 2.1× 264 1.0× 331 1.3× 83 3.9k
Gabriel del Rio Mexico 19 2.2k 1.4× 1.0k 0.8× 593 2.1× 137 0.5× 367 1.5× 45 3.2k
Gerardo Z. Lederkremer Israel 32 1.8k 1.1× 1.7k 1.3× 661 2.3× 378 1.4× 454 1.8× 58 2.9k
Victor C. Yu Singapore 41 4.3k 2.7× 651 0.5× 391 1.4× 250 0.9× 586 2.4× 75 5.8k
Tomohisa Horibe Japan 27 1.3k 0.8× 722 0.6× 262 0.9× 211 0.8× 289 1.2× 67 2.0k
Su‐Chen Li United States 28 1.7k 1.1× 349 0.3× 358 1.3× 646 2.4× 232 0.9× 106 2.6k
Lifeng Pan China 31 1.8k 1.1× 683 0.5× 740 2.6× 180 0.7× 369 1.5× 78 2.7k

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.
Wang, Lei, et al.. (2023). V-ATPase recruitment to ER exit sites switches COPII-mediated transport to lysosomal degradation. Developmental Cell. 58(23). 2761–2775.e5. 15 indexed citations
2.
Zhou, Haitao, Shanshan Ding, Chuanxin Sun, et al.. (2022). Lycium barbarum Extracts Extend Lifespan and Alleviate Proteotoxicity in Caenorhabditis elegans. Frontiers in Nutrition. 8. 815947–815947. 13 indexed citations
3.
Liu, Ping, Xi Wang, Hongyu Zhao, et al.. (2022). SARS-CoV-2 ORF8 reshapes the ER through forming mixed disulfides with ER oxidoreductases. Redox Biology. 54. 102388–102388. 24 indexed citations
4.
Qiao, Xinhua, Yingmin Zhang, Yini Zhang, et al.. (2022). ER reductive stress caused by Ero1α S-nitrosation accelerates senescence. Free Radical Biology and Medicine. 180. 165–178. 24 indexed citations
5.
Zhang, Lihui, et al.. (2016). Novel Roles of the Non-catalytic Elements of Yeast Protein-disulfide Isomerase in Its Interplay with Endoplasmic Reticulum Oxidoreductin 1. Journal of Biological Chemistry. 291(15). 8283–8294. 16 indexed citations
6.
Zhu, Li, et al.. (2014). A Novel Reaction of Peroxiredoxin 4 towards Substrates in Oxidative Protein Folding. PLoS ONE. 9(8). e105529–e105529. 23 indexed citations
7.
8.
Nguyen, Van Dat, Mirva J. Saaranen, Anna‐Riikka Karala, et al.. (2011). Two Endoplasmic Reticulum PDI Peroxidases Increase the Efficiency of the Use of Peroxide during Disulfide Bond Formation. Journal of Molecular Biology. 406(3). 503–515. 217 indexed citations
9.
Wang, Chao, Jiang Yu, Linsheng Huo, et al.. (2011). Human Protein-disulfide Isomerase Is a Redox-regulated Chaperone Activated by Oxidation of Domain a′. Journal of Biological Chemistry. 287(2). 1139–1149. 106 indexed citations
10.
Liu, Xiang, Xinping Chen, Mei Song, et al.. (2010). Drosophila Histone Deacetylase 6 Protects Dopaminergic Neurons against α-Synuclein Toxicity by Promoting Inclusion Formation. Molecular Biology of the Cell. 21(13). 2128–2137. 99 indexed citations
11.
Wang, Chao, Sihong Chen, Xi Wang, et al.. (2010). Plasticity of Human Protein Disulfide Isomerase. Journal of Biological Chemistry. 285(35). 26788–26797. 57 indexed citations
12.
Wang, Lei, Ateesh Sidhu, Li Zhu, et al.. (2008). Reconstitution of Human Ero1-Lα/Protein-Disulfide Isomerase Oxidative Folding Pathway in Vitro. Journal of Biological Chemistry. 284(1). 199–206. 128 indexed citations
13.
Huang, Chunjuan, Guoping Ren, Hui Zhou, & Chih-chen Wang. (2005). A new method for purification of recombinant human α-synuclein in Escherichia coli. Protein Expression and Purification. 42(1). 173–177. 153 indexed citations
14.
Shi, Yuanyuan, Xinguo Hong, & Chih-chen Wang. (2005). The C-terminal (331–376) Sequence of Escherichia coli DnaJ Is Essential for Dimerization and Chaperone Activity. Journal of Biological Chemistry. 280(24). 22761–22768. 43 indexed citations
15.
Hong, Xinguo, et al.. (2005). Annular Arrangement and Collaborative Actions of Four Domains of Protein-disulfide Isomerase. Journal of Biological Chemistry. 281(10). 6581–6588. 37 indexed citations
16.
Ren, Guoping, Zong Lin, Chen‐Lu Tsou, & Chih-chen Wang. (2003). Effects of Macromolecular Crowding on the Unfolding and the Refolding of d-Glyceraldehyde-3-Phosophospate Dehydrogenase. Journal of Protein Chemistry. 22(5). 431–439. 28 indexed citations
17.
Li, Jian, Sen Zhang, & Chih-chen Wang. (2001). Effects of Macromolecular Crowding on the Refolding of Glucose- 6-phosphate Dehydrogenase and Protein Disulfide Isomerase. Journal of Biological Chemistry. 276(37). 34396–34401. 39 indexed citations
18.
Sun, Xiuxia & Chih-chen Wang. (2000). The N-terminal Sequence (Residues 1–65) Is Essential for Dimerization, Activities, and Peptide Binding of Escherichia coli DsbC. Journal of Biological Chemistry. 275(30). 22743–22749. 62 indexed citations
19.
Li, Jian & Chih-chen Wang. (1999). “Half of the Sites” Binding ofd-Glyceraldehyde-3-phosphate Dehydrogenase Folding Intermediate with GroEL. Journal of Biological Chemistry. 274(16). 10790–10794. 18 indexed citations
20.
Wang, Chih-chen. (1998). Protein Disulfide Isomerase Assists Protein Folding as Both an Isomerase and a Chaperonea. Annals of the New York Academy of Sciences. 864(1). 9–13. 36 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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