Chi‐Ching Hwang

1.1k total citations
47 papers, 883 citations indexed

About

Chi‐Ching Hwang is a scholar working on Molecular Biology, Clinical Biochemistry and Cell Biology. According to data from OpenAlex, Chi‐Ching Hwang has authored 47 papers receiving a total of 883 indexed citations (citations by other indexed papers that have themselves been cited), including 32 papers in Molecular Biology, 8 papers in Clinical Biochemistry and 8 papers in Cell Biology. Recurrent topics in Chi‐Ching Hwang's work include Enzyme Structure and Function (7 papers), Aldose Reductase and Taurine (6 papers) and Enzyme Catalysis and Immobilization (6 papers). Chi‐Ching Hwang is often cited by papers focused on Enzyme Structure and Function (7 papers), Aldose Reductase and Taurine (6 papers) and Enzyme Catalysis and Immobilization (6 papers). Chi‐Ching Hwang collaborates with scholars based in Taiwan, United States and Germany. Chi‐Ching Hwang's co-authors include Lea‐Yea Chuang, Paul Cook, Charles B. Grissom, Paul Cook, Shean‐Jaw Chiou, Jinn‐Yuh Guh, William E. Karsten, Michael F. Dunn, Eilika U. Woehl and Tzu-Pin Wang and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and PLoS ONE.

In The Last Decade

Chi‐Ching Hwang

47 papers receiving 873 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Chi‐Ching Hwang Taiwan 19 501 102 101 95 77 47 883
Vikas Rishi India 22 878 1.8× 47 0.5× 90 0.9× 84 0.9× 102 1.3× 56 1.4k
Farah Anjum Saudi Arabia 18 594 1.2× 56 0.5× 99 1.0× 78 0.8× 84 1.1× 72 1.0k
Jeffrey D. Scholten United States 17 769 1.5× 59 0.6× 134 1.3× 86 0.9× 122 1.6× 35 1.1k
Maria Antonietta Belisario Italy 23 697 1.4× 46 0.5× 47 0.5× 85 0.9× 71 0.9× 51 1.2k
Seema Kumari India 16 708 1.4× 87 0.9× 71 0.7× 69 0.7× 169 2.2× 45 1.3k
Silvia Franceschelli Italy 19 760 1.5× 86 0.8× 40 0.4× 158 1.7× 111 1.4× 43 1.2k
D. Perrone Italy 11 825 1.6× 65 0.6× 49 0.5× 107 1.1× 167 2.2× 15 1.4k
Sarwat Fatima Hong Kong 18 610 1.2× 139 1.4× 47 0.5× 68 0.7× 142 1.8× 34 1.1k
Yan Guan China 16 598 1.2× 57 0.6× 47 0.5× 25 0.3× 94 1.2× 26 1.0k
Kaifeng Hu China 19 820 1.6× 53 0.5× 72 0.7× 56 0.6× 39 0.5× 84 1.2k

Countries citing papers authored by Chi‐Ching Hwang

Since Specialization
Citations

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

Fields of papers citing papers by Chi‐Ching Hwang

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Chi‐Ching Hwang. 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 Chi‐Ching Hwang. The network helps show where Chi‐Ching Hwang may publish in the future.

Co-authorship network of co-authors of Chi‐Ching Hwang

This figure shows the co-authorship network connecting the top 25 collaborators of Chi‐Ching Hwang. A scholar is included among the top collaborators of Chi‐Ching Hwang 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 Chi‐Ching Hwang. Chi‐Ching Hwang 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
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Severance, Scott, Chi‐Ching Hwang, Li‐Fang Wang, et al.. (2023). Manipulating Diastereomeric Bicyclononynes to Sensitively Determine Enzyme Activity and Facilitate Macromolecule Conjugations. ACS Omega. 8(48). 46073–46090. 1 indexed citations
3.
Chiou, Shean‐Jaw, et al.. (2022). Rational Engineering of 3α-Hydroxysteroid Dehydrogenase/Carbonyl Reductase for a Biomimetic Nicotinamide Mononucleotide Cofactor. Catalysts. 12(10). 1094–1094. 2 indexed citations
4.
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Chang, Yi‐Ting, Scott Severance, Jui‐Ying Feng, et al.. (2022). Time-dependent effects of storage at –80 °C on the stability of butyrylcholinesterase activity in human serum. Practical Laboratory Medicine. 31. e00298–e00298. 1 indexed citations
6.
Hwang, Chi‐Ching, et al.. (2021). Functional role of residues involved in substrate binding of human 4-hydroxyphenylpyruvate dioxygenase. Biochemical Journal. 478(12). 2201–2215. 5 indexed citations
7.
Hwang, Chi‐Ching, et al.. (2019). Thermodynamic analysis of remote substrate binding energy in 3α-hydroxysteroid dehydrogenase/carbonyl reductase catalysis. Chemico-Biological Interactions. 302. 183–189. 5 indexed citations
8.
Hwang, Chi‐Ching, et al.. (2017). Contribution of remote substrate binding energy to the enzymatic rate acceleration for 3α-hydroxysteroid dehydrogenase/carbonyl reductase. Chemico-Biological Interactions. 276. 133–140. 4 indexed citations
9.
Chiu, Chien‐Chih, Fang‐Rong Chang, Jeff Yi-Fu Chen, et al.. (2010). 4β-Hydroxywithanolide E from Physalis peruviana (golden berry) inhibits growth of human lung cancer cells through DNA damage, apoptosis and G2/M arrest. BMC Cancer. 10(1). 46–46. 80 indexed citations
10.
Eswaramoorthy, Rajalakshmanan, Chih‐Kuang Wang, Wen‐Cheng Chen, et al.. (2010). DDR1 regulates the stabilization of cell surface E‐cadherin and E‐cadherin‐mediated cell aggregation. Journal of Cellular Physiology. 224(2). 387–397. 41 indexed citations
11.
Chuang, Lea‐Yea, et al.. (2009). Role of S114 in the NADH-induced conformational change and catalysis of 3α-hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1794(10). 1459–1466. 6 indexed citations
12.
Wang, Yuanliang, et al.. (2009). Expression, Purification, and Characterization of a Human Recombinant 17β-Hydroxysteroid Dehydrogenase Type 1 in Escherichia coli. Molecular Biotechnology. 44(2). 133–139. 9 indexed citations
13.
Lin, Ching‐Chih, Shen‐Long Howng, Chia‐Yi Hsu, et al.. (2009). GSKIP, an inhibitor of GSK3β, mediates the N‐cadherin/β‐catenin pool in the differentiation of SH‐SY5Y cells. Journal of Cellular Biochemistry. 108(6). 1325–1336. 23 indexed citations
14.
Guh, Jinn‐Yuh, Chi‐Ching Hwang, Shean‐Jaw Chiou, et al.. (2009). Advanced glycation end‐products activate extracellular signal‐regulated kinase via the oxidative stress‐EGF receptor pathway in renal fibroblasts. Journal of Cellular Biochemistry. 109(1). 38–48. 31 indexed citations
15.
Howng, Shen‐Long, Chi‐Ching Hwang, Chia‐Yi Hsu, et al.. (2009). Involvement of the residues of GSKIP, AxinGID, and FRATtide in their binding with GSK3β to unravel a novel C-terminal scaffold-binding region. Molecular and Cellular Biochemistry. 339(1-2). 23–33. 16 indexed citations
16.
Wang, Chau‐Zen, et al.. (2009). Contributions of active site residues to cofactor binding and catalysis of 3α-hydroxysteroid dehydrogenase/carbonyl reductase. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1804(1). 235–241. 4 indexed citations
17.
Chuang, Lea‐Yea, et al.. (2007). Mechanism of Proton Transfer in the 3α-Hydroxysteroid Dehydrogenase/Carbonyl Reductase from Comamonas testosteroni. Journal of Biological Chemistry. 282(47). 34306–34314. 25 indexed citations
18.
Chou, Wen‐Wen, Jinn‐Yuh Guh, Jung‐Fa Tsai, et al.. (2007). Arecoline-induced growth arrest and p21WAF1 expression are dependent on p53 in rat hepatocytes. Toxicology. 243(1-2). 1–10. 45 indexed citations
19.
Hwang, Chi‐Ching, et al.. (2004). Mechanistic Roles of Ser-114, Tyr-155, and Lys-159 in 3α-Hydroxysteroid Dehydrogenase/Carbonyl Reductase from Comamonas testosteroni. Journal of Biological Chemistry. 280(5). 3522–3528. 39 indexed citations
20.

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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