Ho Zoon Chae

10.1k total citations · 5 hit papers
51 papers, 8.7k citations indexed

About

Ho Zoon Chae is a scholar working on Molecular Biology, Biochemistry and Nutrition and Dietetics. According to data from OpenAlex, Ho Zoon Chae has authored 51 papers receiving a total of 8.7k indexed citations (citations by other indexed papers that have themselves been cited), including 43 papers in Molecular Biology, 11 papers in Biochemistry and 8 papers in Nutrition and Dietetics. Recurrent topics in Ho Zoon Chae's work include Redox biology and oxidative stress (35 papers), Heat shock proteins research (13 papers) and Glutathione Transferases and Polymorphisms (12 papers). Ho Zoon Chae is often cited by papers focused on Redox biology and oxidative stress (35 papers), Heat shock proteins research (13 papers) and Glutathione Transferases and Polymorphisms (12 papers). Ho Zoon Chae collaborates with scholars based in South Korea, United States and Italy. Ho Zoon Chae's co-authors include Sue Goo Rhee, Kanghwa Kim, Sang Won Kang, Suk‐Jae Chung, Sue Goo Rhee, Hyun Ae Woo, Stephen J. Taylor, John H. Exton, Earl R. Stadtman and Sung Chul Hwang and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

Ho Zoon Chae

51 papers receiving 8.6k citations

Hit Papers

Peroxiredoxins: A historical overview and speculativ... 1991 2026 2002 2014 2005 1994 1991 1994 1998 250 500 750 1000

Peers

Ho Zoon Chae
Sang Won Kang South Korea
Ho Zoon Chae
Citations per year, relative to Ho Zoon Chae Ho Zoon Chae (= 1×) peers Sang Won Kang

Countries citing papers authored by Ho Zoon Chae

Since Specialization
Citations

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

Fields of papers citing papers by Ho Zoon Chae

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Ho Zoon Chae. 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 Ho Zoon Chae. The network helps show where Ho Zoon Chae may publish in the future.

Co-authorship network of co-authors of Ho Zoon Chae

This figure shows the co-authorship network connecting the top 25 collaborators of Ho Zoon Chae. A scholar is included among the top collaborators of Ho Zoon Chae 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 Ho Zoon Chae. Ho Zoon Chae 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.
Cho, Dong‐Hyung, et al.. (2017). Peroxiredoxins are required for spindle assembly, chromosome organization, and polarization in mouse oocytes. Biochemical and Biophysical Research Communications. 489(2). 193–199. 6 indexed citations
2.
Lee, Hae‐Young, Min-Hee Kim, Dongho Choi, et al.. (2015). Development of real-time PCR assay for genetic identification of the mottled skate, Beringraja pulchra. Forensic Science International. 255. 80–84. 7 indexed citations
3.
Kang, Ji‐Yeon, So Young Kim, Doo‐Il Kim, et al.. (2011). Characterization of diverse natural variants of CYP102A1 found within a species of Bacillus megaterium. AMB Express. 1(1). 1–1. 222 indexed citations
4.
Ahn, Taeho, et al.. (2009). Refolding and reconstitution of human recombinant Bax inhibitor-1 into liposomes from inclusion bodies expressed in Escherichia coli. Protein Expression and Purification. 66(1). 35–38. 3 indexed citations
5.
Kim, Dong‐Hyun, Keonhee Kim, Emre M. Isin, et al.. (2007). Heterologous expression and characterization of wild-type human cytochrome P450 1A2 without conventional N-terminal modification in Escherichia coli. Protein Expression and Purification. 57(2). 188–200. 24 indexed citations
6.
Rhee, Sue Goo, Ho Zoon Chae, & Kanghwa Kim. (2005). Peroxiredoxins: A historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling. Free Radical Biology and Medicine. 38(12). 1543–1552. 1142 indexed citations breakdown →
7.
Choi, Hoon‐In, Kyung Soon Kim, Chae Young Hwang, et al.. (2005). Redox-regulated cochaperone activity of the human DnaJ homolog Hdj2. Free Radical Biology and Medicine. 40(4). 651–659. 22 indexed citations
8.
Hwang, Chae Young, Kwang Dong Kim, Sung Sup Park, et al.. (2004). Thioredoxin modulates activator protein 1 (AP-1) activity and p27Kip1 degradation through direct interaction with Jab1. Oncogene. 23(55). 8868–8875. 64 indexed citations
9.
Woo, Hyun Ae, Sang Won Kang, Hyung Ki Kim, et al.. (2003). Reversible Oxidation of the Active Site Cysteine of Peroxiredoxins to Cysteine Sulfinic Acid. Journal of Biological Chemistry. 278(48). 47361–47364. 213 indexed citations
10.
Koo, Kyung Hee, Songmi Lee, Soo Jeong, et al.. (2002). Regulation of Thioredoxin Peroxidase Activity by C-terminal Truncation. Archives of Biochemistry and Biophysics. 397(2). 312–318. 93 indexed citations
11.
Jung, Haiyoung, et al.. (2001). Regulation of Macrophage Migration Inhibitory Factor and Thiol-specific Antioxidant Protein PAG by Direct Interaction. Journal of Biological Chemistry. 276(18). 15504–15510. 95 indexed citations
12.
Hwang, Young Sun, et al.. (2001). Cyclophilin A Binds to Peroxiredoxins and Activates Its Peroxidase Activity. Journal of Biological Chemistry. 276(32). 29826–29832. 176 indexed citations
13.
Chae, Ho Zoon, et al.. (1999). Characterization of three isoforms of mammalian peroxiredoxin that reduce peroxides in the presence of thioredoxin. Diabetes Research and Clinical Practice. 45(2-3). 101–112. 320 indexed citations
14.
Chae, Ho Zoon, Sang Won Kang, & Sue Goo Rhee. (1999). Isoforms of mammalian peroxiredoxin that reduce peroxides in presence of thioredoxin. Methods in enzymology on CD-ROM/Methods in enzymology. 300. 219–226. 202 indexed citations
15.
Lyu, Myung Soo, Ho Zoon Chae, Tae‐Hoon Lee, et al.. (1999). Genetic mapping of six mouse peroxiredoxin genes and fourteen peroxiredoxin related sequences. Mammalian Genome. 10(10). 1017–1019. 29 indexed citations
16.
Chae, Ho Zoon, et al.. (1998). The type II peroxiredoxin gene family of the mouse: molecular structure, expression and evolution. Gene. 216(1). 197–205. 45 indexed citations
17.
Jin, Dong‐Yan, Ho Zoon Chae, Sue Goo Rhee, & Kuan‐Teh Jeang. (1997). Regulatory Role for a Novel Human Thioredoxin Peroxidase in NF-κB Activation. Journal of Biological Chemistry. 272(49). 30952–30961. 374 indexed citations
18.
Rhee, Sue Goo, Ho Zoon Chae, Moon B. Yim, et al.. (1994). Antioxidant Defense Mechanisms: A New Thiol‐Specific Antioxidant Enzyme. Annals of the New York Academy of Sciences. 738(1). 86–92. 54 indexed citations
19.
Taylor, Stephen J., et al.. (1991). Activation of the β1 isozyme of phospholipase C by α subunits of the Gq class of G proteins. Nature. 350(6318). 516–518. 672 indexed citations breakdown →
20.
Kim, Yu Sam & Ho Zoon Chae. (1990). A model of nitrogen flow by malonamate in Rhizobiumjaponicum-soybean symbiosis. Biochemical and Biophysical Research Communications. 169(2). 692–699. 17 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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