Chong‐Hwan Chang

4.3k total citations · 1 hit paper
51 papers, 3.0k citations indexed

About

Chong‐Hwan Chang is a scholar working on Molecular Biology, Infectious Diseases and Virology. According to data from OpenAlex, Chong‐Hwan Chang has authored 51 papers receiving a total of 3.0k indexed citations (citations by other indexed papers that have themselves been cited), including 30 papers in Molecular Biology, 21 papers in Infectious Diseases and 17 papers in Virology. Recurrent topics in Chong‐Hwan Chang's work include HIV/AIDS drug development and treatment (21 papers), HIV Research and Treatment (17 papers) and Protein Structure and Dynamics (10 papers). Chong‐Hwan Chang is often cited by papers focused on HIV/AIDS drug development and treatment (21 papers), HIV Research and Treatment (17 papers) and Protein Structure and Dynamics (10 papers). Chong‐Hwan Chang collaborates with scholars based in United States, South Korea and Germany. Chong‐Hwan Chang's co-authors include M. Schiffer, Patrick Y. S. Lam, Prabhakar K. Jadhav, David M. Tiede, C. Nicholas Hodge, Lee T. Bacheler, James R. Norris, Susan Erickson‐Viitanen, Marlene M. Rayner and Jau Tang and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Chong‐Hwan Chang

51 papers receiving 2.9k citations

Hit Papers

Rational Design of Potent, Bioavailable, Nonpeptide Cycli... 1994 2026 2004 2015 1994 200 400 600

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Chong‐Hwan Chang United States 28 1.8k 769 700 564 324 51 3.0k
Susan Erickson‐Viitanen United States 40 2.4k 1.4× 1.4k 1.9× 1.2k 1.8× 1.1k 1.9× 272 0.8× 81 5.1k
Maria Miller United States 28 2.7k 1.5× 586 0.8× 1.3k 1.9× 1.2k 2.1× 204 0.6× 68 4.5k
Yuk Y. Sham United States 31 2.2k 1.2× 625 0.8× 289 0.4× 162 0.3× 182 0.6× 85 3.2k
Badry Bursulaya United States 31 1.5k 0.8× 863 1.1× 207 0.3× 74 0.1× 270 0.8× 57 3.4k
Dianne L. DeCamp United States 20 1.1k 0.6× 1.2k 1.5× 312 0.4× 235 0.4× 145 0.4× 32 2.8k
Jonathan M. Friedman United States 35 3.2k 1.8× 367 0.5× 1.7k 2.4× 1.5k 2.6× 70 0.2× 70 5.0k
John A. Secrist United States 38 3.4k 1.9× 1.7k 2.2× 1.4k 2.0× 265 0.5× 225 0.7× 169 5.5k
Robert S. McDowell United States 28 2.8k 1.6× 969 1.3× 166 0.2× 105 0.2× 486 1.5× 44 4.3k
L.S. Beese United States 39 6.1k 3.4× 544 0.7× 672 1.0× 224 0.4× 160 0.5× 73 7.1k
Martin Lepšı́k Czechia 32 1.3k 0.7× 730 0.9× 209 0.3× 132 0.2× 342 1.1× 94 2.9k

Countries citing papers authored by Chong‐Hwan Chang

Since Specialization
Citations

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

Fields of papers citing papers by Chong‐Hwan Chang

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Chong‐Hwan Chang

This figure shows the co-authorship network connecting the top 25 collaborators of Chong‐Hwan Chang. A scholar is included among the top collaborators of Chong‐Hwan 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 Chong‐Hwan Chang. Chong‐Hwan 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.
Park, Minhee, Hookeun Lee, Jong‐Moon Park, et al.. (2017). Enhancement of the Antitumor Effect of Methotrexate on Colorectal Cancer Cells via Lactate Calcium Salt Targeting Methionine Metabolism. Nutrition and Cancer. 69(4). 663–673. 8 indexed citations
2.
Seo, Hee Jeong, Min Ju Kim, Kwang‐Seop Song, et al.. (2009). Methylsulfonylpyrazolyl Oxadiazoles and Thiadiazoles as Potent, Orally Bioavailable Cannabinoid-1 Receptor Antagonists for the Treatment of Obesity. Future Medicinal Chemistry. 1(5). 947–967. 5 indexed citations
3.
Corte, James R., Tianan Fang, Donald Pinto, et al.. (2008). Structure–activity relationships of anthranilamide-based factor Xa inhibitors containing piperidinone and pyridinone P4 moieties. Bioorganic & Medicinal Chemistry Letters. 18(9). 2845–2849. 27 indexed citations
4.
Qiao, Jennifer X., Chong‐Hwan Chang, Daniel L. Cheney, et al.. (2007). SAR and X-ray structures of enantiopure 1,2-cis-(1R,2S)-cyclopentyldiamine and cyclohexyldiamine derivatives as inhibitors of coagulation Factor Xa. Bioorganic & Medicinal Chemistry Letters. 17(16). 4419–4427. 29 indexed citations
5.
Shen, Betty, et al.. (2007). The tertiary structure and domain organization of coagulation factor VIII. Blood. 111(3). 1240–1247. 186 indexed citations
6.
Kuhelj, Robert, Christopher J. Rizzo, Chong‐Hwan Chang, et al.. (2001). Inhibition of Human Endogenous Retrovirus-K10 Protease in Cell-free and Cell-based Assays. Journal of Biological Chemistry. 276(20). 16674–16682. 14 indexed citations
7.
Sielecki, Thais M., Jie Liu, J.K. Muckelbauer, et al.. (2001). Quinazolines as cyclin dependent kinase inhibitors. Bioorganic & Medicinal Chemistry Letters. 11(9). 1157–1160. 73 indexed citations
8.
Wei, Anzhi, Angela Smallwood, Richard Alexander, et al.. (1999). Crystallization and preliminary X-ray diffraction data of the complex of recombinant tick anticoagulant peptide (rTAP) and bovine factor Xa. Acta Crystallographica Section D Biological Crystallography. 55(4). 862–864. 2 indexed citations
9.
Rodgers, James D., Patrick Y. S. Lam, Barry L. Johnson, et al.. (1998). Design and selection of DMP 850 and DMP 851: the next generation of cyclic urea HIV protease inhibitors. Chemistry & Biology. 5(11). R312–R312. 1 indexed citations
10.
Marrone, Tami, J. Andrew McCammon, Haluk Resat, C. Nicholas Hodge, & Chong‐Hwan Chang. (1998). Solvation studies of DMP323 and A76928 bound to HIV protease: Analysis of water sites using grand canonical Monte Carlo simulations. Protein Science. 7(3). 573–579. 14 indexed citations
11.
Rodgers, James D., Barry L. Johnson, Susan Erickson‐Viitanen, et al.. (1998). Potent cyclic urea HIV protease inhibitors with 3-aminoindazole P2/P2′ groups. Bioorganic & Medicinal Chemistry Letters. 8(7). 715–720. 34 indexed citations
12.
Wei, Anzhi, et al.. (1998). Unexpected binding mode of tick anticoagulant peptide complexed to bovine factor Xa. Journal of Molecular Biology. 283(1). 147–154. 69 indexed citations
13.
Paul, J., Prabhakar K. Jadhav, Patrick Y. S. Lam, et al.. (1998). Molecular Recognition of Cyclic Urea HIV-1 Protease Inhibitors. Journal of Biological Chemistry. 273(20). 12325–12331. 37 indexed citations
14.
Huang, D., Chong‐Hwan Chang, G. R. A. Johnson, et al.. (1997). Variable domain structure of κIV human light chain Len: High homology to the murine light chain McPC603. Molecular Immunology. 34(18). 1291–1301. 29 indexed citations
15.
Lucca, George V. De, Jing Liang, Paul E. Aldrich, et al.. (1997). Design, Synthesis, and Evaluation of Tetrahydropyrimidinones as an Example of a General Approach to Nonpeptide HIV Protease Inhibitors. Journal of Medicinal Chemistry. 40(11). 1707–1719. 40 indexed citations
16.
Yamazaki, Toshimasa, Andrew P. Hinck, Yun‐Xing Wang, et al.. (1996). Three‐dimensional solution structure of the HIV‐1 protease complexed with DMP323, a novel cyclic urea‐type inhibitor, determined by nuclear magnetic resonance spectroscopy. Protein Science. 5(3). 495–506. 64 indexed citations
17.
Weber, Patricia C, et al.. (1995). Kinetic and Crystallographic Studies of Thrombin with Ac-(D)Phe-Pro-boroArg-OH and Its Lysine, Amidine, Homolysine, and Ornithine Analogs. Biochemistry. 34(11). 3750–3757. 63 indexed citations
18.
Stevens, Fred J., Chong‐Hwan Chang, Florence A. Westholm, et al.. (1995). A Molecular Model for Self-Assembly of Amyloid Fibrils: Immunoglobulin Light Chains. Biochemistry. 34(34). 10697–10702. 81 indexed citations
19.
Xu, Zhifu, Chong‐Hwan Chang, & M. Schiffer. (1990). Testing the procedure of simulated annealing by refining homologous immunoglobulin light-chain dimers. Protein Engineering Design and Selection. 3(7). 583–589. 3 indexed citations
20.
Schiffer, M., et al.. (1988). Analysis of immunoglobulin domain interactions. Journal of Molecular Biology. 203(3). 799–802. 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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