Chang‐Hyeock Byeon

777 total citations
24 papers, 538 citations indexed

About

Chang‐Hyeock Byeon is a scholar working on Molecular Biology, Virology and Spectroscopy. According to data from OpenAlex, Chang‐Hyeock Byeon has authored 24 papers receiving a total of 538 indexed citations (citations by other indexed papers that have themselves been cited), including 19 papers in Molecular Biology, 6 papers in Virology and 6 papers in Spectroscopy. Recurrent topics in Chang‐Hyeock Byeon's work include HIV Research and Treatment (6 papers), Advanced NMR Techniques and Applications (6 papers) and Protein Structure and Dynamics (5 papers). Chang‐Hyeock Byeon is often cited by papers focused on HIV Research and Treatment (6 papers), Advanced NMR Techniques and Applications (6 papers) and Protein Structure and Dynamics (5 papers). Chang‐Hyeock Byeon collaborates with scholars based in United States, Denmark and United Kingdom. Chang‐Hyeock Byeon's co-authors include Angela M. Gronenborn, In‐Ja L. Byeon, Jin-Woo Ahn, Judith G. Levin, Mithun Mitra, Lisa M. Charlton, Kamil Hercík, Tatyana Polenova, Dustin Singer and Jozef Hritz and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Nucleic Acids Research.

In The Last Decade

Chang‐Hyeock Byeon

24 papers receiving 536 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Chang‐Hyeock Byeon United States 11 342 161 98 83 79 24 538
Lisa M. Charlton United States 8 399 1.2× 153 1.0× 55 0.6× 64 0.8× 75 0.9× 10 570
Paul A. Salinas United States 8 408 1.2× 202 1.3× 142 1.4× 89 1.1× 28 0.4× 11 609
Gregory J. Bedwell United States 17 475 1.4× 237 1.5× 48 0.5× 156 1.9× 118 1.5× 27 806
Kim Wals United Kingdom 12 541 1.6× 174 1.1× 29 0.3× 88 1.1× 80 1.0× 14 844
C.A. Dennis United Kingdom 13 293 0.9× 92 0.6× 25 0.3× 58 0.7× 32 0.4× 20 550
Jenny Erales France 15 506 1.5× 55 0.3× 55 0.6× 34 0.4× 199 2.5× 18 668
Christophe Boutillon France 15 334 1.0× 143 0.9× 83 0.8× 48 0.6× 73 0.9× 24 589
Kent A. Baker United States 12 828 2.4× 101 0.6× 65 0.7× 110 1.3× 234 3.0× 15 1.2k
Ieva Sutkevičiu̅tė France 18 724 2.1× 78 0.5× 47 0.5× 58 0.7× 45 0.6× 27 913
Hugues de Rocquigny France 10 304 0.9× 297 1.8× 35 0.4× 192 2.3× 41 0.5× 10 504

Countries citing papers authored by Chang‐Hyeock Byeon

Since Specialization
Citations

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

Fields of papers citing papers by Chang‐Hyeock Byeon

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Chang‐Hyeock Byeon

This figure shows the co-authorship network connecting the top 25 collaborators of Chang‐Hyeock Byeon. A scholar is included among the top collaborators of Chang‐Hyeock Byeon 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 Chang‐Hyeock Byeon. Chang‐Hyeock Byeon 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.
Byeon, Chang‐Hyeock, et al.. (2025). Ultrasensitive Characterization of Native Bacterial Biofilms via Dynamic Nuclear Polarization‐Enhanced Solid‐State NMR. Angewandte Chemie International Edition. 64(12). e202418146–e202418146. 4 indexed citations
2.
Wieteska, Łukasz, Alexander B. Taylor, Jonathan A. Coleman, et al.. (2025). Structures of TGF-β with betaglycan and signaling receptors reveal mechanisms of complex assembly and signaling. Nature Communications. 16(1). 1778–1778. 7 indexed citations
3.
Byeon, Chang‐Hyeock, et al.. (2024). Intrinsically disordered Pseudomonas chaperone FapA slows down the fibrillation of major biofilm‐forming functional amyloid FapC. FEBS Journal. 291(9). 1925–1943. 3 indexed citations
4.
Byeon, Chang‐Hyeock, et al.. (2024). Structure of biofilm-forming functional amyloid PSMα1 from Staphylococcus aureus. Proceedings of the National Academy of Sciences. 121(33). e2406775121–e2406775121. 12 indexed citations
5.
Singh, Shashi Prakash, Danielle J. Smyth, Kyle T. Cunningham, et al.. (2024). The TGF-β mimic TGM4 achieves cell specificity through combinatorial surface co-receptor binding. EMBO Reports. 26(1). 218–244. 4 indexed citations
6.
Byeon, Chang‐Hyeock, et al.. (2023). Tapping into the native Pseudomonas bacterial biofilm structure by high-resolution multidimensional solid-state NMR. Journal of Magnetic Resonance. 357. 107587–107587. 5 indexed citations
7.
8.
Dinther, Maarten van, Kyle T. Cunningham, Shashi Prakash Singh, et al.. (2023). CD44 acts as a coreceptor for cell-specific enhancement of signaling and regulatory T cell induction by TGM1, a parasite TGF-β mimic. Proceedings of the National Academy of Sciences. 120(34). e2302370120–e2302370120. 8 indexed citations
9.
Byeon, Chang‐Hyeock, Cynthia S. Hinck, Kyle T. Cunningham, et al.. (2022). Convergent evolution of a parasite-encoded complement control protein-scaffold to mimic binding of mammalian TGF-β to its receptors, TβRI and TβRII. Journal of Biological Chemistry. 298(6). 101994–101994. 15 indexed citations
10.
Byeon, In‐Ja L., Guillermo Calero, Ying Wu, et al.. (2021). Structure of HIV-1 Vpr in complex with the human nucleotide excision repair protein hHR23A. Nature Communications. 12(1). 6864–6864. 4 indexed citations
11.
Kim, Sun Kyung, Matthew J. Whitley, Troy C. Krzysiak, et al.. (2019). Structural Adaptation in Its Orphan Domain Engenders Betaglycan with an Alternate Mode of Growth Factor Binding Relative to Endoglin. Structure. 27(9). 1427–1442.e4. 10 indexed citations
12.
Byeon, In‐Ja L., Jinwon Jung, Chang‐Hyeock Byeon, et al.. (2019). Complete 1H, 13C, 15N resonance assignments and secondary structure of the Vpr binding region of hHR23A (residues 223–363). Biomolecular NMR Assignments. 14(1). 13–17. 1 indexed citations
13.
Peng, Wang, Jiong Shi, Chantal L. Márquez, et al.. (2019). Functional analysis of the secondary HIV-1 capsid binding site in the host protein cyclophilin A. Retrovirology. 16(1). 10–10. 17 indexed citations
14.
Wang, Mingzhang, Manman Lu, Caitlin M. Quinn, et al.. (2018). Fast Magic‐Angle Spinning 19F NMR Spectroscopy of HIV‐1 Capsid Protein Assemblies. Angewandte Chemie International Edition. 57(50). 16375–16379. 53 indexed citations
15.
Wang, Mingzhang, Manman Lu, Caitlin M. Quinn, et al.. (2018). Fast Magic‐Angle Spinning 19F NMR Spectroscopy of HIV‐1 Capsid Protein Assemblies. Angewandte Chemie. 130(50). 16613–16617. 6 indexed citations
16.
Byeon, In‐Ja L., Jin-Woo Ahn, Mithun Mitra, et al.. (2013). NMR structure of human restriction factor APOBEC3A reveals substrate binding and enzyme specificity. Nature Communications. 4(1). 1890–1890. 110 indexed citations
17.
Mitra, Mithun, Kamil Hercík, Jin-Woo Ahn, et al.. (2013). Structural determinants of human APOBEC3A enzymatic and nucleic acid binding properties. Nucleic Acids Research. 42(2). 1095–1110. 58 indexed citations
18.
Byeon, In‐Ja L., Guangjin Hou, Yun Han, et al.. (2012). Motions on the Millisecond Time Scale and Multiple Conformations of HIV-1 Capsid Protein: Implications for Structural Polymorphism of CA Assemblies. Journal of the American Chemical Society. 134(14). 6455–6466. 81 indexed citations
19.
Hari, Sanjay B., Chang‐Hyeock Byeon, Jason J. Lavinder, & Thomas J. Magliery. (2010). Cysteine‐free rop: A four‐helix bundle core mutant has wild‐type stability and structure but dramatically different unfolding kinetics. Protein Science. 19(4). 670–679. 11 indexed citations
20.
Ahn, Jin-Woo, In‐Ja L. Byeon, Chang‐Hyeock Byeon, & Angela M. Gronenborn. (2009). Insight into the Structural Basis of Pro- and Antiapoptotic p53 Modulation by ASPP Proteins. Journal of Biological Chemistry. 284(20). 13812–13822. 41 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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