In‐Ja L. Byeon

4.9k total citations
78 papers, 4.0k citations indexed

About

In‐Ja L. Byeon is a scholar working on Molecular Biology, Virology and Spectroscopy. According to data from OpenAlex, In‐Ja L. Byeon has authored 78 papers receiving a total of 4.0k indexed citations (citations by other indexed papers that have themselves been cited), including 60 papers in Molecular Biology, 20 papers in Virology and 17 papers in Spectroscopy. Recurrent topics in In‐Ja L. Byeon's work include Protein Structure and Dynamics (25 papers), HIV Research and Treatment (20 papers) and Advanced NMR Techniques and Applications (16 papers). In‐Ja L. Byeon is often cited by papers focused on Protein Structure and Dynamics (25 papers), HIV Research and Treatment (20 papers) and Advanced NMR Techniques and Applications (16 papers). In‐Ja L. Byeon collaborates with scholars based in United States, Japan and France. In‐Ja L. Byeon's co-authors include Angela M. Gronenborn, Ming‐Daw Tsai, Jin-Woo Ahn, Tatyana Polenova, Guangjin Hou, John M. Louis, Jinwon Jung, Chang‐Hyeock Byeon, Thomas L. Selby and Hua Liao and has published in prestigious journals such as Cell, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

In‐Ja L. Byeon

77 papers receiving 4.0k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
In‐Ja L. Byeon United States 40 2.8k 738 647 564 507 78 4.0k
Linda K. Nicholson United States 41 3.7k 1.3× 684 0.9× 598 0.9× 204 0.4× 475 0.9× 90 5.2k
Elan Eisenmesser United States 30 3.3k 1.2× 487 0.7× 813 1.3× 171 0.3× 305 0.6× 76 4.5k
Malene Ringkjøbing Jensen France 44 4.7k 1.7× 1.2k 1.6× 1.7k 2.7× 271 0.5× 337 0.7× 116 6.3k
John D. Gross United States 37 3.6k 1.3× 726 1.0× 497 0.8× 526 0.9× 175 0.3× 75 5.0k
T. Kigawa Japan 46 6.1k 2.2× 314 0.4× 637 1.0× 282 0.5× 165 0.3× 181 7.5k
Eduardo A. Padlan United States 41 6.4k 2.3× 327 0.4× 1.1k 1.6× 264 0.5× 442 0.9× 110 9.1k
Christian Roumestand France 36 3.2k 1.1× 338 0.5× 466 0.7× 257 0.5× 84 0.2× 117 4.7k
Rodolfo Ghirlando United States 68 9.9k 3.6× 540 0.7× 965 1.5× 919 1.6× 570 1.1× 213 12.4k
Martin Billeter Switzerland 8 6.0k 2.2× 518 0.7× 1.5k 2.3× 151 0.3× 277 0.5× 12 7.1k
Yang Shen United States 23 4.7k 1.7× 1.3k 1.8× 1.5k 2.3× 79 0.1× 397 0.8× 44 5.9k

Countries citing papers authored by In‐Ja L. Byeon

Since Specialization
Citations

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

Fields of papers citing papers by In‐Ja L. Byeon

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of In‐Ja L. Byeon

This figure shows the co-authorship network connecting the top 25 collaborators of In‐Ja L. Byeon. A scholar is included among the top collaborators of In‐Ja L. 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 In‐Ja L. Byeon. In‐Ja L. 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.
Lu, Manman, Dmitri Toptygin, Yufei Xiang, et al.. (2022). The Magic of Linking Rings: Discovery of a Unique Photoinduced Fluorescent Protein Crosslink. Journal of the American Chemical Society. 144(24). 10809–10816. 7 indexed citations
2.
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
3.
Gupta, Rupal, Huilan Zhang, Manman Lu, et al.. (2019). Dynamic Nuclear Polarization Magic-Angle Spinning Nuclear Magnetic Resonance Combined with Molecular Dynamics Simulations Permits Detection of Order and Disorder in Viral Assemblies. The Journal of Physical Chemistry B. 123(24). 5048–5058. 31 indexed citations
4.
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
5.
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
6.
Perilla, Juan R., Gongpu Zhao, Manman Lu, et al.. (2017). CryoEM Structure Refinement by Integrating NMR Chemical Shifts with Molecular Dynamics Simulations. The Journal of Physical Chemistry B. 121(15). 3853–3863. 33 indexed citations
7.
Mitra, Mithun, Dustin Singer, Jozef Hritz, et al.. (2015). Sequence and structural determinants of human APOBEC3H deaminase and anti-HIV-1 activities. Retrovirology. 12(1). 3–3. 30 indexed citations
8.
Wu, Ying, Leonardus M. I. Koharudin, Jennifer Mehrens, et al.. (2015). Structural Basis of Clade-specific Engagement of SAMHD1 (Sterile α Motif and Histidine/Aspartate-containing Protein 1) Restriction Factors by Lentiviral Viral Protein X (Vpx) Virulence Factors. Journal of Biological Chemistry. 290(29). 17935–17945. 12 indexed citations
9.
10.
Byeon, In‐Ja L., Xin Meng, Jinwon Jung, et al.. (2009). Structural Convergence between Cryo-EM and NMR Reveals Intersubunit Interactions Critical for HIV-1 Capsid Function. Cell. 139(4). 780–790. 218 indexed citations
11.
Byeon, In‐Ja L., John M. Louis, & Angela M. Gronenborn. (2004). A Captured Folding Intermediate Involved in Dimerization and Domain-swapping of GB1. Journal of Molecular Biology. 340(3). 615–625. 40 indexed citations
12.
Yongkiettrakul, Suganya, In‐Ja L. Byeon, & Ming‐Daw Tsai. (2004). The Ligand Specificity of Yeast Rad53 FHA Domains at the +3 Position Is Determined by Nonconserved Residues,. Biochemistry. 43(13). 3862–3869. 16 indexed citations
13.
14.
Showalter, Alexander K., et al.. (2001). Solution structure of a viral DNA polymerase X and evidence for a mutagenic function.. Nature Structural Biology. 8(11). 942–946. 62 indexed citations
15.
Liao, Hua, Chunhua Yuan, Suganya Yongkiettrakul, et al.. (2000). Structure of the FHA1 Domain of Yeast Rad53 and Identification of Binding Sites for both FHA1 and its Target Protein Rad9. Journal of Molecular Biology. 304(5). 941–951. 67 indexed citations
16.
Liao, Hua, In‐Ja L. Byeon, & Ming‐Daw Tsai. (1999). Structure and function of a new phosphopeptide-binding domain containing the FHA2 of rad53. Journal of Molecular Biology. 294(4). 1041–1049. 93 indexed citations
17.
Byeon, In‐Ja L., Junan Li, Karen L. Ericson, et al.. (1998). Tumor Suppressor p16INK4A: Determination of Solution Structure and Analyses of Its Interaction with Cyclin-Dependent Kinase 4. Molecular Cell. 1(3). 421–431. 135 indexed citations
18.
Huang, Baohua, Bao-Zhu Yu, Joseph M. Rogers, et al.. (1996). Phospholipase A2 Engineering. Deletion of the C-Terminus Segment Changes Substrate Specificity and Uncouples Calcium and Substrate Binding at the Zwitterionic Interface,. Biochemistry. 35(37). 12164–12174. 26 indexed citations
19.
Byeon, In‐Ja L., Robert F. Kelley, & Miguel Llinás. (1991). Kringle‐2 domain of the tissue‐type plasminogen activator. European Journal of Biochemistry. 197(1). 155–165. 18 indexed citations
20.
Byeon, In‐Ja L. & Miguel Llinás. (1991). Solution structure of the tissue-type plasminogen activator kringle 2 domain complexed to 6-aminohexanoic acid an antifibrinolytic drug. Journal of Molecular Biology. 222(4). 1035–1051. 47 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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