Soo Hyun Eom

7.2k total citations · 1 hit paper
136 papers, 5.5k citations indexed

About

Soo Hyun Eom is a scholar working on Molecular Biology, Materials Chemistry and Cell Biology. According to data from OpenAlex, Soo Hyun Eom has authored 136 papers receiving a total of 5.5k indexed citations (citations by other indexed papers that have themselves been cited), including 106 papers in Molecular Biology, 38 papers in Materials Chemistry and 27 papers in Cell Biology. Recurrent topics in Soo Hyun Eom's work include Enzyme Structure and Function (34 papers), RNA and protein synthesis mechanisms (18 papers) and Biochemical and Molecular Research (13 papers). Soo Hyun Eom is often cited by papers focused on Enzyme Structure and Function (34 papers), RNA and protein synthesis mechanisms (18 papers) and Biochemical and Molecular Research (13 papers). Soo Hyun Eom collaborates with scholars based in South Korea, United States and Japan. Soo Hyun Eom's co-authors include Kalimuthu Kalishwaralal, Sangiliyandi Gurunathan, Ramanathan Vaidyanathan, Jimin Wang, Thomas A. Steitz, Venkataraman Deepak, Young Jun Im, Se Won Suh, Sureshbabu Ram Kumar Pandian and Muniyandi Jeyaraj and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

Soo Hyun Eom

131 papers receiving 5.4k citations

Hit Papers

Biosynthesis, purification and characterization of silver... 2009 2026 2014 2020 2009 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
Soo Hyun Eom South Korea 37 3.3k 1.5k 774 748 654 136 5.5k
Stanley C. Gill United States 19 5.8k 1.8× 832 0.5× 583 0.8× 480 0.6× 833 1.3× 40 7.2k
Haydyn D. T. Mertens Germany 33 4.1k 1.2× 1.5k 1.0× 268 0.3× 557 0.7× 498 0.8× 71 6.6k
Kyeong Kyu Kim South Korea 41 5.8k 1.8× 1.0k 0.7× 363 0.5× 433 0.6× 822 1.3× 229 7.4k
Cy M. Jeffries Germany 33 3.5k 1.1× 1.5k 1.0× 268 0.3× 481 0.6× 399 0.6× 98 5.5k
Masafumi Yohda Japan 40 3.8k 1.2× 1.7k 1.1× 528 0.7× 278 0.4× 263 0.4× 257 5.5k
Robert F. Standaert United States 34 5.5k 1.7× 557 0.4× 612 0.8× 612 0.8× 402 0.6× 74 7.0k
Ning Gao China 51 5.7k 1.8× 662 0.4× 433 0.6× 600 0.8× 795 1.2× 199 8.6k
Rudi Glockshuber Switzerland 59 9.3k 2.8× 1.5k 1.0× 318 0.4× 1.5k 2.0× 1.2k 1.9× 171 11.9k
Hyun Kyu Song South Korea 44 4.6k 1.4× 681 0.4× 270 0.3× 786 1.1× 519 0.8× 162 6.5k
Narasimha Sreerama United States 20 4.8k 1.5× 1.0k 0.7× 178 0.2× 500 0.7× 508 0.8× 32 6.6k

Countries citing papers authored by Soo Hyun Eom

Since Specialization
Citations

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

Fields of papers citing papers by Soo Hyun Eom

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Soo Hyun Eom. 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 Soo Hyun Eom. The network helps show where Soo Hyun Eom may publish in the future.

Co-authorship network of co-authors of Soo Hyun Eom

This figure shows the co-authorship network connecting the top 25 collaborators of Soo Hyun Eom. A scholar is included among the top collaborators of Soo Hyun Eom 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 Soo Hyun Eom. Soo Hyun Eom 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
2.
Lee, Sang‐Kyu, et al.. (2024). Cell Wall Invertases from Maternal Tissues Modulate Sucrose Flux in Apoplastic Pathways During Rice Anther and Seed Development. International Journal of Molecular Sciences. 25(21). 11557–11557.
3.
Lee, Miriam, et al.. (2023). Human atlastins are sufficient to drive the fusion of liposomes with a physiological lipid composition. The Journal of Cell Biology. 222(4). 5 indexed citations
4.
Youn, Hyung‐Seop, Jung‐Gyu Lee, Young Bae Ryu, et al.. (2017). Crystal structure of the catalytic domain of Clostridium perfringens neuraminidase in complex with a non-carbohydrate-based inhibitor, 2-(cyclohexylamino)ethanesulfonic acid. Biochemical and Biophysical Research Communications. 486(2). 470–475. 17 indexed citations
5.
Tong, Junsen, et al.. (2012). Crystallization and preliminary X-ray crystallographic analysis of the oxysterol-binding protein Osh3 fromSaccharomyces cerevisiae. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 68(12). 1498–1502. 3 indexed citations
6.
Jung, Da‐Woon, Jinmi Kim, Gi-Cheon Kim, et al.. (2011). A Triazine Compound S06 Inhibits Proinvasive Crosstalk between Carcinoma Cells and Stromal Fibroblasts via Binding to Heat Shock Protein 90. Chemistry & Biology. 18(12). 1581–1590. 18 indexed citations
7.
Kang, Gil Bu, Dong Yeon Shin, Ji-Hye Yun, et al.. (2010). Structural Basis of E2–25K/UBB+1 Interaction Leading to Proteasome Inhibition and Neurotoxicity. Journal of Biological Chemistry. 285(46). 36070–36080. 45 indexed citations
8.
Song, Dong Woo, Jung‐Gyu Lee, Hyung‐Seop Youn, Soo Hyun Eom, & Do Han Kim. (2010). Ryanodine receptor assembly: A novel systems biology approach to 3D mapping. Progress in Biophysics and Molecular Biology. 105(3). 145–161. 19 indexed citations
9.
Sahoo, Sanjaya Kumar, Tae-Yong Kim, Gil Bu Kang, et al.. (2009). Characterization of Calumenin-SERCA2 Interaction in Mouse Cardiac Sarcoplasmic Reticulum. Journal of Biological Chemistry. 284(45). 31109–31121. 51 indexed citations
10.
Lee, Jun Hyuck, Gil Bu Kang, Hyun–Ho Lim, et al.. (2007). Crystal Structure of the GluR0 Ligand-Binding Core from Nostoc punctiforme in Complex with l-Glutamate: Structural Dissection of the Ligand Interaction and Subunit Interface. Journal of Molecular Biology. 376(2). 308–316. 19 indexed citations
11.
Lee, Jun Hyuck, Dooil Kim, Seong‐Hwan Rho, et al.. (2006). Crystal structure of the apo form of D‐alanine: D‐alanine ligase (Ddl) from Thermus caldophilus: A basis for the substrate‐induced conformational changes. Proteins Structure Function and Bioinformatics. 64(4). 1078–1082. 23 indexed citations
12.
Im, Young Jun, Seong Ho Park, Seong‐Hwan Rho, et al.. (2003). Crystal Structure of GRIP1 PDZ6-Peptide Complex Reveals the Structural Basis for Class II PDZ Target Recognition and PDZ Domain-mediated Multimerization. Journal of Biological Chemistry. 278(10). 8501–8507. 76 indexed citations
13.
Lee, Jae Young, Jae Kwak, Jinho Moon, et al.. (2001). Crystal structure and functional analysis of the SurE protein identify a novel phosphatase family.. Nature Structural Biology. 8(9). 789–794. 179 indexed citations
14.
Wang, J., Ji‐Joon Song, Ihn Sik Seong, et al.. (2001). Nucleotide-Dependent Conformational Changes in a Protease-Associated ATPase HslU. Structure. 9(11). 1107–1116. 141 indexed citations
15.
Kwon, Min Seong, Chun Shik Park, Chul‐Seung Park, et al.. (2000). Calreticulin Couples Calcium Release and Calcium Influx in Integrin-mediated Calcium Signaling. Molecular Biology of the Cell. 11(4). 1433–1443. 108 indexed citations
16.
Kook, Seunghyi, Soo Jeon Choi, Joohong Ahnn, et al.. (2000). Caspase-mediated Cleavage of p130cas in Etoposide-induced Apoptotic Rat-1 Cells. Molecular Biology of the Cell. 11(3). 929–939. 66 indexed citations
17.
Lee, Jae Young, Changsoo Chang, Soo Hyun Eom, et al.. (2000). Crystallization and preliminary X-ray crystallographic analysis of NAD+-dependent DNA ligase fromThermus filiformis. Acta Crystallographica Section D Biological Crystallography. 56(3). 357–358. 2 indexed citations
18.
Steitz, T.A., et al.. (1996). DNA and RNA polymerases: structural diversity and common mechanisms.. Progress in Biophysics and Molecular Biology. 7. 1 indexed citations
19.
Eom, Soo Hyun, Jimin Wang, & Thomas A. Steitz. (1996). Structure of Taq polymerase with DNA at the polymerase active site. Nature. 382(6588). 278–281. 277 indexed citations
20.
Eom, Soo Hyun, Changsoo Chang, Dong Hae Shin, et al.. (1995). Crystallization, molecular replacement solution, and refinement of tetrameric β‐amylase from sweet potato. Proteins Structure Function and Bioinformatics. 21(2). 105–117. 43 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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