Author

C. Seok

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biophysics· 3 Biochemistry· 1 Cancer Biology· 1

Signature Assays, Organisms & Methods

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Assay:structural biology· 3 Organism:virus· 3 Approach:deep learning· 2 Approach:mechanistic / dynamical model· 2 Assay:proteomics· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:drug response / drug discovery· 1 Approach:experimental assay· 1

Frequent Co-Authors

H. Woo· 3 shared M. S. Yeom· 3 shared S.-J. Park· 3 shared W. Im· 3 shared Y. Cao· 3 shared Y. K. Choi· 3 shared J. Lee· 2 shared M. Frank· 2 shared

Activity by Year

2020-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 36 mutual co-author links

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3 shared papersBiophysics

H. Woo

Mutual co-authors in cluster

Author profile →

5 papers

Recent·Most cited

Discovery of Highly Active Kynureninases for Cancer Immunotherapy through Protein Language Model

H. Eom, K. S. Cho, J. Lee, S. Kim, S. Park, H. Kim, J. Yang, Y.-H. Han, J. Lee, C. Seok, M. S. Lee, W. J. Song, M. Steinegger

The paper identifies and validates four kynureninases using homology searches and protein language models, with the most active one showing significant tumor reduction in mouse models.

bioRxiv · Jan 16, 2024Cancer Biology

ECPAS/Ecm29-Mediated 26S Proteasome Disassembly Is an Adaptive Response to Glucose Starvation

W. H. Choi, Y. Yun, I. Byun, S. Lee, J. Sim, S. Levi, S. Kim, S. H. Park, J. Jun, K. P. Kim, Y. T. Kwon, D. Han, T. Chiba, C. Seok, M. H. Glickman, M. J. Lee

This study shows that ECPAS-mediated 26S proteasome disassembly into 20S and 19S subcomplexes occurs during glucose starvation, enhancing proteolysis and cell survival.

bioRxiv · Jun 6, 2022Biochemistry

Dynamic Interactions of Fully Glycosylated SARS-CoV-2 Spike Protein with Various Antibodies

Y. Cao, Y. K. Choi, M. Frank, H. Woo, S.-J. Park, M. S. Yeom, C. Seok, W. Im

This study uses molecular dynamics simulations to analyze SARS-CoV-2 spike protein interactions with antibodies, revealing structural dynamics and mutation impacts on neutralization.

bioRxiv · May 10, 2021Biophysics

Structure, Dynamics, Receptor Binding, and Antibody Binding of Fully-glycosylated Full-length SARS-CoV-2 Spike Protein in a Viral Membrane

Y. K. Choi, Y. Cao, M. Frank, H. Woo, S.-J. Park, M. S. Yeom, T. I. Croll, C. Seok, W. Im

This study uses molecular dynamics simulations to analyze the structure, dynamics, and antibody binding of the fully-glycosylated SARS-CoV-2 spike protein, revealing key roles of glycans in stabilizing RBD conformations and antibody epitope exposure.

bioRxiv · Oct 18, 2020Biophysics

Developing a Fully-glycosylated Full-length SARS-CoV-2 Spike Protein Model in a Viral Membrane

H. Woo, S.-J. Park, Y. K. Choi, T. Park, M. Tanveer, Y. Cao, N. R. Kern, J. Lee, M. S. Yeom, T. I. Croll, C. Seok, W. Im

The paper models and simulates a fully-glycosylated SARS-CoV-2 spike protein in a viral membrane using computational methods and provides the structures for research on COVID-19 prevention and treatment.

bioRxiv · May 20, 2020Biophysics