Author

Seoungjun Lee

King's College LondonORCID 0000-0002-0619-7815Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Signature Assays, Organisms & Methods

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Research Focus:cell signaling & trafficking· 2 Organism:human· 2 Approach:deep learning· 1 Assay:imaging· 1 Approach:microscopy & imaging analysis· 1 Assay:proteomics· 1 Approach:statistical model· 1

Frequent Co-Authors

Sarah MizielinskaiD· 2 shared Alex S. HolehouseiD· 1 shared Daniel A. Solomon· 1 shared Eleanor Wycherley· 1 shared Hermann Broder SchmidtiD· 1 shared Ines Lourenco Cabaco· 1 shared Juan AlcaldeiD· 1 shared Marc‐David RueppiD· 1 shared

Activity by Year

2026-2026 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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2 shared papersCell Biology

Sarah MizielinskaORCID

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2 papers

Recent·Most cited

Cell BiologybioRxivPreprintMar 17, 2026

C9ORF72-derived polyGR polypeptides disrupt passive nucleocytoplasmic transport by tuning protein affinity for the nuclear pore barrier

Daniel A. Solomon, Ryan J. Emenecker, Marie-Therese Salcher-Konrad…·Sarah Mizielinska

This study shows how polyGR polypeptides from C9ORF72 disrupt nucleocytoplasmic transport by altering protein affinity for the nuclear pore FG barrier, leading to biphasic transport outcomes and protein aggregation.

1 citation

humanproteomics

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Cell BiologybioRxivPreprintFeb 18, 2026

Novel single molecule imaging approaches reveal structure-function alterations to the nuclear pore complex in early C9ORF72-associated TDP-43 proteinopathy

Seoungjun Lee, Sarah Mizielinska

The paper develops new single molecule imaging techniques to study how C9ORF72-linked poly(glycine-arginine) peptides disrupt nuclear pore transport and structure, linking these changes to early TDP-43 pathology in ALS/FTD.

DOI 10.64898/2026.02.17.706337

humanimaging

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