Unique molecular architecture of N-glycosylated TM4SF5 dimer highlights evolutionary and structural divergence among small four-transmembrane protein families
Therefore, the unique features in the LEL and the N-glycosylation of TM4SF5 may contribute to dimer formation and cholesterol binding, potentially influencing regulatory roles in liver malignancy development.
Authors
- Sun Choi (ORCID: https://orcid.org/0000-0002-7669-7954)
- Je‐Yoel Cho (ORCID: https://orcid.org/0000-0003-1030-3577)
- Soyeon Kim (ORCID: https://orcid.org/0009-0004-2553-8330)
- Yoonji Lee (ORCID: https://orcid.org/0000-0002-2494-5792)
- Donghyuk Suh (ORCID: https://orcid.org/0000-0002-7478-4579)
- Ri Han (ORCID: https://orcid.org/0000-0001-7266-7996)
- Eun‐Ae Shin (ORCID: https://orcid.org/0000-0001-5728-7151)
- Kyung‐hee Pyo
- Eun-Mi Kim (ORCID: https://orcid.org/0000-0001-6876-462X)
- Jae‐Ho Lee (ORCID: https://orcid.org/0000-0001-5076-4365)
- Sang Eun Lee (ORCID: https://orcid.org/0000-0003-2722-8200)
- Yong‐In Kim (ORCID: https://orcid.org/0000-0002-2877-5110)
- Ji Eon Kim (ORCID: https://orcid.org/0000-0001-6151-2104)
- Wonsik Kim (ORCID: https://orcid.org/0000-0002-8658-6262)
- Sang-Hee Yoon
Institutions
- Ewha Womans University (KR)
- New Generation University College (ET)
- Sejong University (KR)
- National University College (PR)
- Chung-Ang University (KR)
Publication Details
- Journal
- Journal of Advanced Research
- Published
- 2025-12-01
- DOI
- https://doi.org/10.1016/j.jare.2025.11.066
- Primary Topic
- Glycosylation and Glycoproteins Research
- Type
- article
- Field-Weighted Citation Impact
- 0.00