Reversible homodimerization of a small leucine-rich proteoglycan PRELP modulates the interactions with TGFβ1 and IGFI-R
Hirofumi Kosuge, Makoto Nakakido, Daisuke Kuroda, Kouhei Tsumoto · 2026
Read Reversible homodimerization of a small leucine-rich proteoglycan PRELP modulates the interactions with TGFβ1 and IGFI-R by Hirofumi Kosuge, Makoto Nakakido, Daisuke Kuroda, Kouhei Tsumoto (2026) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/pmc-13671038.txt.
Description
Hirofumi Kosuge and co-authors study in 2026 how a small matrix protein in the body joins with itself, and how that pairing shapes its other bonds. The protein, PRELP, belongs to a family that links with many partners to steer tissue work. Some family members pair up, but what pairing does was unclear.
Lab tests showed PRELP forms a loose pair that breaks apart as the protein thins out. A water-shy face seems to drive the pairing, since charged swaps at that face kept the protein single. Single forms bound two growth signals more strongly than pairs did. Pairing, the team concludes, acts as a dial on the protein's reach.
Catalog record
| CREATOR | Hirofumi Kosuge, Makoto Nakakido, Daisuke Kuroda, Kouhei Tsumoto |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 58 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |