Molecular basis of collagen triple helix recognition by VWF A-like domain two of collagen VII: Implications for interlaced anchoring fibril formation
Moe Hashimoto, Hiroya Oki, Kazuki Kawahara, Kazunori K Fujii, Takaki Koide · 2026
Read Molecular basis of collagen triple helix recognition by VWF A-like domain two of collagen VII: Implications for interlaced anchoring fibril formation by Moe Hashimoto, Hiroya Oki, Kazuki Kawahara, Kazunori K Fujii, Takaki Koide (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-13599636.txt.
Description
Anchoring fibrils formed by collagen VII play a critical role in stabilizing the dermal–epidermal junction. The N-terminal non-collagenous (NC1) domain of collagen VII binds firmly to basement membrane components including collagen IV and has also been reported to interact with mesenchymal fibrillar collagens via its von Willebrand factor A-like domain 2 (A2 domain).
Catalog record
| CREATOR | Moe Hashimoto, Hiroya Oki, Kazuki Kawahara, Kazunori K Fujii, Takaki Koide |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 58 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |