Structural mechanism of VWF D’D3 dimer formation-Reference-Cited by-同舟云学术

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Structural mechanism of VWF D’D3 dimer formation

Published:2022-02-15 Issue:1 Volume:8 Page:
ISSN:2056-5968
Container-title:Cell Discovery
language:en
Short-container-title:Cell Discov

Author:

Shu Zimei,Zeng Jianwei,Xia Li,Cai Haiyan,Zhou Aiwu

Funder

National Natural Science Foundation of China

Science Foundation for The Excellent Youth Scholars of Shanghai

Publisher

Springer Science and Business Media LLC

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry

Link

https://www.nature.com/articles/s41421-022-00378-2.pdf

Reference10 articles.

1. Huang, R. H. et al. Assembly of Weibel-Palade body-like tubules from N-terminal domains of von Willebrand factor. Proc. Natl Acad. Sci. USA 105, 482–487 (2008).

2. Springer, T. A. von Willebrand factor, Jedi knight of the bloodstream. Blood 124, 1412–1425 (2014).

3. Lenting, P. J., Christophe, O. D. & Denis, C. V. von Willebrand factor biosynthesis, secretion, and clearance: connecting the far ends. Blood 125, 2019–2028 (2015).

4. Dong, Z. et al. Disulfide bonds required to assemble functional von Willebrand factor multimers. J. Biol. Chem. 269, 6753–6758 (1994).

5. Purvis, A. R. et al. Two Cys residues essential for von Willebrand factor multimer assembly in the Golgi. Proc. Natl Acad. Sci. USA 104, 15647–15652 (2007).

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