Cite
The disulfide bond Cys2724-Cys2774 in the C-terminal cystine knot domain of von Willebrand factor is critical for its dimerization and secretion.
MLA
Zhang, Yuxin, et al. “The Disulfide Bond Cys2724-Cys2774 in the C-Terminal Cystine Knot Domain of von Willebrand Factor Is Critical for Its Dimerization and Secretion.” Thrombosis Journal, vol. 19, no. 1, Nov. 2021, pp. 1–7. EBSCOhost, https://doi.org/10.1186/s12959-021-00348-w.
APA
Zhang, Y., Chen, F., Yang, A., Wang, X., Han, Y., Wu, D., Wu, Y., & Zhang, J. (2021). The disulfide bond Cys2724-Cys2774 in the C-terminal cystine knot domain of von Willebrand factor is critical for its dimerization and secretion. Thrombosis Journal, 19(1), 1–7. https://doi.org/10.1186/s12959-021-00348-w
Chicago
Zhang, Yuxin, Fengwu Chen, Aizhen Yang, Xiaoying Wang, Yue Han, Depei Wu, Yi Wu, and Jingyu Zhang. 2021. “The Disulfide Bond Cys2724-Cys2774 in the C-Terminal Cystine Knot Domain of von Willebrand Factor Is Critical for Its Dimerization and Secretion.” Thrombosis Journal 19 (1): 1–7. doi:10.1186/s12959-021-00348-w.