<<神经科学前沿>> ‘frontiers in Neuroscience’ 杂志， 第15卷，本月18日， 发表了， 代号为689315的论文 ‘兔普里昂部分抵抗通过不同生物辅助因子诱导(生成的)体外(分子病化)聚集’ - ‘Rabbit PrP Is Partially Resistant to in vitro Aggregation Induced by Different Biological Cofactors’。具体参见:

https://www.frontiersin.org/articles/10.3389/fnins.2021.689315/full 

References 

[1] https://www.frontiersin.org/articles/10.3389/fnins.2021.689315/full - ''frontiers in Neuroscience Vol 15: 689315. Published 18 June 2021. doi: 10.3389/fnins.2021.689315 pages 10-11'' cites the papers:

[2] Zhang, J. (2010). Studies on the structural stability of rabbit prion probed by molecular dynamics simulations of its wild-type and mutants. J. Theor. Biol. 264, 119–122. doi: 10.1016/j.jtbi.2010.01.024

[3] Zhang, J. (2011). Comparison studies of the structural stability of rabbit prion protein with human and mouse prion proteins. J. Theor. Biol. 269, 88–95. doi: 10.1016/j.jtbi.2010.10.020

[4] Zhang, J., and Zhang, Y. (2014). Molecular dynamics studies on the NMR and X-ray structures of rabbit prion proteins. J. Theor. Biol. 342, 70–82. doi: 10.1016/ j.jtbi.2013.10.005

[5] https://www.frontiersin.org/articles/10.3389/fncel.2020.00254/full - ''frontiers in Cellular Neuroscience (18 August 2020) 14:254. doi: 10.3389/fncel.2020.00254, page 5'' cites the book:

[6] "Zhang JP (2018) Molecular Dynamics Analyses of Prion Protein Structures (1st ed. 2018 Edition): The Resistance to Prion Diseases Down Under, Springer, ISBN 978-981-10-8814-8'':

"An endeavor to systematically characterize the differences in the secondary structure and in the flexibility of the protein for a large number of PrP species through molecular dynamics simulations was attempted by Zhang (2018) "