34220442 24184221 32496928 30010001 24041958 25297084 28978705 32898162 25810062 21875155 22480824 22954650 22288402 28415023 - Search Results

Year	Number of Results
2011	1
2012	3
2013	2
2014	2
2015	1
2017	2
2018	1
2020	2
2021	2
2023	0

1

Rabbit PrP Is Partially Resistant to in vitro Aggregation Induced by Different Biological Cofactors.

Angelli JN, Passos YM, Brito JMA, Silva JL, Cordeiro Y, Vieira TCRG. Angelli JN, et al. Front Neurosci. 2021 Jun 18;15:689315. doi: 10.3389/fnins.2021.689315. eCollection 2021. Front Neurosci. 2021. PMID: 34220442 Free PMC article.

2

Molecular dynamics studies on the NMR and X-ray structures of rabbit prion proteins.

Zhang J, Zhang Y. Zhang J, et al. J Theor Biol. 2014 Feb 7;342:70-82. doi: 10.1016/j.jtbi.2013.10.005. Epub 2013 Oct 31. J Theor Biol. 2014. PMID: 24184221

3

Molecular dynamics studies of dog prion protein wild-type and its D159N mutant.

Zhang J. Zhang J. J Biomol Struct Dyn. 2021 Aug;39(12):4234-4242. doi: 10.1080/07391102.2020.1776155. Epub 2020 Jun 16. J Biomol Struct Dyn. 2021. PMID: 32496928

4

D159 and S167 are protective residues in the prion protein from dog and horse, two prion-resistant animals.

Sanchez-Garcia J, Fernandez-Funez P. Sanchez-Garcia J, et al. Neurobiol Dis. 2018 Nov;119:1-12. doi: 10.1016/j.nbd.2018.07.011. Epub 2018 Jul 24. Neurobiol Dis. 2018. PMID: 30010001 Free PMC article.

5

Decipher the mechanisms of rabbit's low susceptibility to prion infection.

Yuan Z, Zhao D, Yang L. Yuan Z, et al. Acta Biochim Biophys Sin (Shanghai). 2013 Nov;45(11):899-903. doi: 10.1093/abbs/gmt093. Epub 2013 Sep 15. Acta Biochim Biophys Sin (Shanghai). 2013. PMID: 24041958 Free article. Review.

6

Progress on low susceptibility mechanisms of transmissible spongiform encephalopathies.

Qing LL, Zhao H, Liu LL. Qing LL, et al. Dongwuxue Yanjiu. 2014 Sep;35(5):436-45. doi: 10.13918/j.issn.2095-8137.2014.5.436. Dongwuxue Yanjiu. 2014. PMID: 25297084 Free PMC article. Review.

7

In Vitro Approach To Identify Key Amino Acids in Low Susceptibility of Rabbit Prion Protein to Misfolding.

Eraña H, Fernández-Borges N, Elezgarai SR, Harrathi C, Charco JM, Chianini F, Dagleish MP, Ortega G, Millet Ó, Castilla J. Eraña H, et al. J Virol. 2017 Nov 30;91(24):e01543-17. doi: 10.1128/JVI.01543-17. Print 2017 Dec 15. J Virol. 2017. PMID: 28978705 Free PMC article.

8

Identification of a homology-independent linchpin domain controlling mouse and bank vole prion protein conversion.

Burke CM, Mark KMK, Walsh DJ, Noble GP, Steele AD, Diack AB, Manson JC, Watts JC, Supattapone S. Burke CM, et al. PLoS Pathog. 2020 Sep 8;16(9):e1008875. doi: 10.1371/journal.ppat.1008875. eCollection 2020 Sep. PLoS Pathog. 2020. PMID: 32898162 Free PMC article.

9

Protein misfolding cyclic amplification induces the conversion of recombinant prion protein to PrP oligomers causing neuronal apoptosis.

Yuan Z, Yang L, Chen B, Zhu T, Hassan MF, Yin X, Zhou X, Zhao D. Yuan Z, et al. J Neurochem. 2015 Jun;133(5):722-9. doi: 10.1111/jnc.13098. Epub 2015 Apr 13. J Neurochem. 2015. PMID: 25810062 Free article.

10

The structural stability of wild-type horse prion protein.

Zhang J. Zhang J. J Biomol Struct Dyn. 2011 Oct;29(2):369-77. doi: 10.1080/07391102.2011.10507391. J Biomol Struct Dyn. 2011. PMID: 21875155

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