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For: Ji HF, Zhang HY. beta-sheet constitution of prion proteins. Trends Biochem Sci 2010;35:129-34. [PMID: 20060302 DOI: 10.1016/j.tibs.2009.12.002] [Cited by in Crossref: 15] [Cited by in F6Publishing: 15] [Article Influence: 1.3] [Reference Citation Analysis]
Number Citing Articles
1 Bergasa-Caceres F, Rabitz HA. Identification of Two Early Folding Stage Prion Non-Local Contacts Suggested to Serve as Key Steps in Directing the Final Fold to Be Either Native or Pathogenic. Int J Mol Sci 2021;22:8619. [PMID: 34445324 DOI: 10.3390/ijms22168619] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 1.0] [Reference Citation Analysis]
2 Jeong MJ, Kim YC, Jeong BH. The First Report of the Prion Protein Gene (PRNP) Sequence in Pekin Ducks (Anas platyrhynchos domestica): The Potential Prion Disease Susceptibility in Ducks. Genes (Basel) 2021;12:193. [PMID: 33525657 DOI: 10.3390/genes12020193] [Cited by in Crossref: 3] [Cited by in F6Publishing: 3] [Article Influence: 3.0] [Reference Citation Analysis]
3 Yang R, Liu J. Sensitive and selective photoelectrochemical immunosensing platform based on potential-induced photocurrent-direction switching strategy and a direct Z-scheme CdS//hemin photocurrent-direction switching system. Journal of Electroanalytical Chemistry 2020;873:114346. [DOI: 10.1016/j.jelechem.2020.114346] [Cited by in Crossref: 3] [Cited by in F6Publishing: 3] [Article Influence: 1.5] [Reference Citation Analysis]
4 Vitale M, Migliore S, Tilahun B, Abdurahaman M, Tolone M, Sammarco I, Di Marco Lo Presti V, Gebremedhin EZ. Two novel amino acid substitutions in highly conserved regions of prion protein (PrP) and a high frequency of a scrapie protective variant in native Ethiopian goats. BMC Vet Res 2019;15:128. [PMID: 31053138 DOI: 10.1186/s12917-019-1870-4] [Cited by in Crossref: 5] [Cited by in F6Publishing: 5] [Article Influence: 1.7] [Reference Citation Analysis]
5 Yang R, Zou K, Zhang X, Du C, Chen J. A new photoelectrochemical immunosensor for ultrasensitive assay of prion protein based on hemin-induced photocurrent direction switching. Biosens Bioelectron 2019;132:55-61. [PMID: 30852382 DOI: 10.1016/j.bios.2019.02.035] [Cited by in Crossref: 22] [Cited by in F6Publishing: 23] [Article Influence: 7.3] [Reference Citation Analysis]
6 Li Y, Meng L, Zou K, Zhang X, Chen J. A novel photoelectrochemical immunosensor for prion protein based on CdTe quantum dots and glucose oxidase. Journal of Electroanalytical Chemistry 2018;829:51-8. [DOI: 10.1016/j.jelechem.2018.09.045] [Cited by in Crossref: 7] [Cited by in F6Publishing: 7] [Article Influence: 1.8] [Reference Citation Analysis]
7 Yan X, Li J, Yang R, Li Y, Zhang X, Chen J. A new photoelectrochemical aptasensor for prion assay based on cyclodextrin and Rhodamine B. Sensors and Actuators B: Chemical 2018;255:2187-93. [DOI: 10.1016/j.snb.2017.09.030] [Cited by in Crossref: 21] [Cited by in F6Publishing: 15] [Article Influence: 5.3] [Reference Citation Analysis]
8 Abskharon R, Wang F, Vander Stel KJ, Sinniah K, Ma J. The role of the unusual threonine string in the conversion of prion protein. Sci Rep 2016;6:38877. [PMID: 27982059 DOI: 10.1038/srep38877] [Cited by in Crossref: 13] [Cited by in F6Publishing: 13] [Article Influence: 2.2] [Reference Citation Analysis]
9 Shen X, Huang T, Wang G, Li G. How the Sequence of a Gene Specifies Structural Symmetry in Proteins. PLoS One 2015;10:e0144473. [PMID: 26641668 DOI: 10.1371/journal.pone.0144473] [Cited by in Crossref: 3] [Cited by in F6Publishing: 3] [Article Influence: 0.4] [Reference Citation Analysis]
10 Migliorini C, Sinicropi A, Kozlowski H, Luczkowski M, Valensin D. Copper-induced structural propensities of the amyloidogenic region of human prion protein. J Biol Inorg Chem 2014;19:635-45. [DOI: 10.1007/s00775-014-1132-7] [Cited by in Crossref: 16] [Cited by in F6Publishing: 15] [Article Influence: 2.0] [Reference Citation Analysis]
11 Shen X. Conformation and sequence evidence for two-fold symmetry in left-handed beta-helix fold. J Theor Biol 2011;285:77-83. [PMID: 21708176 DOI: 10.1016/j.jtbi.2011.06.011] [Cited by in Crossref: 4] [Cited by in F6Publishing: 4] [Article Influence: 0.4] [Reference Citation Analysis]
12 Bondy SC. Nanoparticles and colloids as contributing factors in neurodegenerative disease. Int J Environ Res Public Health 2011;8:2200-11. [PMID: 21776226 DOI: 10.3390/ijerph8062200] [Cited by in Crossref: 11] [Cited by in F6Publishing: 13] [Article Influence: 1.0] [Reference Citation Analysis]
13 Shen L, Ji HF. Mutation directional selection sheds light on prion pathogenesis. Biochem Biophys Res Commun 2011;410:159-63. [PMID: 21679685 DOI: 10.1016/j.bbrc.2011.06.007] [Cited by in Crossref: 10] [Cited by in F6Publishing: 11] [Article Influence: 0.9] [Reference Citation Analysis]
14 Shen L, Ji HF. Conformational conversion and prion disease. Nat Rev Mol Cell Biol 2011;12:273; author reply 273. [PMID: 21427768 DOI: 10.1038/nrm3007-c1] [Reference Citation Analysis]
15 Diaz-Espinoza R, Soto C. Generation of prions in vitro and the protein-only hypothesis. Prion 2010;4:53-9. [PMID: 20448454 DOI: 10.4161/pri.4.2.11960] [Cited by in Crossref: 20] [Cited by in F6Publishing: 21] [Article Influence: 1.7] [Reference Citation Analysis]