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For: Moore RA, Herzog C, Errett J, Kocisko DA, Arnold KM, Hayes SF, Priola SA. Octapeptide repeat insertions increase the rate of protease-resistant prion protein formation. Protein Sci 2006;15:609-19. [PMID: 16452616 DOI: 10.1110/ps.051822606] [Cited by in Crossref: 45] [Cited by in F6Publishing: 46] [Article Influence: 2.8] [Reference Citation Analysis]
Number Citing Articles
1 Kim KH, Kim Y, Jeong B. Novel Polymorphisms and Genetic Characteristics of the Prion Protein Gene in Pheasants. Front Vet Sci 2022;9:935476. [DOI: 10.3389/fvets.2022.935476] [Reference Citation Analysis]
2 Brennecke N, Cali I, Mok TH, Speedy H, Genomics England Research Consortium, Hosszu LLP, Stehmann C, Cracco L, Puoti G, Prior TW, Cohen ML, Collins SJ, Mead S, Appleby BS. Characterization of Prion Disease Associated with a Two-Octapeptide Repeat Insertion. Viruses 2021;13:1794. [PMID: 34578375 DOI: 10.3390/v13091794] [Reference Citation Analysis]
3 Candelise N, Scaricamazza S, Salvatori I, Ferri A, Valle C, Manganelli V, Garofalo T, Sorice M, Misasi R. Protein Aggregation Landscape in Neurodegenerative Diseases: Clinical Relevance and Future Applications. Int J Mol Sci 2021;22:6016. [PMID: 34199513 DOI: 10.3390/ijms22116016] [Cited by in Crossref: 2] [Cited by in F6Publishing: 9] [Article Influence: 2.0] [Reference Citation Analysis]
4 Restelli E, Capone V, Pozzoli M, Ortolan D, Quaglio E, Corbelli A, Fiordaliso F, Beznoussenko GV, Artuso V, Roiter I, Sallese M, Chiesa R. Activation of Src family kinase ameliorates secretory trafficking in mutant prion protein cells. J Biol Chem 2021;296:100490. [PMID: 33662396 DOI: 10.1016/j.jbc.2021.100490] [Cited by in F6Publishing: 2] [Reference Citation Analysis]
5 Jen HI, Lin ZY, Guo JX, Lee CI. The Effects of Divalent Cation-Chelated Prion Fibrils on the Immune Response of EOC 13.31 Microglia Cells. Cells 2020;9:E2285. [PMID: 33066249 DOI: 10.3390/cells9102285] [Cited by in Crossref: 2] [Cited by in F6Publishing: 3] [Article Influence: 1.0] [Reference Citation Analysis]
6 Areškevičiūtė A, Høgh P, Bartoletti-Stella A, Melchior LC, Nielsen PR, Parchi P, Capellari S, Broholm H, Scheie D, Lund EL. A Novel Eight Octapeptide Repeat Insertion in PRNP Causing Prion Disease in a Danish Family. J Neuropathol Exp Neurol 2019;78:595-604. [PMID: 31107536 DOI: 10.1093/jnen/nlz037] [Cited by in Crossref: 3] [Cited by in F6Publishing: 4] [Article Influence: 1.5] [Reference Citation Analysis]
7 Kim DJ, Kim YC, Kim AD, Jeong BH. Novel Polymorphisms and Genetic Characteristics of the Prion Protein Gene (PRNP) in Dogs-A Resistant Animal of Prion Disease. Int J Mol Sci 2020;21:E4160. [PMID: 32532135 DOI: 10.3390/ijms21114160] [Cited by in Crossref: 5] [Cited by in F6Publishing: 7] [Article Influence: 2.5] [Reference Citation Analysis]
8 Czech A, Konarev PV, Goebel I, Svergun DI, Wills PR, Ignatova Z. Octa-repeat domain of the mammalian prion protein mRNA forms stable A-helical hairpin structure rather than G-quadruplexes. Sci Rep 2019;9:2465. [PMID: 30792490 DOI: 10.1038/s41598-019-39213-2] [Cited by in Crossref: 2] [Cited by in F6Publishing: 2] [Article Influence: 0.7] [Reference Citation Analysis]
9 Bagyinszky E, Giau VV, Youn YC, An SSA, Kim S. Characterization of mutations in PRNP (prion) gene and their possible roles in neurodegenerative diseases. Neuropsychiatr Dis Treat 2018;14:2067-85. [PMID: 30147320 DOI: 10.2147/NDT.S165445] [Cited by in Crossref: 33] [Cited by in F6Publishing: 31] [Article Influence: 8.3] [Reference Citation Analysis]
10 Kim MO, Takada LT, Wong K, Forner SA, Geschwind MD. Genetic PrP Prion Diseases. Cold Spring Harb Perspect Biol 2018;10:a033134. [PMID: 28778873 DOI: 10.1101/cshperspect.a033134] [Cited by in Crossref: 34] [Cited by in F6Publishing: 38] [Article Influence: 8.5] [Reference Citation Analysis]
11 Takada LT, Kim MO, Cleveland RW, Wong K, Forner SA, Gala II, Fong JC, Geschwind MD. Genetic prion disease: Experience of a rapidly progressive dementia center in the United States and a review of the literature. Am J Med Genet B Neuropsychiatr Genet 2017;174:36-69. [PMID: 27943639 DOI: 10.1002/ajmg.b.32505] [Cited by in Crossref: 57] [Cited by in F6Publishing: 46] [Article Influence: 11.4] [Reference Citation Analysis]
12 Yen CF, Harischandra DS, Kanthasamy A, Sivasankar S. Copper-induced structural conversion templates prion protein oligomerization and neurotoxicity. Sci Adv 2016;2:e1600014. [PMID: 27419232 DOI: 10.1126/sciadv.1600014] [Cited by in Crossref: 35] [Cited by in F6Publishing: 40] [Article Influence: 5.8] [Reference Citation Analysis]
13 Fernández-Borges N, Eraña H, Venegas V, Elezgarai SR, Harrathi C, Castilla J. Animal models for prion-like diseases. Virus Res 2015;207:5-24. [PMID: 25907990 DOI: 10.1016/j.virusres.2015.04.014] [Cited by in Crossref: 7] [Cited by in F6Publishing: 8] [Article Influence: 1.0] [Reference Citation Analysis]
14 Didonna A, Venturini AC, Hartman K, Vranac T, Čurin Šerbec V, Legname G. Characterization of four new monoclonal antibodies against the distal N-terminal region of PrP(c). PeerJ 2015;3:e811. [PMID: 25802800 DOI: 10.7717/peerj.811] [Cited by in Crossref: 5] [Cited by in F6Publishing: 5] [Article Influence: 0.7] [Reference Citation Analysis]
15 Godsave SF, Peters PJ, Wille H. Subcellular distribution of the prion protein in sickness and in health. Virus Res 2015;207:136-45. [PMID: 25683509 DOI: 10.1016/j.virusres.2015.02.004] [Cited by in Crossref: 13] [Cited by in F6Publishing: 14] [Article Influence: 1.9] [Reference Citation Analysis]
16 Moulick R, Udgaonkar JB. Thermodynamic characterization of the unfolding of the prion protein. Biophys J 2014;106:410-20. [PMID: 24461016 DOI: 10.1016/j.bpj.2013.11.4491] [Cited by in Crossref: 19] [Cited by in F6Publishing: 22] [Article Influence: 2.4] [Reference Citation Analysis]
17 Kojima A, Konishi M, Akizawa T. Prion fragment peptides are digested with membrane type matrix metalloproteinases and acquire enzyme resistance through Cu²⁺-binding. Biomolecules 2014;4:510-26. [PMID: 24970228 DOI: 10.3390/biom4020510] [Cited by in Crossref: 8] [Cited by in F6Publishing: 12] [Article Influence: 1.0] [Reference Citation Analysis]
18 Taguchi Y, Schätzl HM. Identifying critical sites of PrP(c)-PrP(Sc) interaction in prion-infected cells by dominant-negative inhibition. Prion 2013;7:452-6. [PMID: 24401595 DOI: 10.4161/pri.27500] [Cited by in Crossref: 5] [Cited by in F6Publishing: 3] [Article Influence: 0.6] [Reference Citation Analysis]
19 Paucar M, Xiang F, Moore R, Walker R, Winnberg E, Svenningsson P. Genotype-phenotype analysis in inherited prion disease with eight octapeptide repeat insertional mutation. Prion 2013;7:501-10. [PMID: 24275071 DOI: 10.4161/pri.27260] [Cited by in Crossref: 14] [Cited by in F6Publishing: 12] [Article Influence: 1.6] [Reference Citation Analysis]
20 Antony H, Wiegmans AP, Wei MQ, Chernoff YO, Khanna KK, Munn AL. Potential roles for prions and protein-only inheritance in cancer. Cancer Metastasis Rev 2012;31:1-19. [PMID: 22138778 DOI: 10.1007/s10555-011-9325-9] [Cited by in Crossref: 19] [Cited by in F6Publishing: 19] [Article Influence: 1.9] [Reference Citation Analysis]
21 Imran M, Mahmood S, Hussain R, Abid NB, Lone KP. Frequency distribution of PRNP polymorphisms in the Pakistani population. Gene 2012;492:186-94. [PMID: 22062631 DOI: 10.1016/j.gene.2011.10.029] [Cited by in Crossref: 4] [Cited by in F6Publishing: 4] [Article Influence: 0.4] [Reference Citation Analysis]
22 Li B, Qing L, Yan J, Kong Q. Instability of the octarepeat region of the human prion protein gene. PLoS One 2011;6:e26635. [PMID: 22028931 DOI: 10.1371/journal.pone.0026635] [Cited by in Crossref: 4] [Cited by in F6Publishing: 5] [Article Influence: 0.4] [Reference Citation Analysis]
23 Jones EM, Wu B, Surewicz K, Nadaud PS, Helmus JJ, Chen S, Jaroniec CP, Surewicz WK. Structural polymorphism in amyloids: new insights from studies with Y145Stop prion protein fibrils. J Biol Chem 2011;286:42777-84. [PMID: 22002245 DOI: 10.1074/jbc.M111.302539] [Cited by in Crossref: 32] [Cited by in F6Publishing: 26] [Article Influence: 2.9] [Reference Citation Analysis]
24 Azevedo J, Cooke R, Lagrange T. Taking RISCs with Ago hookers. Current Opinion in Plant Biology 2011;14:594-600. [DOI: 10.1016/j.pbi.2011.07.002] [Cited by in Crossref: 19] [Cited by in F6Publishing: 14] [Article Influence: 1.7] [Reference Citation Analysis]
25 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]
26 Cruite JT, Abalos GC, Bellon A, Solforosi L. Histidines in the octapeptide repeat of PrPC react with PrPSc at an acidic pH. Biochemistry 2011;50:1618-23. [PMID: 21268659 DOI: 10.1021/bi1017683] [Reference Citation Analysis]
27 Lawson VA, Lumicisi B, Welton J, Machalek D, Gouramanis K, Klemm HM, Stewart JD, Masters CL, Hoke DE, Collins SJ, Hill AF. Glycosaminoglycan sulphation affects the seeded misfolding of a mutant prion protein. PLoS One 2010;5:e12351. [PMID: 20808809 DOI: 10.1371/journal.pone.0012351] [Cited by in Crossref: 18] [Cited by in F6Publishing: 20] [Article Influence: 1.5] [Reference Citation Analysis]
28 Helmus JJ, Surewicz K, Surewicz WK, Jaroniec CP. Conformational flexibility of Y145Stop human prion protein amyloid fibrils probed by solid-state nuclear magnetic resonance spectroscopy. J Am Chem Soc 2010;132:2393-403. [PMID: 20121096 DOI: 10.1021/ja909827v] [Cited by in Crossref: 115] [Cited by in F6Publishing: 104] [Article Influence: 9.6] [Reference Citation Analysis]
29 Yam AY, Gao CM, Wang X, Wu P, Peretz D. The octarepeat region of the prion protein is conformationally altered in PrP(Sc). PLoS One 2010;5:e9316. [PMID: 20195363 DOI: 10.1371/journal.pone.0009316] [Cited by in Crossref: 18] [Cited by in F6Publishing: 17] [Article Influence: 1.5] [Reference Citation Analysis]
30 Choi CJ, Anantharam V, Martin DP, Nicholson EM, Richt JA, Kanthasamy A, Kanthasamy AG. Manganese upregulates cellular prion protein and contributes to altered stabilization and proteolysis: relevance to role of metals in pathogenesis of prion disease. Toxicol Sci 2010;115:535-46. [PMID: 20176619 DOI: 10.1093/toxsci/kfq049] [Cited by in Crossref: 31] [Cited by in F6Publishing: 28] [Article Influence: 2.6] [Reference Citation Analysis]
31 Taubner LM, Bienkiewicz EA, Copié V, Caughey B. Structure of the flexible amino-terminal domain of prion protein bound to a sulfated glycan. J Mol Biol 2010;395:475-90. [PMID: 19913031 DOI: 10.1016/j.jmb.2009.10.075] [Cited by in Crossref: 37] [Cited by in F6Publishing: 34] [Article Influence: 2.8] [Reference Citation Analysis]
32 Hiraga C, Kobayashi A, Kitamoto T. The number of octapeptide repeat affects the expression and conversion of prion protein. Biochemical and Biophysical Research Communications 2009;382:715-9. [DOI: 10.1016/j.bbrc.2009.03.093] [Cited by in Crossref: 1] [Cited by in F6Publishing: 2] [Article Influence: 0.1] [Reference Citation Analysis]
33 Stevens DJ, Walter ED, Rodríguez A, Draper D, Davies P, Brown DR, Millhauser GL. Early onset prion disease from octarepeat expansion correlates with copper binding properties. PLoS Pathog 2009;5:e1000390. [PMID: 19381258 DOI: 10.1371/journal.ppat.1000390] [Cited by in Crossref: 54] [Cited by in F6Publishing: 47] [Article Influence: 4.2] [Reference Citation Analysis]
34 Moore RA, Taubner LM, Priola SA. Prion protein misfolding and disease. Curr Opin Struct Biol 2009;19:14-22. [PMID: 19157856 DOI: 10.1016/j.sbi.2008.12.007] [Cited by in Crossref: 55] [Cited by in F6Publishing: 48] [Article Influence: 4.2] [Reference Citation Analysis]
35 True HL, Kalastavadi T, Tank EM. Insights into intragenic and extragenic effectors of prion propagation using chimeric prion proteins. Prion 2008;2:45-7. [PMID: 19098443 DOI: 10.4161/pri.2.2.6509] [Reference Citation Analysis]
36 Leliveld SR, Stitz L, Korth C. Expansion of the octarepeat domain alters the misfolding pathway but not the folding pathway of the prion protein. Biochemistry 2008;47:6267-78. [PMID: 18473442 DOI: 10.1021/bi800253c] [Cited by in Crossref: 18] [Cited by in F6Publishing: 16] [Article Influence: 1.3] [Reference Citation Analysis]
37 Helmus JJ, Surewicz K, Nadaud PS, Surewicz WK, Jaroniec CP. Molecular conformation and dynamics of the Y145Stop variant of human prion protein in amyloid fibrils. Proc Natl Acad Sci U S A 2008;105:6284-9. [PMID: 18436646 DOI: 10.1073/pnas.0711716105] [Cited by in Crossref: 167] [Cited by in F6Publishing: 145] [Article Influence: 11.9] [Reference Citation Analysis]
38 Kalastavadi T, True HL. Prion protein insertional mutations increase aggregation propensity but not fiber stability. BMC Biochem 2008;9:7. [PMID: 18366654 DOI: 10.1186/1471-2091-9-7] [Cited by in Crossref: 8] [Cited by in F6Publishing: 8] [Article Influence: 0.6] [Reference Citation Analysis]
39 Erlich P, Cesbron JY, Lemaire-Vieille C, Curt A, Andrieu JP, Schoehn G, Jamin M, Gagnon J. PrP N-terminal domain triggers PrP(Sc)-like aggregation of Dpl. Biochem Biophys Res Commun 2008;365:478-83. [PMID: 17997980 DOI: 10.1016/j.bbrc.2007.10.202] [Cited by in Crossref: 5] [Cited by in F6Publishing: 5] [Article Influence: 0.3] [Reference Citation Analysis]
40 Dong J, Bloom JD, Goncharov V, Chattopadhyay M, Millhauser GL, Lynn DG, Scheibel T, Lindquist S. Probing the role of PrP repeats in conformational conversion and amyloid assembly of chimeric yeast prions. J Biol Chem 2007;282:34204-12. [PMID: 17893150 DOI: 10.1074/jbc.M704952200] [Cited by in Crossref: 25] [Cited by in F6Publishing: 22] [Article Influence: 1.7] [Reference Citation Analysis]
41 Tank EM, Harris DA, Desai AA, True HL. Prion protein repeat expansion results in increased aggregation and reveals phenotypic variability. Mol Cell Biol 2007;27:5445-55. [PMID: 17548473 DOI: 10.1128/MCB.02127-06] [Cited by in Crossref: 33] [Cited by in F6Publishing: 35] [Article Influence: 2.2] [Reference Citation Analysis]
42 Li A, Piccardo P, Barmada SJ, Ghetti B, Harris DA. Prion protein with an octapeptide insertion has impaired neuroprotective activity in transgenic mice. EMBO J 2007;26:2777-85. [PMID: 17510630 DOI: 10.1038/sj.emboj.7601726] [Cited by in Crossref: 26] [Cited by in F6Publishing: 26] [Article Influence: 1.7] [Reference Citation Analysis]
43 Yu S, Yin S, Li C, Wong P, Chang B, Xiao F, Kang SC, Yan H, Xiao G, Tien P, Sy MS. Aggregation of prion protein with insertion mutations is proportional to the number of inserts. Biochem J 2007;403:343-51. [PMID: 17187581 DOI: 10.1042/BJ20061592] [Cited by in Crossref: 18] [Cited by in F6Publishing: 18] [Article Influence: 1.2] [Reference Citation Analysis]
44 Kocisko DA, Bertholet N, Moore RA, Caughey B, Vaillant A. Identification of prion inhibitors by a fluorescence-polarization-based competitive binding assay. Analytical Biochemistry 2007;363:154-6. [DOI: 10.1016/j.ab.2006.11.007] [Cited by in Crossref: 10] [Cited by in F6Publishing: 9] [Article Influence: 0.7] [Reference Citation Analysis]
45 Sun Y, Breydo L, Makarava N, Yang Q, Bocharova OV, Baskakov IV. Site-specific Conformational Studies of Prion Protein (PrP) Amyloid Fibrils Revealed Two Cooperative Folding Domains within Amyloid Structure. Journal of Biological Chemistry 2007;282:9090-7. [DOI: 10.1074/jbc.m608623200] [Cited by in Crossref: 46] [Cited by in F6Publishing: 41] [Article Influence: 3.1] [Reference Citation Analysis]
46 Shiraishi N, Utsunomiya H, Nishikimi M. Combination of NADPH and copper ions generates proteinase K-resistant aggregates from recombinant prion protein. J Biol Chem 2006;281:34880-7. [PMID: 16990274 DOI: 10.1074/jbc.M606581200] [Cited by in Crossref: 9] [Cited by in F6Publishing: 8] [Article Influence: 0.6] [Reference Citation Analysis]