References
- Prusiner SB. Prions. Proc Natl Acad Sci USA. 1998;95:13363–13383.
- Prusiner SB. Molecular biology of prion diseases. Science. 1991;252:1515–1522.
- Collinge J, Sidle KC, Meads J, et al. Molecular analysis of prion strain variation and the aetiology of ‘new variant’ CJD. Nature. 1996;383:685–690.
- Seelig DM, Goodman PA, Skinner PJ. Potential approaches for heterologous prion protein treatment of prion diseases. Prion. 2016;10:18–24.
- Scheckel C, Aguzzi A. Prions, prionoids and protein misfolding disorders. Nat Rev Genet. 2018;19:405–418.
- Antony H, Wiegmans AP, Wei MQ, et al. Potential roles for prions and protein-only inheritance in cancer. Cancer Metastasis Rev. 2012;31:1–19.
- Imberdis T, Heeres JT, Yueh H, et al. Identification of anti-prion compounds using a novel cellular assay. J Biol Chem. 2016;291:26164–26176.
- Maplestone RA, Stone MJ, Williams DH. The evolutionary role of secondary metabolites – a review. Gene. 1992;115:151–157.
- Newman DJ, Cragg GM. Natural products as sources of new drugs from 1981 to 2014. J Nat Prod. 2016;79:629–661.
- Solassol J, Crozet C, Lehmann S. Prion propagation in cultured cells. Br Med Bull. 2003;66:87–97.
- Wickner RB. [URE3] as an altered Ure2 protein: evidence for a prion analog in Saccharomyces cerevisiae. Science. 1994;264:566–569.
- Bach S, Talarek N, Andrieu T, et al. Isolation of drugs active against mammalian prions using a yeast-based screening assay. Nat Biotechnol. 2003;21:1075–1081.
- Tribouillard D, Bach S, Gug F, et al. Using budding yeast to screen for anti-prion drugs. Biotechnol J. 2006;1:58–67.
- Wickner RB, Masison DC, Edskes HK. [PSI+] and [URE3] as yeast prions. Yeast. 1995;11:1671–1685.
- Smirnov M, Smirnov V, Budowsky E, et al. Red pigment of adenine-deficient yeast Saccharomyces cerevisiae. Biochem Biophys Res Commun. 1967;27:299–304.
- Shewmaker F, Mull L, Nakayashiki T, et al. Ure2p function is enhanced by its prion domain in Saccharomyces cerevisiae. Genetics. 2007;176:1557–1565.
- Liebman SW, Chernoff YO. Prions in yeast. Genetics. 2012;191:1041–1072.
- Coschigano PW, Magasanik B. The URE2 gene product of Saccharomyces cerevisiae plays an important role in the cellular response to the nitrogen source and has homology to glutathione s-transferases. Mol Cell Biol. 1991;11:822–832.
- Bach S, Tribouillard D, Talarek N, et al. A yeast-based assay to isolate drugs active against mammalian prions. Methods. 2006;39:72–77.
- Bruschi CV, Chuba PJ. Nonselective enrichment for yeast adenine mutants by flow cytometry. Cytometry. 1988;9:60–67.
- Teasdale PR, Hayward S, Davison W. In situ, high-resolution measurement of dissolved sulfide using diffusive gradients in thin films with computer-imaging densitometry. Anal Chem. 1999;71:2186–2191.
- Tribouillard-Tanvier D, Beringue V, Desban N, et al. Antihypertensive drug Guanabenz is active in vivo against both yeast and mammalian prions. PLoS One. 2008;3:e1981.
- Feher M, Schmidt JM. Property distributions: differences between drugs, natural products, and molecules from combinatorial chemistry. J Chem Inf Comput Sci. 2003;43:218–227.
- Xynas R, Capon R. Two new bromotyrosine-derived metabolites from an Australian marine sponge, Aplysina sp. Aust J Chem. 1989;42:1427–1433.
- Kobayashi J, Honma K, Sasaki T, et al. Purealidins J-R, new bromotyrosine alkaloids from the Okinawan marine sponge Psammaplysilla purea. Chem Pharm Bull. 1995;43:403–407.
- Hamann MT, Scheuer PJ, Kelly-Borges M. Biogenetically diverse, bioactive constituents of a sponge, order Verongida: bromotyramines and sesquiterpene-shikimate derived metabolites. J Org Chem. 1993;58:6565–6569.
- Tsukamoto S, Kato H, Hirota H, et al. Ceratinamine: an unprecedented antifouling cyanoformamide from the marine sponge Pseudoceratina purpurea. J Org Chem. 1996;61:2936–2937.
- Tilvi S, Rodrigues C, Naik CG, et al. New bromotyrosine alkaloids from the marine sponge Psammaplysilla purpurea. Tetrahedron. 2004;60:10207–10215.
- Ishibashi M, Tsuda M, Ohizumi Y, et al. Purealidin A, a new cytotoxic bromotyrosine-derived alkaloid from the Okinawan marine sponge Psammaplysilla purea. Experientia. 1991;47:299–300.
- Ortlepp S, Sjoegren M, Dahlstroem M, et al. Antifouling activity of bromotyrosine-derived sponge metabolites and synthetic analogues. Mar Biotechnol. 2007;9:776–785.
- Gotsbacher MP, Karuso P. New antimicrobial bromotyrosine analogues from the sponge Pseudoceratina purpurea and its predator Tylodina corticalis. Mar Drugs. 2015;13:1389–1409.
- Olatunji OJ, Ogundajo AL, Oladosu IA, et al. Non-competitive inhibition of acetylcholinesterase by bromotyrosine alkaloids. Nat Prod Commun. 2014;9:1559–1561.
- Tian L-W, Feng Y, Shimizu Y, et al. Aplysinellamides A–C, bromotyrosine-derived metabolites from an Australian Aplysinella sp. Marine Sponge J Nat Prod. 2014;77:1210–1214.
- Schoenfeld RC, Lumb J-P, Fantini J, et al. Total synthesis of mololipids: a new series of anti-HIV Moloka’iamine derivatives. Bioorg Med Chem Lett. 2000;10:2679–2681.
- Brogan JT, Stoops SL, Crews BC, et al. Total synthesis of (+)-7-bromotrypargine and unnatural analogues: biological evaluation uncovers activity at CNS targets of therapeutic relevance. ACS Chem Neurosci. 2011;2:633–639.
- Morisset S, Rouleau A, Ligneau X, et al. High constitutive activity of native H3 receptors regulates histamine neurons in brain. Nature. 2000;408:860–864.
- Torrent J, Vilchez-Acosta A, Muñoz-Torrero D, et al. Interaction of prion protein with acetylcholinesterase: potential pathobiological implications in prion diseases. Acta Neuropathol Commun. 2015;3:18.
- Doh-Ura K, Ishikawa K, Murakami-Kubo I, et al. Treatment of transmissible spongiform encephalopathy by intraventricular drug infusion in animal models. J Virol. 2004;78:4999–5006.
- Vishnevskaya AB, Kushnirov VV, Ter-Avanesyan MD. Neurodegenerative amyloidoses: yeast model. Mol Biol. 2007;41:308–315.
- Prusiner SB, Woerman AL, Mordes DA, et al. Evidence for α-synuclein prions causing multiple system atrophy in humans with parkinsonism. Proc Natl Acad Sci USA. 2015;112:E5308–E5317.