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Table representation of search results timeline featuring number of search results per year.

Year Number of Results
1956 2
1962 1
1964 1
1965 14
1966 3
1967 16
1968 19
1969 23
1970 12
1971 24
1972 34
1973 18
1974 17
1975 9
1976 23
1977 11
1978 14
1979 8
1980 17
1981 11
1982 23
1983 28
1984 28
1985 50
1986 70
1987 65
1988 62
1989 61
1990 98
1991 166
1992 139
1993 190
1994 262
1995 240
1996 341
1997 380
1998 365
1999 461
2000 540
2001 673
2002 668
2003 711
2004 835
2005 868
2006 951
2007 1005
2008 987
2009 1045
2010 920
2011 982
2012 1012
2013 1021
2014 949
2015 990
2016 943
2017 996
2018 941
2019 908
2020 1007
2021 954
2022 613
2023 1
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22,038 results
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Page 1
Prion disease and the 'protein-only hypothesis'.
Ma J, Wang F. Ma J, et al. Essays Biochem. 2014;56:181-91. doi: 10.1042/bse0560181. Essays Biochem. 2014. PMID: 25131595 Free PMC article. Review.
Prion disease is the only naturally occurring infectious protein misfolding disorder. ...Decades of studies have provided overwhelming evidence to support this hypothesis. The latest advances in generating infectious prions with bacterially expressed recombinant
Prion disease is the only naturally occurring infectious protein misfolding disorder. ...Decades of studies have provided overwhelmin
The Prion Concept and Synthetic Prions.
Legname G, Moda F. Legname G, et al. Prog Mol Biol Transl Sci. 2017;150:147-156. doi: 10.1016/bs.pmbts.2017.06.002. Epub 2017 Jul 20. Prog Mol Biol Transl Sci. 2017. PMID: 28838659 Review.
Transmissible spongiform encephalopathies or prion diseases are a group of fatal neurodegenerative diseases caused by unconventional infectious agents, known as prions (PrP(Sc)). Prions derive from a conformational conversion of the normally folded prion
Transmissible spongiform encephalopathies or prion diseases are a group of fatal neurodegenerative diseases caused by unconventional …
Understanding prion structure and conversion.
Spagnolli G, Requena JR, Biasini E. Spagnolli G, et al. Prog Mol Biol Transl Sci. 2020;175:19-30. doi: 10.1016/bs.pmbts.2020.07.005. Epub 2020 Sep 11. Prog Mol Biol Transl Sci. 2020. PMID: 32958233 Review.
Since their original identification, prions have represented enigmatic agents that defy the classical concept of genetic inheritance. ...As a result, such a lack of information has critically hampered the search for an effective therapy against prion diseases. Never …
Since their original identification, prions have represented enigmatic agents that defy the classical concept of genetic inheritance. …
Prion-like proteins: from computational approaches to proteome-wide analysis.
Gil-Garcia M, Iglesias V, Pallarès I, Ventura S. Gil-Garcia M, et al. FEBS Open Bio. 2021 Sep;11(9):2400-2417. doi: 10.1002/2211-5463.13213. Epub 2021 Jun 17. FEBS Open Bio. 2021. PMID: 34057308 Free PMC article. Review.
Prions are self-perpetuating proteins able to switch between a soluble state and an aggregated-and-transmissible conformation. ...The notion that such proteins could play functional roles and be positively selected by evolution has triggered the development of computationa
Prions are self-perpetuating proteins able to switch between a soluble state and an aggregated-and-transmissible conformation. ...The
[Prion diseases].
Stoĭda NI, Zavalishin IA. Stoĭda NI, et al. Zh Nevrol Psikhiatr Im S S Korsakova. 2012;112(9 Pt 2):59-63. Zh Nevrol Psikhiatr Im S S Korsakova. 2012. PMID: 23235426 Review. Russian.
Prion diseases are a family of progressive neurodegenerative disorders caused by prions. There are four human prion diseases: Creutzfeldt-Jakob disease, Gerstmann-Straussler-Scheinker syndrome, fatal insomnia and Kuru. ...
Prion diseases are a family of progressive neurodegenerative disorders caused by prions. There are four human prion dis
[Prion].
Sakaguchi S. Sakaguchi S. Uirusu. 2002 Jun;52(1):163-7. Uirusu. 2002. PMID: 12227168 Free article. Review. Japanese. No abstract available.
Role of sialylation in prion disease pathogenesis and prion structure.
Baskakov IV. Baskakov IV. Prog Mol Biol Transl Sci. 2020;175:31-52. doi: 10.1016/bs.pmbts.2020.07.004. Epub 2020 Aug 24. Prog Mol Biol Transl Sci. 2020. PMID: 32958238 Review.
Mammalian prion or PrP(Sc) is a proteinaceous infectious agent that consists of a misfolded, self-replicating state of a sialoglycoprotein called the prion protein or PrP(C). ...This chapter summarizes current knowledge on the role of sialylation of the prion
Mammalian prion or PrP(Sc) is a proteinaceous infectious agent that consists of a misfolded, self-replicating state of a sialoglycopr …
Environmental and host factors that contribute to prion strain evolution.
Bartz JC. Bartz JC. Acta Neuropathol. 2021 Jul;142(1):5-16. doi: 10.1007/s00401-021-02310-6. Epub 2021 Apr 25. Acta Neuropathol. 2021. PMID: 33899132 Free PMC article. Review.
Prions are novel pathogens that are composed entirely of PrP(Sc), the self-templating conformation of the host prion protein, PrP(C). ...The relative abundance of PrP(C), post-translational modifications of PrP(C) and cellular co-factors involved in prion con
Prions are novel pathogens that are composed entirely of PrP(Sc), the self-templating conformation of the host prion protein,
Prion Function and Pathophysiology in Non-Mammalian Models.
Guerrero N, Meynard MM, Borgonovo J, Palma K, Concha ML, Hetz C. Guerrero N, et al. Curr Mol Med. 2017;17(1):13-23. doi: 10.2174/1566524017666170220100715. Curr Mol Med. 2017. PMID: 28231753 Review.
More than thirty years have passed since the discovery of the prion protein (PrP) and its causative role in transmissible spongiform encephalopathy. ...Historically, the primary strategy for prion research has involved the use of human tissue, cell cultures and mamm …
More than thirty years have passed since the discovery of the prion protein (PrP) and its causative role in transmissible spongiform …
Prion protein oligomerization.
Rezaei H. Rezaei H. Curr Alzheimer Res. 2008 Dec;5(6):572-8. doi: 10.2174/156720508786898497. Curr Alzheimer Res. 2008. PMID: 19075584 Review.
In most cases, TSE is associated with the accumulation in the brain of an abnormally folded protease-resistant protein, PrP Sc or PrPres, which is derived from a cellular host-encoded protease-sensitive conformer, designated PrP C. The prion propagation in the brain is pos …
In most cases, TSE is associated with the accumulation in the brain of an abnormally folded protease-resistant protein, PrP Sc or PrPres, wh …
22,038 results
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