2003
DOI: 10.1007/s00705-002-0958-4
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Early detection of PrP res in BSE-infected bovine PrP transgenic mice

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Cited by 118 publications
(66 citation statements)
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“…All but the bovine PrP expressing mice (tgBov) were established on the same mouse PrP Ko background (Zurich I) [28][30]. In each of these mouse lines relative PrP expression level in the brain, by comparison to the natural host species, was described (tga20: 10-fold–tg338: 6–8 fold, tgBov/tg110: 8-fold, tgShpXI: 3–4-fold, tg650: 6-fold) [28], [31][34] …”
Section: Methodsmentioning
confidence: 99%
“…All but the bovine PrP expressing mice (tgBov) were established on the same mouse PrP Ko background (Zurich I) [28][30]. In each of these mouse lines relative PrP expression level in the brain, by comparison to the natural host species, was described (tga20: 10-fold–tg338: 6–8 fold, tgBov/tg110: 8-fold, tgShpXI: 3–4-fold, tg650: 6-fold) [28], [31][34] …”
Section: Methodsmentioning
confidence: 99%
“…This line is homozygous and exhibits approximately 6-fold overexpression of human PrP C (Met 129 allele) in the brain. The bovine PrP tg110 line has been described previously (25).…”
Section: Ethics Statementmentioning
confidence: 99%
“…It can also be found, but at lower levels, in neuroglia, the reproductive tract, spleen, lymph nodes, and immune cells (Brown et al 2000, Ford et al 2002. Its role in prion diseases has been well described, wherein a conformational isoform of this protein (PrP Sc ) could lead to the appearance of typical pathognomonic symptoms (Prusiner 1982, Castilla et al 2003. The first knockout (KO) mouse models were generated in the 1990s (Bueler et al 1992, Manson et al 1994, which helped to demonstrate that PrP C is essential in these neurodegenerative diseases.…”
Section: Introductionmentioning
confidence: 99%