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Keywords: prion
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Articles
Biochem J (2023) 480 (19): 1485–1501.
Published: 04 October 2023
...Alana M. Thackray; Erin E. McNulty; Amy V. Nalls; Alzbeta Cardova; Linh Tran; Glenn Telling; Sylvie L. Benestad; Sabine Gilch; Candace K. Mathiason; Raymond Bujdoso Chronic wasting disease is a fatal prion condition of cervids such as deer, elk, moose and reindeer. Secretion and excretion of prion...
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Biochem J (2017) 474 (20): 3439–3454.
Published: 05 October 2017
... or chemical inactivation of the ATPase activity of TorA blocks this activity. We also find that TorA can inhibit the propagation of certain conformational variants of [ PSI + ], the aggregated prion form of the endogenous Sup35 protein. Finally, we show that while cellular localisation remains unchanged...
Includes: Supplementary data
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Biochem J (2017) 474 (19): 3253–3267.
Published: 20 September 2017
...Alana M. Thackray; Alzbeta Cardova; Hanna Wolf; Lydia Pradl; Ina Vorberg; Walker S. Jackson; Raymond Bujdoso Inherited human prion diseases, such as fatal familial insomnia (FFI) and familial Creutzfeldt–Jakob disease (fCJD), are associated with autosomal dominant mutations in the human prion...
Includes: Supplementary data
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Biochem J (2017) 474 (17): 3045–3058.
Published: 22 August 2017
... oligomers had similar potency to soluble Aβ oligomers derived from the brains of Alzheimer's patients. Although the conditioned media from 7PA2 cells treated with the cellular prion protein (PrP C ) contained Aβ, it did not cause synapse damage. The loss of toxicity was associated with a reduction in Aβ...
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Biochem J (2017) 474 (1): 123–147.
Published: 22 December 2016
...Ankit Srivastava; Sakshi Sharma; Sandhya Sadanandan; Sakshi Gupta; Jasdeep Singh; Sarika Gupta; V. Haridas; Bishwajit Kundu Misfolding and aggregation of cellular prion protein is associated with a large array of neurological disorders commonly called the transmissible spongiform encephalopathies...
Includes: Supplementary data
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Biochem J (2016) 473 (23): 4399–4412.
Published: 25 November 2016
...Alana M. Thackray; Olivier Andreoletti; Raymond Bujdoso In pursuit of a tractable bioassay to assess blood prion infectivity, we have generated prion protein (PrP) transgenic Drosophila , which show a neurotoxic phenotype in adulthood after exposure to exogenous prions at the larval stage. Here, we...
Articles
Biochem J (2013) 454 (2): 217–225.
Published: 09 August 2013
... of misfolded protein aggregates in the cell and generation of oxidative stress remains poorly understood. Expression of RNQ1-RFP in Saccharomyces cerevisiae cells led to the generation of the prion form of the protein and increased oxidative stress. In the present study, we show that disruption of Hsp104...
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Biochem J (2011) 433 (1): 19–29.
Published: 15 December 2010
..., Huntington's and Parkinson's diseases, and the rarer prion diseases, are separate entities clinically but have common features, including aggregates of misfolded proteins and varying patterns of neurodegeneration. A key barrier to effective treatment is that patients present clinically with advanced...
Includes: Supplementary data
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Biochem J (2010) 428 (1): 95–101.
Published: 28 April 2010
...Clive Bate; Mourad Tayebi; Alun Williams The prion diseases occur following the conversion of the cellular prion protein (PrP C ) into an alternatively folded, disease-associated isoform (PrP Sc ). However, the spread of PrP Sc from cell to cell is poorly understood. In the present manuscript we...
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Biochem J (2006) 399 (3): 435–444.
Published: 13 October 2006
...Mark A. Wells; Graham S. Jackson; Samantha Jones; Laszlo L. P. Hosszu; C. Jeremy Craven; Anthony R. Clarke; John Collinge; Jonathan P. Waltho It has been shown previously that the unfolded N-terminal domain of the prion protein can bind up to six Cu 2+ ions in vitro . This domain contains four...
Includes: Supplementary data
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Biochem J (2004) 380 (1): e5–e6.
Published: 15 May 2004
...Elizabeth F. HOUNSELL Prion proteins that are normal cellular components or involved in pathology can vary little or not at all in primary amino acid sequence, but their glycosylation is different, e.g. in scrapie versus normal forms; in mouse strain-specific isolates; and in BSE (bovine spongiform...
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Biochem J (2003) 372 (1): 129–136.
Published: 15 May 2003
...Mar PÉREZ; Ana I. ROJO; Francisco WANDOSELL; Javier DÍAZ-NIDO; Jesús AVILA Prion diseases are characterized by neuronal cell death, glial proliferation and deposition of prion peptide aggregates. An abnormal misfolded isoform of the prion protein (PrP) is considered to be responsible...
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Biochem J (1999) 344 (3): 723–730.
Published: 08 December 1999
... in these proteoglycans were found to be primarily in the smaller glycosaminoglycan chains. The heparan sulphate proteoglycans were also heavily glycosylated with O-linked glycans and no glycosylphosphatidyl- inositol anchor could be detected. Key words: glycan analysis, glycosaminoglycan, glypican, heparin, prion...
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Biochem J (1999) 342 (3): 605–613.
Published: 05 September 1999
...Debbie B. BRIMACOMBE; Alan D. BENNETT; Fred S. WUSTEMAN; Andrew C. GILL; Janine C. DANN; Christopher J. BOSTOCK Certain polysulphated polyanions have been shown to have prophylactic effects on the progression of transmissible spongiform encephalopathy disease, presumably because they bind to prion...