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Keywords: Prion
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Journal Articles
J Cell Sci (2021) 134 (11): jcs258316.
Published: 4 June 2021
... by The Company of Biologists Ltd 2021 Summary: Prion-like p53 amyloids impart oncogenic properties to non-cancerous cells, leading to tumorigenesis, and can therefore play a vital role in cancer initiation. p53 Amyloid Prion Tumor suppressor Tumorigenesis Cancer initiation p53 has...
Includes: Supplementary data
Journal Articles
J Cell Sci (2018) 131 (8): jcs189928.
Published: 13 April 2018
... inhibitors rapidly rescue synaptic plasticity deficits by reducing aberrant tau . Biol. Psychiatry   74 , 367 - 374 . 10.1016/j.biopsych.2013.02.027 Aguzzi , A. and Calella , A. M. ( 2009 ). Prions: protein aggregation and infectious diseases . Physiol. Rev.   89 , 1105 - 1152...
Journal Articles
J Cell Sci (2017) 130 (18): 3050–3059.
Published: 15 September 2017
...Ewan West; Craig Osborne; Clive Bate ABSTRACT Cholesterol is required for the formation and function of some signalling platforms. In synaptosomes, amyloid-β (Aβ) oligomers, the causative agent in Alzheimer's disease, bind to cellular prion proteins (PrP C ) resulting in increased cholesterol...
Journal Articles
J Cell Sci (2017) 130 (2): 480–489.
Published: 15 January 2017
...Kensuke Kataoka; Kazufumi Mochizuki ABSTRACT Regulated aggregations of prion and prion-like proteins play physiological roles in various biological processes. However, their structural roles in the nucleus are poorly understood. Here, we show that the prion-like protein Jub6p is involved...
Includes: Supplementary data
Journal Articles
J Cell Sci (2015) 128 (7): 1434–1443.
Published: 1 April 2015
...Yang-In Yim; Bum-Chan Park; Rajgopal Yadavalli; Xiaohong Zhao; Evan Eisenberg; Lois E. Greene ABSTRACT The conversion of the properly folded prion protein, PrPc, to its misfolded amyloid form, PrPsc, occurs as the two proteins traffic along the endocytic pathway and PrPc is exposed to PrPsc...
Includes: Supplementary data
Journal Articles
J Cell Sci (2010) 123 (8): 1191–1201.
Published: 15 April 2010
...Mimi Cushman; Brian S. Johnson; Oliver D. King; Aaron D. Gitler; James Shorter Prions are proteins that access self-templating amyloid forms, which confer phenotypic changes that can spread from individual to individual within or between species. These infectious phenotypes can be beneficial...
Journal Articles
Journal Articles
J Cell Sci (2009) 122 (10): 1518–1528.
Published: 15 May 2009
...Cathryn L. Haigh; Simon C. Drew; Martin P. Boland; Colin L. Masters; Kevin J. Barnham; Victoria A. Lawson; Steven J. Collins Beta-cleavage of the neurodegenerative disease-associated prion protein (PrP) protects cells from death induced by oxidative insults. The beta-cleavage event produces two...
Includes: Supplementary data
Journal Articles
J Cell Sci (2007) 120 (15): 2663–2671.
Published: 1 August 2007
...Kyung-Jin Lee; Antony Panzera; David Rogawski; Lois E. Greene; Evan Eisenberg The effect of normal cellular prion protein (PrP C ) on abnormal protein aggregation was examined by transfecting huntingtin fragments (Htt) into SN56 neuronal-derived cells depleted of PrP C by RNA interference. PrP C...
Journal Articles
Journal Articles
J Cell Sci (2004) 117 (23): 5591–5597.
Published: 1 November 2004
...Carole Crozet; Yea-Lih Lin; Clément Mettling; Chantal Mourton-Gilles; Pierre Corbeau; Sylvain Lehmann; Véronique Perrier Currently, there is no treatment to cure transmissible spongiform encephalopathies. By taking advantage of the `prion-resistant' polymorphisms Q171R and E219K that naturally...
Journal Articles
Journal Articles
Journal Articles
J Cell Sci (2003) 116 (13): 2775–2779.
Published: 1 July 2003
...Nathalie Daude; Mathieu Marella; Joëlle Chabry Development of transmissible spongiform encephalopathies (TSEs)pathogenesis requires the presence of both the normal host prion protein(PrP-sen) and the abnormal pathological proteinase-K resistant isoform(PrP-res). PrP-res forms highly insoluble...