A General Model of Prion Strains and Their Pathogenicity

By J. Collinge, A. Clarke. Science, 2007

1,055 citations recorded by the source corpus.

Subfields: Molecular Biology, Neurology, Nutrition and Dietetics

View Paper: https://www.semanticscholar.org/paper/10de6d9a88998767a68ea177ed0a35810704d4f7

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Citations in the corpus

Distinct tau prion strains propagate in cells and mice and define different tauopathies (2014, background): “Similar to what has been reported for PrP amyloids (Collinge and Clarke, 2007; Li et al., 2010), we speculate that these clouds of tau conformers are prone to selective pressures at the cellular level, which might have implications for therapies that target extracellular tau (Holmes et al., 2013;…”
Protein Metamorphosis: The Two-State Behavior of Mad2 (2008, background): “…are the protein-only infectious agents that cause neurodegenerative diseases in mammals, including scrapie in sheep and goat, bovine spongiform encephalopathy (BSE or “Mad cow disease”), human Creutzfeldt-Jakob disease (CJD), and human variant CJD (vCJD) (Collinge and Clarke, 2007; Prusiner, 1998).”
Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade. (2017, background): “Despite the fact that all these processes have coevolved in all living organisms, protein aggregation inevitably occurs as a consequence of aging (31, 81, 196), environmental stress, and certain aspects of lifestyle, such as obesity (81, 190, 196, 222), sustained increases in protein concentration (”
The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease (2012, background): “…agents of infectious neurodegenerative diseases in mammals, including bovine spongiform encephalopathy, which can even traverse species barriers via the food chain and cause variant Creutzfeldt–Jakob disease in humans (Colby and Prusiner, 2011; Collinge and Clarke, 2007; Weissmann et al., 2011).”
Alzheimer’s Disease and the β-Amyloid Peptide (2010, positive): “An analogy of this situation is found in prion diseases in which the same protein sequence can assume multiple disease-causing conformations, each causing neurodegeneration in a distinct distribution of brain regions resulting in different clinical presentations [4,5].”
Proteopathic tau seeding predicts tauopathy in vivo (2014, background): “Our laboratory previously demonstrated that template-based seeding requires homotypic interactions between seed and substrate (20), consistent with the existence of seeding barriers (33).”