The physical basis of how prion conformations determine strain phenotypes

By Motomasa Tanaka, Sean R. Collins, Brandon H. Toyama, Jonathan S. Weissman. Nature, 2006

619 citations recorded by the source corpus.

Subfields: Molecular Biology, Neurology, Nutrition and Dietetics

View Paper: https://www.semanticscholar.org/paper/13f2a45fb595a613f2845bf9b68ea68c5dfc0d77

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Citations in the corpus

Nanomechanics of functional and pathological amyloid materials. (2011, background): “This fact may be a manifestation of the general tendency of amyloid materials towards polymorphism through the existence of many strains of fibrils formed by the same polypeptide sequence but characterized by subtle changes in the molecular packing of the chains within the fibril”
The amyloid state and its association with protein misfolding diseases (2014, background): “Paired betasheet structure of an Aβ(1-40) amyloid fibril revealed by electron microscopy.”
Molecular structural basis for polymorphism in Alzheimer's β-amyloid fibrils (2008, background): “The predominant morphology may be influenced by a variety of competing factors, including rates of spontaneous nucleation, fibril extension, and fibril fragmentation (35, 36).”
A systematic survey identifies prions and illuminates sequence features of prionogenic proteins (2009, methodology): “Fiber transformation 25 In vitro-generated Mot3PrD-M-His7 aggregates were examined by transmission electron microscopy to confirm a fibrillar amyloid appearance, and transformed into dan1::URA3 reporter strains using methodology as described (Tanaka et al., 2006).”
Atomic structures of amyloid cross-β spines reveal varied steric zippers (2007, background): “2 each form two polymorphs, offering a glimpse of the possible molecular basis of the phenomena of prion strains and amyloid polymorphism 39–45 .”
Prion-like Mechanisms in Neurodegenerative Diseases (2009, background): “The rate of growth and fibril fragility determine the efficiency with which protein aggregates are passed from mother to daughter cell”
Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism (2013, background): “The highly complex self-assembly behavior exhibited by this peptide has, however, prevented its mechanism of aggregation from being defined in terms of molecular events in the manner that has been possible for other biomolecular assemblies, such as actin (10) and some prions (11, 12).”
Distinct tau prion strains propagate in cells and mice and define different tauopathies (2014, methodology): “Thus, the clone 10 fibrils might not be as readily fragmented into smaller species (Tanaka et al., 2006).”