Results 11 to 20 of about 97,942 (322)
A structural basis for prion strain diversity
bioRxiv, 2022 Recent cryogenic electron microscopy (cryo-EM) studies of infectious, ex vivo, prion fibrils from hamster 263K and mouse RML prion strains revealed a similar, parallel in-register intermolecular β-sheet (PIRIBS) amyloid architecture. Rungs of the fibrils
S. Manka +6 more
semanticscholar +1 more source
Nature Communications, 2022 Little is known about the structural basis of prion strains. Here we provide a high (3.0 Å) resolution cryo-electron microscopy-based structure of infectious brain-derived fibrils of the mouse anchorless RML scrapie strain which, like the recently ...
Forrest H Hoyt +13 more
semanticscholar +1 more source
The Future of Seed Amplification Assays and Clinical Trials
Frontiers in Aging Neuroscience, 2022 Prion-like seeded misfolding of host proteins is the leading hypothesised cause of neurodegenerative diseases. The exploitation of the mechanism in the protein misfolding cyclic amplification (PMCA) and real-time quaking-induced conversion (RT-QuIC ...
Thomas Coysh +3 more
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Case report of homozygous E200D mutation of PRNP in apparently sporadic Creutzfeldt-Jakob disease
BMC Neurology, 2021 Background Inherited prion diseases are rare autosomal dominant disorders associated with diverse clinical presentations. All are associated with mutation of the gene that encodes prion protein (PRNP).
Ahamad Hassan +6 more
doaj +1 more source
Cold Spring Harbor Perspectives in Biology, 2011 The discovery of infectious proteins, denoted prions, was unexpected. After much debate over the chemical basis of heredity, resolution of this issue began with the discovery that DNA, not protein, from pneumococcus was capable of genetically transforming bacteria (Avery et al. 1944).
David W, Colby, Stanley B, Prusiner
openaire +2 more sources
Prions: Portable prion domains [PDF]
Current Biology, 2000 Self-propagating abnormal proteins, prions, have been identified in yeast; asparagine/glutamine-rich 'prion domains' within these proteins can inactivate the linked functional domains; new prion domains and reporters have been used to make 'synthetic prions', leading to discoveries of new natural prions.
Wickner, R.B. +3 more
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Gene-Edited Cell Models to Study Chronic Wasting Disease
Viruses, 2022 Prion diseases are fatal infectious neurodegenerative disorders affecting both humans and animals. They are caused by the misfolded isoform of the cellular prion protein (PrPC), PrPSc, and currently no options exist to prevent or cure prion diseases ...
Simrika Thapa +5 more
doaj +1 more source
Diagnosis of prion diseases by RT-QuIC results in improved surveillance
Neurology, 2020 Objective To present the National Prion Disease Pathology Surveillance Center's (NPDPSC’s) experience using CSF real-time quaking-induced conversion (RT-QuIC) as a diagnostic test, to examine factors associated with false-negative RT-QuIC results, and to
D. Rhoads +11 more
semanticscholar +1 more source
bioRxiv, 2020 Lowering of prion protein (PrP) expression in the brain is a genetically validated therapeutic hypothesis in prion disease. We recently showed that antisense oligonucleotide (ASO)-mediated PrP suppression extends survival and delays disease onset in ...
E. Minikel +23 more
semanticscholar +1 more source
Simultaneous expression of MMB-FOXM1 complex components enables efficient bypass of senescence
Scientific Reports, 2021 Cellular senescence is a stable cell cycle arrest that normal cells undergo after a finite number of divisions, in response to a variety of intrinsic and extrinsic stimuli. Although senescence is largely established and maintained by the p53/p21WAF1/CIP1
Ruchi Kumari +7 more
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