... by their proteolytic stability. Correspondence: Marcus Fändrich ( marcus.faendrich@uni-ulm.de ) 11 3 2021 8 4 2021 12 4 2021 © 2021 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society 2021 aggregation amyloid prion protein misfolding...

...Li-Jun Chen; Elizabeth B. Sawyer; Sarah Perrett Ure2, a regulator of nitrogen metabolism, is the protein determinant of the [ URE3 ] prion state in Saccharomyces cerevisiae . Upon conversion into the prion form, Ure2 undergoes a heritable conformational change to an amyloid-like aggregated state...

... 2010 cytoplasmic polyadenylation element-binding protein (CPEB) fragile X mental retardation protein (FMRP) prion RNA metabolism synaptic plasticity translational control Long-lasting changes in synaptic strength, usually referred to as synaptic plasticity, pertains to the ability...

..., hyperphosphorylation has been observed in prion disease. We have investigated the expression of hyperphosphorylated tau in the hippocampus of mice infected with the ME7 prion agent. In ME7-infected animals, there is a selective loss of CA1 synapse, first discernable at 13 weeks of disease. There is a potential...

...Zuzana Sisková; Nik K. Sanyal; Adam Orban; Vincent O'Connor; V. Hugh Perry Prion diseases are characteristically accompanied by extensive synaptic pathology that can occur during the preclinical phase of the disease and, in animal models, correlates with the first decline of hippocampus-dependent...

...Nigel M. Hooper; David R. Taylor; Nicole T. Watt The cellular form of the prion protein, PrP c , is critically required for the establishment of prion diseases, such as Creutzfeldt–Jakob disease. Within the N-terminal half of PrP c are four octapeptide repeats that bind Cu 2+ . Exposure of neuronal...

...-amyloid from the protein. PrP (prion protein) binds copper, and this appears to be necessary for its normal function and might also reduce its probability of conversion into an infectious prion. α-Synuclein, a protein associated with Parkinson's disease, also binds copper, but, in this case...

...Mick Tuite; Klement Stojanovski; Frederique Ness; Gloria Merritt; Nadejda Koloteva-Levine Prions represent an unusual structural form of a protein that is ‘infectious’. In mammals, prions are associated with fatal neurodegenerative diseases such as CJD (Creutzfeldt–Jakob disease), while in fungi...

...F. Wiseman; E. Cancellotti; J. Manson The TSEs (transmissible spongiform encephalopathies) are not only devastating neurological diseases but also provide a biochemical conundrum; how can a disease agent replicate in the apparent absence of genetic material? The prion hypothesis proposes...

...J. Hardy Loci underlying autosomal dominant forms of most neurodegenerative disease have been identified: prion mutations cause Gerstmann Straussler syndrome and hereditary Creutzfeldt–Jakob disease, tau mutations cause autosomal dominant frontal temporal dementia and α-synuclein mutations cause...

...B.J. Tabner; S. Turnbull; N.J. Fullwood; M. German; D. Allsop By means of an ESR spin-trapping method, we have shown that Aβ (amyloid β), α-synuclein and various toxic forms of the prion protein all appear to generate H 2 O 2 in vitro . A fundamental molecular mechanism underlying the pathogenesis...

...D. R. Brown Transmissible spongiform encephalopathies are diseases of animals and humans that are also termed prion diseases. These diseases are linked together because a normal brain glycoprotein termed the prion protein is converted to a readily detectable protease-resistant isoform. There is now...

... with these complexes, modulating the activity of this efficient and spatially restricted proteolytic system. Recent observations demonstrate that certain forms of the prion protein can stimulate tissue plasminogen activator-catalysed plasminogen activation, which raises the possibility that these proteases may also...