Results 21 to 30 of about 36,884 (188)
Neural Regeneration Research, 2021 The baker’s yeast Saccharomyces (S.) cerevisiae is a single-celled eukaryotic model organism widely used in research on life sciences. Being a unicellular organism, S. cerevisiae has some evident limitations in application to neuroscience. However, yeast
Takao Ishikawa
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Spreading of a prion domain from cell-to-cell by vesicular transport in Caenorhabditis elegans. [PDF]
PLoS Genetics, 2013 Prion proteins can adopt self-propagating alternative conformations that account for the infectious nature of transmissible spongiform encephalopathies (TSEs) and the epigenetic inheritance of certain traits in yeast.
Carmen I Nussbaum-Krammer +4 more
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Frontiers in Aging Neuroscience, 2018 Prion diseases are fatal neurological disorders affecting various mammalian species including humans. Lack of proper diagnostic tools and non-availability of therapeutic remedies are hindering the control strategies for prion diseases. MicroRNAs (miRNAs)
Syed Zahid Ali Shah +4 more
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Dissection and design of yeast prions. [PDF]
PLoS Biology, 2004 Many proteins can misfold into beta-sheet-rich, self-seeding polymers (amyloids). Prions are exceptional among such aggregates in that they are also infectious.
Lev Z Osherovich +3 more
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Viruses, 2014 The key event in prion pathogenesis is the structural conversion of the normal cellular protein, PrPC, into an aberrant and partially proteinase K resistant isoform, PrPSc.
Evgenia Salta +5 more
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Hsp40/JDP Requirements for the Propagation of Synthetic Yeast Prions
Viruses, 2022 Yeast prions are protein-based transmissible elements, most of which are amyloids. The chaperone protein network in yeast is inexorably linked to the spreading of prions during cell division by fragmentation of amyloid prion aggregates. Specifically, the
Sarah C. Miller +5 more
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Prion, 2019 A number of fungal proteins are capable of adopting multiple alternative, self-perpetuating prion conformations. These prion variants are associated with functional alterations of the prion-forming protein and thus the generation of new, heritable traits
Ben Allwein +4 more
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AMYCO: evaluation of mutational impact on prion-like proteins aggregation propensity
BMC Bioinformatics, 2019 Background Around 1% of human proteins are predicted to contain a disordered and low complexity prion-like domain (PrLD). Mutations in PrLDs have been shown promote a transition towards an aggregation-prone state in several diseases. Results Recently, we
Valentin Iglesias +3 more
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Computational Analysis of Candidate Prion-Like Proteins in Bacteria and Their Role
Frontiers in Microbiology, 2015 Prion proteins were initially associated with diseases such as Creutzfeldt Jakob and transmissible spongiform encephalopathies. However, deeper research revealed them as versatile tools, exploited by the cells to execute fascinating functions, acting as ...
Valentin eIglesias +2 more
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Evolutionary descent of prion genes from the ZIP family of metal ion transporters. [PDF]
PLoS ONE, 2009 In the more than twenty years since its discovery, both the phylogenetic origin and cellular function of the prion protein (PrP) have remained enigmatic.
Gerold Schmitt-Ulms +4 more
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