Recent High-Resolution Structures of Amyloids Involved in Neurodegenerative Diseases
Frontiers in Aging Neuroscience, 2021 Amyloids are highly ordered aggregates composed of proteins or peptides. They are involved in several pathologies, including hallmark neurodegenerative disorders such as Alzheimer’s (AD) and Parkinson’s (PD).
Rodrigo Diaz-Espinoza
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Molecular dynamics as an approach to study prion protein misfolding and the effect of pathogenic mutations [PDF]
, 2011 Computer simulation of protein dynamics offers unique high-resolution information that complements experiment. Using experimentally derived structures of the natively folded prion protein (PrP), physically realistic dynamics and conformational changes ...
Daggett, Valerie, van der Kamp, Marc W
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Biomolecular condensate phase diagrams with a combinatorial microdroplet platform
Nature Communications, 2022 A central concept for characterising phase-separating systems is the phase diagram but generation of such diagrams for biomolecular systems is typically slow and low-throughput.
William E. Arter +16 more
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Force-induced misfolding in RNA [PDF]
, 2009 RNA folding is a kinetic process governed by the competition of a large number of structures stabilized by the transient formation of base pairs that may induce complex folding pathways and the formation of misfolded structures. Despite of its importance
D. Herschlag +5 more
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Synthetic biology tools to promote the folding and function of RNA aptamers in mammalian cells
RNA Biology, 2023 RNA aptamers are structured RNAs that can bind to diverse ligands, including proteins, metabolites, and other small molecules. RNA aptamers are widely used as in vitro affinity reagents.
Qian Hou, Samie R. Jaffrey
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The Transthyretin/Oleuropein Aglycone Complex: A New Tool against TTR Amyloidosis
Pharmaceuticals, 2022 The release of monomers from the homotetrameric protein transthyretin (TTR) is the first event of a cascade, eventually leading to sporadic or familial TTR amyloidoses.
Francesco Bemporad +4 more
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Structural Specificity of Polymorphic Forms of α-Synuclein Amyloid
Biomedicines, 2023 The structural transformation producing amyloids is a phenomenon that sheds new light on the protein folding problem. The analysis of the polymorphic structures of the α-synuclein amyloid available in the PDB database allows analysis of the amyloid ...
Irena Roterman +2 more
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All-atom simulations reveal how single point mutations promote serpin misfolding
, 2018 Protein misfolding is implicated in many diseases, including the serpinopathies. For the canonical inhibitory serpin {\alpha}1-antitrypsin (A1AT), mutations can result in protein deficiencies leading to lung disease, and misfolded mutants can accumulate ...
Beccara, Silvio a +7 more
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Recombinant Mammalian Prions: The “Correctly” Misfolded Prion Protein Conformers
Viruses, 2022 Generating a prion with exogenously produced recombinant prion protein is widely accepted as the ultimate proof of the prion hypothesis. Over the years, a plethora of misfolded recPrP conformers have been generated, but despite their seeding capability ...
Jiyan Ma, Jingjing Zhang, Runchuan Yan
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Missense mutations in the perforin (PRF1) gene as a cause of hereditary cancer predisposition [PDF]
, 2016 Perforin, a pore-forming toxin released from secretory granules of NK cells and CTLs, is essential for their cytotoxic activity against infected or cancerous target cells.
Chaudhry, MS +7 more
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