Month: September 2022

PRION FITNESS. "The evolution and adaption of human prions is enabled by a dynamic collection of distinct populations of particles, whose evolution is governed by the selection of progressively less stable, faster replicating PrP(Sc) conformers." https://lnkd.in/eE_2Z_t View in LinkedIn

DARWINIAN EVOLUTION of prions in culture showing mutation and selection, albeit without having DNA. Competition between differently adapted prion populations. https://lnkd.in/ek8f7jH View in LinkedIn

STRUCTURAL FORMS. "The prion protein displays a unique structural ambiguity in that it can adopt multiple stable conformations under physiological conditions. In our view, this puzzling feature resulted from a sudden environmental change in evolution when the prion, previously an integral membrane protein, got expelled into the extracellular space." https://lnkd.in/ec4HvKS View in LinkedIn

MOLECULAR BIOLOGY OF PRIONS. "Most proteins do not act in isolation but partner with other proteins to exert their biological roles. Thus, the function of a protein can sometimes be deduced by characterizing its binding partners. Following this ‘guilt-by-association’ logic, we set out to identify the function of the cellular prion protein through a comprehensive interactome investigation." https://lnkd.in/eZjPby9 View in LinkedIn

HOMOLOGIES from "bioinformatic analysis revealed the unexpected presence of a PrP-like amino acid sequence within the N-terminal, extracellular domain of a distinct sub-branch of the ZIP protein family that includes ZIP5, ZIP6 and ZIP10. Additional structural threading and orthologous sequence alignment analyses argued that the prion gene family is phylogenetically derived from a ZIP-like ancestral molecule." https://lnkd.in/eZjPby9 View in LinkedIn

PRION ORIGINS. "This finding provides a rationale for structural and biological features within modern-day prion proteins as remnants of an ancient involvement in the sensing and/or import of metal ions from the extracellular milieu." https://lnkd.in/eZjPby9 View in LinkedIn

JUNK HABITS of humans in space. "Millions of pieces of junk orbiting Earth." https://lnkd.in/e4vyWBE View in LinkedIn

"PRION DISEASES are devastating neurological disorders caused by the propagation of particles containing an alternative β−sheet-rich form of the prion protein (PrP). Genes paralogous to PrP, called Doppel and Shadoo, have been identified, that also have neuropathological relevance. PrP is highly conserved across mammals, typically with > 50% sequence identity relative to human." https://lnkd.in/e8tmC2k View in LinkedIn

PROTEIN MISFOLDING DISEASES. "The misfolding and aggregation of specific proteins is a common hallmark of many neurodegenerative disorders, including highly prevalent illnesses such as Alzheimer’s and Parkinson’s diseases, as well as rarer disorders such as Huntington’s and prion diseases. Among these, only prion diseases are ‘infectious’." https://lnkd.in/eZzxrZc View in LinkedIn

SEQUENCE COMPARISONS. "Many residues and regions in the prion protein have been implicated in functioning, pathogenicity, and species barrier. Sequence comparison of mammalian prion proteins may help to evaluate such proposals and gain insight in the molecular evolution of PrP...it is now possible to better reconstruct the molecular evolution of the mammalian prion." https://lnkd.in/eMKg3pR View in LinkedIn