Results 31 to 40 of about 6,771,465 (361)
Octarepeat region flexibility impacts prion function, endoproteolysis and disease manifestation
EMBO Molecular Medicine, 2015 The cellular prion protein (PrPC) comprises a natively unstructured N‐terminal domain, including a metal‐binding octarepeat region (OR) and a linker, followed by a C‐terminal domain that misfolds to form PrPSc in Creutzfeldt‐Jakob disease.
Agnes Lau +19 more
doaj +1 more source
Movement of Chronic Wasting Disease Prions in Prairie, Boreal and Alpine Soils
Pathogens, 2023 Chronic wasting disease (CWD) is a transmissible spongiform encephalopathy negatively impacting cervids on three continents. Soil can serve as a reservoir for horizontal transmission of CWD by interaction with the infectious prion protein (PrPCWD) shed ...
Alsu Kuznetsova +4 more
doaj +1 more source
Intrinsic protein disorder and conditional folding in AlphaFoldDB
Protein Science, 2022 Intrinsically disordered regions (IDRs) defying the traditional protein structure–function paradigm have been difficult to analyze. The availability of accurate structure predictions on a large scale in AlphaFoldDB offers a fresh perspective on IDR ...
Damiano Piovesan +2 more
semanticscholar +1 more source
Frontiers in Neuroscience, 2015 Organotypic cerebellar slices represent a suitable model for characterizing and manipulating prion replication in complex cell environments. Organotypic slices recapitulate prion pathology and are amenable to drug testing in the absence of a blood-brain ...
Hanna eWolf +7 more
doaj +1 more source
Cold Spring Harbor Perspectives in Biology, 2019 Most of the secreted and plasma membrane proteins are synthesized on membrane-bound ribosomes on the endoplasmic reticulum (ER). They require engagement of ER-resident chaperones and foldases that assist in their folding and maturation.
G. E. Karagöz +2 more
semanticscholar +1 more source
Funnels, pathways, and the energy landscape of protein folding: A synthesis [PDF]
Proteins: Structure, Function, and Bioinformatics, 1994 The understanding, and even the description of protein folding is impeded by the complexity of the process. Much of this complexity can be described and understood by taking a statistical approach to the energetics of protein conformation, that is, to ...
J. Bryngelson +3 more
semanticscholar +1 more source
Progress in Nuclear Magnetic Resonance Spectroscopy, 2017 Protein folding is a highly complex process proceeding through a number of disordered and partially folded nonnative states with various degrees of structural organization. These transiently and sparsely populated species on the protein folding energy landscape play crucial roles in driving folding toward the native conformation, yet some of these ...
Zhuravleva, A, Korzhnev, DM
openaire +3 more sources
Biomolecules, 2020 Prion diseases are fatal, transmissible neurodegenerative disorders whose pathogenesis is driven by the misfolding, self-templating and cell-to-cell spread of the prion protein.
Hailey Pineau, Valerie Sim
doaj +1 more source
Sheep scrapie and deer rabies in England prior to 1800
Prion, 2023 Eighteenth-century England witnessed the emergence of two neurological diseases in animals. Scrapie, a transmissible spongiform encephalopathy, is a fatal neurodegenerative disease of sheep and goats that appears in classical and atypical forms.
Anthony Ness +2 more
doaj +1 more source
Folding nuclei in proteins [PDF]
FEBS Letters, 2001 When a protein folds or unfolds, it passes through many half‐folded microstates. Only a few of them can accumulate and be seen experimentally, and this happens only when the folding (or unfolding) occurs far from the point of thermodynamic equilibrium between the native and denatured states.
Galzitskaya, Oxana V +2 more
openaire +2 more sources