Results 31 to 40 of about 92,071 (194)
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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Stress and viral insults do not trigger E200K PrP conversion in human cerebral organoids.
PLoS ONE, 2022 Prion diseases are a group of rare, transmissible, and invariably fatal neurodegenerative diseases that affect both humans and animals. The cause of these diseases is misfolding of the prion protein into pathological isoforms called prions.
Anna Smith +9 more
doaj +1 more source
Protein Misfolding Diseases [PDF]
The Open Biology Journal, 2009 Diseases caused by protein misfolding are an emerging pathologic category that are thought to share some basic common mechanisms and display impressive heterogeneity in terms of tissue involvement, age of onset and clinical features. The growing recognition of the impact that protein misfolding has on human diseases is certainly related to the ...
Vittorio Bellotti, Monica Stoppini
openaire +1 more source
Protein misfolding and cellular stress in disease and ageing - Concepts and protocols
European Journal of Histochemistry, 2011 To those readers that already got the Protein misfolding and disease volume, this new title can sound as an update or a second edition of the previous volume: well, this is not the case.
Carlo Alberto Redi
doaj +1 more source
Scientific Reports, 2021 Misfolding of the cellular prion protein, PrPC, into the amyloidogenic isoform, PrPSc, which forms infectious protein aggregates, the so-called prions, is a key pathogenic event in prion diseases.
Hideyuki Hara +6 more
doaj +1 more source
Progress in spondylarthritis immunopathogenesis of spondyloarthritis: which cells drive disease? [PDF]
, 2009 Spondyloarthritides, or SpA, form a cluster of chronic inflammatory diseases with the axial skeleton as the most typical disease localisation, although extra-articular manifestations such as intestinal inflammation may frequently occur during the course ...
Melis, Lode, Elewaut, Dirk
core +2 more sources
Prion protein misfolding and disease [PDF]
Current Opinion in Structural Biology, 2009 Transmissible spongiform encephalopathies (TSEs or prion diseases) are a rare group of invariably fatal neurodegenerative disorders that affect humans and other mammals. TSEs are protein misfolding diseases that involve the accumulation of an abnormally aggregated form of the normal host prion protein (PrP).
Roger A, Moore +2 more
openaire +2 more sources
Different outcome of sarcoglycan missense mutation between human and mouse [PDF]
, 2018 Sarcoglycanopathies are rare autosomic limb girdle muscular dystrophies caused by mutations in one of the genes coding for sarcoglycan (α, β, δ, and γ-sarcoglycans).
Bourg, Nathalie +6 more
core +5 more sources
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
core +1 more source
Bridging the gap: From protein misfolding to protein misfolding diseases
FEBS Letters, 2009 Protein misfolding and aggregation are pathognomic for a number of the most common age‐related degenerative diseases. Great progress has been made in studying protein aggregation in the test tube and also in replicating protein aggregation in vertebrate animal models of these diseases.
Luheshi, Leila M. +1 more
openaire +2 more sources