Results 31 to 40 of about 92,941 (293)
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
core +2 more sources
β-Cell failure in type 2 diabetes: a case of asking too much of too few? [PDF]
, 2013 The islet in type 2 diabetes (T2DM) is characterized by a deficit in β-cells, increased β-cell apoptosis, and extracellular amyloid deposits derived from islet amyloid polypeptide (IAPP). In the absence of longitudinal studies, it is unknown if the low β-
Butler, Peter C +4 more
core +1 more source
Divergent effects of PERK and IRE1 signaling on cell viability.
PLoS ONE, 2009 Protein misfolding in the endoplasmic reticulum (ER) activates a set of intracellular signaling pathways, collectively termed the Unfolded Protein Response (UPR). UPR signaling promotes cell survival by reducing misfolded protein levels.
Jonathan H Lin +4 more
doaj +1 more source
Matrin3: Disorder and ALS Pathogenesis
Frontiers in Molecular Biosciences, 2022 Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disorder characterized by the degeneration of both upper and lower motor neurons in the brain and spinal cord.
Ahmed Salem +7 more
doaj +1 more source
Heat shock factor 1 regulates lifespan as distinct from disease onset in prion disease [PDF]
, 2008 Prion diseases are fatal, transmissible, neurodegenerative diseases caused by the misfolding of the prion protein (PrP). At present, the molecular pathways underlying prion-mediated neurotoxicity are largely unknown.
Aguzzi, Adriano +8 more
core +3 more sources
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
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 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
Prion degradation pathways: Potential for therapeutic intervention [PDF]
, 2015 Prion diseases are fatal neurodegenerative disorders. Pathology is closely linked to the misfolding of native cellular PrP(C) into the disease-associated form PrP(Sc) that accumulates in the brain as disease progresses. Although treatments have yet to be
Goold, R, McKinnon, C, Tabrizi, SJ
core +1 more source
Nanomedicine and protein misfolding diseases [PDF]
Nanomedicine: Nanotechnology, Biology and Medicine, 2005 Misfolding and self assembly of proteins in nano-aggregates of different sizes and morphologies (nano-ensembles, primarily nanofilaments and nano-rings) is a complex phenomenon that can be facilitated, impeded, or prevented, by interactions with various intracellular metabolites, intracellular nanomachines controlling protein folding and interactions ...
Alexey V, Kransnoslobodtsev +5 more
openaire +2 more sources