Results 61 to 70 of about 95,914 (208)
Protein folding disorders: Toward a basic biological paradigm [PDF]
, 2010 Mechanistic 'physics' models of protein folding fail to account for the observed spectrum of protein folding and aggregation disorders, suggesting that a more appropriately biological paradigm will be needed for understanding the etiology ...
Rodrick Wallace
core +3 more sources
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
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Molecular Systems BiologyAlzheimer’s disease is characterized by the aggregation of the Aβ peptide into amyloid fibrils. According to the amyloid hypothesis, pharmacologically targeting Aβ aggregation could result in disease-modifying treatments. The identification of inhibitors
Michaela Brezinova +8 more
doaj +1 more source
Protein evolution speed depends on its stability and abundance and on chaperone concentrations. [PDF]
, 2018 Proteins evolve at different rates. What drives the speed of protein sequence changes? Two main factors are a protein's folding stability and aggregation propensity. By combining the hydrophobic-polar (HP) model with the Zwanzig-Szabo-Bagchi rate theory,
Agozzino, Luca, Dill, Ken A
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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
α-Synuclein oligomers form by secondary nucleation
Nature CommunicationsOligomeric species arising during the aggregation of α-synuclein are implicated as a major source of toxicity in Parkinson’s disease, and thus a major potential drug target.
Catherine K. Xu +14 more
doaj +1 more source
Without magic bullets: the biological basis for public health interventions against protein folding disorders [PDF]
, 2010 Protein folding disorders of aging like Alzheimer's and Parkinson's diseases currently present intractable medical challenges. 'Small molecule' interventions - drug treatments - often have, at best, palliative impact, failing to alter
Rodrick Wallace
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
Sequence-based virtual screening using transformers
Nature CommunicationsProtein-ligand interactions play central roles in myriad biological processes and are of key importance in drug design. Deep learning approaches are becoming cost-effective alternatives to high-throughput experimental methods for ligand identification ...
Shengyu Zhang +6 more
doaj +1 more source
Extragenic Suppression analysis of TS mutations using Sec61p [PDF]
, 2007 During synthesis, secretory and membrane proteins are cotranslationally translocated into the lumen of the endoplasmic reticulum through an aqueous gated channel.
Sterling Smith
core +2 more sources