Results 51 to 60 of about 92,941 (293)

AAA+ protein unfoldases—the Moirai of the proteome

FEBS Letters, EarlyView.
AAA+ unfoldases are essential molecular motors that power protein degradation and disaggregation. This review integrates recent cryo‐electron microscopy (cryo‐EM) structures and single‐molecule biophysical data to reconcile competing models of substrate translocation.
Stavros Azinas, Marta Carroni
wiley   +1 more source

Protein aggregation in progressive myoclonus epilepsies and related syndromes [PDF]

Exploration of Neuroscience
For this review paper, data on protein misfolding and aggregation in progressive myoclonus epilepsies and some developmental encephalopathies are gathered.
Eva Žerovnik
doaj   +1 more source

Methionine 129 variant of human prion protein oligomerizes more rapidly than the valine 129 variant - Implications for disease susceptibility to Creutzfeldt-Jakob disease [PDF]

, 2004
The human PrP gene (PRNP) has two common alleles that encode either methionine or valine at codon 129. This polymorphism modulates disease susceptibility and phenotype of human transmissible spongiform encyphalopathies, but the molecular mechanism by ...
Abdessamad Tahiri-Alaoui, Andrew C. Gill, Petra Disterer, William James, Prusiner, Weissmann, Will, Bruce, Hill, Prusiner, Prusiner, Collinge, Windl, Palmer, Brown, Baker, Cervenakova, Parchi, Hill, Collinge, Hauw, Goldfarb, Goldfarb, Dlouhy, Dermaut, Croes, Liemann, Riek, Alonso, Baskakov, Jackson, Baskakov, Gill, Lu, Lu, Landon, Safar, Bessen, Zahn, Riek, Nguyen, Tahiri-Alaoui, Santini, Wong, Wildegger, Matouschek, Vendruscolo, Kim, Fasman, Baskakov, Qin, Oesch, Conway, Sayer, Rhie, Schatzl, Mead   +56 more
core   +1 more source

Differential regulation of ZFAS1 splice variants by endoplasmic reticulum stress in hepatocyte cell lines

FEBS Open Bio, EarlyView.
ZFAS1 is a lncRNA promoting cell proliferation and migration, exhibiting high expression in various cancers. It is conserved, widely expressed, and produces multiple splice variants with unclear roles. We identified several splice variants in hepatocyte models, and found that inhibiting or suppressing regulators of the unfolded protein response (PERK ...
Sébastien Soubeyrand, Paulina Lau, Ruth McPherson   +2 more
wiley   +1 more source

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

Large‐scale bidirectional arrayed genetic screens identify OXR1 and EMC4 as modifiers of αSynuclein aggregation

FEBS Open Bio, EarlyView.
Activation of the mitochondrial protein OXR1 increases pSyn129 αSynuclein aggregation by lowering ATP levels and altering mitochondrial membrane potential, particularly in response to MSA‐derived fibrils. In contrast, ablation of the ER protein EMC4 enhances autophagic flux and lysosomal clearance, broadly reducing α‐synuclein aggregates.
Sandesh Neupane, Lea Nikolić, Lorenzo Maraio, Thomas Goiran, Nathan Karpilovsky, Stefano Sellitto, Vangelis Bouris, Jiang‐An Yin, Ronald Melki, Edward A Fon, Adriano Aguzzi, Elena De Cecco   +11 more
wiley   +1 more source

Effect of primary structural variation on cervid prion protein in flexibility, stability, and spontaneous misfolding propensity

Neurobiology of Disease
Protein misfolding is central to numerous neurodegenerative disorders, collectively known as proteinopathies, which include Alzheimer's disease, Parkinson's disease, and prion diseases, among others.
Carlos M. Díaz-Domínguez, Hasier Eraña, Francesca Peccati, Enric Vidal, Jorge M. Charco, Cristina Sampedro-Torres-Quevedo, Miguel A. Pérez-Castro, Nuria L. Lorenzo, Samanta Giler, Glenn C. Telling, Mariví Geijo, Jesús R. Requena, Gonzalo Jiménez-Osés, Joaquín Castilla   +13 more
doaj   +1 more source

The potential role of dietary polyphenols in Parkinson’s disease [PDF]

, 2011
Cumulative evidence now suggests that the abnormal aggregation of the neuronal protein alpha-synuclein is critically involved in the pathogenesis of synucleinopathies, of which Parkinson’s disease (PD) is the most prevalent. Development of neuropathology
Caruana, Mario, Vassallo, Neville
core  

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

Misfolded Proteins and Retinal Dystrophies [PDF]

, 2009
Many mutations associated with retinal degeneration lead to the production of misfolded proteins by cells of the retina. Emerging evidence suggests that these abnormal proteins cause cell death by activating the Unfolded Protein Response, a set of conserved intracellular signaling pathways that detect protein misfolding within the endoplasmic reticulum
Jonathan H, Lin, Matthew M, Lavail
openaire   +2 more sources