Results 51 to 60 of about 57,548 (261)
Copper Binding Regulates Cellular Prion Protein Function
Molecular Neurobiology, 2018 The cellular prion protein (PrP C ), mainly known for its role in neurodegenerative diseases, is involved in several physiological processes including neuritogenesis. By combining genomic approaches, cellular assays and focal stimulation technique, we have explored the molecular mechanism ...
Nguyen, Xuan T. A. +3 more
openaire +3 more sources
Molecular Dynamics Studies on 3D Structures of the Hydrophobic Region PrP(109-136) [PDF]
, 2013 Prion diseases caused by the conversion from a soluble normal cellular prion protein into insoluble abnormally folded infectious prions, are invariably fatal and highly infectious degenerative diseases that affect a wide variety of mammalian species. The
Zhang, Jiapu, Zhang, Yuanli
core +4 more sources
PLoS Genetics, 2015 The role of Hsp70 chaperones in yeast prion propagation is well established. Highly conserved Hsp90 chaperones participate in a number of cellular processes, such as client protein maturation, protein degradation, cellular signalling and apoptosis, but ...
Navinder Kumar +4 more
doaj +1 more source
Evolutionary descent of prion genes from a ZIP metal ion transport ancestor [PDF]
, 2009 In the more than 20 years since its discovery, both the phylogenetic origin and cellular function of the prion protein (PrP) have remained enigmatic.
David Westaway +4 more
core +1 more source
Amyloidogenic Peptide Fragments Designed From Bacterial Collagen‐like Proteins Form Hydrogel
Advanced Functional Materials, EarlyView.This study identified amyloidogenic sequence motifs in bacterial collagen‐like proteins and exploited these to design peptides that self‐assemble into β‐sheet fibers and form hydrogels. One hydrogel supported healthy fibroblast growth, showing promise for biocompatible materials. Our work demonstrates that bacterial sequences can be harnessed to create
Vamika Sagar +5 more
wiley +1 more source
Synthesis and anti-prion aggregation activity of acylthiosemicarbazide analogues
Journal of Enzyme Inhibition and Medicinal Chemistry, 2023 Prions are infectious protein particles known to cause prion diseases. The biochemical entity of the pathogen is the misfolded prion protein (PrPSc) that forms insoluble amyloids to impair brain function. PrPSc interacts with the non-pathogenic, cellular
Dong Hwan Kim +16 more
doaj +1 more source
Prion-induced neurotoxicity: Possible role for cell cycle activity and DNA damage response. [PDF]
, 2015 Protein misfolding neurodegenerative diseases arise through neurotoxicity induced by aggregation of host proteins. These conditions include Alzheimer's disease, Huntington's disease, Parkinson's disease, motor neuron disease, tauopathies and prion ...
core +1 more source
A novel, resistance-linked ovine PrP variant and its equivalent mouse variant modulate the in vitro cell-free conversion of rPrP to PrPres [PDF]
, 2006 Prion diseases are associated with the conversion of the normal cellular prion protein, PrPc, to the abnormal, disease-associated form, PrPSc. This conversion can be mimicked in vitro by using a cell-free conversion assay. It has recently been shown that
Gill, Andrew C. +4 more
core +1 more source
Advanced Healthcare Materials, EarlyView.Cerebral organoids are transforming brain research, yet the field remains fragmented. This comprehensive systematic review maps 738 studies published between 2014 and 2024 to uncover trends, gaps, and opportunities across neuroscience. Introducing OrganoidMap—an interactive, open‐access platform to explore and compare models—this work enables ...
Anna Wolfram +10 more
wiley +1 more source
Thermodynamic Stabilization of the Folded Domain of Prion Protein Inhibits Prion Infection in Vivo
Cell Reports, 2013 Prion diseases, or transmissible spongiform encephalopathies (TSEs), are associated with the conformational conversion of the cellular prion protein, PrPC, into a protease-resistant form, PrPSc.
Qingzhong Kong +12 more
doaj +1 more source