MARK4 enhances stress granule formation under oxidative stress and increases tau accumulation
MARK4 (red dots) localizes to stress granules (orange dots) and promotes their formation under oxidative stress by modulating TIA1 (blue dots). MARK4 and TIA1 synergistically increase tau (purple) accumulation, and the reduction of the TIA1 ortholog suppresses neurodegeneration in a fly model.
Sho Nakajima +8 more
wiley +1 more source
Aspects of prion protein dynamics in cell culture models. [PDF]
The cell biology of Prion formation and transfer is not well understood. In order to further elucidate the dynamics of PrPc and PrPsc in a cellular context, fusions between Green Fluorescent Protein (GFP) and PrP were constructed and infected/uninfected ...
Landy, Timothy Adam, Landy, T.A.
core
ABSTRACT Objective To characterize the demographic, clinical, and laboratory features of the Chinese patients of genetic Creutzfeldt‐Jakob disease with T188K variant (T188K‐gCJD), the most common subtype of genetic prion diseases (gPrDs) in China. Methods In this nationwide retrospective study, data from 98 genetically confirmed T188K‐gCJD patients ...
Chun‐Jie Li +11 more
wiley +1 more source
Effect of enzymatic deimination on the conformation of recombinant prion protein [PDF]
Deimination is the post-translational conversion of arginine residues to citrulline. It has been implicated as a causative factor in autoimmune diseases such as multiple sclerosis and rheumatoid arthritis and more recently, as a marker of ...
Oxley, David +6 more
core
Characterizing Cutaneous α‐Synuclein Deposition and Seeding Activity in Parkinson's Disease Subtypes
ABSTRACT Objective Cutaneous phosphorylated α‐synuclein (p‐syn) and α‐synuclein seeding activity are promising biomarkers for Parkinson's disease (PD), but their clinical value remains uncertain due to disease heterogeneity. This study evaluates these two biomarkers in PD patients to inform phenotype‐specific diagnosis and disease severity assessment ...
Yuting Jin +8 more
wiley +1 more source
Prion degradation pathways: Potential for therapeutic intervention [PDF]
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
McKinnon, C, Tabrizi, SJ, Goold, R
core
Raman optical activity demonstrates poly(L-proline) II helix in the N-terminal region of the ovine prion protein: Implications for function and misfunction [PDF]
The aqueous solution structure of the full-length recombinant ovine prion protein PrP25-233, together with that of the N-terminal truncated version PrP94-233, have been studied using vibrational Raman optical activity (ROA) and ultraviolet circular ...
Rhie, A G O +18 more
core +1 more source
High‐resolution proton detection is preserved under cryogenic dynamic nuclear polarization (DNP) by combining fast MAS, extensive deuteration and selective methyl protonation. This strategy enables proton‐detected structural studies of biomolecular solids with enhanced sensitivity under DNP conditions.
James Tolchard +16 more
wiley +2 more sources
Prion protein inhibits fast axonal transport through a mechanism involving casein kinase 2. [PDF]
Prion diseases include a number of progressive neuropathies involving conformational changes in cellular prion protein (PrPc) that may be fatal sporadic, familial or infectious.
Emiliano Zamponi +13 more
doaj +1 more source
Structural Polymorphism of polyG Inclusions Revealed by In Situ Cryo‐Electron Tomography
Correlative cryo‐electron tomography in primary cortical neurons and NIID mouse brain tissue reveals that polyG inclusions are interconnected ribbon‐like assemblies rather than canonical amyloid fibrils. Multiple compartment‐specific ribbon states show distinct 26S proteasome accessibility, while cytoplasmic ribbons contact and deform ER‐like ...
Yunwen Qian +12 more
wiley +1 more source

