Results 61 to 70 of about 57,548 (261)
The Molecular Pathology of Prion Diseases [PDF]
Prion diseases, or transmissible spongiform encephalopathies (TSEs), are a group of invariably fatal neurodegenerative disorders. Uniquely, they may present as sporadic, inherited, or infectious forms, all of which involve conversion of the normal ...
Herms, Jochen +2 more
core
Fibrinogen-cellular prion protein complex formation on astrocytes [PDF]
For the first time we showed that fibrinogen (Fg) can associate with cellular prion protein (PrPC) on the surface of cultured mouse brain astrocytes. At high levels, Fg causes upregulation of astrocyte PrPC and astrocyte activation accompanied with overexpression of tyrosine receptor kinase B (TrkB), which results in nitric oxide (NO) production and ...
Mariam Charkviani +3 more
openaire +2 more sources
RNF213 is characterized as a dual‐functional antiviral effector. It directly mediates the degradation of the influenza A virus nucleoprotein (NP) while simultaneously activating the MDA5‐mediated innate immune signaling pathway. This coordinated response establishes a powerful host defense system against viral infection. ABSTRACT Influenza A virus (IAV)
Haoning Li +5 more
wiley +1 more source
A Sequence-Dependent DNA Condensation Induced by Prion Protein
Different studies indicated that the prion protein induces hybridization of complementary DNA strands. Cell culture studies showed that the scrapie isoform of prion protein remained bound with the chromosome. In present work, we used an oxazole dye, YOYO,
Alakesh Bera, Sajal Biring
doaj +1 more source
This research identified cardiac amyloid pathology, neurotrophic factor depletion, and reduced myocardial nerve function in a transgenic model of cerebral amyloidosis (Tg2576), Aβ‐challenged cardiomyocytes, and in human AD heart tissue. These findings carry significant diagnostic and therapeutic implications, emphasizing the role of neuro‐signaling ...
Andrea Elia +6 more
wiley +1 more source
Helices 2 and 3 are the initiation sites in the PrPc -> PrPsc transition
It is established that prion protein is the sole causative agent in a number of diseases in humans and animals. However, the nature of conformational changes that the normal cellular form PrPC undergoes in the conversion process to a self-replicating ...
Chen, Jie, Thirumalai, Devarajan
core +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
Goold, R, McKinnon, C, Tabrizi, SJ
core +1 more source
Cellular prion protein: on the road for functions [PDF]
Cellular prion (PrPc) is a plasma membrane glycosyphosphatidylinositol‐anchored protein present in neurons but also in other cell types. Protein conservation among species suggests that PrPc may have important physiological roles. Cellular and molecular approaches have established several novel features of the regulation of PrPc expression, cellular ...
Martins, Vilma R +6 more
openaire +2 more sources
Selective Targeting of Tip Endothelial Cells as a Therapeutic Strategy for Tumor Angiogenesis
Doppel protein is selectively expressed in tip endothelial cells within the tumor vasculature, where it promotes tip cell motility and stabilizes the tip cell phenotype. Targeting Doppel with monoclonal antibodies disrupts this stabilization, impairs angiogenic sprouting, and reduces tumor angiogenesis, offering a selective and druggable switch for ...
Byoungmo Kim +16 more
wiley +1 more source
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

