Results 101 to 110 of about 3,400,014 (272)
The prion protein (PrP) plays an essential role in the pathogenesis of a group of sporadic, genetically determined and infectious fatal degenerative diseases, referred to as “prion diseases”, affecting the central nervous system of humans and other mammals. The cellular PrP is encoded by a single copy gene, highly conserved across mammalian species. In
B, Ghetti +9 more
openaire +2 more sources
Prion Protein in Glioblastoma Multiforme [PDF]
The cellular prion protein (PrPc) is an evolutionarily conserved cell surface protein encoded by the PRNP gene. PrPc is ubiquitously expressed within nearly all mammalian cells, though most abundantly within the CNS. Besides being implicated in the pathogenesis and transmission of prion diseases, recent studies have demonstrated that PrPc contributes ...
Larisa Ryskalin +6 more
openaire +2 more sources
Prion propagation can occur in a prokaryote and requires the ClpB chaperone
Prions are self-propagating protein aggregates that are characteristically transmissible. In mammals, the PrP protein can form a prion that causes the fatal transmissible spongiform encephalopathies.
Andy H Yuan +3 more
doaj +1 more source
Prion‐Like Protein LENG8‐Mediated Nucleation Drives Stress Granule Assembly
LENG8 is a newly identified stress granule (SG) nucleator required for SG assembly. Following stress, nuclear LENG8 granules disassemble, allowing LENG8 to translocate into the cytoplasm and form independent nucleation foci. These foci fuse with canonical early G3BP1/TIA1 seeds via LENG8‐TIA1 binding to drive SG maturation.
Mingxing Zhang +6 more
wiley +1 more source
Endogenous Viral Etiology of Prion Diseases [PDF]
Transmissible spongiform encephalopathies (TSEs), or prion diseases, are a group of incurable neurodegenerative disorders, including Kuru and Creutzfeldt-Jakob disease in humans, “mad cow” disease in cattle, and scrapie in sheep. This paper
Claudiu I. Bandea
core
The Prion-like domain in the exomer-dependent cargo Pin2 serves as a trans-Golgi retention motif [PDF]
Prion and prion-like domains (PLDs) are found in many proteins throughout the animal kingdom. We found that the PLD in the S. cerevisiae exomer-depen- dent cargo protein Pin2 is involved in the regulation of protein transport and localization. The domain
Ritz, Alicja M. +11 more
core +1 more source
Objective Amyotrophic lateral sclerosis (ALS) has a markedly distinctive clinical and neuroradiological signature, with the preferential involvement of specific brain networks and the apparent sparing of others. The molecular underpinnings of the strikingly selective anatomical vulnerability have not been fully elucidated to date despite the potential ...
Marlene Tahedl +10 more
wiley +1 more source
Carrion ecology: concepts, interdisciplinary synthesis, and perspectives
ABSTRACT Carrion is a ubiquitous resource in both terrestrial and aquatic ecosystems, yet it has long been overlooked in ecological research. Over the past two decades, studies on carrion and the many organisms that exploit it have flourished, revealing not only wide‐ranging ecological functions but also significance far beyond ecology.
Marcos Moleón +38 more
wiley +1 more source
DNA Nanotechnology Meets Peptide and Protein Self‐Assembly
Combining DNA nanotechnology with peptide and protein assembly provides complementary platforms for the rational engineering of functional biomaterials. This Perspective discusses the emerging field of self‐assembling DNA‐peptide and DNA‐protein hybrid systems that combine the structural precision and programmability of DNA nanotechnology with the ...
Marcel Hanke +4 more
wiley +1 more source
Bovine spongiform encephalopathy (BSE) and BSE-related disorders have been associated with a single major prion strain. Recently, 2 atypical, presumably sporadic forms of BSE have been associated with 2 distinct prion strains that are characterized ...
Juan-María Torres +7 more
doaj +1 more source

