Results 91 to 100 of about 5,604,422 (355)
Cellular Prion Protein Mediates Impairment of Synaptic Plasticity by Amyloid-β Oligomers
Nature, 2009 A pathological hallmark of Alzheimer’s disease is an accumulation of insoluble plaque containing the amyloid-β peptide of 40–42 amino acid residues. Prefibrillar, soluble oligomers of amyloid-β have been recognized to be early and key intermediates in ...
J. Laurén +4 more
semanticscholar +1 more source
2.7 Å cryo-EM structure of ex vivo RML prion fibrils
Nature Communications, 2021 Mammalian prions propagate as distinct strains and are composed of multichain assemblies of misfolded host-encoded prion protein (PrP). Here, we present a near-atomic resolution cryo-EM structure of PrP fibrils present in highly infectious prion rod ...
S. Manka +7 more
semanticscholar +1 more source
Advances in Single‐Cell Sequencing for Infectious Diseases: Progress and Perspectives
Advanced Science, EarlyView.Single‐cell sequencing technologies uncover novel, unknown, and emergent features of many diseases. This review describes recent progress of single‐cell sequencing technologies and their applications in infectious diseases, summarizes the underlying commonalities of different infections and discusses future research directions, facilitating the ...
Mengyuan Lyu +13 more
wiley +1 more source
Frontiers in BioinformaticsThe Prion protein is the molecular hallmark of the incurable prion diseases affecting mammals, including humans. The protein-only hypothesis states that the misfolding, accumulation, and deposition of the Prion protein play a critical role in toxicity ...
Patricia Soto +7 more
doaj +1 more source
Astrocyte in prion disease: a double-edged sword
Neural Regeneration Research, 2022 Prion diseases are infectious protein misfolding disorders of the central nervous system that result from misfolding of the cellular prion protein (PrPC) into the pathologic isoform PrPSc.
Waqas Tahir +2 more
doaj +1 more source
The structure of the infectious prion protein
Prion, 2014 The structures of the infectious prion protein, PrPSc, and that of its proteolytically truncated variant, PrP 27–30, have evaded experimental determination due to their insolubility and propensity to aggregate.
J. Requena, H. Wille
semanticscholar +1 more source
Single‐Cell RNA Sequencing Delineates Renal Anti‐Fibrotic Mechanisms Mediated by TRPC6 Inhibition
Advanced Science, EarlyView.Single‐cell transcriptomics reveals how TRPC6 inhibition alters renal cell composition and gene expression in CKD. The study uncovers a novel endothelial subpopulation (ECRIN), highlights key inflammatory and fibrotic pathways, and identifies a Prnp‐driven network linked to fibrosis resolution, offering mechanistic insight into TRPC6 as a potential ...
Yao Xu +12 more
wiley +1 more source
A Review on the Salt Bridge Between ASP177 and ARG163 of Wild-Type Rabbit Prion Protein
, 2015 Prion diseases are invariably fatal and highly infectious neurodegenerative diseases that affect a wide variety of mammalian species such as sheep and goats, cattle, deer, elks, humans and mice etc., but rabbits have a low susceptibility to be infected ...
Wang, Feng, Zhang, Jiapu
core +2 more sources
Advanced Science, EarlyView.Polyglutamine (polyQ) tract expansion (≥ 36 amino acids) within the N‐terminal region of the Huntingtin protein (Httex1) causes Huntington's disease (HD), for which the underlying causes are not well‐understood. The authors performed computer simulations to understand the cause of HD at the molecular level.
Priyesh Mohanty +2 more
wiley +1 more source
Multifaceted role of sialylation in prion diseases
Frontiers in Neuroscience, 2016 Mammalian prion or PrPSc is a proteinaceous infectious agent that consists of a misfolded, self-replicating state of a sialoglycoprotein called the prion protein or PrPC. Sialylation of the prion protein N-linked glycans was discovered more than 30 years
Ilia V Baskakov +3 more
doaj +1 more source