Results 71 to 80 of about 71,281 (314)
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
Conformational diversity in purified prions produced in vitro.
PLoS Pathogens, 2023 Prion diseases are caused by misfolding of either wild-type or mutant forms of the prion protein (PrP) into self-propagating, pathogenic conformers, collectively termed PrPSc.
Daniel J Walsh +3 more
doaj +1 more source
Mapping the Beta-Sheet Structure of the Yeast Prion Sup35 through Creation of Targeted Mutant Forms [PDF]
, 2013 Proteins with an aggregated form rich in beta-sheet structure are known as amyloids, of which a subset are infectious. These infectious proteins are known as prions and cause diseases including bovine spongiform encephalopathy (“Mad Cow” disease ...
Davis, Emily K. +2 more
core +1 more source
Advanced Science, EarlyView.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
The Molecular Pathology of Prion Diseases [PDF]
, 2004 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
Cellular Prion Protein Mediates Toxic Signaling of Amyloid Beta [PDF]
, 2011 Prion diseases in humans and animals comprise a group of invariably fatal neurodegenerative diseases characterized by the formation of a pathogenic protein conformer designated PrPSc and infectious particles denoted prions.
Resenberger, Ulrike K. +2 more
core +1 more source
Selective Targeting of Tip Endothelial Cells as a Therapeutic Strategy for Tumor Angiogenesis
Advanced Science, EarlyView.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
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
Inactivation of Prions and Amyloid Seeds with Hypochlorous Acid
PLoS Pathogens, 2016 Hypochlorous acid (HOCl) is produced naturally by neutrophils and other cells to kill conventional microbes in vivo. Synthetic preparations containing HOCl can also be effective as microbial disinfectants.
A. Hughson +14 more
semanticscholar +1 more source
Advanced Science, EarlyView.Astrocytic TIA1‐mediated stress granules (SGs) promote demyelination by sequestering the mRNA of cholesterol synthesis genes. In this model, astrocytic TIA1‐mediated SGs were increased in the optic nerves of EAE mice, leading to the downregulation of cholesterol synthesis genes such as HMGCS1 through sequestration of their mRNA into SGs, which ...
Zheyu Fang +11 more
wiley +1 more source