Results 21 to 30 of about 97,377 (307)

ALK1 controls hepatic vessel formation, angiodiversity, and angiocrine functions in hereditary hemorrhagic telangiectasia of the liver

Hepatology, EarlyView., 2022
Hepatic endothelial Alk1 signaling protects from development of vascular malformations while maintaining organ‐specific endothelial differentiation and angiocrine portmanteau of the names Wingless and Int‐1 signaling. Abstract Background and Aims In hereditary hemorrhagic telangiectasia (HHT), severe liver vascular malformations are associated with ...
Christian David Schmid, Victor Olsavszky, Manuel Reinhart, Vanessa Weyer, Felix A. Trogisch, Carsten Sticht, Manuel Winkler, Sina W. Kürschner, Johannes Hoffmann, Roxana Ola, Theresa Staniczek, Joerg Heineke, Beate K. Straub, Jens Mittler, Kai Schledzewski, Peter ten Dijke, Karsten Richter, Steven Dooley, Cyrill Géraud, Sergij Goerdt, Philipp‐Sebastian Koch   +20 more
wiley   +1 more source

Deposition pattern and subcellular distribution of disease-associated prion protein in cerebellar organotypic slice cultures infected with scrapie

Frontiers in Neuroscience, 2015
Organotypic cerebellar slices represent a suitable model for characterizing and manipulating prion replication in complex cell environments. Organotypic slices recapitulate prion pathology and are amenable to drug testing in the absence of a blood-brain ...
Hanna eWolf, Andre eHossinger, Andrea eFehlinger, Sven eBuettner, Valerie eSim, Debbie eMcKenzie, Ina Maja Vorberg, Ina Maja Vorberg   +7 more
doaj   +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

Prion protein interconversions† [PDF]

Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences, 2001
The transmissible spongiform encephalopathies (TSEs), or prion diseases, remain mysterious neurodegenerative diseases that involve perturbations in prion protein (PrP) structure. This article summarizes our use ofin vitromodels to describe how PrP is converted to the disease–associated, protease–resistant form.
openaire   +2 more sources

Prion Neurotoxicity: Insights from Prion Protein Mutants [PDF]

Current Issues in Molecular Biology, 2010
The chemical nature of prions and the mechanism by which they propagate are now reasonably well understood. In contrast, much less is known about the identity of the toxic prion protein (PrP) species that are responsible for neuronal death, and the cellular pathways that these forms activate.
Solomon, Isaac H., Schepker, Jessie A., Harris, David A.   +2 more
openaire   +3 more sources

Novel insertion/deletion polymorphisms and genetic features of the shadow of prion protein gene (SPRN) in dogs, a prion-resistant animal

Frontiers in Veterinary Science, 2022
Prion diseases are fatal infectious neurodegenerative disorders that are induced by misfolded prion protein (PrPSc). Previous studies have reported that the shadow of prion protein (Sho) encoded by the shadow of prion protein gene (SPRN) plays a critical
Yong-Chan Kim, Yong-Chan Kim, Hyeon-Ho Kim, Hyeon-Ho Kim, An-Dang Kim, Byung-Hoon Jeong, Byung-Hoon Jeong   +6 more
doaj   +1 more source

The cellular prion protein beyond prion diseases

Swiss Medical Weekly, 2020
The cellular prion protein (PrPC), a cell surface glycoprotein originally identified for its central role in prion diseases (also called transmissible spongiform encephalopathies), has recently been implicated in the pathogenesis of other neurodegenerative disorders, such as Alzheimer’s and Parkinson’s diseases, by acting as a toxicity-transducing ...
Manni, Giorgia, Lewis, Victoria, Senesi, Matteo, Spagnolli, Giovanni, Fallarino, Francesca, Collins, Steven, Mouillet-Richard, Sophie, Biasini, Emiliano   +7 more
openaire   +6 more sources

Prion protein and aging [PDF]

Frontiers in Cell and Developmental Biology, 2014
The cellular prion protein (PrP(C)) has been widely investigated ever since its conformational isoform, the prion (or PrP(Sc)), was identified as the etiological agent of prion disorders. The high homology shared by the PrP(C)-encoding gene among mammals, its high turnover rate and expression in every tissue strongly suggest that PrP(C) may possess key
Gasperini, Lisa, Legname, Giuseppe
openaire   +4 more sources

Morphine Withdrawal Modifies Prion Protein Expression in Rat Hippocampus. [PDF]

PLoS ONE, 2017
The hippocampus is a vulnerable brain structure susceptible to damage during aging and chronic stress. Repeated exposure to opioids may alter the brain so that it functions normally when the drugs are present, thus, a prolonged withdrawal might lead to ...
Vincenzo Mattei, Stefano Martellucci, Francesca Santilli, Valeria Manganelli, Tina Garofalo, Niccolò Candelise, Alessandra Caruso, Maurizio Sorice, Sergio Scaccianoce, Roberta Misasi   +9 more
doaj   +1 more source

Heat shock factor 1 regulates lifespan as distinct from disease onset in prion disease [PDF]

, 2008
Prion diseases are fatal, transmissible, neurodegenerative diseases caused by the misfolding of the prion protein (PrP). At present, the molecular pathways underlying prion-mediated neurotoxicity are largely unknown.
Aguzzi, Adriano, Borkowski, Andrew W., Heppner, Frank L., Hutter, Gregor, Jackson, Walter S., King, Oliver D., Lindquist, Susan, Raymond, Gregory J., Steele, Andrew D.   +8 more
core   +3 more sources