Results 31 to 40 of about 37,766 (292)

Medium-throughput zebrafish optogenetic platform identifies deficits in subsequent neural activity following brief early exposure to cannabidiol and Δ9-tetrahydrocannabinol

Scientific Reports, 2021
In light of legislative changes and the widespread use of cannabis as a recreational and medicinal drug, delayed effects of cannabis upon brief exposure during embryonic development are of high interest as early pregnancies often go undetected.
Richard Kanyo, Md Ruhul Amin, Laszlo F. Locskai, Danika D. Bouvier, Alexandria M. Olthuis, W. Ted Allison, Declan W. Ali   +6 more
doaj   +1 more source

Mimosine functionalized gold nanoparticles (Mimo-AuNPs) suppress β-amyloid aggregation and neuronal toxicity

Bioactive Materials, 2021
Evidence suggests that increased level/aggregation of beta-amyloid (Aβ) peptides initiate neurodegeneration and subsequent development of Alzheimer's disease (AD). At present, there is no effective treatment for AD. In this study, we reported the effects
Bibin G. Anand, Qi Wu, Govindarajan Karthivashan, Kiran P. Shejale, Sara Amidian, Holger Wille, Satyabrata Kar   +6 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

The CNS in inbred transgenic models of 4-repeat Tauopathy develops consistent tau seeding capacity yet focal and diverse patterns of protein deposition

Molecular Neurodegeneration, 2017
Background MAPT mutations cause neurodegenerative diseases such as frontotemporal dementia but, strikingly, patients with the same mutation may have different clinical phenotypes.
Ghazaleh Eskandari-Sedighi, Nathalie Daude, Hristina Gapeshina, David W. Sanders, Razieh Kamali-Jamil, Jing Yang, Beipei Shi, Holger Wille, Bernardino Ghetti, Marc I. Diamond, Christopher Janus, David Westaway   +11 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

Distinct amino acid compositional requirements for formation and maintenance of the [PSI+] prion in yeast [PDF]

, 2015
Multiple yeast prions have been identified that result from the structural conversion of proteins into a self-propagating amyloid form. Amyloid-based prion activity in yeast requires a series of discrete steps.
Ben-Musa, Zobaida, Gruca, Margaret, MacLea, Kyle S., Paul, Kacy R., Ross, Eric D., Shattuck, Jenifer E., Waechter, Aubrey   +6 more
core   +2 more sources

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

Octarepeat region flexibility impacts prion function, endoproteolysis and disease manifestation

EMBO Molecular Medicine, 2015
The cellular prion protein (PrPC) comprises a natively unstructured N‐terminal domain, including a metal‐binding octarepeat region (OR) and a linker, followed by a C‐terminal domain that misfolds to form PrPSc in Creutzfeldt‐Jakob disease.
Agnes Lau, Alex McDonald, Nathalie Daude, Charles E Mays, Eric D Walter, Robin Aglietti, Robert CC Mercer, Serene Wohlgemuth, Jacques van der Merwe, Jing Yang, Hristina Gapeshina, Chae Kim, Jennifer Grams, Beipei Shi, Holger Wille, Aru Balachandran, Gerold Schmitt‐Ulms, Jiri G Safar, Glenn L Millhauser, David Westaway   +19 more
doaj   +1 more source

Prions [PDF]

Proceedings of the National Academy of Sciences, 1984
Prions are unprecedented infectious pathogens that cause a group of invariably fatal neurodegenerative diseases by an entirely novel mechanism. Prion diseases may present as genetic, infectious, or sporadic disorders, all of which involve modification of the prion protein (PrP).
openaire   +3 more sources

Resistance of soil-bound prions to rumen digestion. [PDF]

PLoS ONE, 2012
Before prion uptake and infection can occur in the lower gastrointestinal system, ingested prions are subjected to anaerobic digestion in the rumen of cervids and bovids.
Samuel E Saunders, Shannon L Bartelt-Hunt, Jason C Bartz   +2 more
doaj   +1 more source