Results 21 to 30 of about 5,604,422 (355)

Prion Protein Biology [PDF]

open access: yesCell, 1998
We thank G. Carlson, N. Nathanson, and J. Safar for carefully reviewing sections of this manuscript. This research was supported by grants from the National Institute of Aging and the National Institute of Neurologic Diseases and Stroke of the National Institutes of Health, International Human Frontiers of Science Program, and American Health ...
Fred E. Cohen   +3 more
openaire   +3 more sources

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

open access: yesPLoS 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   +9 more
doaj   +1 more source

The biological function of the cellular prion protein: an update

open access: yesBMC Biology, 2017
The misfolding of the cellular prion protein (PrPC) causes fatal neurodegenerative diseases. Yet PrPC is highly conserved in mammals, suggesting that it exerts beneficial functions preventing its evolutionary elimination. Ablation of PrPC in mice results
M. Wulf, Assunta Senatore, A. Aguzzi
semanticscholar   +1 more source

Membrane-enriched proteome changes and prion protein expression during neural differentiation and in neuroblastoma cells

open access: yesBMC Genomics, 2017
Background The function of the prion protein, involved in the so-called prion diseases, remains a subject of intense debate and the possibility that it works as a pleiotropic protein through the interaction with multiple membrane proteins is somehow ...
J. A. Macedo   +7 more
doaj   +1 more source

Transition of the prion protein from a structured cellular form (PrPC) to the infectious scrapie agent (PrPSc)

open access: yesProtein Science, 2019
Prion diseases in mammals are caused by a conformational transition of the cellular prion protein from its native conformation (PrPC) to a pathological isoform called “prion protein scrapie” (PrPSc).
P. K. Baral   +3 more
semanticscholar   +1 more source

Prion Protein in Milk

open access: yesPLoS ONE, 2006
Prions are known to cause transmissible spongiform encephalopathies (TSE) after accumulation in the central nervous system. There is increasing evidence that prions are also present in body fluids and that prion infection by blood transmission is possible.
Franscini, Nicola   +8 more
openaire   +5 more sources

A companion to the preclinical common data elements and case report forms for neuropathology studies in epilepsy research. A report of the TASK3 WG2 Neuropathology Working Group of the ILAE/AES Joint Translational Task Force

open access: yesEpilepsia Open, EarlyView., 2022
Abstract The International League Against Epilepsy/American Epilepsy Society (ILAE/AES) Joint Translational Task Force initiated the TASK3 working group to create common data elements (CDEs) for various aspects of preclinical epilepsy research studies, which could help improve the standardization of experimental designs.
Eleonora Aronica   +6 more
wiley   +1 more source

Physiological Functions of the Cellular Prion Protein

open access: yesFrontiers in Molecular Biosciences, 2017
The prion protein, PrPC, is a small, cell-surface glycoprotein notable primarily for its critical role in pathogenesis of the neurodegenerative disorders known as prion diseases.
Andrew R. Castle, A. Gill
semanticscholar   +1 more source

Prion Protein Misfolding [PDF]

open access: yesCurrent Molecular Medicine, 2009
The crucial event in the development of transmissible spongiform encephalopathies (TSEs) is the conformational change of a host-encoded membrane protein - the cellular PrP(C) - into a disease associated, fibril-forming isoform PrP(Sc). This conformational transition from the alpha-helix-rich cellular form into the mainly beta-sheet containing ...
Martin H. Groschup   +2 more
openaire   +2 more sources

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

open access: yesFrontiers 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   +7 more
doaj   +1 more source

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