Results 51 to 60 of about 5,604,422 (355)

Molecular Barriers to Zoonotic Transmission of Prions

Emerging Infectious Diseases, 2014
The risks posed to human health by individual animal prion diseases cannot be determined a priori and are difficult to address empirically. The fundamental event in prion disease pathogenesis is thought to be the seeded conversion of normal prion protein
Marcelo A. Barria, Aru Balachandran, Masanori Morita, Tetsuyuki Kitamoto, Rona Barron, Jean Manson, Richard Knight, James W. Ironside, Mark W. Head   +8 more
doaj   +1 more source

Enhanced phosphorylation of PERK in primary cultured neurons as an autonomous neuronal response to prion infection.

PLoS ONE, 2020
Conversion of cellular prion protein (PrPC) into the pathogenic isoform of prion protein (PrPSc) in neurons is one of the key pathophysiological events in prion diseases.
Misaki Tanaka, Takeshi Yamasaki, Rie Hasebe, Akio Suzuki, Motohiro Horiuchi   +4 more
doaj   +1 more source

Prion protein glycosylation [PDF]

Journal of Neurochemistry, 2005
AbstractThe transmissible spongiform encephalopathies (TSE), or prion diseases are a group of transmissible neurodegenerative disorders of humans and animals. Although the infectious agent (the ‘prion’) has not yet been formally defined at the molecular level, much evidence exists to suggest that the major or sole component is an abnormal isoform of ...
Lawson, Victoria A, Collins, Steven J, Masters, Colin L, Hill, Andrew F   +3 more
openaire   +4 more sources

Prion pathogenesis is unaltered in the absence of SIRPα-mediated "don't-eat-me" signaling. [PDF]

PLoS ONE, 2017
Prion diseases are neurodegenerative conditions caused by misfolding of the prion protein, leading to conspicuous neuronal loss and intense microgliosis.
Mario Nuvolone, Marta Paolucci, Silvia Sorce, Veronika Kana, Rita Moos, Takashi Matozaki, Adriano Aguzzi   +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

Prion-like low-complexity sequences: Key regulators of protein solubility and phase behavior

Journal of Biological Chemistry, 2018
Many proteins, such as RNA-binding proteins, have complex folding landscapes. How cells maintain the solubility and folding state of such proteins, particularly under stress conditions, is largely unknown.
Titus M. Franzmann, S. Alberti
semanticscholar   +1 more source

Conformational conversion of prion protein in prion diseases [PDF]

Acta Biochimica et Biophysica Sinica, 2013
Prion diseases are a group of infectious fatal neurodegenerative diseases. The conformational conversion of a cellular prion protein (PrP(C)) into an abnormal misfolded isoform (PrP(Sc)) is the key event in prion diseases pathology. Under normal conditions, the high-energy barrier separates PrP(C) from PrP(Sc) isoform.
Gengfu Xiao, Zheng Zhou
openaire   +3 more sources

A cationic tetrapyrrole inhibits toxic activities of the cellular prion protein [PDF]

, 2016
Prion diseases are rare neurodegenerative conditions associated with the conformational conversion of the cellular prion protein (PrPC) into PrPSc, a self-replicating isoform (prion) that accumulates in the central nervous system of affected individuals.
Biasini, Emiliano, Borsello, Tiziana, Castilla, Joaqu\uedn, Cerovic, Milica, Cimini, Sara, Elezgarai, Saioa R., Gobbi, Marco, Massignan, Tania, Moreno, Jorge, Negro, Alessandro, Nonno, Romolo, Restelli, Elena, Riccardi, Geraldina, Sangiovanni, Valeria, Stincardini, Claudia, Stravalaci, Matteo, Vanni, Ilaria   +16 more
core   +1 more source

Absence of single nucleotide polymorphisms (SNPs) in the open reading frame (ORF) of the prion protein gene (PRNP) in a large sampling of various chicken breeds

BMC Genomics, 2019
Background Prion diseases are zoonotic diseases with a broad infection spectrum among mammalian hosts and are caused by the misfolded prion protein (PrPSc) derived from the normal prion protein (PrPC), which encodes the prion protein gene (PRNP ...
Yong-Chan Kim, Sae-Young Won, Byung-Hoon Jeong   +2 more
doaj   +1 more source

Electrostatics in the Stability and Misfolding of the Prion Protein: Salt Bridges, Self-Energy, and Solvation

, 2010
Using a recently developed mesoscopic theory of protein dielectrics, we have calculated the salt bridge energies, total residue electrostatic potential energies, and transfer energies into a low dielectric amyloid-like phase for 12 species and mutants of
Cashman, Neil R., Guest, Will, Plotkin, Steven S.   +2 more
core   +1 more source