Results 61 to 70 of about 7,097 (179)

Quantifying the Role of Lysine in Prion Replication by Nano-LC Mass Spectrometry and Bioassay

Frontiers in Bioengineering and Biotechnology, 2020
Prions propagate by a template driven process, inducing the normal cellular isoform (PrPC) to adopt the prion (PrPSc) conformation. In PrPC, the positions of lysines are highly conserved and strongly influence prion propagation.
Christopher J. Silva, Melissa L. Erickson-Beltran, Irina C. Dynin   +2 more
doaj   +1 more source

Prion Diseases and their Prpsc-Based Molecular Diagnostics [PDF]

Journal of Neurology and Neuroscience, 2015
Prion diseases, also known as Transmissible Spongiform Encephalopathies (TSEs), are fatal neurodegenerative disorders with characteristic sponge-like microscopic appearance in the infected brain. They are caused by a protein-only particle consisting of an abnormal isoform (PrPSc) of the normal ubiquitous cellular prion protein PrPc.
Jianhui Wang, Xiaochun Wang, Xiaobin Gao
openaire   +1 more source

Human Brain Contusions Contain Pathogenic Transmissible Species that Induce Progressive Cognitive Decline and Tau Pathology in Mice

Annals of Neurology, Volume 99, Issue 4, Page 897-911, April 2026.
Objective Traumatic brain injury (TBI) is an established risk factor for dementia, although the underlying mechanisms remain unclear. Our previous research demonstrated that a single severe TBI in wild‐type (WT) mice induces a prion‐like form of tau (tauTBI) that spreads throughout the brain, leading to memory deficits.
Gloria Vegliante, Francesca Pischiutta, Elena Restelli, Federico Moro, Maria Antonietta Chiaravalloti, Ilaria Raimondi, Ilaria Bertani, Ilaria Lisi, Eliana Sammali, Rosaria Pascente, Serena Scozzari, Laura Pasetto, Carly Douglas, Marco Locatelli, Fabrizio Ortolano, Valentina Bonetto, David J. Loane, Nino Stocchetti, Roberto Chiesa, Elisa R. Zanier   +19 more
wiley   +1 more source

Toward the Atomic Structure of PrP^Sc [PDF]

Cold Spring Harbor Perspectives in Biology, 2017
In this review, we detail our current knowledge of PrPSc structure on the basis of structural and computational studies. We discuss the progress toward an atomic resolution description of PrPSc and results from the broader field of amyloid studies that may further inform our knowledge of this structure. Moreover, we summarize work that investigates the
Rodriguez, Jose A, Jiang, Lin, Eisenberg, David S   +2 more
openaire   +4 more sources

Toxic mechanisms of amyloid oligomers and therapeutic strategies

Protein Science, Volume 35, Issue 4, April 2026.
Abstract Amyloid oligomers are increasingly recognized as the major toxic contributors across protein‐misfolding disorders. In this review, we cover mechanistic evidence showing how these transient and structurally heterogeneous oligomers disrupt cellular homeostasis by: (i) permeabilizing lipid membranes and forming ion‐conducting pores; (ii ...
Magdalena I. Ivanova, Carmelo La Rosa, Ayyalusamy Ramamoorthy   +2 more
wiley   +1 more source

Full atomistic model of prion structure and conversion.

PLoS Pathogens, 2019
Prions are unusual protein assemblies that propagate their conformationally-encoded information in absence of nucleic acids. The first prion identified, the scrapie isoform (PrPSc) of the cellular prion protein (PrPC), caused epidemic and epizootic ...
Giovanni Spagnolli, Marta Rigoli, Simone Orioli, Alejandro M Sevillano, Pietro Faccioli, Holger Wille, Emiliano Biasini, Jesús R Requena   +7 more
doaj   +1 more source

Possible alignment of the EU BSE surveillance with the new WOAH provisions

EFSA Journal, Volume 24, Issue 4, April 2026.
Abstract The European Commission requested the assessment of the capacity of the surveillance provisions of the World Organization for Animal Health (WOAH) to detect bovine spongiform encephalopathy (BSE) cases (C‐, H‐ and L‐type) in the European Union (EU) and to propose if any current EU surveillance provisions should be kept.
EFSA Panel on Animal Health and Welfare (AHAW), Søren Saxmose Nielsen, Julio Alvarez, Anette Boklund, Sabine Dippel, Fernanda Dórea, Jordi Figuerola, Mette S. Herskin, Virginie Michel, Miguel Angel Miranda Chueca, Eleonora Nannoni, Anja B. Riber, Karl Stahl, Jan Arend Stegeman, Hans‐Hermann Thulke, Frank Tuyttens, Christoph Winckler, Mark Arnold, Christian Ducrot, John Griffin, Giuseppe Ru, Marion Simmons, Sean Ashe, Angel Ortiz‐ Pelaez, Kamela Kryemadhi, Romolo Nonno   +25 more
wiley   +1 more source

Change in the characteristics of ferritin induces iron imbalance in prion disease affected brains

Neurobiology of Disease, 2012
Prion disease associated neurotoxicity is mainly attributed to PrP-scrapie (PrPSc), the disease associated isoform of a normal protein, the prion protein (PrPC).
Ajay Singh, Liuting Qing, Qingzhong Kong, Neena Singh   +3 more
doaj   +1 more source

Proteinase K and the structure of PrPSc: The good, the bad and the ugly

Virus Research, 2015
Infectious proteins (prions) are, ironically, defined by their resistance to proteolytic digestion. A defining characteristic of the transmissible isoform of the prion protein (PrP(Sc)) is its partial resistance to proteinase K (PK) digestion. Diagnosis of prion disease typically relies upon immunodetection of PK-digested PrP(Sc) by Western blot, ELISA
Christopher J, Silva, Ester, Vázquez-Fernández, Bruce, Onisko, Jesús R, Requena   +3 more
openaire   +2 more sources

Plasmonics‐Enhanced Characterization of Cervid PrP (87–114) Fragment Aggregates in Solution

Journal of Biophotonics, Volume 19, Issue 3, March 2026.
Multimodal nanophotonics platform combining plasmon‐enhanced imaging, label‐free SERS, and optical staining reveals new insights into the aggregation of the cervid PrP (87–114) fragment, an amyloidogenic sequence linked to chronic wasting disease susceptibility.ABSTRACTWe performed a multimodal characterisation of self‐assembled fibrillar aggregates ...
Shinki Midha, Aishwarya Sriraman, Lyudmyla Dorosh, Holger Wille, Maria Stepanova   +4 more
wiley   +1 more source