Results 31 to 40 of about 45,606 (277)

Intra- and interspecies interactions between prion proteins and effects of mutations and polymorphisms [PDF]

, 2003
Recently, crystallization of the prion protein in a dimeric form was reported. Here we show that native soluble homogenous FLAG-tagged prion proteins from hamster, man and cattle expressed in the baculovirus system are predominantly dimeric.
Hundt, C., Weiss, S., Riley, M. L., Gauczynski, S., Leucht, C.   +4 more
core   +1 more source

Prion Diseases [PDF]

Continuum, 2015
This article presents an update on the clinical aspects of human prion disease, including the wide spectrum of their presentations.Prion diseases, a group of disorders caused by abnormally shaped proteins called prions, occur in sporadic (Jakob-Creutzfeldt disease), genetic (genetic Jakob-Creutzfeldt disease, Gerstmann-Sträussler-Scheinker syndrome ...
openaire   +7 more sources

Syntaxin-6 delays prion protein fibril formation and prolongs the presence of toxic aggregation intermediates

eLife
Prions replicate via the autocatalytic conversion of cellular prion protein (PrPC) into fibrillar assemblies of misfolded PrP. While this process has been extensively studied in vivo and in vitro, non-physiological reaction conditions of fibril formation
Daljit Sangar, Elizabeth Hill, Kezia Jack, Mark Batchelor, Beenaben Mistry, Juan M Ribes, Graham S Jackson, Simon Mead, Jan Bieschke   +8 more
doaj   +1 more source

Gene expression profiling en association with prion-related lesions in the medulla oblongata of symptomatic natural scrapie animals. [PDF]

, 2011
The pathogenesis of natural scrapie and other prion diseases remains unclear. Examining transcriptome variations in infected versus control animals may highlight new genes potentially involved in some of the molecular mechanisms of prion-induced ...
Bossers, A., Rosa Bolea, Hicham Filali, Varona, L., Filalil, Hicham, Harders, F., Inmaculada Martin-Burriel, Alex Bossers, Zaragoza, P., Badiola, J.J., Juan J. Badiola, Bossers, Alex, Pumarola i Batlle, Martí, Lyahyai, Jaber, Lyahyai, J., Martín Burriel, Inmaculada, Pilar Zaragoza, Juan J Badiola, Bolea, Rosa, Filali, H., Bolea, R., Acín, Cristina, Luis Varona, Frank Harders, Filali, Hicham, Pumarola, M., Harders, Frank, Zaragoza, Pilar, Badiola, Juan J, Varona, Luis, Martí Pumarola, Jaber Lyahyai, Martin-Burriel, I., Badiola, Juan José, Pumarola, Martí   +34 more
core   +1 more source

Loss of Homeostatic Microglia Signature in Prion Diseases

Cells, 2022
Prion diseases are neurodegenerative diseases that affect humans and animals. They are always fatal and, to date, no treatment exists. The hallmark of prion disease pathophysiology is the misfolding of an endogenous protein, the cellular prion protein ...
Yue Wang, Kristin Hartmann, Edda Thies, Behnam Mohammadi, Hermann Altmeppen, Diego Sepulveda-Falla, Markus Glatzel, Susanne Krasemann   +7 more
doaj   +1 more source

Water‐Mediated Phosphoryl Wires Stabilize Pathological Tau Fibrils

Angewandte Chemie, EarlyView.
Extended 1D phosphoryl “wires” stabilize in‐register amyloid tau fibrils, as demonstrated by multiple‐quantum spin‐counting NMR, TEM, and MD simulations, using fibrils of tau peptide jR2R3‐P301L (tau295–313) with phosphorylation at S305 or Y310. ABSTRACT Hyperphosphorylation of tau is a hallmark of tauopathies, with specific phosphorylation sites ...
Lokeswara Rao Potnuru, Austin DuBose, Fiona Mon, Mesopotamia S. Nowotarski, Michael Vigers, Boqin Zhang, Chung‐Ta Han, John E. Straub, Songi Han   +8 more
wiley   +2 more sources

Differential Accumulation of Misfolded Prion Strains in Natural Hosts of Prion Diseases

Viruses, 2021
Prion diseases, also known as transmissible spongiform encephalopathies (TSEs), are a group of neurodegenerative protein misfolding diseases that invariably cause death.
Zoe J. Lambert, Justin J. Greenlee, Eric D. Cassmann, M. Heather West Greenlee   +3 more
doaj   +1 more source

The Molecular Pathology of Prion Diseases [PDF]

, 2004
Prion diseases, or transmissible spongiform encephalopathies (TSEs), are a group of invariably fatal neurodegenerative disorders. Uniquely, they may present as sporadic, inherited, or infectious forms, all of which involve conversion of the normal ...
Vassallo, Neville, Herms, Jochen, Kretzschmar, Hans A.   +2 more
core  

Effects of post-translational modifications on prion protein aggregation and the propagation of scrapie-like characteristics in vitro [PDF]

, 2007
Prion diseases, or transmissible spongiform encephalopathies (TSEs) are typically characterised by CNS accumulation of PrPSc, an aberrant conformer of a normal cellular protein PrPC.
Oxley, David, Meersman, Filip, Webster, Judith, Kazlauskaite, Jurate, Pinheiro, Teresa J. T., Young, Duncan S., Dear, Denise V., Lowe, Christopher R., Gill, Andrew C., Bronstein, Igor   +9 more
core   +1 more source

From energy provision to protein synthesis: Tunnelling nanotubes as mediators of intercellular metabolic cooperation in cancer

FEBS Open Bio, EarlyView.
The cytoskeleton‐mediated transport of mitochondria via tunnelling nanotubes restores respiration, increases ATP production, rescues cells from apoptosis, activates the AKT/mTOR signalling pathway, promotes cell migration and invasiveness, contributes to cancer progression and treatment resistance.
Stanislava Martínková, Jan Trnka
wiley   +1 more source