Are fibrinaloid microclots a cause of autoimmunity in Long Covid and other post-infection diseases?

DB Kell, E Pretorius - Biochemical Journal, 2023 - portlandpress.com
It is now well established that the blood-clotting protein fibrinogen can polymerise into an
anomalous form of fibrin that is amyloid in character; the resultant clots and microclots entrap …

The structure of the infectious prion protein: experimental data and molecular models

JR Requena, H Wille - Prion, 2014 - Taylor & Francis
The structures of the infectious prion protein, PrPSc, and that of its proteolytically truncated
variant, PrP 27–30, have evaded experimental determination due to their insolubility and …

Prion disease blood test using immunoprecipitation and improved quaking-induced conversion

CD Orrú, JM Wilham, LD Raymond, F Kuhn… - MBio, 2011 - Am Soc Microbiol
ABSTRACT A key challenge in managing transmissible spongiform encephalopathies
(TSEs) or prion diseases in medicine, agriculture, and wildlife biology is the development of …

Mutant prion protein expression causes motor and memory deficits and abnormal sleep patterns in a transgenic mouse model

S Dossena, L Imeri, M Mangieri, A Garofoli, L Ferrari… - Neuron, 2008 - cell.com
A familial form of Creutzfeldt-Jakob disease (CJD) is linked to the D178N/V129 prion protein
(PrP) mutation. Tg (CJD) mice expressing the mouse homolog of this mutant PrP synthesize …

Transgenic fatal familial insomnia mice indicate prion infectivity-independent mechanisms of pathogenesis and phenotypic expression of disease

I Bouybayoune, S Mantovani, F Del Gallo… - PLoS …, 2015 - journals.plos.org
Fatal familial insomnia (FFI) and a genetic form of Creutzfeldt-Jakob disease (CJD178) are
clinically different prion disorders linked to the D178N prion protein (PrP) mutation. The …

Pharmacological agents targeting the cellular prion protein

ML Barreca, N Iraci, S Biggi, V Cecchetti, E Biasini - Pathogens, 2018 - mdpi.com
Prion diseases are associated with the conversion of the cellular prion protein (PrPC), a
glycoprotein expressed at the surface of a wide variety of cell types, into a misfolded …

Propagation of PrPSc in mice reveals impact of aggregate composition on prion disease pathogenesis

SC Chang, S Hannaoui, MI Arifin, YH Huang… - Communications …, 2023 - nature.com
Infectious prions consist of PrPSc, a misfolded, aggregation-prone isoform of the host's prion
protein. PrPSc assemblies encode distinct biochemical and biological properties. They …

Cryo-immunogold electron microscopy for prions: toward identification of a conversion site

SF Godsave, H Wille, P Kujala, D Latawiec… - Journal of …, 2008 - Soc Neuroscience
Prion diseases are caused by accumulation of an abnormally folded isoform (PrPSc) of the
cellular prion protein (PrPC). The subcellular distribution of PrPSc and the site of its …

Aggregated, wild-type prion protein causes neurological dysfunction and synaptic abnormalities

R Chiesa, P Piccardo, E Biasini, B Ghetti… - Journal of …, 2008 - Soc Neuroscience
The neurotoxic forms of the prion protein (PrP) that cause neurodegeneration in prion
diseases remain to be conclusively identified. Considerable evidence points to the …

N-terminal regions of prion protein: Functions and roles in prion diseases

H Hara, S Sakaguchi - International journal of molecular sciences, 2020 - mdpi.com
The normal cellular isoform of prion protein, designated PrPC, is constitutively converted to
the abnormally folded, amyloidogenic isoform, PrPSc, in prion diseases, which include …