Cargando…

Two alternative pathways for generating transmissible prion disease de novo

INTRODUCTION: Previous studies established that prion disease with unique strain-specific phenotypes could be induced by in vitro-formed recombinant PrP (rPrP) fibrils with structures different from that of authentic prions, or PrP(Sc). To explain the etiology of prion diseases, new mechanism propos...

Descripción completa

Detalles Bibliográficos
Autores principales:	Makarava, Natallia, Savtchenko, Regina, Baskakov, Ilia V.
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	BioMed Central 2015
Materias:	Research
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4641408/ https://www.ncbi.nlm.nih.gov/pubmed/26556038 http://dx.doi.org/10.1186/s40478-015-0248-5

Ejemplares similares

Sialylation of the prion protein glycans controls prion replication rate and glycoform ratio
por: Katorcha, Elizaveta, et al.
Publicado: (2015)

Preserving prion strain identity upon replication of prions in vitro using recombinant prion protein
por: Makarava, Natallia, et al.
Publicado: (2018)

Correction to: preserving prion strain identity upon replication of prions in vitro using recombinant prion protein
por: Makarava, Natallia, et al.
Publicado: (2018)

Genesis of Mammalian Prions: From Non-infectious Amyloid Fibrils to a Transmissible Prion Disease
por: Makarava, Natallia, et al.
Publicado: (2011)

Sialylation of Prion Protein Controls the Rate of Prion Amplification, the Cross-Species Barrier, the Ratio of PrP(Sc) Glycoform and Prion Infectivity
por: Katorcha, Elizaveta, et al.
Publicado: (2014)

Recombinant prion protein induces a new transmissible prion disease in wild-type animals
por: Makarava, Natallia, et al.
Publicado: (2010)

The Evolution of Transmissible Prions: The Role of Deformed Templating
por: Makarava, Natallia, et al.
Publicado: (2013)

Fast and ultrasensitive method for quantitating prion infectivity titer
por: Makarava, Natallia, et al.
Publicado: (2012)

Region-Specific Sialylation Pattern of Prion Strains Provides Novel Insight into Prion Neurotropism
por: Makarava, Natallia, et al.
Publicado: (2020)

Prion Strain-Specific Structure and Pathology: A View from the Perspective of Glycobiology
por: Baskakov, Ilia V., et al.
Publicado: (2018)

Prion replication environment defines the fate of prion strain adaptation
por: Katorcha, Elizaveta, et al.
Publicado: (2018)

Non-cell autonomous astrocyte-mediated neuronal toxicity in prion diseases
por: Kushwaha, Rajesh, et al.
Publicado: (2021)

Region-Specific Response of Astrocytes to Prion Infection
por: Makarava, Natallia, et al.
Publicado: (2019)

Molecular Structure of Amyloid Fibrils Controls the Relationship between Fibrillar Size and Toxicity
por: Lee, Young Jin, et al.
Publicado: (2011)

The degree of astrocyte activation is predictive of the incubation time to prion disease
por: Makarava, Natallia, et al.
Publicado: (2021)

Cross-seeding of prions by aggregated α-synuclein leads to transmissible spongiform encephalopathy
por: Katorcha, Elizaveta, et al.
Publicado: (2017)

Multiple steps of prion strain adaptation to a new host
por: Bocharova, Olga, et al.
Publicado: (2023)

Loss of Cellular Sialidases Does Not Affect the Sialylation Status of the Prion Protein but Increases the Amounts of Its Proteolytic Fragment C1
por: Katorcha, Elizaveta, et al.
Publicado: (2015)

Phagocytic Activities of Reactive Microglia and Astrocytes Associated with Prion Diseases Are Dysregulated in Opposite Directions
por: Sinha, Anshuman, et al.
Publicado: (2021)

Reversible off and on switching of prion infectivity via removing and reinstalling prion sialylation
por: Katorcha, Elizaveta, et al.
Publicado: (2016)

Deficiency in ST6GAL1, one of the two α2,6-sialyltransferases, has only a minor effect on the pathogenesis of prion disease
por: Makarava, Natallia, et al.
Publicado: (2022)

Reactive astrocytes associated with prion disease impair the blood brain barrier
por: Kushwaha, Rajesh, et al.
Publicado: (2023)

Reactive astrocytes associated with prion disease impair the blood brain barrier
por: Kushwaha, Rajesh, et al.
Publicado: (2023)

Inflammatory response of microglia to prions is controlled by sialylation of PrP(Sc)
por: Srivastava, Saurabh, et al.
Publicado: (2018)

Genesis of tramsmissible protein states via deformed templating
por: Makarava, Natallia, et al.
Publicado: (2012)

Strain-dependent profile of misfolded prion protein aggregates
por: Morales, Rodrigo, et al.
Publicado: (2016)

Contrasting Effects of Two Lipid Cofactors of Prion Replication on the Conformation of the Prion Protein
por: Srivastava, Saurabh, et al.
Publicado: (2015)

On the reactive states of astrocytes in prion diseases
por: Baskakov, Ilia V.
Publicado: (2021)

Multifaceted Role of Sialylation in Prion Diseases
por: Baskakov, Ilia V., et al.
Publicado: (2016)

Alzheimer’s disease-associated β-amyloid does not protect against herpes simplex virus 1 infection in the mouse brain
por: Bocharova, Olga, et al.
Publicado: (2021)

Highly Efficient Protein Misfolding Cyclic Amplification
por: Gonzalez-Montalban, Nuria, et al.
Publicado: (2011)

PrP charge structure encodes interdomain interactions
por: Martínez, Javier, et al.
Publicado: (2015)

De novo prions
por: Benetti, Federico, et al.
Publicado: (2010)

Aβ plaques do not protect against HSV‐1 infection in a mouse model of familial Alzheimer's disease, and HSV‐1 does not induce Aβ pathology in a model of late onset Alzheimer's disease
por: Bocharova, Olga V., et al.
Publicado: (2022)

De Novo Generation of Infectious Prions In Vitro Produces a New Disease Phenotype
por: Barria, Marcelo A., et al.
Publicado: (2009)

Correction: De Novo Generation of Infectious Prions In Vitro Produces a New Disease Phenotype
por: Barria, Marcelo A., et al.
Publicado: (2013)

Unraveling prion structures and biological functions
por: Ter-Avanesyan, Michael, et al.
Publicado: (2005)

Anti-Prion Systems Block Prion Transmission, Attenuate Prion Generation, Cure Most Prions as They Arise and Limit Prion-Induced Pathology in Saccharomyces cerevisiae
por: Wickner, Reed B., et al.
Publicado: (2022)

De novo [PSI(+)] prion formation involves multiple pathways to form infectious oligomers
por: Sharma, Jaya, et al.
Publicado: (2017)

Silent Prions and Covert Prion Transmission
por: Mathiason, Candace K.
Publicado: (2015)

Cannot write session to /tmp/vufind_sessions/sess_gdshn68l30alggu4igf32ish33