Results 31 to 40 of about 5,185,837 (206)

Seeded assembly in vitro does not replicate the structures of α‐synuclein filaments from multiple system atrophy

FEBS Open Bio, 2021
The propagation of conformational strains by templated seeding is central to the prion concept. Seeded assembly of α‐synuclein into filaments is believed to underlie the prion‐like spreading of protein inclusions in a number of human neurodegenerative ...
Sofia Lövestam, Manuel Schweighauser, Tomoyasu Matsubara, Shigeo Murayama, Taisuke Tomita, Takashi Ando, Kazuko Hasegawa, Mari Yoshida, Airi Tarutani, Masato Hasegawa, Michel Goedert, Sjors H. W. Scheres   +11 more
doaj   +1 more source

Hsp110 chaperones regulate prion formation and propagation in S. cerevisiae by two discrete activities. [PDF]

PLoS ONE, 2008
The cytosolic chaperone network of Saccharomyces cerevisiae is intimately associated with the emergence and maintenance of prion traits. Recently, the Hsp110 protein, Sse1, has been identified as a nucleotide exchange factor (NEF) for both cytosolic ...
Heather Sadlish, Heike Rampelt, James Shorter, Renee D Wegrzyn, Claes Andréasson, Susan Lindquist, Bernd Bukau   +6 more
doaj   +1 more source

Prion-like Propagation Model of Tau

YAKUGAKU ZASSHI, 2019
Abnormal proteins such as tau or α-synuclein that accumulate in brains with dementia have been shown to propagate like prion proteins. However, the expression patterns of tau in the mouse brain are different from those in humans, and the pathogenesis in the animal model of abnormal tau propagation remains incompletely understood.
Masato, Hosokawa, Masato, Hasegawa
openaire   +3 more sources

POSCAbilities: The Application of the Prion Organotypic Slice Culture Assay to Neurodegenerative Disease Research

Biomolecules, 2020
Prion diseases are fatal, transmissible neurodegenerative disorders whose pathogenesis is driven by the misfolding, self-templating and cell-to-cell spread of the prion protein.
Hailey Pineau, Valerie Sim
doaj   +1 more source

Pros and cons of a prion-like pathogenesis in Parkinson's disease [PDF]

, 2011
Background: Parkinson's disease (PD) is a slowly progressive neurodegenerative disorder which affects widespread areas of the brainstem, basal ganglia and cerebral cortex.
Chapman Joab, Hilker, Ruediger, Brotchie, Jonathan M, Hilker, Rüdiger, Hilker Ruediger, Brotchie, Jonathan M., Joab Chapman, Ruediger Hilker, Chapman, Joab, Jonathan M Brotchie, Brotchie Jonathan M   +10 more
core   +2 more sources

Conservation of Prion-Like Composition and Sequence in Prion-Formers and Prion-Like Proteins of Saccharomyces cerevisiae

Frontiers in Molecular Biosciences, 2019
Prions in eukaryotes have been linked to diseases, evolutionary capacitance, large-scale genetic control, and long-term memory formation. Prion formation and propagation have been studied extensively in the budding yeast Saccharomyces cerevisiae.
Ting-Yi Su, Paul M. Harrison
doaj   +1 more source

Prion-like propagation of cytosolic protein aggregates [PDF]

Prion, 2009
Amyloid formation is a hallmark of several systemic and neurodegenerative diseases. Extracellular amyloid deposits or intracellular inclusions arise from the conformational transition of normally soluble proteins into highly ordered fibrillar aggregates.
Carmen, Krammer, Hermann M, Schätzl, Ina, Vorberg   +2 more
openaire   +2 more sources

Dissection and design of yeast prions. [PDF]

, 2004
Many proteins can misfold into beta-sheet-rich, self-seeding polymers (amyloids). Prions are exceptional among such aggregates in that they are also infectious.
Cox Brian S, Lev Z Osherovich (26522), Lev Z Osherovich, Cox, Brian S., Mick F Tuite, Brian S Cox (26523), Osherovich Lev Z, Tuite, Mick F., Osherovich, Lev Z., Jonathan S Weissman (23734), Brian S Cox, Mick F Tuite (26524), Jonathan S Weissman, Weissman, Jonathan S., Tuite Mick F, Weissman Jonathan S   +15 more
core   +2 more sources

The crystal structure of the globular domain of sheep prion protein [PDF]

, 2004
The prion protein PrP is a naturally occurring polypeptide that becomes transformed from a normal conformation to that of an aggregated form, characteristic of pathological states in fatal transmissible spongiform conditions such as Creutzfeld–Jacob ...
Vasisht N, Whyte, SM, Dodson EJ, Vasisht, N, Gill, A.C., Whyte, S.M., Dodson, G.G., Whyte, S M, Vasisht, N., Bayley, P M, Verma, C., Verma C, Gill, A C, Bayley, PM, Bayley, P.M., Whyte SM, Haire LF, Gill AC, Gill, AC, Bayley PM, Dodson, EJ, Haire, L.F., Dodson, GG, Dodson, E.J., Haire, L F, Verma, C, Haire, LF, Dodson, E J, Dodson, G G   +28 more
core   +1 more source

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