Results 11 to 20 of about 36,884 (188)
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
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Background The function of the prion protein, involved in the so-called prion diseases, remains a subject of intense debate and the possibility that it works as a pleiotropic protein through the interaction with multiple membrane proteins is somehow ...
J. A. Macedo +7 more
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Sequence features governing aggregation or degradation of prion-like proteins. [PDF]
Enhanced protein aggregation and/or impaired clearance of aggregates can lead to neurodegenerative disorders such as Alzheimer's Disease, Huntington's Disease, and prion diseases.
Sean M Cascarina +3 more
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Prion-Like Proteins in Phase Separation and Their Link to Disease
Aberrant protein folding underpins many neurodegenerative diseases as well as certain myopathies and cancers. Protein misfolding can be driven by the presence of distinctive prion and prion-like regions within certain proteins. These prion and prion-like
Macy L. Sprunger, Meredith E. Jackrel
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Prion Diseases: A Unique Transmissible Agent or a Model for Neurodegenerative Diseases?
The accumulation and propagation in the brain of misfolded proteins is a pathological hallmark shared by many neurodegenerative diseases such as Alzheimer’s disease (Aβ and tau), Parkinson’s disease (α-synuclein), and prion disease (prion protein ...
Diane L. Ritchie, Marcelo A. Barria
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Hepatic endothelial Alk1 signaling protects from development of vascular malformations while maintaining organ‐specific endothelial differentiation and angiocrine portmanteau of the names Wingless and Int‐1 signaling. Abstract Background and Aims In hereditary hemorrhagic telangiectasia (HHT), severe liver vascular malformations are associated with ...
Christian David Schmid +20 more
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Prion-Like Domains in Phagobiota
Prions are molecules characterized by self-propagation, which can undergo a conformational switch leading to the creation of new prions. Prion proteins have originally been associated with the development of mammalian pathologies; however, recently they ...
George Tetz, Victor Tetz
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Evolution of sequence traits of prion-like proteins linked to amyotrophic lateral sclerosis (ALS) [PDF]
Prions are proteinaceous particles that can propagate an alternative conformation to further copies of the same protein. They have been described in mammals, fungi, bacteria and archaea.
Jiayi Luo, Paul M. Harrison
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Understanding the Phenotypic Heterogeneity Within the Sporadic Creutzfeldt-Jakob Disease MV1 Subtype. [PDF]
We present the clinical, pathological and prion biophysical features of three atypical cases of the MV1 subtype of sporadic Creutzfeldt–Jakob disease (sCJD). We propose that these heterozygous cases exist on a spectrum ranging from MM1‐like to VV1‐like phenotypes and recommend that subtyping be performed at pH 6.9 to avoid missing atypical or mixed ...
Nemani SK +6 more
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Increasing evidence suggests that neurodegenerative disorders share a common pathogenic feature: the presence of deposits of misfolded proteins with altered physicochemical properties in the Central Nervous System.
Carlo Scialò +3 more
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