Results 21 to 30 of about 1,598,142 (264)

Prion-Like Proteins in Phase Separation and Their Link to Disease

open access: yesBiomolecules, 2021
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
doaj   +1 more source

Anti-prion drug mPPIg5 inhibits PrP(C) conversion to PrP(Sc). [PDF]

open access: yes, 2013
Prion diseases, also known as transmissible spongiform encephalopathies, are a group of fatal neurodegenerative diseases that include scrapie in sheep, bovine spongiform encephalopathy (BSE) in cattle and Creutzfeldt-Jakob disease (CJD) in humans.
Jeremy C. Simpson (29225)   +31 more
core   +2 more sources

Sequence features governing aggregation or degradation of prion-like proteins. [PDF]

open access: yesPLoS Genetics, 2018
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
doaj   +1 more source

Prion Diseases: A Unique Transmissible Agent or a Model for Neurodegenerative Diseases?

open access: yesBiomolecules, 2021
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
doaj   +1 more source

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

open access: yes, 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   +10 more
core   +2 more sources

Raman optical activity demonstrates poly(L-proline) II helix in the N-terminal region of the ovine prion protein: Implications for function and misfunction [PDF]

open access: yes, 2004
The aqueous solution structure of the full-length recombinant ovine prion protein PrP25-233, together with that of the N-terminal truncated version PrP94-233, have been studied using vibrational Raman optical activity (ROA) and ultraviolet circular ...
Rhie, A G O   +18 more
core   +1 more source

Prion protein self-peptides modulate prion interactions and conversion [PDF]

open access: yes, 2009
Background: Molecular mechanisms underlying prion agent replication, converting host-encoded cellular prion protein (PrPC) into the scrapie associated isoform (PrPSc), are poorly understood.
Bossers, A.   +12 more
core   +1 more source

Prion-Like Domains in Phagobiota

open access: yesFrontiers in Microbiology, 2017
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
doaj   +1 more source

Evolution of sequence traits of prion-like proteins linked to amyotrophic lateral sclerosis (ALS) [PDF]

open access: yesPeerJ, 2022
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
doaj   +2 more sources

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