Results 131 to 140 of about 71,281 (314)

On the statistical mechanics of prion diseases

open access: yes, 2001
We simulate a two-dimensional, lattice based, protein-level statistical mechanical model for prion diseases (e.g., Mad Cow disease) with concommitant prion protein misfolding and aggregation.
A. Coghlan   +25 more
core   +1 more source

Tau‐targeting active immunotherapy slows progression and reduces pathology in mouse models of tauopathy

open access: yesBrain Pathology, EarlyView.
The efficacy of the novel anti‐tau active immunotherapy, p5555kb, was tested using two mouse models of tau pathology. p5555kb inoculation increased the survival rate and reduced tau pathology in tau‐overexpressing P301L mice and decreased tau seeding in the brains of C57BL/6 mice injected with human‐purified Alzheimer's disease tau.
Christopher M. Brown   +7 more
wiley   +1 more source

Rapid generation of prion disease models using AAV‐delivered PrP variants in knockout mice

open access: yesBrain Pathology, EarlyView.
We developed a rapid AAV‐based system to generate prion disease models in weeks rather than months. Following systemic AAV9P31 delivery of modified PrP to knockout mice, we achieved brain‐wide expression and successful propagation of both classical (RML) and atypical (GSS‐A117V) prion strains.
Maitena San‐Juan‐Ansoleaga   +11 more
wiley   +1 more source

The L108I polymorphism in mouse prion protein drives spontaneous disease and enhances transmission of atypical and classical prion strains

open access: yesBrain Pathology, EarlyView.
A single amino acid change (L108I) combined with PrP overexpression drives spontaneous atypical prion formation in mice, enabling also efficient propagation of diverse prion strains. This model allows studying how spontaneous prion diseases arise and provides powerful tools for investigating strain emergence, transmission barriers, and mechanisms ...
Hasier Eraña   +20 more
wiley   +1 more source

Prion-induced neurotoxicity: Possible role for cell cycle activity and DNA damage response. [PDF]

open access: yes, 2015
Protein misfolding neurodegenerative diseases arise through neurotoxicity induced by aggregation of host proteins. These conditions include Alzheimer's disease, Huntington's disease, Parkinson's disease, motor neuron disease, tauopathies and prion ...

core   +1 more source

BOLL‐Containing Aggregates Mediate the Translational Regulation During Human Oogenesis

open access: yesCell Proliferation, EarlyView.
This work elucidates that BOLL‐containing aggregate‐mediated translational control is essential for human oogenesis. These aggregates recruit PABPC1 and FXR1 to activate the translation of U‐rich mRNAs encoding cell cycle proteins, thereby ensuring successful meiotic progression.
Ying Li   +5 more
wiley   +1 more source

Spatial Sequestration and Oligomer Remodeling During \u3cem\u3ede novo\u3c/em\u3e [\u3cem\u3ePSI\u3c/em\u3e\u3csup\u3e+\u3c/sup\u3e] Formation [PDF]

open access: yes, 2017
Prions are misfolded, aggregated, infectious proteins found in a range of organisms from mammals to bacteria. In mammals, prion formation is difficult to study because misfolding and aggregation take place prior to symptom presentation.
Lyke, Douglas, Manogaran, Anita L.
core   +1 more source

Assessment of land‐based threats to Atlantic pelagic seabirds

open access: yesConservation Science and Practice, EarlyView.
Highly mobile pelagic seabirds face numerous land‐based threats during their breeding seasons, including invasive alien species, climate change, and diseases, which drive population declines. Using field expertise and a literature review, we collated a dataset assessing 18 threats affecting 49 species across 38 Atlantic Large Marine Ecosystems. We used
Ioannis Kalaitzakis   +38 more
wiley   +1 more source

Self-Templated Nucleation in Peptide and Protein aggregation

open access: yes, 2008
Peptides and proteins exhibit a common tendency to assemble into highly ordered fibrillar aggregates, whose formation proceeds in a nucleation-dependent manner that is often preceded by the formation of disordered oligomeric assemblies.
Amos Maritan   +5 more
core   +1 more source

MAVS oligomerization drives a faster and more efficient antiviral signaling activation at peroxisomes compared to mitochondria

open access: yesThe FEBS Journal, EarlyView.
Cells rely on mitochondria and peroxisomes to trigger antiviral defenses via the protein MAVS. This manuscript demonstrates that the robust production of antiviral effectors resulting from MAVS activation at peroxisomes is faster than at mitochondria due to a swifter oligomerization of this protein at peroxisomal membranes. These results underscore the
Bruno Ramos   +4 more
wiley   +1 more source

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