Results 41 to 50 of about 8,574 (264)

Water and the Biology of Prions and Plaques [PDF]

open access: yes, 2007
This is an attempt to account for the insolubility and/or aggregation of prions and plaques in terms of a model of water consisting of an equilibrium between high density and low density microdomains.
Graham K. Steel, Phillippa M. Wiggins
core  

From energy provision to protein synthesis: Tunnelling nanotubes as mediators of intercellular metabolic cooperation in cancer

open access: yesFEBS Open Bio, EarlyView.
The cytoskeleton‐mediated transport of mitochondria via tunnelling nanotubes restores respiration, increases ATP production, rescues cells from apoptosis, activates the AKT/mTOR signalling pathway, promotes cell migration and invasiveness, contributes to cancer progression and treatment resistance.
Stanislava Martínková, Jan Trnka
wiley   +1 more source

Key points concerning amyloid infectivity and prion-like neuronal invasion

open access: yesFrontiers in Molecular Neuroscience, 2016
Amyloid aggregation has been related to an increasing number of human illnesses, from Alzheimer and Parkinson’s diseases to Creutzfeldt-Jakob disease. Traditionally only prions have been considered as infectious agents with a high capacity of propagation.
Alba eEspargaró   +3 more
doaj   +1 more source

A new method for the Characterization of Strain-Specific Conformational Stability of Protease-Sensitive and Protease Resistant PrPSc [PDF]

open access: yes, 2010
Although proteinacious in nature, prions exist as strains with specific self-perpetuating biological properties. Prion strains are thought to be associated with different conformers of PrPSc, a disease-associated isoform of the host-encoded cellular ...
Gabriele Vaccari   +34 more
core   +2 more sources

Treatment with KCL‐286, a first‐in‐class retinoic acid receptor‐β (RARβ) agonist, ameliorates neuronal DNA damage and inflammation in a mouse model of Alzheimer's disease

open access: yesFEBS Open Bio, EarlyView.
Repair of neuronal DNA damage in Alzheimer's disease by KCL‐286. (A) Amyloid‐β oligomers and plaques impair neuronal DNA repair pathways, leading to DNA double‐strand breaks and glial activation. (B) KCL‐286 activates RARβ/RXR signalling via retinoic acid response elements (RAREs), associated with increased BRCA1 expression, enhanced DNA repair and ...
Natasha Hill   +6 more
wiley   +1 more source

Scrapie at Abattoir: Monitoring, Control, and Differential Diagnosis of Wasting Conditions during Meat Inspection

open access: yesAnimals, 2021
Wasting disease in small ruminants is frequently detected at slaughterhouses. The wasting disorder is manifested by the deterioration of the nutritional and physiological state of the animal indicated by thinness, emaciation, and cachexia.
Alexandra Esteves   +22 more
doaj   +1 more source

Adenosine triphosphate as a modulator of protein interactions and stability

open access: yesFEBS Open Bio, EarlyView.
ATP is best known as the cell's energy currency, but it also shapes how proteins fold, interact, aggregate and form biomolecular condensates. This review explains the emerging physical principles behind these effects, including weak binding to charged protein regions, magnesium‐dependent behaviour and concentration‐dependent control of protein ...
Shuyuan Tan, Robin Curtis
wiley   +1 more source

Oral Transmission of L-type Bovine Spongiform Encephalopathy in Primate Model

open access: yesEmerging Infectious Diseases, 2012
We report transmission of atypical L-type bovine spongiform encephalopathy to mouse lemurs after oral or intracerebral inoculation with infected bovine brain tissue.
Nadine Mestre-Francés   +7 more
doaj   +1 more source

Pathogenic mutations in the hydrophobic core of the human prion protein can promote structural instability and misfolding [PDF]

open access: yes, 2010
Transmissible spongiform encephalopathies, or prion diseases, are caused by misfolding and aggregation of the prion protein PrP. These diseases can be hereditary in humans and four of the many disease-associated missense mutants of PrP are in the ...
Valerie Daggett   +3 more
core   +1 more source

MARK4 enhances stress granule formation under oxidative stress and increases tau accumulation

open access: yesFEBS Open Bio, EarlyView.
MARK4 (red dots) localizes to stress granules (orange dots) and promotes their formation under oxidative stress by modulating TIA1 (blue dots). MARK4 and TIA1 synergistically increase tau (purple) accumulation, and the reduction of the TIA1 ortholog suppresses neurodegeneration in a fly model.
Sho Nakajima   +8 more
wiley   +1 more source

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