Results 61 to 70 of about 16,136 (210)

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

Brain 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, Eva Fernández‐Muñoz, Jorge M. Charco, Enric Vidal, Diego Herrero‐Martínez, Josu Galarza‐Ahumada, Cristina Sampedro‐Torres‐Quevedo, Samanta Giler, Mariví Geijo, Gloria González‐Aseguinolaza, Hasier Eraña, Joaquín Castilla   +11 more
wiley   +1 more source

Plasma PolyQ-ATXN3 Levels Associate With Cerebellar Degeneration and Behavioral Abnormalities in a New AAV-Based SCA3 Mouse Model

Frontiers in Cell and Developmental Biology, 2022
Spinocerebellar ataxia type 3 (SCA3) is a dominantly inherited cerebellar ataxia caused by the expansion of a polyglutamine (polyQ) repeat in the gene encoding ATXN3.
Karen Jansen-West, Tiffany W. Todd, Tiffany W. Todd, Lillian M. Daughrity, Mei Yue, Jimei Tong, Yari Carlomagno, Yari Carlomagno, Giulia Del Rosso, Giulia Del Rosso, Aishe Kurti, Caroline Y. Jones, Judith A. Dunmore, Monica Castanedes-Casey, Dennis W. Dickson, Dennis W. Dickson, Zbigniew K. Wszolek, John D. Fryer, John D. Fryer, Leonard Petrucelli, Leonard Petrucelli, Mercedes Prudencio, Mercedes Prudencio   +22 more
doaj   +1 more source

E3 ligase Praja1 mediates ubiquitination and degradation of microtubule‐associated protein tau

The FEBS Journal, EarlyView.
E3 ligase Praja1, but not its paralogue Praja2, recognizes and ubiquitinates tau protein for proteasomal degradation. This newly identified function of Praja1‐mediated tau degradation suggests its role in protein quality control, which may provide insights into the pathogenesis of tauopathies.
Shiho Aoki, Wataru Onodera, Akihiko Takashima, Kotaro Kawasaki, Kazuki Imadegawa, Hikaru Kurahashi, Mizuho Oishi, Toru Asahi, Yoshiyuki Soeda   +8 more
wiley   +1 more source

Autophagy and polyglutamine diseases

Progress in Neurobiology, 2012
In polyglutamine diseases, an abnormally elongated polyglutamine tract results in protein misfolding and accumulation of intracellular aggregates. The length of the polyglutamine expansion correlates with the tendency of the mutant protein to aggregate, as well as with neuronal toxicity and earlier disease onset.
Jimenez-Sanchez, Maria, Thomson, Frances, Zavodszky, Eszter, Rubinsztein, David C.   +3 more
openaire   +5 more sources

Noncanonical usage of stop codons in ciliates expands proteins with structurally flexible Q-rich motifs

eLife
Serine(S)/threonine(T)-glutamine(Q) cluster domains (SCDs), polyglutamine (polyQ) tracts and polyglutamine/asparagine (polyQ/N) tracts are Q-rich motifs found in many proteins.
Chi-Ning Chuang, Hou-Cheng Liu, Tai-Ting Woo, Ju-Lan Chao, Chiung-Ya Chen, Hisao-Tang Hu, Yi-Ping Hsueh, Ting-Fang Wang   +7 more
doaj   +1 more source

Conditional deletion of the multiple sclerosis susceptibility gene ATXN1 identifies cell‐autonomous effects in the B‐cell compartment

The FEBS Journal, EarlyView.
Ataxin‐1 is a polyglutamine protein associated with the etiology of spinocerebellar ataxia type 1 (SCA1) that has been recently found implicated in the risk of developing the autoimmune disorder multiple sclerosis (MS). Here, we took a conditional knockout approach to ablate ataxin‐1 exclusively in the B‐cell compartment and we found that this protein ...
Jonathan Jacob Carver, Rachael Riley Denbrock, Cindy Carolina Martines, Alessandro Didonna   +3 more
wiley   +1 more source

Polyglutamines Placed into Context

Neuron, 2003
Nine inherited neurodegenerative disorders result from polyglutamine expansions. Two recently published papers on spinocerebellar ataxia type 1, together with studies on spinobulbar muscular atrophy last year, indicate that host protein context is the key arbiter of polyglutamine disease protein toxicity.
La Spada, Albert R, Taylor, J.Paul
openaire   +2 more sources

Hosting Neurotoxicity in Polyglutamine Disease [PDF]

Cell, 2006
Polyglutamine diseases are caused by an expanded glutamine domain thought to confer a toxic activity onto the respective disease proteins. In this issue, propose that toxicity of the polyglutamine protein Ataxin-1 may not be due to abberant protein interactions mediated by the polyglutamine expansion.
Liu, Nan, Bonini, Nancy M.
openaire   +2 more sources

Redox environment modulates aggregation of ataxin‐3 in vitro — Implications for drug screening of cysteine‐rich proteins

The FEBS Journal, EarlyView.
Redox environment modulates in vitro aggregation of Ataxin‐3, the protein implicated in spinocerebellar ataxia type 3. Reducing conditions stabilize native monomers and prevent aggregation, whereas oxidative conditions promote the formation of non‐native conformers and disulfide‐linked oligomers within the Josephin domain (JD).
Martyna Podlasiak, Martina Sollazzo, Elisa Monaca, Raffaele Sabbatella, Maria Agnese Morando, Oleg Chertkov, Laura Puglisi, Martina Mascellino, Anna Fricano, Sandra Macedo‐Ribeiro, Caterina Alfano   +10 more
wiley   +1 more source

Executive Impairment in Huntington's Disease: Insights From a Systematic Review of the Literature

Brain and Behavior, Volume 16, Issue 2, February 2026.
Executive dysfunction in Huntington's disease follows a selective, stage‐dependent pattern, with early deficits in psychomotor speed, cognitive flexibility, inhibition, and working‐memory updating. Progression is associated with broader impairments in planning and attention.
Simone Migliore, Martina Marcaccio, Ilaria Di Pompeo, Massimo Marano, Giuseppe Curcio   +4 more
wiley   +1 more source