Results 81 to 90 of about 33,090 (271)

Functional disruption of the prion protein gene in cloned goats

Journal of General Virology, 2006
The cellular prion protein (PrPC), a membrane glycoprotein anchored to the outer surface of neurons, lymphocytes and other cells, is associated directly with the pathogenesis of the transmissible spongiform encephalopathies (TSEs) occurring mainly in humans, cattle, sheep and goats.
Guohua, Yu, Jianquan, Chen, Huiqing, Yu, Siguo, Liu, Juan, Chen, Xujun, Xu, Hongying, Sha, Xufeng, Zhang, Guoxiang, Wu, Shaofu, Xu, Guoxiang, Cheng   +10 more
openaire   +2 more sources

p300 Degradation by the p53‐SIAH1 Axis Relieves TBK1 Acetylation to Enhance Innate Antiviral Immunity

Advanced Science, EarlyView.
This study identifies p300 as the acetyltransferase that acetylates TBK1 and inhibits its phosphorylation. Activation of the p53‐SIAH1 axis by immune response downregulates p300 expression to sustain innate antiviral immunity. Conditional p300 knockout in alveolar epithelial cells in vivo promotes antiviral responses and suppresses virus replication ...
Huidi Yu, Zhihao Zhan, Xiaoxiang Pan, Xinyue Zhang, Penggang Liu, Jing Sun, Xiulong Xu   +6 more
wiley   +1 more source

Dissection and design of yeast prions. [PDF]

, 2004
Many proteins can misfold into beta-sheet-rich, self-seeding polymers (amyloids). Prions are exceptional among such aggregates in that they are also infectious.
Cox Brian S, Lev Z Osherovich (26522), Lev Z Osherovich, Cox, Brian S., Mick F Tuite, Brian S Cox (26523), Osherovich Lev Z, Tuite, Mick F., Osherovich, Lev Z., Jonathan S Weissman (23734), Brian S Cox, Mick F Tuite (26524), Jonathan S Weissman, Weissman, Jonathan S., Tuite Mick F, Weissman Jonathan S   +15 more
core   +1 more source

Prion protein gene polymorphisms in natural goat scrapie

Journal of General Virology, 2002
A total of 51 goats, including seven clinical cases, from the first herd in Greece reported to have scrapie was examined to discern an association between scrapie susceptibility and polymorphisms of the gene encoding the prion protein (PrP). Each animal was evaluated for clinical signs of the disease, histopathological lesions associated with scrapie ...
Charalambos, Billinis, Cynthia H, Panagiotidis, Vassilios, Psychas, Stamatis, Argyroudis, Anna, Nicolaou, Sotirios, Leontides, Orestis, Papadopoulos, Theodoros, Sklaviadis   +7 more
openaire   +2 more sources

TDP‐43 Aggregation: The Healthy‐Toxic Balance of the Prion‐Like Domain

Advanced Science, EarlyView.
TDP‐43 function relies on a delicate balance between reversible phase‐separated states and irreversible aggregation. Under physiological conditions, TDP‐43 forms dynamic droplets and oligomers that support normal cellular functions. In pathological contexts, this balance shifts toward aberrant aggregation, leading to toxic species.
Luca Zangrando, Emanuele Buratti, Francesca Paron   +2 more
wiley   +1 more source

Different isoforms of the non-integrin laminin receptor are present in mouse brain and bind PrP [PDF]

, 2003
The prion protein (PrP) plays a central role in prion diseases, and identifying its cellular receptor appears to be of crucial interest. We previously showed in the yeast twohybrid system that PrP interacts with the 37 kDa precursor (LRP) of the high ...
S. Weiss, J.-P. Deslys, Weiss, S., D. Dormont, Simoneau, S., S. Simoneau, Deslys, J.-P., Lasmézas, C., S. Haïk, C. Leucht, Haik, S., Leucht, C., Dormont, D., C. Lasmézas   +13 more
core   +1 more source

Bioinformatic Analysis of Deleterious Non-Synonymous Single Nucleotide Polymorphisms (nsSNPs) in the Coding Regions of Human Prion Protein Gene (PRNP) [PDF]

Journal of Advanced Biomedical Sciences, 2016
Background & Objective: Single nucleotide polymorphisms are the cause of genetic variation to living organisms. Single nucleotide polymorphisms alter residues in the protein sequence.
Kourosh Bamdad, Fatemeh Rahimi Gharemirshamlu, Sirous Naeimi   +2 more
doaj   +2 more sources

Dopaminergic neurodegeneration in Gerstmann–Sträussler–Scheinker (P102L) disease: insights from imaging and pathological examination

Frontiers in Neurology
Gerstmann–Sträussler–Scheinker (GSS) disease is an inherited prion disease characterized by dementia, cerebellar ataxia, and painful sensory disturbances.
Ken-Ichi Irie, Ken-Ichi Irie, Hiroyuki Honda, Takahisa Tateishi, Shinichiro Mori, Shinichiro Mori, Akifumi Yamamoto, Makoto Morimitsu, Kikuchi Shinsuke, Taiga Moritaka, Seiji Kurata, Hiroyuki Kumazoe, Masahiro Shijo, Masahiro Shijo, Naokazu Sasagasako, Takayuki Taniwaki   +15 more
doaj   +1 more source

Interaction networks of prion, prionogenic and prion-like proteins in budding yeast, and their role in gene regulation. [PDF]

PLoS ONE, 2014
Prions are transmissible, propagating alternative states of proteins. Prions in budding yeast propagate heritable phenotypes and can function in large-scale gene regulation, or in some cases occur as diseases of yeast.
Djamel Harbi, Paul M Harrison
doaj   +1 more source

Equine models in translational medicine: A comparative approach to human health

Animal Models and Experimental Medicine, EarlyView.
This diagram summarizes and contrasts rodent and equine models, outlining their strengths, limitations, and applications. Horses offer naturally occurring diseases, genetic and physiological similarities to humans, and suitability for longitudinal and clinical‐scale studies.
Shayan Boozarjomehri Amnieh, Katarzyna Ropka‐Molik   +1 more
wiley   +1 more source