Results 91 to 100 of about 48,246 (290)

Retention of prions in the polychaete Hediste diversicolor and black soldier fly, Hermetia illucens, larvae after short-term experimental immersion and feeding with brain homogenate from scrapie infected sheep

Heliyon
Finding alternative protein and lipid sources for aquafeeds is crucial for the sustainable growth of fed aquaculture. Upcycling industrial side streams and byproducts using extractive species can reduce waste and help reduce the sector's dependence on ...
Sylvie L. Benestad, Linh Tran, Arne M. Malzahn, Nina S. Liland, Ikram Belghit, Andreas Hagemann   +5 more
doaj   +1 more source

A Phase‐Resolved Geometric Deep Learning Framework Maps Structural Determinants of Disease‐Associated Protein Aggregation and Guides Suppressor Design

Advanced Science, EarlyView.
SKALE 2.0 maps disease‐associated protein aggregation as a phase‐resolved structural process, linking mutation‐induced geometric perturbations to nucleation, elongation, and suppressor design. Across neurodegenerative proteins, the framework reveals cryptic aggregation vulnerabilities, separates phase‐concordant and phase‐switching mutations, and ...
Jia Shen Sio, Wei Xuan Wilson Loo, Yan Shan Loo, Wen Xin Tan, Hui Xuan Lim, Huitao Liu, Chen Seng Ng   +6 more
wiley   +1 more source

Prions in Yeast [PDF]

Genetics, 2012
AbstractThe concept of a prion as an infectious self-propagating protein isoform was initially proposed to explain certain mammalian diseases. It is now clear that yeast also has heritable elements transmitted via protein. Indeed, the “protein only” model of prion transmission was first proven using a yeast prion.
Susan W, Liebman, Yury O, Chernoff
openaire   +2 more sources

Horizontal Transmission of Cytosolic Sup35 Prions by Extracellular Vesicles

mBio, 2016
Prions are infectious protein particles that replicate by templating their aggregated state onto soluble protein of the same type. Originally identified as the causative agent of transmissible spongiform encephalopathies, prions in yeast (Saccharomyces ...
Shu Liu, André Hossinger, J. Hofmann, Philip Denner, I. Vorberg   +4 more
semanticscholar   +1 more source

Structural Polymorphism of polyG Inclusions Revealed by In Situ Cryo‐Electron Tomography

Advanced Science, EarlyView.
Correlative cryo‐electron tomography in primary cortical neurons and NIID mouse brain tissue reveals that polyG inclusions are interconnected ribbon‐like assemblies rather than canonical amyloid fibrils. Multiple compartment‐specific ribbon states show distinct 26S proteasome accessibility, while cytoplasmic ribbons contact and deform ER‐like ...
Yunwen Qian, Yalan Wan, Chen Chen, Xiaoyu Zheng, Wenjing Du, Junhan Yang, Zhihao Quan, Biyu Yang, Jiaxi Yu, Jie Zheng, Zhaoxia Wang, Jianwen Deng, Qiang Guo   +12 more
wiley   +1 more source

Comparing the Folds of Prions and Other Pathogenic Amyloids

Pathogens, 2018
Pathogenic amyloids are the main feature of several neurodegenerative disorders, such as Creutzfeldt–Jakob disease, Alzheimer’s disease, and Parkinson’s disease. High resolution structures of tau paired helical filaments (PHFs), amyloid-
José Miguel Flores-Fernández, Vineet Rathod, Holger Wille   +2 more
doaj   +1 more source

A Phosphorylation‐Induced Micellization Switch in the Low‐Complexity Domain of TDP‐43

Advanced Science, EarlyView.
Phosphorylation of TAR DNA‐binding protein's 43 kDa (TDP‐43) low‐complexity domain by casein kinase 1 delta (CK1δ) acts as a molecular switch, redirecting its self‐assembly from macroscopic phase separation toward finite‐sized, spherical block‐copolymer micelles of ∼30 nm.
Rodrigo F. Dillenburg, Anastasia Lopatina, Hao Ruan, Tom Scheidt, Simone Mosna, Emre Pekbilir, Julia Bieber, Frank Schäfer‐Depoix, Katharina Landfester, Carla Schmidt, Martin M. Möckel, Svenja Morsbach, Friederike Schmid, Dorothee Dormann, Lukas Stelzl, Martin Girard, Edward A. Lemke   +16 more
wiley   +1 more source

Accelerated high fidelity prion amplification within and across prion species barriers.

PLoS Pathogens, 2008
Experimental obstacles have impeded our ability to study prion transmission within and, more particularly, between species. Here, we used cervid prion protein expressed in brain extracts of transgenic mice, referred to as Tg(CerPrP), as a substrate for ...
Kristi M Green, Joaquín Castilla, Tanya S Seward, Dana L Napier, Jean E Jewell, Claudio Soto, Glenn C Telling   +6 more
doaj   +1 more source

Grass plants bind, retain, uptake and transport infectious prions

Cell Reports, 2015
Prions are the protein-based infectious agents responsible for prion diseases. Environmental prion contamination has been implicated in disease transmission. Here we analyzed the binding and retention of infectious prion protein (PrPSc) to plants.
S. Pritzkow, R. Morales, Fabio Moda, Uffaf Khan, G. Telling, E. Hoover, C. Soto   +6 more
semanticscholar   +1 more source

PolyG Fibrils Coalesce Into Nuclear Ribbons That Engage Proteostasis Machinery in Neuronal Intranuclear Inclusion Disease

Advanced Science, EarlyView.
In NIID, expanded NOTCH2NLC repeats give rise to nuclear polyG inclusions. Tracer‐guided in situ cryo‐electron tomography enables cross‐scale structural analysis from mouse brain to native neuronal nuclei, revealing dense‐core/peripheral‐halo inclusions built from compact polyG ribbons.
Hui Dong, Yongcheng Pan, Zhiyao Tang, Yuxuan Yao, Guicong Zhang, Junpu Wang, Haonan Xiao, Yun Tian, Beisha Tang, Dan Li, Qiang Guo, Ruijun Tian, Qiong Liu, Cong Liu   +13 more
wiley   +1 more source