Results 81 to 90 of about 1,598,142 (264)

Synthesis and structural characterization of a mimetic membrane-anchored prion protein [PDF]

, 2006
During pathogenesis of transmissible spongiform encephalopathies (TSEs) an abnormal form (PrPSc) of the host encoded prion protein (PrPC) accumulates in insoluble fibrils and plaques. The two forms of PrP appear to have identical covalent structures, but
Hicks, M R, David H. Crout, Crout, D H, Teresa J. T. Pinheiro, Ian D. Sylvester, Andrew C. Gill, Imanpreet K. Bath, Atvinder K. Rullay, Gill, A C, Bath, I K, Pinheiro, T J T, Matthew R. Hicks, Sylvester, I D, Rullay, A K   +13 more
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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

Aspects of prion protein dynamics in cell culture models. [PDF]

, 2005
The cell biology of Prion formation and transfer is not well understood. In order to further elucidate the dynamics of PrPc and PrPsc in a cellular context, fusions between Green Fluorescent Protein (GFP) and PrP were constructed and infected/uninfected ...
Landy, Timothy Adam, Landy, T.A.
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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

Yeast Models of Prion-Like Proteins That Cause Amyotrophic Lateral Sclerosis Reveal Pathogenic Mechanisms

Frontiers in Molecular Neuroscience, 2018
Many proteins involved in the pathogenic mechanisms of amyotrophic lateral sclerosis (ALS) are remarkably similar to proteins that form prions in the yeast Saccharomyces cerevisiae. These ALS-associated proteins are not orthologs of yeast prion proteins,
Zachary T. Monahan, Shannon N. Rhoads, Debra S. Yee, Frank P. Shewmaker   +3 more
doaj   +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

The Molecular Pathology of Prion Diseases [PDF]

, 2004
Prion diseases, or transmissible spongiform encephalopathies (TSEs), are a group of invariably fatal neurodegenerative disorders. Uniquely, they may present as sporadic, inherited, or infectious forms, all of which involve conversion of the normal ...
Vassallo, Neville, Herms, Jochen, Kretzschmar, Hans A.   +2 more
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To develop with or without the prion protein [PDF]

Frontiers in Cell and Developmental Biology, 2014
The deletion of the cellular form of the prion protein (PrP(C)) in mouse, goat, and cattle has no drastic phenotypic consequence. This stands in apparent contradiction with PrP(C) quasi-ubiquitous expression and conserved primary and tertiary structures in mammals, and its pivotal role in neurodegenerative diseases such as prion and Alzheimer's ...
Sophie eHalliez, Bruno ePasset, Séverine eMartin-Lannerée, Séverine eMartin-Lannerée, Julia eHernandez-Rapp, Julia eHernandez-Rapp, Hubert eLaude, Sophie eMouillet-Richard, Sophie eMouillet-Richard, Jean-Luc eVilotte, Vincent eBéringue   +10 more
openaire   +5 more sources

A Unifying Thermodynamic Model for Phase Separation and Aging of Biopolymers

Advanced Science, EarlyView.
Phase separation and aging of intrinsically disordered proteins are placed in a unifying framework. A thermodynamically consistent time‐dependent version of associating‐polymer theory shows how the processes are intricately coupled. Assuming aging to occur through interacting sites resulting from reversible conformational transitions, the model ...
Jasper J. Michels, Joana Caria, Edward A. Lemke   +2 more
wiley   +1 more source

Prion degradation pathways: Potential for therapeutic intervention [PDF]

, 2015
Prion diseases are fatal neurodegenerative disorders. Pathology is closely linked to the misfolding of native cellular PrP(C) into the disease-associated form PrP(Sc) that accumulates in the brain as disease progresses. Although treatments have yet to be
McKinnon, C, Tabrizi, SJ, Goold, R
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