Results 61 to 70 of about 4,254,953 (206)

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

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
core  

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

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 protein modulates cellular iron uptake: a novel function with implications for prion disease pathogenesis. [PDF]

PLoS ONE, 2009
Converging evidence leaves little doubt that a change in the conformation of prion protein (PrP(C)) from a mainly alpha-helical to a beta-sheet rich PrP-scrapie (PrP(Sc)) form is the main event responsible for prion disease associated neurotoxicity ...
Ajay Singh, Maradumane L Mohan, Alfred Orina Isaac, Xiu Luo, Jiri Petrak, Daniel Vyoral, Neena Singh   +6 more
doaj   +1 more source

RSF1‐Dependent PAR Turnover Promotes 53BP1 Liquid Condensate Formation at DNA Damage Sites

Advanced Science, EarlyView.
At sites of DNA damage, RSF1 recruits PARG to accelerate PAR turnover, triggering a switch from PAR‐driven condensates to 53BP1 condensates. This condensate transition enables p53‐dependent gene transcription and coordinates the DNA damage response.
Yungyeong Heo, Yonghyeon Kim, Nangyeong Hwang, Gwanho Sung, Sujin Jo, Yeonhu Lee, Ho‐Chul Kang, Jae‐Ho Lee, Yong Won Choi, Hyeseong Cho, Sunwoo Min   +10 more
wiley   +1 more source

Synthetic prions generated in vitro are similar to a newly identified subpopulation of PrPSc from sporadic Creutzfeldt-Jakob disease [PDF]

, 2005
In recent studies, the amyloid form of recombinant prion protein (PrP) encompassing residues 89-230 (rPrP 89-230) produced in vitro induced transmissible prion disease in mice.
Bocharova, O V, Salnikov, V V, Gill, A C, Vadim V. Salnikov, Ilia V. Baskakov, Leonid Breydo, Breydo, L, Olga V. Bocharova, Andrew C. Gill, Baskakov, I V   +9 more
core   +1 more source

Use of bovine recombinant prion protein and real-time quaking-induced conversion to detect cattle transmissible mink encephalopathy prions and discriminate classical and atypical L- and H-Type bovine spongiform encephalopathy. [PDF]

PLoS ONE, 2017
Prions are amyloid-forming proteins that cause transmissible spongiform encephalopathies through a process involving conversion from the normal cellular prion protein to the pathogenic misfolded conformation (PrPSc).
Soyoun Hwang, Justin J Greenlee, Eric M Nicholson   +2 more
doaj   +1 more source

Tau Aggregate Imaging and Transcriptomics of Alzheimer's Disease Brain at Different Stages of Disease

Advanced Science, EarlyView.
The protein aggregates and gene expression in the middle temporal gyrus (MTG) and somatosensory cortex (SOM) of the postmortem brains of 13 Alzheimer's disease patients were studied in detail, revealing that small hyperphosphorylated tau aggregates increase with Braak stage driven by microglial inflammation.
Elizabeth A. English, Dorothea Böken, Matthew W. Cotton, Matthew R. Cheetham, Johanna S. Jackson, Georg Meisl, John S. H. Danial, Paul M. Matthews, Nurun N. Fancy, David Klenerman   +9 more
wiley   +1 more source

A novel, resistance-linked ovine PrP variant and its equivalent mouse variant modulate the in vitro cell-free conversion of rPrP to PrPres [PDF]

, 2006
Prion diseases are associated with the conversion of the normal cellular prion protein, PrPC, to the abnormal, disease-associated form, PrPSc. This conversion can be mimicked in vitro by using a cell-free conversion assay. It has recently been shown that
Kirby, Louise, Manson, Jean C., Houston, Fiona, Goldmann, Wilfred, Gill, Andrew C.   +4 more
core   +1 more source