Results 71 to 80 of about 49,492 (243)
A Phosphorylation‐Induced Micellization Switch in the Low‐Complexity Domain of TDP‐43
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 +16 more
wiley +1 more source
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 +13 more
wiley +1 more source
Chronic wasting disease (CWD) is a contagious prion disorder affecting cervids such as deer, elk, caribou, and moose, causing progressive and severe neurological degeneration followed by eventual death.
Madeline K. Grunklee +9 more
doaj +1 more source
A Unifying Thermodynamic Model for Phase Separation and Aging of Biopolymers
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 +2 more
wiley +1 more source
Current Challenges of Transcription Compartmentalization Research
Transcription factors, coactivators, and RNA polymerase II assemble into transcription compartments ranging from small, defined complexes to liquid‐like condensates. This review unifies these seemingly competing descriptions along a single continuum and asks what these compartments have been shown to do, and what they have not, revealing that the most ...
Thomas Quail, Sina Wittmann
wiley +1 more source
Yeast Prions and Their Prion-Forming Domain [PDF]
We have learned much about prion biology through the study of yeast prions and their associated PrDs, but caution must be exercised in extrapolating these findings directly to mammalian prion behavior. It must not be forgotten that mammalian PrPSc is an infectious agent that can spread from cell to cell while there is no evidence of cell-to-cell ...
openaire +2 more sources
ABSTRACT This Correspondence is a formal response to the Comment by Dr. Machado regarding our publication “Creatine Promotes Endometriosis by Inducing Ferroptosis Resistance via Suppression of PrP.” We address several conceptual concerns raised in the Comment and clarify the physiological relevance of creatine concentrations, the methodological ...
Siman Chen +6 more
wiley +1 more source
Prion and prion-like diseases in animals
Transmissible spongiform encephalopaties (TSEs) are fatal neurodegenerative diseases characterized by the aggregation and accumulation of the misfolded prion protein in the brain. Other proteins such as β-amyloid, tau or Serum Amyloid-A (SAA) seem to share with prions some aspects of their pathogenic mechanism; causing a variety of so called prion-like
Aguilar-Calvo, Patricia +4 more
openaire +4 more sources
ABSTRACT This study explored the mediating influences of access to social activities, social services, and health and medical services on the relationship between social determinants of health and health‐related quality of life. A survey of 602 adults was conducted in a regional area of Australia.
Candice Oster +4 more
wiley +1 more source
Although misfolded and aggregated α‐synuclein (α‐syn) is recognized in the disease progression of synucleinopathies, its role in the impairment of cortical circuitries and synaptic plasticity remains incompletely understood.
Sonja Blumenstock +6 more
doaj +1 more source

