Category Ranking
98%
Total Visits
921
Avg Visit Duration
2 minutes
Citations
20
Article Abstract
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10552624 | PMC |
| http://dx.doi.org/10.3389/fmolb.2023.1294465 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Chromatin binding regulates phase behavior and morphology of condensates formed by prion-like domains.
J Mol Biol
August 2025
Department of Biological Sciences, The State University of New York at Buffalo, Buffalo, NY 14260, USA; Department of Physics, The State University of New York at Buffalo, Buffalo, NY 14260, USA. Electronic address:
Many transcription factors (TFs) contain intrinsically disordered regions (IDRs) and are thought to form biomolecular condensates in the nucleus. These proteins can be conceptualized as block co-polymers, with the IDRs driving both homotypic and heterotypic protein-protein interactions and the DNA-binding domain (DBD) mediating heterotypic interactions with chromatin. While in vitro studies have predominantly reported micron-scale, spherical condensates in the absence of chromatin, TF condensates in live cells exhibit strikingly different behavior-adopting diverse, nanoscale, often aspherical morphologies and displaying sub-diffusive dynamics.
View Article and Find Full Text PDFPreface to the Special Issue "History, Biology and Pathobiology of Prions: A Field of Renewed Hopes".
J Neurochem
July 2025
Institute of Medical Biochemistry Leopoldo de Meis and National Institute of Science and Technology for Structural Biology and Bioimaging, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil.
Research in the field of prion diseases has not only shed light on the mechanisms underlying transmissible spongiform encephalopathies (TSEs) but has also influenced the broader understanding of protein misfolding disorders, including Alzheimer's disease (AD), Parkinson's disease (PD), and other tauopathies and synucleinopathies. Although prion diseases are rare and invariably fatal, they have provided an invaluable conceptual framework for the study of age-associated neurodegenerative disorders. On the occasion of the "Prion 2023" meeting in Faro, Portugal, which brought together leading experts in prion biology and neurodegeneration to discuss emerging data and evolving concepts, we put together a special issue on the topic to discuss new structural insights, diagnostic technologies, and the increasing recognition of prion-like mechanisms in a wide range of proteinopathies.
View Article and Find Full Text PDFTunable metastability of condensates reconciles their dual roles in amyloid fibril formation.
Mol Cell
June 2025
Department of Structural Biology, St. Jude Children's Research Hospital, Memphis, TN 38105, USA. Electronic address:
Stress granules form via co-condensation of RNA-binding proteins (RBPs) containing prion-like low-complexity domains (PLCDs) with RNA molecules. Homotypic interactions among PLCDs can drive amyloid fibril formation that is enhanced by amyotrophic lateral sclerosis (ALS)-associated mutations. We report that condensation- versus fibril-driving homotypic interactions are separable for A1-LCD, the PLCD of hnRNPA1.
View Article and Find Full Text PDFSequence-specific interactions determine viscoelasticity and aging dynamics of protein condensates.
Nat Phys
September 2024
Department of Physics, The State University of New York at Buffalo, Buffalo, NY 14260, USA.
Biomolecular condensates are viscoelastic materials. Here, we investigate the determinants of sequence-encoded and age-dependent viscoelasticity of condensates formed by the prion-like low-complexity domain of the protein hnRNP A1 and its designed variants. We find that the dominantly viscous forms of the condensates are metastable Maxwell fluids.
View Article and Find Full Text PDF"Prion-like" seeding and propagation of oligomeric protein assemblies in neurodegenerative disorders.
Front Neurosci
August 2024
Krembil Brain Institute, University Health Network, Toronto, ON, Canada.
Intra- or extracellular aggregates of proteins are central pathogenic features in most neurodegenerative disorders. The accumulation of such proteins in diseased brains is believed to be the end-stage of a stepwise aggregation of misfolded monomers to insoluble cross-β fibrils via a series of differently sized soluble oligomers/protofibrils. Several studies have shown how α-synuclein, amyloid-β, tau and other amyloidogenic proteins can act as nucleating particles and thereby share properties with misfolded forms, or strains, of the prion protein.
View Article and Find Full Text PDF