International Journal of Biological Macromolecules, Journal Year: 2025, Volume and Issue: unknown, P. 140467 - 140467
Published: Jan. 1, 2025
Language: Английский
International Journal of Biological Macromolecules, Journal Year: 2025, Volume and Issue: unknown, P. 140467 - 140467
Published: Jan. 1, 2025
Language: Английский
Science China Life Sciences, Journal Year: 2024, Volume and Issue: 67(9), P. 1792 - 1832
Published: July 17, 2024
Language: Английский
Citations
4International Journal of Biological Macromolecules, Journal Year: 2025, Volume and Issue: 294, P. 139447 - 139447
Published: Jan. 5, 2025
Language: Английский
Citations
0bioRxiv (Cold Spring Harbor Laboratory), Journal Year: 2025, Volume and Issue: unknown
Published: Jan. 9, 2025
Molecular rotor-based fluorophores (RBFs) that are target-selective and sensitive to both polarity viscosity valuable for diverse biological applications. Here, we have designed next-generation RBFs based on the underexplored bimane fluorophore through either changing in aryl substitution or varying π-linkages between rotatable electron donors acceptors produce red-shifted fluorescence emissions with large Stokes shifts. exhibit a twisted intramolecular charge transfer mechanism enables control of sensitivity, as well target selectivity. These features enable their application in: (1) turn-on fluorescent detection α-synuclein (αS) fibrils, hallmark Parkinson's disease (PD), including amplified fibrils from patient samples; (2) monitoring early misfolding oligomer formation during αS aggregation; (3) selective imaging condensates formed by liquid-liquid phase separation (LLPS). In all three cases, show our probes high levels selectivity versus other aggregating proteins. properties one study interplay tau amyloid aggregation mechanisms underlying neurodegenerative disorders.
Language: Английский
Citations
0Science Advances, Journal Year: 2025, Volume and Issue: 11(4)
Published: Jan. 22, 2025
Distinct tau amyloid assemblies underlie diverse tauopathies but defy rapid classification. Cell and animal experiments indicate functions as a prion, different strains propagated in cells cause unique, transmissible neuropathology after inoculation. Strain amplification requires compatibility of the monomer template. We used cryo–electron microscopy to study one cell-based yellow fluorescent protein (YFP)–tagged strain, resolving its nature. then sequential alanine (Ala) substitution (scan) within repeat domain (RD) measure incorporation preexisting RD-YFP aggregates. This robustly discriminated strains, defining sequences critical for incorporation. created 3R/4R or 4R wild-type RD (amino acids 246 408) biosensors. Ala scan recombinant seeds with Alzheimer’s disease (AD) fold matched that AD homogenate. scanned 22 brain lysates comprising four tauopathies. clustered cases by neuropathological syndrome, revealed role amino protofilament folds, allowed strain discrimination based on acid requirements prion replication.
Language: Английский
Citations
0International Journal of Biological Macromolecules, Journal Year: 2025, Volume and Issue: unknown, P. 140467 - 140467
Published: Jan. 1, 2025
Language: Английский
Citations
0