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UnknownFRET-based Tau seeding assay does not represent prion-like templated assembly of Tau filaments.
Tau aggregation into amyloid fibers based on the cross-beta structure is a hallmark of several Tauopathies, including Alzheimer Disease (AD). Trans-cellular propagation of Tau with pathological conformation has been suggested as a key disease mechanism. This is thought to cause the spreading of Tau ...
S-EPMC7364478 | biostudies-literature
UnknownAnillin facilitates septin assembly to prevent pathological outfoldings of central nervous system myelin.
Myelin serves as an axonal insulator that facilitates rapid nerve conduction along axons. By transmission electron microscopy, a healthy myelin sheath comprises compacted membrane layers spiraling around the cross-sectioned axon. Previously we identified the assembly of septin filaments in the inner...
S-EPMC6344079 | biostudies-literature
UnknownHistidine modulates amyloid-like assembly of peptide nanomaterials and confers enzyme-like activity.
Amyloid-like assembly is not only associated with pathological events, but also leads to the development of novel nanomaterials with unique properties. Herein, using Fmoc diphenylalanine peptide (Fmoc-F-F) as a minimalistic model, we found that histidine can modulate the assembly behavior of Fmoc-F-...
S-EPMC10509148 | biostudies-literature
UnknownTau Filament Self-Assembly and Structure: Tau as a Therapeutic Target.
Tau plays an important pathological role in a group of neurodegenerative diseases called tauopathies, including Alzheimer's disease, Pick's disease, chronic traumatic encephalopathy and corticobasal degeneration. In each disease, tau self-assembles abnormally to form filaments that deposit in the br...
S-EPMC7688747 | biostudies-literature
UnknownStructural basis for lamin assembly at the molecular level.
Nuclear structure and function are governed by lamins, which are intermediate filaments that mostly consist of α-helices. Different lamin assembly models have been proposed based on low resolution and fragmented structures. However, their assembly mechanisms are still poorly understood at the molecu...
S-EPMC6704074 | biostudies-literature
UnknownDirect redox regulation of F-actin assembly and disassembly by Mical.
Different types of cell behavior, including growth, motility, and navigation, require actin proteins to assemble into filaments. Here, we describe a biochemical process that was able to disassemble actin filaments and limit their reassembly. Actin was a specific substrate of the multidomain oxidatio...
S-EPMC3612955 | biostudies-literature
UnknownBeta-sheet assembly of Tau and neurodegeneration in Drosophila melanogaster.
The assembly of Tau into abundant β-sheet-rich filaments characterizes human tauopathies. A pathological pathway leading from monomeric to filamentous Tau is believed to be at the heart of these diseases. However, in Drosophila models of Tauopathy, neurodegeneration has been observed in the absence ...
S-EPMC6327151 | biostudies-literature
UnknownTau filaments are tethered within brain extracellular vesicles in Alzheimer's disease.
The abnormal assembly of tau protein in neurons is a pathological hallmark of multiple neurodegenerative diseases, including Alzheimer's disease (AD). Assembled tau associates with extracellular vesicles (EVs) in the central nervous system of individuals with AD, which is linked to its clearance and...
S-EPMC11706778 | biostudies-literature
Unknownα-Synuclein filaments from transgenic mouse and human synucleinopathy-containing brains are major seed-competent species.
Assembled α-synuclein in nerve cells and glial cells is the defining pathological feature of neurodegenerative diseases called synucleinopathies. Seeds of α-synuclein can induce the assembly of monomeric protein. Here, we used sucrose gradient centrifugation and transiently transfected HEK 293T cell...
S-EPMC7212628 | biostudies-literature
UnknownDeterministic chaos in the self-assembly of β sheet nanotubes from an amphipathic oligopeptide.
The self-assembly of designed peptides into filaments and other higher-order structures has been the focus of intense interest because of the potential for creating new biomaterials and biomedical devices. These peptide assemblies have also been used as models for understanding biological processes,...
S-EPMC8494133 | biostudies-literature
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