Neuroscience articles within Nature Chemistry

Featured

  • Article |

    The composition of toxic protein aggregates associated with neurodegenerative diseases is difficult to determine. Now, a method has been developed that can capture amyloid-containing aggregates in human biofluids using a structure-specific chemical dimer. This method—known as amyloid precipitation—enables unbiased determination of the molecular composition and structural features of the in vivo aggregates.

    • M. Rodrigues
    • , P. Bhattacharjee
    •  & D. Klenerman

  • Article |

    SynGAP and PSD-95 are two abundant proteins that form a complex and undergo liquid–liquid phase separation (LLPS) in the postsynaptic density of neurons. Now, O-GlcNAcylation of SynGAP has been found to suppress LLPS of the SynGAP/PSD-95 complex, and O-GlcNAc-dependent LLPS was also shown to be dynamically regulated by the enzymes O-GlcNAc transferase and O-GlcNAcase.

    • Pinou Lv
    • , Yifei Du
    •  & Xing Chen

  • Article |

    The mechanism of nucleation for α-synuclein (α-Syn) aggregation and amyloid formation in Parkinson’s disease is unclear. Now, α-Syn has been shown to undergo liquid–liquid phase separation and a liquid-to-solid-like transition leading to amyloid fibril formation. This raises the possibility that liquid–liquid phase separation is a key pathogenic mechanism behind α-Syn aggregation in Parkinson’s disease.

    • Soumik Ray
    • , Nitu Singh
    •  & Samir K. Maji

  • Article |

    Cholesterol embedded in lipid membranes strongly promotes the aggregation of Aβ42 that is associated with Alzheimer's disease. Now, a kinetic analysis has shown that the mechanism of action responsible for this effect involves the introduction of a heterogeneous nucleation pathway that enhances the primary nucleation rate of Aβ42 aggregation by up to 20-fold.

    • Johnny Habchi
    • , Sean Chia
    •  & Michele Vendruscolo

  • Article |

    The self-propagation of misfolded conformations of tau occurs in neurodegenerative diseases, including Alzheimer's disease. The microtubule-binding region, tau244-372, reproduces much of the aggregation behaviour of tau in cells and animal models. Now, it has been shown that a 31-residue peptide from tau's R3 domain forms a cross-β conformation that efficiently seeds aggregation of tau244-372 in cells.

    • Jan Stöhr
    • , Haifan Wu
    •  & William F. DeGrado

  • News & Views |

    Sensing neuronal activity using fluorescence has many potential advantages over current methods. Now, by taking advantage of photoinduced electron transfer, fluorescent sensors have been developed that allow high-fidelity recording of neural signals in real time.

    • A. Prasanna de Silva

  • Research Highlights |

    Small-molecule microarrays facilitate the search for Alzheimer's disease therapeutics by screening compounds that bind to the amyloid-β peptide.

    • Anne Pichon

  • Thesis |

    As we learn more about the complexities of water, Bruce Gibb argues that organic chemists shouldn't be afraid to take the plunge into aqueous environments.

    • Bruce C. Gibb

Browse broader subjects

Browse narrower subjects

Browse Neuroscience across other nature.com journals