Submit site search
  • RAW 264.7 LRRK2 KO + HALO-human LRRK2 + HA-human GABARAP

    By on

    RAW 264.7 LRRK2 KO + HALO-human LRRK2 + HA-human GABARAP cell line

  • Alterations in neurotransmitter co-release in Parkinson’s disease

    By on

    Parkinson's disease involves degeneration of dopamine neurons, leading to basal ganglia circuit changes. These neurons also release glutamate and GABA. Understanding co-release dynamics could help identify circuit dysfunction in Parkinson's disease.

  • Dopamine across timescales and cell types: Relevance for phenotypes in Parkinson’s disease progression

    By on

    Dopamine neurons in the SNc are crucial for movement and learning. In Parkinson's Disease, their degeneration leads to various symptoms. Recent research highlights heterogeneity in these neurons, impacting PD progression and treatment development.

  • Proportion and distribution of neurotransmitter-defined cell types in the ventral tegmental area and substantia nigra pars compacta

    By on

    This is the most complete anatomical description of transmitter-defined cell types across SNc and VTA to date. Emphasizing the heterogeneity within these dopamine-rich regions, 57% of SNc neurons express glutamate or GABA markers, as do 78% in VTA.

  • Role of dopamine neuron activity in Parkinson’s disease pathophysiology

    By on

    Neural activity disruptions in neurodegenerative diseases like Parkinson's may occur early. Abnormal dopamine neuron activity in PD could worsen neurotoxic effects, offering insight for future treatments to protect these neurons.

  • The role of α-synuclein in exocytosis

    By on

    Review focuses on α-synuclein's role in exocytosis, a key process in Parkinson's disease. Despite unclear pathogenesis, evidence points to αsyn's involvement in regulating cellular processes.

  • Live cell Imaging of yeast cells expressing human PINK1-GFP and the TOM complex subunits

    By on

    A protocol for live-cell imaging of yeast cells expressing human PINK1 with GFP tag at the C-terminus as well as all the human TOM complex subunits (TOMs 5, 6, 7, 20, 22, 40 and 70).

  • A proteome-wide quantitative platform for nanoscale spatially resolved extraction of membrane proteins into native nanodiscs

    By on

    The intricate molecular environment of the native membrane profoundly influences every aspect of membrane protein (MP) biology. Despite this, the most prevalent method of studying MPs uses detergent- like molecules that disrupt and remove this vital local membrane context. This severely impedes our ability to quantitatively decipher the local molecular context and comprehend its regulatory role in the structure, function, and biogenesis of MPs. Using a library of membrane-active polymers we have developed a platform for the high-throughput analysis of the membrane proteome. The platform enables near-complete spatially resolved extraction of target MPs directly from their endogenous membranes into native nanodiscs that maintain the local membrane context. We accompany this advancement with an open-access quantitative database that provides the most efficient extraction conditions of 2065 unique mammalian MPs. Our method enables rapid and near-complete extraction and purification of target MPs directly from their endogenous organellar membranes at physiological expression levels while maintaining the nanoscale local membrane environment. Going beyond the plasma membrane proteome, our platform enables extraction from any target organellar membrane including the endoplasmic reticulum, mitochondria, lysosome, Golgi, and even transient organelles such as the autophagosome. To further validate this platform we took several independent MPs and demonstrated how our resource can enable rapid extraction and purification of target MPs from different organellar membranes with high efficiency and purity. Further, taking two synaptic vesicle MPs, we show how the database can be extended to capture multiprotein complexes between overexpressed MPs. We expect these publicly available resources to empower researchers across disciplines to capture membrane ‘nano-scoops’ containing a target MP efficiently and interface with structural, functional, and other bioanalytical approaches. We demonstrate an example of this by combining our extraction platform with single-molecule TIRF imaging to demonstrate how it can enable rapid determination of homo-oligomeric states of target MPs in native cell membranes.

  • Comparative study of enriched dopaminergic neurons from siblings with Gaucher disease discordant for parkinsonism

    By on

    Comparative studies of dopaminergic neurons differentiated from iPSCs derived from siblings with Gaucher disease discordant for parkinsonism provide an avenue to explore genetic modifiers contributing to GBA1-associated parkinsonism.

  • Dysfunction of Motor Cortices in Parkinson’s disease

    By on

    In this review, the authors discuss PD-related changes in frontal cortical motor regions, focusing on neuropathology, changes in neurotransmission, and altered network interactions.

  • Single-Molecule Antibody Slides For Fluorescence Microscopy

    By on

    This protocol describes how to create single-molecule antibody slides for fluorescence microscopy.

  • RASP: A new method for single puncta detection in complex cellular backgrounds_data

    By on

    RASP: A new method for single puncta detection in complex cellular backgrounds_data.

  • pMX-IG-ATG3

    By on

    Expresses untagged ATG3 in mammalian cells.

  • Tetraspeck Bead Imaging V.2

    By on

    Protocol for imaging tetraspeck beads on glass coverslips.

  • RASP: A new method for single puncta detection in complex cellular backgrounds

    By on

    RASP, a bioimaging-segmentation method, excels in detecting fluorescent puncta in complex biological systems by removing false positives and detecting features at various spatial scales.

  • pMX-IG-ATG3 (Y209A)

    By on

    Expresses untagged ATG3 (Y209A) in mammalian cells.

  • pMX-IG-ATG3 (C264A)

    By on

    Expresses untagged ATG3 (C264A) in mammalian cells.

  • pMX-IG-ATG3 (Y210A)

    By on

    Expresses untagged ATG3 (Y210A) in mammalian cells.

  • pMX-IG-ATG3 (R265A)

    By on

    Expresses untagged ATG3 (R265A) in mammalian cells.

  • pMX-IG-ATG3 (T244A)

    By on

    Expresses untagged ATG3 (T244A) in mammalian cells.

Load More