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      <image:caption>GFP expressing neurons allow for visualization of dendritic spines within complex neuronal networks</image:caption>
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      <image:caption>Schematic diagrams show published protocols for the generation of midbrain dopamine (mDA) neurons for the potential treatment of Parkinson's disease, striatal neurons for the treatment of Huntington's disease and glial precursors for the treatment of demyelinating disorders. Small molecules and growth factors that are used to direct cell fate are indicated below the arrows; the factors that are induced or inhibited are shown in parentheses. Nature Reviews Genetics (2014) 15:82–92</image:caption>
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      <image:caption>VGAT vesicular transporter in human induced pluriopotent stem cell derived neurons</image:caption>
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      <image:caption>Nature (2010) 465, 704-712 Nature</image:caption>
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      <image:caption>GFP expressing neurons allow for visualization of dendritic spines within complex neuronal networks</image:caption>
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      <image:caption>Schematic diagrams show published protocols for the generation of midbrain dopamine (mDA) neurons for the potential treatment of Parkinson's disease, striatal neurons for the treatment of Huntington's disease and glial precursors for the treatment of demyelinating disorders. Small molecules and growth factors that are used to direct cell fate are indicated below the arrows; the factors that are induced or inhibited are shown in parentheses. Nature Reviews Genetics (2014) 15:82–92</image:caption>
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  </url>
  <url>
    <loc>http://www.neurobiology.ca/resaerch</loc>
    <changefreq>daily</changefreq>
    <priority>0.75</priority>
    <lastmod>2026-08-09</lastmod>
    <image:image>
      <image:loc>https://images.squarespace-cdn.com/content/v1/5319f7a7e4b02dddf759ee70/1718328171048-B50JDN12KEPYFJ4NUUZ3/CorticalVGATt-488Tuj1-5551-1_Maximumintensityprojection_ModifySeries.jpeg</image:loc>
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      <image:title>Research - Make it stand out</image:title>
      <image:caption>BIOMOLECULAR CONDENSATES AND LIQUID-LIQUID PHASE SEPARATION Cells organize many biochemical reactions within biomolecular condensates, dynamic assemblies that form without a surrounding membrane through processes that include liquid-liquid phase separation (LLPS). We investigate how these assemblies organize the presynaptic active zone and how alpha-synuclein alters their formation, material properties and effects on neurotransmission. In parallel, we determine how tau and alpha-synuclein influence chromatin condensates assembled from DNA and associated proteins. Together, these studies define how disease-associated proteins disrupt condensate biology in synaptic and nuclear environments. Fibrillization resulting from the phase transition of condensates from liquid to solid. Liquid-like condensates can undergo maturation into less dynamic, solid-phase assemblies. Specific experimental conditions promote fibril formation within or at the interface of condensates, whereas other condensates remain reversible or follow pathways that are partly independent of fibrillation. Illustration created using Affinity Suite.</image:caption>
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      <image:title>Research - Make it stand out</image:title>
      <image:caption>AMYLOID FIBRILS Amyloid diseases arise when normally soluble proteins misfold and assemble into ordered fibrils, yet the pathways that generate these structures depend on the protein and cellular environment. We investigate how metabolism and membrane binding regulate alpha-synuclein structure and fibril seeding, how alpha-synuclein promotes tau fibril formation, and how transthyretin (TTR) stability controls its transition from a native transport protein to pathogenic amyloid. This comparative program identifies shared principles of fibril formation while preserving the distinct biology of alpha-synuclein, tau and TTR. Schematic illustrating the self-templating of misfolded protein monomers into oligomers and protofibrils that mimic the structure of the original misfolded seed. These protofibrils give rise to fibril “strains” that propagate in neurodegenerative disease (ND). The strain hypothesis proposes that distinct structural strains spread through different brain regions, disrupting local neural networks and giving rise to discrete neurological phenotypes. Thus, strains (i) and (ii) result in different disease subtypes.</image:caption>
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      <image:title>Research - Make it stand out</image:title>
      <image:caption>HUMAN MODELS OF DEVELOPMENT AND DISEASE We develop cerebral organoids and microfluidic systems to evaluate the impact of choroid plexus-secreted factors in neural development, 2D and 3D hiPSC-derived models of neurodegeneration, and hiPSC-derived cardiac models of heart failure and ATTR amyloidosis. hiPSC-derived human neurons from a person with Parkinson’s disease labelled for Tuj1 (purple) and TH (green), showing accumulated hyperphosphorylated alpha-synuclein (red).</image:caption>
    </image:image>
  </url>
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    <lastmod>2024-06-14</lastmod>
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      <image:caption>Hotchkiss Brain Institute, Foothills Medical Centre</image:caption>
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    <lastmod>2026-06-02</lastmod>
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      <image:caption>Whatever it is, the way you tell your story online can make all the difference.</image:caption>
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      <image:caption>Whatever it is, the way you tell your story online can make all the difference.</image:caption>
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  </url>
  <url>
    <loc>http://www.neurobiology.ca/biomolecular-condensates-and-llps</loc>
    <changefreq>daily</changefreq>
    <priority>0.75</priority>
    <lastmod>2026-08-09</lastmod>
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      <image:title>Biomolecular Condensates and LLPS</image:title>
      <image:caption>Neurotransmitter release depends on the precise spatial and temporal organization of the presynaptic active zone. Rather than functioning as a static scaffold, the active zone is assembled through dynamic interactions that concentrate synaptic vesicles, calcium channels and release machinery at defined sites. LLPS provides a mechanism through which these components can organize rapidly while remaining responsive to neuronal activity.</image:caption>
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  <url>
    <loc>http://www.neurobiology.ca/amyloid-fibrils</loc>
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    <lastmod>2026-08-09</lastmod>
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      <image:title>Amyloid Fibrils - Make it stand out</image:title>
      <image:caption>Alpha-synuclein condensates form on the surface of lipid membranes in response to changes in lipid dynamics. (A) TEM images of alpha-synuclein with large unilamellar vesicles (LUVs) show accumulation of the protein at the vesicle surface. (B) Solid-state NMR with increasing phosphatidic acid (PA) indicates that high-affinity membrane interactions are concentrated within the N-terminal region. (C) Proposed model in which membrane binding drives a transition from liquid–lipid to liquid–liquid phase separation and ultimately liquid–solid aggregation; bold segments indicate potential beta-folds.</image:caption>
    </image:image>
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      <image:loc>https://images.squarespace-cdn.com/content/v1/5319f7a7e4b02dddf759ee70/737a7ced-c586-4a14-a248-f0359e1620a3/exec-81e24897-1796-4d09-beb0-934d792519a7.png</image:loc>
      <image:title>Amyloid Fibrils</image:title>
      <image:caption>Transthyretin (TTR) is a transport protein whose native stability is essential to its physiological function. When TTR destabilizes, it can misfold and assemble into amyloid fibrils that accumulate in tissues and contribute to hereditary or age-associated disease. TTR therefore provides a complementary system for determining which principles of amyloid formation are general and which depend on the structure, normal function and tissue context of the aggregating protein. We investigate the molecular conditions that destabilize native TTR, promote the accumulation of monomers and oligomers, and initiate fibril nucleation and growth. Defining this progression may also establish whether non-native TTR species in blood can support earlier diagnosis. Comparing TTR assemblies with alpha-synuclein and tau identifies shared structural principles while preserving the distinct biological context of ATTR amyloidosis. This program makes TTR a mechanistic bridge between amyloid biophysics, neural development and tissue-specific cardiac disease.</image:caption>
    </image:image>
  </url>
  <url>
    <loc>http://www.neurobiology.ca/human-models-of-disease</loc>
    <changefreq>daily</changefreq>
    <priority>0.75</priority>
    <lastmod>2026-08-10</lastmod>
    <image:image>
      <image:loc>https://images.squarespace-cdn.com/content/v1/5319f7a7e4b02dddf759ee70/5706b418-362b-4f3a-995a-cfb9fc24094d/ttr-organoid-csf-pathways-v1.png</image:loc>
      <image:title>Human Models of Disease - Make it stand out</image:title>
      <image:caption>Human neural development depends on coordinated interactions among emerging neural tissues, extracellular signals and barrier-forming structures that cannot be fully reproduced in conventional monolayer cultures. We therefore develop organoid and engineered model systems that reproduce defined features of early human neural development while allowing experimental control over cellular composition and tissue interactions. A central focus is the choroid plexus, a specialized structure that contributes to the environment in which the developing brain forms. We generate organoids that form choroid plexus structures alongside developing neural tissue and use these models to determine how the choroid plexus emerges, how it changes the developmental environment and how TTR influences neural development. Microfluidic platforms complement the organoids by controlling the spatial and temporal interaction of tissues, soluble factors and extracellular environments. Integrating these approaches distinguishes the physiological role of TTR during development from its later association with amyloid disease and provides experimental access to developmental relationships that are difficult to isolate in conventional culture.</image:caption>
    </image:image>
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      <image:loc>https://images.squarespace-cdn.com/content/v1/5319f7a7e4b02dddf759ee70/2e3b4964-5b2c-41b4-a7d1-e1c05dac6599/Human+models.jpg</image:loc>
      <image:title>Human Models of Disease - Make it stand out</image:title>
      <image:caption>PD neurons exhibit greater pathology and larger aggregates when cultured for extended periods in either 3D organoids or following cell engraftment. a–c, Organoids derived from A53T and WT hESCs stained for MAP2 (a, neurons), TH (b, dopaminergic neurons) and pS129 α-synuclein (c). d–e, A53T hiPSCs were grafted into the putamen of 6-week-old NOD scid gamma (NSG) mice. At 120 days post-engraftment, sections were stained for human nuclear antigen (HNA) and TH (d). Antibodies specific for human α-synuclein (h-α-syn) were co-stained with pS129 (e). f, PD tissue immunolabeled for α-synuclein shows Lewy bodies in the amygdala and cortex. g, Organoid and engraftment models show aggregates similar in size to Lewy bodies.</image:caption>
    </image:image>
    <image:image>
      <image:loc>https://images.squarespace-cdn.com/content/v1/5319f7a7e4b02dddf759ee70/08c81f58-ef1f-4261-9142-5d9071e9c59a/cardiac-attr-organ-on-chip-v3.png</image:loc>
      <image:title>Human Models of Disease - Make it stand out</image:title>
      <image:caption>Heart failure is a complex endpoint produced by convergent changes in metabolism, contractile function and tissue homeostasis. Transthyretin amyloid cardiomyopathy adds a distinct protein-assembly mechanism in which misfolded TTR accumulates within the heart and contributes to progressive dysfunction. Human induced pluripotent stem cell-derived cardiac models provide a defined system in which these mechanisms can be examined in a relevant human genetic and cellular context. We develop hiPSC-derived cardiac models that reproduce defined cellular features of heart failure and allow us to determine how metabolic dysfunction, cellular stress and impaired contractile organization interact within human cardiomyocytes. In parallel, we investigate how TTR amyloid alters cardiomyocyte structure, metabolism and function. Integrating molecular and cellular measurements with functional assessment establishes when metabolic or protein-homeostasis deficits emerge and how they relate to impaired cardiac performance. Together, these models define how metabolic and amyloid mechanisms converge in heart failure and ATTR cardiomyopathy.</image:caption>
    </image:image>
  </url>
  <url>
    <loc>http://www.neurobiology.ca/platforms</loc>
    <changefreq>daily</changefreq>
    <priority>0.75</priority>
    <lastmod>2026-08-10</lastmod>
  </url>
</urlset>

