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#llps — Public Fediverse posts

Live and recent posts from across the Fediverse tagged #llps, aggregated by home.social.

  1. The type I regulatory subunit of #ProteinKinaseA undergoes #LiquidLiquidPhaseSeparation #LLPS to help compartmentalize cAMP. This study shows that this tunes Ca2+ & cAMP oscillations in pancreatic #BetaCells, controlling #insulin secretion & regulating proliferation @PLOSBiology plos.io/4o9onKQ

  2. The type I regulatory subunit of #ProteinKinaseA undergoes #LiquidLiquidPhaseSeparation #LLPS to help compartmentalize cAMP. This study shows that this tunes Ca2+ & cAMP oscillations in pancreatic #BetaCells, controlling #insulin secretion & regulating proliferation @PLOSBiology plos.io/4o9onKQ

  3. The type I regulatory subunit of #ProteinKinaseA undergoes #LiquidLiquidPhaseSeparation #LLPS to help compartmentalize cAMP. This study shows that this tunes Ca2+ & cAMP oscillations in pancreatic #BetaCells, controlling #insulin secretion & regulating proliferation @PLOSBiology plos.io/4o9onKQ

  4. The type I regulatory subunit of #ProteinKinaseA undergoes #LiquidLiquidPhaseSeparation #LLPS to help compartmentalize cAMP. This study shows that this tunes Ca2+ & cAMP oscillations in pancreatic #BetaCells, controlling #insulin secretion & regulating proliferation @PLOSBiology plos.io/4o9onKQ

  5. The type I regulatory subunit of #ProteinKinaseA undergoes #LiquidLiquidPhaseSeparation #LLPS to help compartmentalize cAMP. This study shows that this tunes Ca2+ & cAMP oscillations in pancreatic #BetaCells, controlling #insulin secretion & regulating proliferation @PLOSBiology plos.io/4o9onKQ

  6. Please share …. 🙏
    📣 Very soon, we’ll have an open PhD position starting in fall 2025 — this time not on cilia, but on YAP & TAZ in podocytes and their regulation via LLPS. Interested candidates are welcome to contact us directly.

    Supervision by Inês Cabrita and me, embedded within PodoSigN!
    Within this project, close collab. with Beate Vollenbröker‘s team.

    #Podocyte #Trr422 #Fsgs #Nephrolab #PhdPosition #Biology #Genetics #LLPS #HippoSignaling #phd

    @CECAD
    @cilia

  7. Please share …. 🙏
    📣 Very soon, we’ll have an open PhD position starting in fall 2025 — this time not on cilia, but on YAP & TAZ in podocytes and their regulation via LLPS. Interested candidates are welcome to contact us directly.

    Supervision by Inês Cabrita and me, embedded within PodoSigN!
    Within this project, close collab. with Beate Vollenbröker‘s team.

    #Podocyte #Trr422 #Fsgs #Nephrolab #PhdPosition #Biology #Genetics #LLPS #HippoSignaling #phd

    @CECAD
    @cilia

  8. Please share …. 🙏
    📣 Very soon, we’ll have an open PhD position starting in fall 2025 — this time not on cilia, but on YAP & TAZ in podocytes and their regulation via LLPS. Interested candidates are welcome to contact us directly.

    Supervision by Inês Cabrita and me, embedded within PodoSigN!
    Within this project, close collab. with Beate Vollenbröker‘s team.

    #Podocyte #Trr422 #Fsgs #Nephrolab #PhdPosition #Biology #Genetics #LLPS #HippoSignaling #phd

    @CECAD
    @cilia

  9. Please share …. 🙏
    📣 Very soon, we’ll have an open PhD position starting in fall 2025 — this time not on cilia, but on YAP & TAZ in podocytes and their regulation via LLPS. Interested candidates are welcome to contact us directly.

    Supervision by Inês Cabrita and me, embedded within PodoSigN!
    Within this project, close collab. with Beate Vollenbröker‘s team.

    #Podocyte #Trr422 #Fsgs #Nephrolab #PhdPosition #Biology #Genetics #LLPS #HippoSignaling #phd

    @CECAD
    @cilia

  10. Please share …. 🙏
    📣 Very soon, we’ll have an open PhD position starting in fall 2025 — this time not on cilia, but on YAP & TAZ in podocytes and their regulation via LLPS. Interested candidates are welcome to contact us directly.

    Supervision by Inês Cabrita and me, embedded within PodoSigN!
    Within this project, close collab. with Beate Vollenbröker‘s team.

    #Podocyte #Trr422 #Fsgs #Nephrolab #PhdPosition #Biology #Genetics #LLPS #HippoSignaling #phd

    @CECAD
    @cilia

  11. Two new articles from our lab:

    Calcium-Dependent S100A8 Amyloid Fibril Formation via S100A1-Mediated Transient Interaction pubs.acs.org/doi/10.1021/acsch

    Heterotypic Droplet Formation by Pro-Inflammatory S100A9 and Neurodegenerative Disease-Related α-Synuclein pubs.acs.org/doi/10.1021/acs.b

    #VU #ACS #amyloid #LLPS #science

  12. Liprin-α & RIM form presynaptic liquid phase-separated condensates #LLPS. This Primer explores a @PLOSBiology study of how these assemblies shape #synaptic fidelity and what their disruption might mean in #neurodevelopmental disease. Paper: plos.io/3Tj5CX7 Primer: plos.io/3HTacJ9

  13. Liprin-α & RIM form presynaptic liquid phase-separated condensates #LLPS. This Primer explores a @PLOSBiology study of how these assemblies shape #synaptic fidelity and what their disruption might mean in #neurodevelopmental disease. Paper: plos.io/3Tj5CX7 Primer: plos.io/3HTacJ9

  14. Liprin-α & RIM form presynaptic liquid phase-separated condensates #LLPS. This Primer explores a @PLOSBiology study of how these assemblies shape #synaptic fidelity and what their disruption might mean in #neurodevelopmental disease. Paper: plos.io/3Tj5CX7 Primer: plos.io/3HTacJ9

  15. Liprin-α & RIM form presynaptic liquid phase-separated condensates #LLPS. This Primer explores a @PLOSBiology study of how these assemblies shape #synaptic fidelity and what their disruption might mean in #neurodevelopmental disease. Paper: plos.io/3Tj5CX7 Primer: plos.io/3HTacJ9

  16. Liprin-α & RIM form presynaptic liquid phase-separated condensates #LLPS. This Primer explores a @PLOSBiology study of how these assemblies shape #synaptic fidelity and what their disruption might mean in #neurodevelopmental disease. Paper: plos.io/3Tj5CX7 Primer: plos.io/3HTacJ9

  17. This allows condensate behaviour to respond to different inputs, such as lysine #acetylation in IDRs in other CBP domains. It can help to explain how #transcription factors binding to different regions of CBP differentially regulate CBP activity. #enhancers #generegulation #llps #chromatin #imaging #biochemistry #molecularbiology #CellBiology

  18. This allows condensate behaviour to respond to different inputs, such as lysine #acetylation in IDRs in other CBP domains. It can help to explain how #transcription factors binding to different regions of CBP differentially regulate CBP activity. #enhancers #generegulation #llps #chromatin #imaging #biochemistry #molecularbiology #CellBiology

  19. This allows condensate behaviour to respond to different inputs, such as lysine #acetylation in IDRs in other CBP domains. It can help to explain how #transcription factors binding to different regions of CBP differentially regulate CBP activity. #enhancers #generegulation #llps #chromatin #imaging #biochemistry #molecularbiology #CellBiology

  20. This allows condensate behaviour to respond to different inputs, such as lysine #acetylation in IDRs in other CBP domains. It can help to explain how #transcription factors binding to different regions of CBP differentially regulate CBP activity. #enhancers #generegulation #llps #chromatin #imaging #biochemistry #molecularbiology #CellBiology

  21. This allows condensate behaviour to respond to different inputs, such as lysine #acetylation in IDRs in other CBP domains. It can help to explain how #transcription factors binding to different regions of CBP differentially regulate CBP activity. #enhancers #generegulation #llps #chromatin #imaging #biochemistry #molecularbiology #CellBiology

  22. Check out our new preprint titled "Diverse effects of fluorescent labels on alpha-synuclein condensate formation during liquid-liquid phase separation"

    biorxiv.org/content/10.1101/20

    #LLPS, #vilniusuniversity, #lifesciencescenter #Research

  23. Check out our new preprint titled "Diverse effects of fluorescent labels on alpha-synuclein condensate formation during liquid-liquid phase separation"

    biorxiv.org/content/10.1101/20

    #LLPS, #vilniusuniversity, #lifesciencescenter #Research

  24. Check out our new preprint titled "Diverse effects of fluorescent labels on alpha-synuclein condensate formation during liquid-liquid phase separation"

    biorxiv.org/content/10.1101/20

    #LLPS, #vilniusuniversity, #lifesciencescenter #Research

  25. Check out our new preprint titled "Diverse effects of fluorescent labels on alpha-synuclein condensate formation during liquid-liquid phase separation"

    biorxiv.org/content/10.1101/20

    #LLPS, #vilniusuniversity, #lifesciencescenter #Research

  26. Check out our new preprint titled "Diverse effects of fluorescent labels on alpha-synuclein condensate formation during liquid-liquid phase separation"

    biorxiv.org/content/10.1101/20

    #LLPS, #vilniusuniversity, #lifesciencescenter #Research

  27. Hello Mastodon,

    Our first post is about Liquid-liquid phase separation (LLPS) phenomena, during which proteins form liquid droplets, followed by amyloid aggregation. LLPS is observed in neurodegenerative disorders, cancers and certain cases is related to protein functions in the cell nucleus. Watch below as alpha-synuclein, a protein linked to Parkinson's disease, undergoes LLPS.

    #LLPS #Science #LifeSciencesCenter #VilniusUniversity

  28. Hello Mastodon,

    Our first post is about Liquid-liquid phase separation (LLPS) phenomena, during which proteins form liquid droplets, followed by amyloid aggregation. LLPS is observed in neurodegenerative disorders, cancers and certain cases is related to protein functions in the cell nucleus. Watch below as alpha-synuclein, a protein linked to Parkinson's disease, undergoes LLPS.

    #LLPS #Science #LifeSciencesCenter #VilniusUniversity

  29. Hello Mastodon,

    Our first post is about Liquid-liquid phase separation (LLPS) phenomena, during which proteins form liquid droplets, followed by amyloid aggregation. LLPS is observed in neurodegenerative disorders, cancers and certain cases is related to protein functions in the cell nucleus. Watch below as alpha-synuclein, a protein linked to Parkinson's disease, undergoes LLPS.

    #LLPS #Science #LifeSciencesCenter #VilniusUniversity

  30. Hello Mastodon,

    Our first post is about Liquid-liquid phase separation (LLPS) phenomena, during which proteins form liquid droplets, followed by amyloid aggregation. LLPS is observed in neurodegenerative disorders, cancers and certain cases is related to protein functions in the cell nucleus. Watch below as alpha-synuclein, a protein linked to Parkinson's disease, undergoes LLPS.

    #LLPS #Science #LifeSciencesCenter #VilniusUniversity

  31. Hello Mastodon,

    Our first post is about Liquid-liquid phase separation (LLPS) phenomena, during which proteins form liquid droplets, followed by amyloid aggregation. LLPS is observed in neurodegenerative disorders, cancers and certain cases is related to protein functions in the cell nucleus. Watch below as alpha-synuclein, a protein linked to Parkinson's disease, undergoes LLPS.

    #LLPS #Science #LifeSciencesCenter #VilniusUniversity

  32. Meta-analysis of postsynaptic proteomes reveals 97 poorly studied proteins; @TakeshiKaizuka @ToruTakumi &co find that FAM81A regulates condensation of #postsynaptic proteins via #LLPS to affect the size & function of #synapses #PLOSBiology plos.io/48KDPnO

  33. Meta-analysis of postsynaptic proteomes reveals 97 poorly studied proteins; @TakeshiKaizuka @ToruTakumi &co find that FAM81A regulates condensation of #postsynaptic proteins via #LLPS to affect the size & function of #synapses #PLOSBiology plos.io/48KDPnO

  34. Meta-analysis of postsynaptic proteomes reveals 97 poorly studied proteins; @TakeshiKaizuka @ToruTakumi &co find that FAM81A regulates condensation of #postsynaptic proteins via #LLPS to affect the size & function of #synapses #PLOSBiology plos.io/48KDPnO

  35. Meta-analysis of postsynaptic proteomes reveals 97 poorly studied proteins; @TakeshiKaizuka @ToruTakumi &co find that FAM81A regulates condensation of #postsynaptic proteins via #LLPS to affect the size & function of #synapses #PLOSBiology plos.io/48KDPnO

  36. Meta-analysis of postsynaptic proteomes reveals 97 poorly studied proteins; @TakeshiKaizuka @ToruTakumi &co find that FAM81A regulates condensation of #postsynaptic proteins via #LLPS to affect the size & function of #synapses #PLOSBiology plos.io/48KDPnO

  37. Nuclear localization of #TDP43 is crucial for its function during #RNAprocessing & #neurodegeneration. @AyalaLab1 &co show that #RNAbinding & macromolecular assembly, including via #LLPS, play a central role in TDP-43 nuclear retention #PLOSBiology plos.io/3v372fT

  38. Nuclear localization of #TDP43 is crucial for its function during #RNAprocessing & #neurodegeneration. @AyalaLab1 &co show that #RNAbinding & macromolecular assembly, including via #LLPS, play a central role in TDP-43 nuclear retention #PLOSBiology plos.io/3v372fT

  39. Nuclear localization of #TDP43 is crucial for its function during #RNAprocessing & #neurodegeneration. @AyalaLab1 &co show that #RNAbinding & macromolecular assembly, including via #LLPS, play a central role in TDP-43 nuclear retention #PLOSBiology plos.io/3v372fT

  40. Nuclear localization of #TDP43 is crucial for its function during #RNAprocessing & #neurodegeneration. @AyalaLab1 &co show that #RNAbinding & macromolecular assembly, including via #LLPS, play a central role in TDP-43 nuclear retention #PLOSBiology plos.io/3v372fT

  41. Nuclear localization of #TDP43 is crucial for its function during #RNAprocessing & #neurodegeneration. @AyalaLab1 &co show that #RNAbinding & macromolecular assembly, including via #LLPS, play a central role in TDP-43 nuclear retention #PLOSBiology plos.io/3v372fT

  42. In developing #presynapses, the #ActiveZone structure assembles via liquid-liquid #PhaseSeparation (#LLPS). This study shows that the #kinase SAD-1 phosphorylates the scaffold protein SYD-2/Liprin-α, relieving autoinhibition & triggering LLPS #PLOSBiology plos.io/3Ne6OZg

  43. In developing #presynapses, the #ActiveZone structure assembles via liquid-liquid #PhaseSeparation (#LLPS). This study shows that the #kinase SAD-1 phosphorylates the scaffold protein SYD-2/Liprin-α, relieving autoinhibition & triggering LLPS #PLOSBiology plos.io/3Ne6OZg

  44. In developing #presynapses, the #ActiveZone structure assembles via liquid-liquid #PhaseSeparation (#LLPS). This study shows that the #kinase SAD-1 phosphorylates the scaffold protein SYD-2/Liprin-α, relieving autoinhibition & triggering LLPS #PLOSBiology plos.io/3Ne6OZg

  45. In developing #presynapses, the #ActiveZone structure assembles via liquid-liquid #PhaseSeparation (#LLPS). This study shows that the #kinase SAD-1 phosphorylates the scaffold protein SYD-2/Liprin-α, relieving autoinhibition & triggering LLPS #PLOSBiology plos.io/3Ne6OZg