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#dyrk1a — Public Fediverse posts

Live and recent posts from across the Fediverse tagged #dyrk1a, aggregated by home.social.

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  1. One Compound Repairs Neurons with Autism Mutations

    Summary: Because autism spectrum disorder (ASD) is linked to over 100 different genes, a “one-size-fits-all” medication has proven…
    #NewsBeep #News #Health #ASD #autismspectrumdisorder #Dyrk1A #GB #Genetics #Levocarnitine #neuropharmacology #Neuroscience #SCN2A #UK #UnitedKingdom #Yale
    newsbeep.com/uk/523092/

  2. One Compound Repairs Neurons with Autism Mutations

    Summary: Because autism spectrum disorder (ASD) is linked to over 100 different genes, a “one-size-fits-all” medication has proven…
    #NewsBeep #News #US #USA #UnitedStates #UnitedStatesOfAmerica #Health #ASD #autismspectrumdisorder #Dyrk1A #Genetics #Levocarnitine #neuropharmacology #Neuroscience #SCN2A #Yale
    newsbeep.com/us/573489/

  3. α⧸ω ST & Y phosphorylation diagrams for human & mouse dual specificity tyrosine phosphorylation regulated kinase 1A (#DYRK1A:p). Both species have similar patterns of phosphorylation, including a high occupancy Y+phosphoryl acceptor on an unstructured loop inside their central protein kinase domains.

  4. α⧸ω ST & Y phosphorylation diagrams for human & mouse dual specificity tyrosine phosphorylation regulated kinase 1A (#DYRK1A:p). Both species have similar patterns of phosphorylation, including a high occupancy Y+phosphoryl acceptor on an unstructured loop inside their central protein kinase domains.

  5. α⧸ω ST & Y phosphorylation diagrams for human & mouse dual specificity tyrosine phosphorylation regulated kinase 1A (#DYRK1A:p). Both species have similar patterns of phosphorylation, including a high occupancy Y+phosphoryl acceptor on an unstructured loop inside their central protein kinase domains.

  6. α⧸ω ST & Y phosphorylation diagrams for human & mouse dual specificity tyrosine phosphorylation regulated kinase 1A (#DYRK1A:p). Both species have similar patterns of phosphorylation, including a high occupancy Y+phosphoryl acceptor on an unstructured loop inside their central protein kinase domains.