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ProteomicsPhospho-tyrosine proteomic analysis in Ptprd-meB+/– mice
PTPδ, encoded by PTPRD, is implicated in various neurological, psychiatric, and neurodevelopmental disorders, but the underlying mechanisms remain unclear. PTPδ trans-synaptically interacts with multiple postsynaptic adhesion molecules, which involves its extracellular alternatively spliced mini-exo...
ORGANISM(S): Mus musculus (Mouse) 
2025-04-01 | PXD053554 | Pride
Phospho-tyrosine proteomic analysis Ptprd-meb Lc-ms/ms 
ProteomicsAlternatively spliced mini exon B in PTPRD regulates hippocampal excitatory synapses through trans synaptic PTPRD IL1RAP interaction
PTP?, encoded by PTPRD, is implicated in various neurological, psychiatric, and neurodevelopmental disorders, but the underlying mechanisms remain unclear. PTP? trans-synaptically interacts with multiple postsynaptic adhesion molecules, which involves its extracellular alternatively spliced mini-exo...
ORGANISM(S): Mus Musculus (ncbitaxon:10090) 
2024-06-04 | MSV000094934 | MassIVE
ProteomicsIdentification of PTPD meA splicing variants
Leukocyte common antigen-related receptor protein tyrosine phosphatases (LAR-RPTPs) are evolutionarily conserved presynaptic cell-adhesion molecules that orchestrate multifarious synaptic adhesion pathways. Extensive alternative splicing of LAR-RPTP mRNAs, similar to neurexins, may produce innumerab...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2023-05-08 | MSV000091879 | MassIVE
UnknownSpecification of neural circuit architecture shaped by context-dependent patterned LAR-RPTP microexons.
Not available
S-EPMC10883964 | biostudies-literature
UnknownRemoval of developmentally regulated microexons has a minimal impact on larval zebrafish brain morphology and function.
Not available
S-EPMC12626420 | biostudies-literature
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