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Showing 1 to 4 of 4 for “"SV2A"”.

  1. Synaptic vesicle protein 2A-dependent function and dysfunction at the presynapse

    … key SV proteins, synaptic vesicle protein 2A (SV2A) and synaptotagmin I (SYT1), was investigated. SYT1 predominantly acts as the Ca2+ sensor for fast synchronous release at the presynapse, whilst the exact function of SV2A remains unknown to this day. In this study, the ablation of the AP-2 …

    edinburgh Repository record for Synaptic vesicle protein 2A-dependent function and dysfunction at the presynapse (opens in a new tab)

  2. Investigation of the physiological function of TTBK2 (tau tubulin kinase 2), a protein kinase mutated in spinocerebellar ataxia type 11 (SCA11)

    … identified synaptic vesicle glycoprotein 2A (SV2A) as a substrate of TTBK2. Phosphopeptide mapping revealed that SV2A is phosphorylated at two clusters of three highly-conserved residues by TTBK2. These two phosphorylation clusters were then shown to mediate the phospho-dependent interactions …

    dundee Repository record for Investigation of the physiological function of TTBK2 (tau tubulin kinase 2), a protein kinase mutated in spinocerebellar ataxia type 11 (SCA11) (opens in a new tab)

  3. Late stage 18F-difluoromethylation of N-heteroaromatics

    … to the preparation of a novel SV2A PET tracer was performed and shows promising results.

    liege Repository record for Late stage 18F-difluoromethylation of N-heteroaromatics (opens in a new tab)

  4. Identification of the TPC2 interactome reveals TSPAN10 and OCA7 as key players in the biogenesis of melanosomes

    … confirmed several proteins, including PLD1, SV2A, TSPAN10, and OCA7/C10orf11/LRMDA all colocalize highly with TPC2-EGFP, confirming they are new melanosome proteins. In follow-up functional studies, TSPAN10 and OCA7 were confirmed to be involved in pigmentation, with severe melanin depletion …

    colostate Repository record for Identification of the TPC2 interactome reveals TSPAN10 and OCA7 as key players in the biogenesis of melanosomes (opens in a new tab)