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1999 (v1)PublicationUploaded on: April 14, 2023
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2014 (v1)Publication
Several proteins encoded by PD genes are implicated in synaptic vesicle traffic. Endophilin, a key factor in the endocytosis of synaptic vesicles, was shown to bind to, and be ubiquitinated by, the PD-linked E3 ubiquitin ligase Parkin. Here we report that Parkin's level is specifically upregulated in brain and fibroblasts of endophilin mutant...
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2014 (v1)Publication
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2004 (v1)Publication
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2015 (v1)Publication
Synapsin III (SynIII) is a neuron-specific phosphoprotein that plays a unique role in neuronal development. SynIII is phosphorylated by cAMP-dependent protein kinase (PKA) at a highly conserved phosphorylation site and by cyclin-dependent kinase-5 (Cdk5) at a newly described site. Although SynIII is known to be involved in axon elongation in...
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2003 (v1)Publication
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2014 (v1)Publication
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2013 (v1)Publication
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2013 (v1)Publication
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2013 (v1)Publication
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2007 (v1)Publication
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2004 (v1)Publication
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2012 (v1)Publication
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2009 (v1)Publication
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2004 (v1)Publication
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2014 (v1)Publication
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Uploaded on: April 14, 2023 -
2003 (v1)Publication
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Uploaded on: April 14, 2023 -
2014 (v1)Publication
Synapsins (Syns) are synaptic vesicle (SV)-associated proteins involved in the regulation of synaptic transmission and plasticity, which display a highly conserved ATP binding site in the central C-domain, whose functional role is unknown. Using molecular dynamics simulations, we demonstrated that ATP binding to SynI is mediated by a...
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2000 (v1)Publication
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1997 (v1)Publication
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2004 (v1)Publication
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2015 (v1)Publication
Synapsin III (SynIII) is a phosphoprotein that is highly expressed at early stages of neuronal development. Whereas in vitro evidence suggests a role for SynIII in neuronal differentiation, in vivo evidence is lacking. Here, we demonstrate that in vivo downregulation of SynIII expression affects neuronal migration and orientation. By contrast,...
Uploaded on: April 14, 2023