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</script>doi: 10.1038/nrn961
pmid: 12415293
Post-translational modification by the attachment of ubiquitin seems to have a crucial role in regulating synaptic structure and function. By controlling the stability, activity and localization of target proteins, this versatile regulatory system can shape the pattern, activity and plasticity of synaptic connections. Here, we discuss the myriad ways in which ubiquitin functions to sculpt synapses during development, and to remodel synapses for the acquisition and storage of memory.
Proteasome Endopeptidase Complex, Neuronal Plasticity, Ubiquitin, Cell Membrane, Presynaptic Terminals, Cell Differentiation, Nervous System, Synaptic Transmission, Cysteine Endopeptidases, Protein Transport, Multienzyme Complexes, Animals, Humans
Proteasome Endopeptidase Complex, Neuronal Plasticity, Ubiquitin, Cell Membrane, Presynaptic Terminals, Cell Differentiation, Nervous System, Synaptic Transmission, Cysteine Endopeptidases, Protein Transport, Multienzyme Complexes, Animals, Humans
| citations This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | 147 | |
| popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network. | Top 10% | |
| influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | Top 10% | |
| impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network. | Top 1% |
