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- W2588138461 abstract "The covalent posttranslational modifications of proteins are critical events in signaling cascades that enable cells to efficiently, rapidly and reversibly respond to extracellular stimuli. This is especially important in the CNS where the processes affecting synaptic communication between neurons are highly complex and very tightly regulated. Sumoylation regulates the function and fate of a diverse array of proteins and participates in the complex cell signaling pathways required for cell survival. One of the most complex signaling pathways is synaptic transmission. Correct synaptic function is critical to the working of the brain and its alteration through synaptic plasticity mediates learning, mental disorders and stroke. The investigation of neuronal sumoylation is a new and exciting field and the functional and pathophysiological implications are far-reaching. Sumoylation has already been implicated in a diverse array of neurological disorders. Here we provide an overview of current literature highlighting recent insights into the role of sumoylation in neurodegeneration. In addition we present a brief assessment of drug discovery in the analogous ubiquitin system and extrapolate on the potential for development of novel therapies that might target SUMO-associated mechanisms of neurodegenerative disease." @default.
- W2588138461 created "2017-02-24" @default.
- W2588138461 creator A5029421130 @default.
- W2588138461 creator A5082068871 @default.
- W2588138461 creator A5089948921 @default.
- W2588138461 creator A5090377961 @default.
- W2588138461 date "2017-01-01" @default.
- W2588138461 modified "2023-09-25" @default.
- W2588138461 title "Sumoylation: Implications for Neurodegenerative Diseases" @default.
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