Over 25 years ago, a seminal paper demonstrated that the ubiquitin-proteasome system
(UPS) was involved in activity-dependent synaptic plasticity. Interest in this topic began to …

Over the last 20 years, a number of studies have provided strong support for protein
degradation mediated by the ubiquitin-proteasome system in synaptic plasticity and memory …

The ubiquitin-proteasome pathway (UPP) of protein degradation has many roles in synaptic
plasticity that underlies memory. Work on both invertebrate and vertebrate model systems …

Cellular models of memory formation have focused on the need for protein synthesis.
Recently, evidence has emerged that protein degradation mediated by the ubiquitin …

The ubiquitin-proteasome system (UPS) is a ubiquitous, major pathway of protein
degradation that is involved in most cellular processes by regulating the abundance of …

A proteolytic pathway in which attachment of a small protein, ubiquitin, marks the substrates
for degradation by a multi-subunit complex called the proteasome has been shown to …

Proteolysis by the ubiquitin-proteasome pathway (UPP) has emerged as a new molecular
mechanism that controls wide-ranging functions in the nervous system, including fine-tuning …

A balance of protein synthesis and degradation is critical for the dynamic regulation and
implementation of long-term memory storage. The role of the ubiquitin-proteasome system …

Synaptic Plasticity: Importance of Proteasome-Mediated Protein Turnover: Current Biology Skip
to Main Content Advertisement Current Biology This journal offers authors two options (open …

Synaptic plasticity—the modulation of synaptic strength between a presynaptic terminal and
a postsynaptic dendrite—is thought to be a mechanism that underlies learning and memory …