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Related Concept Videos

Long-term Potentiation01:35

Long-term Potentiation

Long-term potentiation, or LTP, is one of the ways by which synaptic plasticity—changes in the strength of chemical synapses—can occur in the brain. LTP is the process of synaptic strengthening that occurs over time between pre- and postsynaptic neuronal connections. The synaptic strengthening of LTP works in opposition to the synaptic weakening of long-term depression (LTD) and together are the main mechanisms that underlie learning and memory.
Long-term Potentiation01:25

Long-term Potentiation

Long-term potentiation, or LTP, is one of the ways by which synaptic plasticity—changes in the strength of chemical synapses—can occur in the brain. LTP is the process of synaptic strengthening that occurs over time between pre and postsynaptic neuronal connections. The synaptic strengthening of LTP works in opposition to the synaptic weakening of long-term depression (LTD) and together are the main mechanisms that underlie learning and memory.
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LTP can occur when presynaptic neurons...
Long-term Depression01:03

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Long-term depression, or LTD, is one of the ways by which synaptic plasticity—changes in the strength of chemical synapses—can occur in the brain. LTD is the process of synaptic weakening that occurs over time between pre and postsynaptic neuronal connections. The synaptic weakening of LTD works in opposition to synaptic strengthening by long-term potentiation (LTP) and together are the main mechanisms that underlie learning and memory.
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If over time, all...
Long-term Depression01:05

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Long-term depression, or LTD, is one of the ways by which synaptic plasticity—changes in the strength of chemical synapses—can occur in the brain. LTD is the process of synaptic weakening that occurs over time between pre and postsynaptic neuronal connections. The synaptic weakening of LTD works in opposition to synaptic strengthening by long-term potentiation (LTP) and together are the main mechanisms that underlie learning and memory.
Amyloid Fibrils03:03

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Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
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Related Experiment Video

Updated: Jul 11, 2026

Improved Preparation and Preservation of Hippocampal Mouse Slices for a Very Stable and Reproducible Recording of Long-term Potentiation
09:39

Improved Preparation and Preservation of Hippocampal Mouse Slices for a Very Stable and Reproducible Recording of Long-term Potentiation

Published on: June 26, 2013

Altered protein synthesis is a trigger for long-term memory formation.

Eric Klann1, J David Sweatt

  • 1Center for Neural Science, New York University, New York, NY, USA. eklann@cns.nyu.edu

Neurobiology of Learning and Memory
|October 9, 2007
PubMed
Summary

New protein synthesis, specifically altered neuronal translation patterns, is proposed as a trigger for memory consolidation and stabilization. This model suggests a minimal, requisite role for specific protein alterations in long-term memory formation.

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Last Updated: Jul 11, 2026

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09:39

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Quantifying Subcellular Ubiquitin-proteasome Activity in the Rodent Brain
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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Cognitive Science

Background:

  • The necessity of new protein synthesis for memory formation and storage remains debated.
  • Existing models often lack precise definitions for the role of protein synthesis in memory.

Purpose of the Study:

  • To present a contemporary model for the role of altered protein synthesis in memory formation and stabilization.
  • To clarify the specific mechanisms by which protein translation contributes to memory consolidation.

Main Methods:

  • Review and synthesis of existing experimental data on protein synthesis and memory.
  • Theoretical modeling of protein synthesis's role in memory engram initialization and perpetuation.

Main Results:

  • Proposes that specific alterations in neuronal protein translation patterns initiate long-term memory formation.
  • Suggests a positive feedback mechanism perpetuates these altered protein expression patterns locally.
  • Highlights a critical initial time window for specific protein translation in engram initialization.

Conclusions:

  • The presented model posits altered protein synthesis as a requisite trigger for memory consolidation.
  • Specific, localized protein translation changes, not general synthesis, are key.
  • Available data support this model's role for protein synthesis in memory.