Evidence map›Paper›PMID 24484700›Full record

ReviewProgress in molecular biology and translational science2014

Mechanisms of translation control underlying long-lasting synaptic plasticity and the consolidation of long-term memory.

Emanuela Santini, Thu N Huynh, Eric Klann

Abstract readReview
In one paragraph

Review in Progress in molecular biology and translational science, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

73 citing papers in PubMed.

  1. Article
  2. Article
  3. The ISR downstream effector ATF4 promotes mGluR-dependent long-term depression and associated behavior.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Making memories.eLife · 2024
    Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review

13 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

Emanuela SantiniCenter for Neural Science, New York University, New York, USA.
Thu N HuynhCenter for Neural Science, New York University, New York, USA.
Eric KlannCenter for Neural Science, New York University, New York, USA.

Funding

Translation Regulation in Hippocampal LTP and LTDR01NS047384 · NINDS · NEW YORK UNIVERSITY · PI KLANN, ERIC · 2005 to 2020
$5.2M
NINDS NIH HHS R01 NS047384
6 · The paper itself

Abstract

The complexity of memory formation and its persistence is a phenomenon that has been studied intensely for centuries. Memory exists in many forms and is stored in various brain regions. Generally speaking, memories are reorganized into broadly distributed cortical networks over time through systems level consolidation. At the cellular level, storage of information is believed to initially occur via altered synaptic strength by processes such as long-term potentiation. New protein synthesis is required for long-lasting synaptic plasticity as well as for the formation of long-term memory. The mammalian target of rapamycin complex 1 (mTORC1) is a critical regulator of cap-dependent protein synthesis and is required for numerous forms of long-lasting synaptic plasticity and long-term memory. As such, the study of mTORC1 and protein factors that control translation initiation and elongation has enhanced our understanding of how the process of protein synthesis is regulated during memory formation. Herein we discuss the molecular mechanisms that regulate protein synthesis as well as pharmacological and genetic manipulations that demonstrate the requirement for proper translational control in long-lasting synaptic plasticity and long-term memory formation.

Indexed as

Protein BiosynthesisAnimalsHumansLong-Term PotentiationMechanistic Target of Rapamycin Complex 1Memory, Long-TermMultiprotein ComplexesNeuronal PlasticitySignal TransductionTOR Serine-Threonine KinasesMechanistic Target of Rapamycin Complex 1Multiprotein ComplexesTOR Serine-Threonine Kinases4E-BPConsolidationeIF2αeIF4ELong-term potentiationMemorymTORProtein synthesisS6K1

Identifiers

PMID24484700
PMCPMC6019682

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.