Evidence map›Paper›PMID 34304995›Full record

ReviewSeminars in cell & developmental biology2022

eIF2-dependent translation initiation: Memory consolidation and disruption in Alzheimer's disease.

Mauricio M Oliveira, Eric Klann

Open access · greenAbstract readReview
In one paragraph

Review in Seminars in cell & developmental biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.7field-weighted citation impact, top 9% of its field
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

23 citing papers in PubMed, 40 citations in OpenAlex.

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  9. ISR Modulators in Neurological Diseases.Current neuropharmacology · 2025
    Review
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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

2 authors at 1 institution in 1 country.

Mauricio M OliveiraCenter for Neural Science, New York University, New York, NY, USA.
Eric KlannCenter for Neural Science, New York University, New York, NY, USA; NYU Neuroscience Institute, New York University Grossman School of Medicine, New York, NY, USA. Electronic address: ek65@nyu.edu.
New York University · US

Funding

Translational Control in Memory and Brain DisordersR35NS122316 · NINDS · NEW YORK UNIVERSITY · PI Eric Klann · 2021 to 2026
$6.5M
Translation Regulation in Hippocampal LTP and LTDR01NS047384 · NINDS · NEW YORK UNIVERSITY · PI KLANN, ERIC · 2005 to 2020
$5.2M
Reactive Oxygen Species Signaling in the HippocampusR01NS034007 · NINDS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI KLANN, ERIC · 2000 to 2012
$4.2M
eIF2alpha Phosphorylation in Synaptic Plasticity, Memory, and Brain DisordersR37NS034007 · NINDS · NEW YORK UNIVERSITY · PI KLANN, ERIC · 2014 to 2020
$3.3M
OXIDATIVE ACTIVATION OF PKC DURING INDUCTION OF LTPR29NS034007 · NINDS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI KLANN, ERIC · 1995 to 1999
–
NINDS NIH HHS R01 NS034007NINDS NIH HHS R01 NS047384NINDS NIH HHS R29 NS034007NINDS NIH HHS R35 NS122316NINDS NIH HHS R37 NS034007
6 · The paper itself

Abstract

Memory storage is a conserved survivability feature, present in virtually any complex species. During the last few decades, much effort has been devoted to understanding how memories are formed and which molecular switches define whether a memory should be stored for a short or a long period of time. Among these, de novo protein synthesis is known to be required for the conversion of short- to long-term memory. There are a number translational control pathways involved in synaptic plasticity and memory consolidation, including the phosphorylation of the eukaryotic initiation factor 2 alpha (eIF2α), which has emerged as a critical molecular switch for long-term memory consolidation. In this review, we discuss findings pertaining to the requirement of de novo protein synthesis to memory formation, how local dendritic and axonal translation is regulated in neurons, and how these can influence memory consolidation. We also highlight the importance of eIF2α-dependent translation initiation to synaptic plasticity and memory formation. Finally, we contextualize how aberrant phosphorylation of eIF2α contributes to Alzheimer's disease (AD) pathology and how preventing disruption of eIF2-dependent translation may be a therapeutic avenue for preventing and/or restoring memory loss in AD.

Indexed as

Alzheimer DiseaseMemory ConsolidationEukaryotic Initiation Factor-2HumansMemory, Long-TermNeuronal PlasticityPhosphorylationProtein BiosynthesisEukaryotic Initiation Factor-2Alzheimer’s diseaseEIF2αIntegrated stress responseMemory consolidationMRNA translationProtein synthesis

Identifiers

PMID34304995
PMCPMC8782933
OpenAlexW3185499591

What OpenQuestion holds

Textmetadata
LicenceTDM
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.