Evidence map›Paper›PMID 29610302›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

Identification of long-lived synaptic proteins by proteomic analysis of synaptosome protein turnover.

Seok Heo, Graham H Diering, Chan Hyun Na, Raja Sekhar Nirujogi, Julia L Bachman, Akhilesh Pandey, Richard L Huganir

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 93 papers.

0numbers the graph read from it
0cells of the map it votes in
93citing papers in PubMed
9.3field-weighted citation impact, top 1% 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

93 citing papers in PubMed, 169 citations in OpenAlex.

  1. Sex- and experience-dependent regulation of synaptic protein turnover.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
  3. Article
  4. Review
  5. Sex and experience dependent regulation of synaptic protein turnover.bioRxiv : the preprint server for biology · 2025
    Article
  6. Review
  7. AnalysisbioRxiv : the preprint server for biology · 2025
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Understanding the molecular diversity of synapses.Nature reviews. Neuroscience · 2025
    Review
  14. Biomarkers Unveiling the Interplay of Mind, Nervous System, and Immunity.Methods in molecular biology (Clifton, N.J.) · 2025
    Review
  15. Article
  16. Article
  17. Article
  18. Developing forebrain synapses are uniquely vulnerable to sleep loss.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  19. Article
  20. Article

33 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

7 authors at 1 institution in 2 countries.

Seok HeoSolomon H. Snyder Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, MD 21205.
Graham H DieringSolomon H. Snyder Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, MD 21205.
Chan Hyun NaDepartment of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205.
Raja Sekhar NirujogiDepartment of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205.
Julia L BachmanSolomon H. Snyder Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, MD 21205.
Akhilesh PandeyDepartment of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205.ORCID 0000-0001-9943-6127
Richard L HuganirSolomon H. Snyder Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, MD 21205; rhuganir@jhmi.edu.
Johns Hopkins University · US

Funding

Understanding Mechanisms of a-synuclein pathologyP50NS038377 · NINDS · JOHNS HOPKINS UNIVERSITY · PI ROSENTHAL, LIANA ISA SHAPIRO · 1998 to 2019
$38.8M
Semaphorin Signaling and Plasticity at the Excitatory SynapseP50MH100024 · NIMH · JOHNS HOPKINS UNIVERSITY · PI HUGANIR, RICHARD L · 2013 to 2017
$9.5M
PDZ DOMAINS AND EXCITATORY SYNAPTIC FUNCTIONR01NS036715 · NINDS · JOHNS HOPKINS UNIVERSITY · PI HUGANIR, RICHARD L · 1997 to 2020
$8.6M
Long-Lived Synaptic ProteinsR01MH112152 · NIMH · JOHNS HOPKINS UNIVERSITY · PI HUGANIR, RICHARD L · 2017 to 2021
$2.9M
Personalized Therapy of Hormone Refractory Breast CancerR01CA184165 · NCI · MAYO CLINIC ROCHESTER · PI PANDEY, AKHILESH · 2015 to 2019
$1.8M
Fourier Transform Orbitrap Fusion Lumos Tribrid Mass Spectrometer with ETDS10OD021844 · OD · JOHNS HOPKINS UNIVERSITY · PI PANDEY, AKHILESH · 2016 to 2016
$1.1M
CIHRNCI NIH HHS R01 CA184165NIH HHS S10 OD021844NIMH NIH HHS P50 MH100024NIMH NIH HHS R01 MH112152NINDS NIH HHS P50 NS038377NINDS NIH HHS R01 NS036715
6 · The paper itself

Abstract

Memory formation is believed to result from changes in synapse strength and structure. While memories may persist for the lifetime of an organism, the proteins and lipids that make up synapses undergo constant turnover with lifetimes from minutes to days. The molecular basis for memory maintenance may rely on a subset of long-lived proteins (LLPs). While it is known that LLPs exist, whether such proteins are present at synapses is unknown. We performed an unbiased screen using metabolic pulse-chase labeling in vivo in mice and in vitro in cultured neurons combined with quantitative proteomics. We identified synaptic LLPs with half-lives of several months or longer. Proteins in synaptic fractions generally exhibited longer lifetimes than proteins in cytosolic fractions. Protein turnover was sensitive to pharmacological manipulations of activity in neuronal cultures or in mice exposed to an enriched environment. We show that synapses contain LLPs that may underlie stabile long-lasting changes in synaptic structure and function.

Indexed as

AnimalsCytosolHalf-LifeLearningMass SpectrometryMemoryMiceNeuronal PlasticityProteinsProteolysisProteomicsSynapsesSynaptosomesProteinsenriched environmentlong-lived proteinsmass spectrometryneuronal activityprotein turnover

Identifiers

PMID29610302
PMCPMC5910858
OpenAlexW2795560655

What OpenQuestion holds

Textmetadata
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.