Evidence map›Paper›PMID 39169951›Full record

ReviewFrontiers in molecular neuroscience2024

Human apolipoprotein E glycosylation and sialylation: from structure to function.

Hee-Jung Moon, Yan Luo, Diksha Chugh, Liqin Zhao

Abstract readReview
In one paragraph

Review in Frontiers in molecular neuroscience, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Review
  2. Review
  3. Review
  4. Review
  5. Article
  6. Review
  7. Review
  8. ApoE3 Christchurch and tau interaction as a protective mechanism against Alzheimer's disease.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2025
    Article
  9. Proteomic and metabolic profiling revealsbioRxiv : the preprint server for biology · 2025
    Article
  10. Article
  11. Review
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

4 authors.

Hee-Jung MoonDepartment of Pharmacology and Toxicology, School of Pharmacy, University of Kansas, Lawrence, KS, United States.
Yan LuoDepartment of Pharmacology and Toxicology, School of Pharmacy, University of Kansas, Lawrence, KS, United States.
Diksha ChughDepartment of Pharmacology and Toxicology, School of Pharmacy, University of Kansas, Lawrence, KS, United States.
Liqin ZhaoDepartment of Pharmacology and Toxicology, School of Pharmacy, University of Kansas, Lawrence, KS, United States.

Funding

University of Kansas Alzheimer's Disease Research Center (KU ADRC)P30AG072973 · NIA · UNIVERSITY OF KANSAS MEDICAL CENTER · PI Jaime Perales Puchalt · 2021 to 2026
$25.3M
Reshaping ApoE4 and Alzheimer's Brains with ApoE2R01AG071682 · NIA · UNIVERSITY OF KANSAS LAWRENCE · PI TERUNA J. SIAHAAN, Liqin Zhao · 2022 to 2026
$3.4M
Sporadic Alzheimer's Disease: A Bioenergetic Etiology?R01AG061038 · NIA · UNIVERSITY OF KANSAS LAWRENCE · PI ZHAO, LIQIN · 2019 to 2023
$1.9M
Role of Clusterin in Brain MitochondriaR21AG055964 · NIA · UNIVERSITY OF KANSAS LAWRENCE · PI ZHAO, LIQIN · 2017 to 2018
$587k
ApoE, Energy, and Synaptic V-ATPaseR21AG059177 · NIA · UNIVERSITY OF KANSAS LAWRENCE · PI ZHAO, LIQIN · 2018 to 2019
$406k
NIA NIH HHS P30 AG072973NIA NIH HHS R01 AG061038NIA NIH HHS R01 AG071682NIA NIH HHS R21 AG055964NIA NIH HHS R21 AG059177
6 · The paper itself

Abstract

Human apolipoprotein E (ApoE) was first identified as a polymorphic gene in the 1970s; however, the genetic association of ApoE genotypes with late-onset sporadic Alzheimer's disease (sAD) was only discovered 20 years later. Since then, intensive research has been undertaken to understand the molecular effects of ApoE in the development of sAD. Despite three decades' worth of effort and over 10,000 papers published, the greatest mystery in the ApoE field remains: human ApoE isoforms differ by only one or two amino acid residues; what is responsible for their significantly distinct roles in the etiology of sAD, with ApoE4 conferring the greatest genetic risk for sAD whereas ApoE2 providing exceptional neuroprotection against sAD. Emerging research starts to point to a novel and compelling hypothesis that the sialoglycans posttranslationally appended to human ApoE may serve as a critical structural modifier that alters the biology of ApoE, leading to the opposing impacts of ApoE isoforms on sAD and likely in the peripheral systems as well. ApoE has been shown to be posttranslationally glycosylated in a species-, tissue-, and cell-specific manner. Human ApoE, particularly in brain tissue and cerebrospinal fluid (CSF), is highly glycosylated, and the glycan chains are exclusively attached via an

Indexed as

Alzheimer’s diseaseapolipoprotein E (ApoE)glycosylationposttranslational modification (PTM)sialylation

Identifiers

PMID39169951
PMCPMC11335735

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Registered trials

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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.