ArticleBiophysical journal2017
Atomistic Insights into Structural Differences between E3 and E4 Isoforms of Apolipoprotein E.
Article in Biophysical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 25 citations in OpenAlex.
- APOE Genotype Difference in the Biphasic Modulation of Amyloid-β Aggregation by Direct Binding and Lowering the Nucleation Barrier.Biomacromolecules · 2025Article
- Domino-like effect of C112R mutation on ApoE4 aggregation and its reduction by Alzheimer's Disease drug candidate.Molecular neurodegeneration · 2023Article
- Extracranial carotid artery atherosclerotic plaque and APOE polymorphisms: a systematic review and meta-analysis.Frontiers in cardiovascular medicine · 2023Article
- Cognitive impairment in long-living adults: a genome-wide association study, polygenic risk score model and molecular modeling of the APOE protein.Frontiers in aging neuroscience · 2023Article
- In Silico Analysis of the Antagonist Effect of Enoxaparin on the ApoE4-Amyloid-Beta (ABiomolecules · 2022Article
- Interpretable artificial intelligence and exascale molecular dynamics simulations to reveal kinetics: Applications to Alzheimer's disease.Current opinion in structural biology · 2022Review
- Review
- APOE in the normal brain.Neurobiology of disease · 2020Review
- Apolipoprotein E particle size is increased in Alzheimer's disease.Alzheimer's & dementia (Amsterdam, Netherlands) · 2019Article
- Association between APOE polymorphisms and lipid profile in Mexican Amerindian population.Molecular genetics & genomic medicine · 2019Article
- Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Among various isoforms of Apolipoprotein E (ApoE), the E4 isoform (ApoE4) is considered to be the strongest risk factor for Alzheimer's disease, whereas the E3 isoform (ApoE3) is neutral to the disease. Interestingly, the sequence of ApoE4 differs from its wild-type ApoE3 by a single amino acid C112R in the 299-amino-acid-long sequence. Hence, the puzzle remains: how a single-amino-acid difference between the ApoE3 and ApoE4 sequences can give rise to structural dissimilarities between the two isoforms, which can potentially lead to functional differences with significant pathological consequences. The major obstacle in addressing this question has been the lack of a 3D atomistic structure of ApoE4 to date. In this work, we resolve the issue by computationally modeling a plausible atomistic 3D structure of ApoE4. Our microsecond-long atomistic simulations elucidate key structural differences between monomeric ApoE3 and ApoE4, which renders ApoE4 thermodynamically less stable, less structured, and topologically less rigid compared to ApoE3. Consistent with an experimental report of the molten globule state of ApoE4, simulations identify multiple partially folded intermediates for ApoE4, which are implicated in the stronger aggregation propensity of ApoE4.
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