The DOI matches its Crossref record; 194 of the 194 references it cites were found in a registry or an index.
Apolipoprotein E: Structure-Function Relationships
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In the citing paper
“We identified Gly145Asp and Arg154Cys in the same J o u r n a l P r e -p r o o f region (amino acids ~ 148 to 168) [47]”
From APOE and vascular disease: Sequencing and genotyping in general population cohorts (2023) · cites this paper as [47]
In the citing paper
“Variants predicted by models to be deleterious or being located near or in the receptor binding region (amino acids ~ 148 to 168) [47] could be suspected to pose ε2-like qualities.”
From APOE and vascular disease: Sequencing and genotyping in general population cohorts (2023) · cites this paper as [47]
In the citing paper
“Additional support comes from the present data, where Gly145Asp and Arg154Cys are located in the receptor binding region (amino acids ≈148 to 168) 28 and display a phenotype similar to the ɛ2‐defining Arg176Cys residue with high apoE levels and seemingly low risk of dementia (no events).”
From APOE and dementia – resequencing and genotyping in 105,597 individuals (2020) · cites this paper as [28]
In the citing paper
“Val254Glu and Arg269Gly are located in the lipid‐binding carboxyl‐terminal domain (amino acids ≈243 to 317). 28 , 42”
From APOE and dementia – resequencing and genotyping in 105,597 individuals (2020) · cites this paper as [28]
In the citing paper
“However, the receptor-binding sites (AA136-150) for lipoprotein receptors such as the low-density lipoprotein receptor (LDLR), lipoprotein-related receptor 1 (LRP1), and heparan sulfate proteoglycans (HSPGs) are located in a region conserved between species (Fig. 1a) [11–14].”
From APOE Christchurch enhances a disease-associated microglial response to plaque but suppresses response to tau pathology (2025) · cites this paper as [12]
In the citing paper
“Notably, an HSPG and LDLR binding site in the APOE sequence is conserved in mice (blue boxed area, AA136-150), including arginine 136, which is replaced by serine in the Christchurch (Ch) variant [12, 39].”
From APOE Christchurch enhances a disease-associated microglial response to plaque but suppresses response to tau pathology (2025) · cites this paper as [12]
In the citing paper
“However, mAPOE and hAPOE have a conserved LDLR and HSPG binding motif between AA136 to 150 (human numbering) [11, 12, 39], which includes the R136S Christchurch variant.”
From APOE Christchurch enhances a disease-associated microglial response to plaque but suppresses response to tau pathology (2025) · cites this paper as [12]
In the citing paper
“The mature apoE protein consists of 299 amino acids and an 18amino acid signal peptide is removed post-translationally [17,28].”
From Plasma levels of apolipoprotein E, APOE genotype and risk of dementia and ischemic heart disease: A review (2016) · cites this paper as [28]
In the citing paper
“The APOE gene is located on chromosome 19 and consists of four exons [28].”
From Plasma levels of apolipoprotein E, APOE genotype and risk of dementia and ischemic heart disease: A review (2016) · cites this paper as [28]
In the citing paper
“Lipid-free apoE consists of two domains connected by a “hinge region”: the amino-terminal domain (amino acids 1 to 191) contains the receptor-binding function and the carboxyl-terminal domain (~amino acids 225 to 299) contains the lipid-binding function [28,33].”
From Plasma levels of apolipoprotein E, APOE genotype and risk of dementia and ischemic heart disease: A review (2016) · cites this paper as [28]
In the citing paper
“The low density lipoprotein (LDL) receptor binding region is situated in helix four between amino acids 136 and 150 [17,28].”
From Plasma levels of apolipoprotein E, APOE genotype and risk of dementia and ischemic heart disease: A review (2016) · cites this paper as [28]
In the citing paper
“ApoE2 exhibits a lower affinity to the LDL receptor compared to apoE3: ~1% of the binding activity of apoE3 and apoE4 [28,36].”
From Plasma levels of apolipoprotein E, APOE genotype and risk of dementia and ischemic heart disease: A review (2016) · cites this paper as [28]
In the citing paper
“Furthermore, apoE and apoB share the sequence with highest affinity for arterial proteoglycans, a key phenomenon for lipoprotein deposition in the arterial wall [28,63].”
From Plasma levels of apolipoprotein E, APOE genotype and risk of dementia and ischemic heart disease: A review (2016) · cites this paper as [28]
In the citing paper
“ApoE contains two independently folded functional domains; these are a 22-kDa N-terminal domain (residues 1–191) and a 10-kDa C-terminal domain (residues 216–299) linked by a hinge region (18, 19).”
From Role of the N- and C-Terminal Domains in Binding of Apolipoprotein E Isoforms to Heparan Sulfate and Dermatan Sulfate: A Surface Plasmon Resonance Study (2008) · cites this paper as [18]
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Metadata
- Authors
- Weisgraber, K. H.
- Affiliations
- Gladstone Institutes (US)
- Corresponding author
- Weisgraber, Karl H.
- Venue
- Advances in Protein Chemistry
- Publisher
- Elsevier
- Published
- 1994
- Volume
- 45
- Pages
- 249-302
- ISSN
- 0065-3233 (ISSN-L)
- OpenAlex
- W98152484
- Cited by
- 830
- References
- 194
- Citations by year
- 2026: 16 · 2025: 25 · 2024: 14 · 2023: 17 · 2022: 12 · 2021: 20 · 2020: 12 · 2019: 13 · 2018: 14 · 2017: 20 · 2016: 18 · 2015: 15 · 2014: 18 · 2013: 23 · 2012: 26
- FWCI
- 89.45
- Type
- book chapter
- Language
- en
- Open access
- closed
- Locations
- Advances in protein chemistry (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Heart, Lung, and Blood Institute (HL-41633, P01HL041633)
- Topics
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Lipid metabolism and disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Cholesterol and Lipid Metabolism
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Lipoproteins and Cardiovascular Health
- Keywords
- apolipoprotein E, lipoprotein metabolism, apolipoprotein structure, APOE isoforms, lipid transfer proteins, lipoprotein receptors, triglyceride-rich lipoproteins, reverse cholesterol transport, lipolysis, serum lipoproteins
- MeSH terms
- Amino Acid Sequence, Animals, Apolipoproteins E, Humans, Molecular Sequence Data, Protein Conformation, Structure-Activity Relationship, Lipid Metabolism
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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