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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Self-citation
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
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