The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Model of Biologically Active Apolipoprotein E Bound to Dipalmitoylphosphatidylcholine
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
As DPPC lipidation results in small particles, typically of the size referred to as "lipid-poor" ApoE, this conformation may reflect nascent ApoE prior to further lipidation by ABCA1.
“As DPPC lipidation results in small particles, typically of the size referred to as “lipid-poor” ApoE, this conformation may reflect nascent ApoE prior to further lipidation by ABCA1 [17, 25, 57, 58].”
From ApoE lipoproteins in the central nervous system under homeostasis and role in Alzheimer’s disease and related disorders (2026) · cites this paper as [57]
The paper’s summary of the diffraction analysis (Figure 5, page unavailable) describes apoE4–DPPC particles with a diameter of 60.8 Å, supporting the small-particle premise. Our copy does not call them “lipid-poor” or relate their conformation to nascent apoE or further lipidation by ABCA1. (LLM, conf=0.85)
Experimental — accuracy not yet measuredComparing recombinant ApoE lipidated with either DPPC or DMPC showed that particles made with DMPC had higher affinity to LDLR than particles made with DPPC.
“Comparing recombinant ApoE lipidated with either DPPC or DMPC showed that particles made with DMPC had higher affinity to LDLR than particles made with DPPC [57].”
From ApoE lipoproteins in the central nervous system under homeostasis and role in Alzheimer’s disease and related disorders (2026) · cites this paper as [57]
The LDLR-binding Activity section reports a competition assay comparing apoE4–DPPC particles with apoE–DMPC and says the DPPC particles bind LDLR with high affinity. The Figure 1 caption says DPPC particles are expected to have lower binding activity because they carry two apoE molecules per particle versus four for DMPC; it does not establish that DMPC itself confers higher LDLR affinity. (LLM, conf=0.84)
Experimental — accuracy not yet measuredThe increased binding of ApoE to LDLR compared to LDL is attributable to stoichiometry.
“For illustration, the increased binding of ApoE to LDLR compared to LDL is attributable to stoichiometry.”
From ApoE lipoproteins in the central nervous system under homeostasis and role in Alzheimer’s disease and related disorders (2026) · cites this paper as [57]
The Figure 1 caption says that the number of apoE molecules per phospholipid particle influences LDLR binding: particles with four apoE molecules are expected to bind more strongly than those with two. It does not attribute stronger LDLR binding by apoE than by LDL to stoichiometry; LDL is used in the binding assay as a competitor, not evaluated in that comparison. No page number is available in our copy. (LLM, conf=0.84)
Experimental — accuracy not yet measuredNascent ApoE secreted by astrocytes which typically contain two ApoE per particle would have lower avidity to LDLR than more mature particles.
“This would suggest that nascent ApoE secreted by astrocytes which typically contain two ApoE per particle would have lower avidity to LDLR than more mature particles [17, 57].”
From ApoE lipoproteins in the central nervous system under homeostasis and role in Alzheimer’s disease and related disorders (2026) · cites this paper as [57]
The Figure 1 section says that apoE–DPPC particles with two apoE molecules are expected to have lower LDLR-binding activity than apoE–DMPC particles with four. The LDLR-binding Activity section identifies the two-apoE particles as an experimental apoE4–DPPC preparation. Our copy does not establish that astrocyte-secreted nascent particles typically contain two apoE molecules or compare nascent with mature particles. (LLM, conf=0.86)
Experimental — accuracy not yet measuredThere is a stepwise increase in LpE affinity with the number of ApoE proteins per particle.
“This leads to a stepwise increase in LpE affinity with the number of ApoE proteins per particle [57].”
From ApoE lipoproteins in the central nervous system under homeostasis and role in Alzheimer’s disease and related disorders (2026) · cites this paper as [57]
The Figure 1 LDLR-binding passage says that the number of apoE molecules per particle influences receptor-binding activity and predicts lower activity for particles with two apoE molecules than for those with four. It does not establish a stepwise increase in affinity across successive apoE counts; the two particle types also contain different phospholipids. No page number is available in our copy. (LLM, conf=0.86)
Experimental — accuracy not yet measured
Resolution of this model was limited to around 10Å.
“However, resolution of this model was limited to around 10Å.”
From ApoE lipoproteins in the central nervous system under homeostasis and role in Alzheimer’s disease and related disorders (2026) · cites this paper as [57]
In this model, the helical domains self-associate and form a semicircular arc around the spheroidal particle.
“In this model, the helical domains self-associate and form a semicircular arc around the spheroidal particle.”
From ApoE lipoproteins in the central nervous system under homeostasis and role in Alzheimer’s disease and related disorders (2026) · cites this paper as [57]
X-ray crystallography of DPPC lipidated ApoE revealed that ApoE was present in a spheroidal particle and proposed a "horseshoe" conformation of ApoE.
“Studies using X-ray crystallography of dipalmitoylphosphatidylcholine (DPPC) lipidated ApoE revealed that ApoE was present in a spheroidal particle and proposed a “horseshoe” conformation of ApoE [57, 58].”
From ApoE lipoproteins in the central nervous system under homeostasis and role in Alzheimer’s disease and related disorders (2026) · cites this paper as [57]
It is unclear if the crystallization procedure altered the structure of the lipoprotein as a result of the crystal packing.
“It is also unclear if the crystallization procedure altered the structure of the lipoprotein as a result of the crystal packing.”
From ApoE lipoproteins in the central nervous system under homeostasis and role in Alzheimer’s disease and related disorders (2026) · cites this paper as [57]
The Experimental Procedures describe crystallization, and the particle-scattering discussion says the crystals dissolve into particles similar in size to those used to form them. Neither passage addresses whether crystal packing altered the lipoprotein’s structure; searches for packing-induced changes found no passage that does. (LLM, conf=0.70)
Experimental — accuracy not yet measuredThe degree and type of lipidation also impacts binding of ApoE to its receptors.
“The degree and type of lipidation also impacts binding of ApoE to its receptors.”
From ApoE lipoproteins in the central nervous system under homeostasis and role in Alzheimer’s disease and related disorders (2026) · cites this paper as [57]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Apolipoprotein E polymorphism and atherosclerosis.
Davignon, J., Gregg, R. E., & Sing, C. F. (1988) · Arteriosclerosis: An Official Journal of the American Heart Association, Inc. · doi:10.1161/01.atv.8.1.1 · Cited by 1,981
Apolipoprotein E: Structure-Function Relationships
Weisgraber, K. H. (1994) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60642-7 · Cited by 830
Self-citationThree-Dimensional Structure of the LDL Receptor-Binding Domain of Human Apolipoprotein E
Wilson, C., Wardell, M. R., Weisgraber, K. H., Mahley, R. W., & Agard, D. A. (1991) · Science · doi:10.1126/science.2063194 · Cited by 678
Self-citationWeisgraber, K. H. (1990) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)42621-5 · Cited by 304
Self-citationAggerbeck, L. P., Wetterau, J. R., Weisgraber, K. H., Wu, C. S., & Lindgren, F. T. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)68779-4 · Cited by 229
Self-citation
Flagged first, then by citations
Research works printed but not linked: 34
- Segrest, 2001, J. Lipid Res., 42, 1346, 10.1016/S0022-2275(20)30267-4 · DOI
- Mahley, 1988, Science, 240, 622, 10.1126/science.3283935 · DOI · Paper page
- Weisgraber, 1996, FASEB J., 10, 1485, 10.1096/fasebj.10.13.8940294 · DOI
- Saunders, 1993, Neurology, 43, 1467, 10.1212/WNL.43.8.1467 · DOI · Paper page
- Corder, 1993, Science, 261, 921, 10.1126/science.8346443 · DOI · Paper page
- Strittmatter, 1995, Proc. Natl. Acad. Sci. U. S. A., 92, 4725, 10.1073/pnas.92.11.4725 · DOI
- Mayeux, 1995, Neurology, 45, 555, 10.1212/WNL.45.3.555 · DOI · Paper page
- Slooter, 1997, J. Am. Med. Assoc., 277, 818, 10.1001/jama.1997.03540340052032 · DOI
- Fazekas, 2000, J. Neurol. Neurosurg. Psychiatry, 69, 25, 10.1136/jnnp.69.1.25 · DOI
- Drory, 2001, J. Neurol. Sci., 190, 17, 10.1016/S0022-510X(01)00569-X · DOI
- Eichner, 2002, Am. J. Epidemiol., 155, 487, 10.1093/aje/155.6.487 · DOI · Paper page
- Nolte, 1992, Biophys. J., 63, 1221, 10.1016/S0006-3495(92)81698-3 · DOI
- Segrest, 1992, J. Lipid Res., 33, 141, 10.1016/S0022-2275(20)41536-6 · DOI
- Innerarity, 1979, J. Biol. Chem., 254, 4186, 10.1016/S0021-9258(18)50713-4 · DOI · Paper page
- Lu, 2000, J. Biol. Chem., 275, 20775, 10.1074/jbc.M003508200 · DOI · Paper page
- Morrow, 1999, Protein Expr. Purif., 16, 224, 10.1006/prep.1999.1069 · DOI
- Matz, 1982, J. Biol. Chem., 257, 4535, 10.1016/S0021-9258(18)34756-2 · DOI
- Newhouse, 2005, Acta Crystallogr. F, 61, 981, 10.1107/S1744309105032410 · DOI · Paper page
- Kabsch, 1993, J. Appl. Crystallogr., 26, 795, 10.1107/S0021889893005588 · DOI
- Vagin, 2000, Acta Crystallogr. Sect. D, 56, 1622, 10.1107/S0907444900013780 · DOI
- McIntosh, 1986, Biochemistry, 25, 4058, 10.1021/bi00362a011 · DOI
- De Pauw, 1995, Biochemistry, 34, 10953, 10.1021/bi00034a030 · DOI
- Raussens, 1998, J. Biol. Chem., 273, 25825, 10.1074/jbc.273.40.25825 · DOI
- Nagle, 2000, Biochim. Biophys. Acta, 1469, 159, 10.1016/S0304-4157(00)00016-2 · DOI
- Kumar, 2002, Biochemistry, 41, 11681, 10.1021/bi026069w · DOI
- Borhani, 1997, Proc. Natl. Acad. Sci. U. S. A., 94, 12291, 10.1073/pnas.94.23.12291 · DOI
- Weisgraber, 1986, J. Biol. Chem., 261, 2068, 10.1016/S0021-9258(17)35898-2 · DOI · Paper page
- Segall, 2002, J. Lipid Res., 43, 1688, 10.1194/jlr.M200157-JLR200 · DOI
- Morrow, 2000, J. Biol. Chem., 275, 2576, 10.1074/jbc.275.4.2576 · DOI
- Lalazar, 1989, J. Biol. Chem., 264, 8447, 10.1016/S0021-9258(18)81806-3 · DOI
- Raffaï, 1995, J. Lipid Res., 36, 1905, 10.1016/S0022-2275(20)41109-5 · DOI · Paper page
- Raussens, 2003, J. Biol. Chem., 278, 25998, 10.1074/jbc.M301753200 · DOI
- Segelke, 2000, Protein Sci., 9, 886, 10.1110/ps.9.5.886 · DOI
- Pitas, 1979, Proc. Natl. Acad. Sci. U. S. A., 76, 2311, 10.1073/pnas.76.5.2311 · DOI · Paper page
Cited by
Sorted by citations
Apolipoprotein E: from cardiovascular disease to neurodegenerative disorders
Mahley, R. W. (2016) · Journal of Molecular Medicine · doi:10.1007/s00109-016-1427-y · Cited by 837
Apolipoprotein E structure: insights into function
Hatters, D. M., Peters-Libeu, C. A., & Weisgraber, K. H. (2006) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2006.06.008 · Cited by 583
Self-citationApolipoprotein E: structure determines function, from atherosclerosis to Alzheimer's disease to AIDS
Mahley, R. W., Weisgraber, K. H., & Huang, Y. (2009) · Journal of Lipid Research · doi:10.1194/jlr.r800069-jlr200 · Cited by 580
Self-citationApolipoprotein E and cholesterol in aging and disease in the brain
de Chaves, E. P., Narayanaswami, V., Christoffersen, C., & Nielsen, L. B. (2008) · Future Lipidology · doi:10.2217/17460875.3.5.505 · Cited by 164
Direct Transcriptional Effects of Apolipoprotein E
Theendakara, V., Peters-Libeu, C. A., Spilman, P., Poksay, K. S., Bredesen, D. E., & Rao, R. V. (2016) · The Journal of Neuroscience · doi:10.1523/jneurosci.3562-15.2016 · Cited by 152
Self-citationAmino-terminal domain stability mediates apolipoprotein E aggregation into neurotoxic fibrils
Hatters, D. M., Zhong, N., Rutenber, E., & Weisgraber, K. H. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.06.080 · Cited by 105
Self-citationThe cell biology of APOE in the brain
Windham, I. A., & Cohen, S. (2024) · Trends in Cell Biology · doi:10.1016/j.tcb.2023.09.004 · Cited by 103
Current insights into apolipoprotein E and the immune response in Alzheimer's disease
Lin, P. B., & Holtzman, D. M. (2024) · Immunological Reviews · doi:10.1111/imr.13414 · Cited by 19
Strickland, M. R., & Holtzman, D. M. (2026) · Molecular Neurodegeneration · doi:10.1186/s13024-026-00970-0
Metadata
- Authors
- Peters-Libeu, C. A., Newhouse, Y., Hatters, D. M., & Weisgraber, K. H.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2006-01
- Volume
- 281
- Issue
- 2
- Pages
- 1073-1079
- ISSN
- 0021-9258
- Cited by
- 82
- References
- 5
- Language
- en
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 ›
Are you an author, or do you see a problem with this page? Request a review