Cited by 82

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

Peters-Libeu, Clare A., Newhouse, Yvonne, Hatters, Danny M., Weisgraber, Karl H.·2006·Journal of Biological Chemistry

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Crossref · 10.1074/jbc.m510851200

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  • 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 measured
  • 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.

    “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 measured
  • The 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 measured
  • Nascent 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 measured
  • There 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

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Citations

Cites

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Research works printed but not linked: 34

  1. Segrest, 2001, J. Lipid Res., 42, 1346, 10.1016/S0022-2275(20)30267-4 · DOI
  2. Mahley, 1988, Science, 240, 622, 10.1126/science.3283935 · DOI · Paper page
  3. Weisgraber, 1996, FASEB J., 10, 1485, 10.1096/fasebj.10.13.8940294 · DOI
  4. Saunders, 1993, Neurology, 43, 1467, 10.1212/WNL.43.8.1467 · DOI · Paper page
  5. Corder, 1993, Science, 261, 921, 10.1126/science.8346443 · DOI · Paper page
  6. Strittmatter, 1995, Proc. Natl. Acad. Sci. U. S. A., 92, 4725, 10.1073/pnas.92.11.4725 · DOI
  7. Mayeux, 1995, Neurology, 45, 555, 10.1212/WNL.45.3.555 · DOI · Paper page
  8. Slooter, 1997, J. Am. Med. Assoc., 277, 818, 10.1001/jama.1997.03540340052032 · DOI
  9. Fazekas, 2000, J. Neurol. Neurosurg. Psychiatry, 69, 25, 10.1136/jnnp.69.1.25 · DOI
  10. Drory, 2001, J. Neurol. Sci., 190, 17, 10.1016/S0022-510X(01)00569-X · DOI
  11. Eichner, 2002, Am. J. Epidemiol., 155, 487, 10.1093/aje/155.6.487 · DOI · Paper page
  12. Nolte, 1992, Biophys. J., 63, 1221, 10.1016/S0006-3495(92)81698-3 · DOI
  13. Segrest, 1992, J. Lipid Res., 33, 141, 10.1016/S0022-2275(20)41536-6 · DOI
  14. Innerarity, 1979, J. Biol. Chem., 254, 4186, 10.1016/S0021-9258(18)50713-4 · DOI · Paper page
  15. Lu, 2000, J. Biol. Chem., 275, 20775, 10.1074/jbc.M003508200 · DOI · Paper page
  16. Morrow, 1999, Protein Expr. Purif., 16, 224, 10.1006/prep.1999.1069 · DOI
  17. Matz, 1982, J. Biol. Chem., 257, 4535, 10.1016/S0021-9258(18)34756-2 · DOI
  18. Newhouse, 2005, Acta Crystallogr. F, 61, 981, 10.1107/S1744309105032410 · DOI · Paper page
  19. Kabsch, 1993, J. Appl. Crystallogr., 26, 795, 10.1107/S0021889893005588 · DOI
  20. Vagin, 2000, Acta Crystallogr. Sect. D, 56, 1622, 10.1107/S0907444900013780 · DOI
  21. McIntosh, 1986, Biochemistry, 25, 4058, 10.1021/bi00362a011 · DOI
  22. De Pauw, 1995, Biochemistry, 34, 10953, 10.1021/bi00034a030 · DOI
  23. Raussens, 1998, J. Biol. Chem., 273, 25825, 10.1074/jbc.273.40.25825 · DOI
  24. Nagle, 2000, Biochim. Biophys. Acta, 1469, 159, 10.1016/S0304-4157(00)00016-2 · DOI
  25. Kumar, 2002, Biochemistry, 41, 11681, 10.1021/bi026069w · DOI
  26. Borhani, 1997, Proc. Natl. Acad. Sci. U. S. A., 94, 12291, 10.1073/pnas.94.23.12291 · DOI
  27. Weisgraber, 1986, J. Biol. Chem., 261, 2068, 10.1016/S0021-9258(17)35898-2 · DOI · Paper page
  28. Segall, 2002, J. Lipid Res., 43, 1688, 10.1194/jlr.M200157-JLR200 · DOI
  29. Morrow, 2000, J. Biol. Chem., 275, 2576, 10.1074/jbc.275.4.2576 · DOI
  30. Lalazar, 1989, J. Biol. Chem., 264, 8447, 10.1016/S0021-9258(18)81806-3 · DOI
  31. Raffaï, 1995, J. Lipid Res., 36, 1905, 10.1016/S0022-2275(20)41109-5 · DOI · Paper page
  32. Raussens, 2003, J. Biol. Chem., 278, 25998, 10.1074/jbc.M301753200 · DOI
  33. Segelke, 2000, Protein Sci., 9, 886, 10.1110/ps.9.5.886 · DOI
  34. Pitas, 1979, Proc. Natl. Acad. Sci. U. S. A., 76, 2311, 10.1073/pnas.76.5.2311 · DOI · Paper page

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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

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