The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
The number of amphipathic alpha-helical segments of apolipoproteins A-I, E, and A-IV determines the size and functional properties of their reconstituted lipoprotein particles.
Abstract
The objective of this work was to determine the role of the amphipathic alpha-helical structural units of human apolipoproteins A-I, E, and A-IV in defining the sizes and reactivities with lecithin:cholesterol acyltransferase (LCAT) of their reconstituted lipoprotein particles. We prepared reconstituted high density lipoprotein (rHDL) particles with each of the three apolipoproteins in two weight ratios with lipid: 2.7/0.07/1 and 1.35/0.04/1, palmitoyloleoylphosphatidylcholine/cholesterol/apolipoprotein, by the sodium cholate dialysis procedure; and examined the rHDL product sizes and distributions by nondenaturing gradient gel electrophoresis. The rHDL particles were also incubated with low density lipoprotein (LDL), and with LDL plus LCAT, to observe any structural modifications due to phospholipid transfers to LDL and to cholesterol esterification by LCAT. In addition, we examined the average structural properties of the original rHDL by several fluorescence methods and circular dichroism spectroscopy, and determined their reaction kinetics with LCAT. The results indicate that the diameters of the largest rHDL particles, containing two apolipoproteins per particle, correlate with the maximum number of putative amphipathic alpha-helical segments in their sequences, and that smaller particles of this class may arise from the removal of one or more alpha-helical segments from contact with lipid. Furthermore, the larger particles may be converted into the smaller ones upon los…
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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?
ApoE formed using the sodium cholate dialysis method forms particles ranging from 8 to 15 nm.
“ApoE formed using the sodium cholate dialysis method forms particles ranging from 8 to 15 nm [17, 56].”
From ApoE lipoproteins in the central nervous system under homeostasis and role in Alzheimer’s disease and related disorders (2026) · cites this paper as [56]
Generation of discoidal ApoE using recombinant protein and lipidation with lipids such as POPC and DMPC result in the formation of discoidal lipoprotein similar in diameter and conformation to astrocyte secreted human LpE.
“Generation of discoidal ApoE using recombinant protein and lipidation with lipids such as 1-palmitoyl-2-oleoyl-glycero-3-phosphocholine (POPC) and dimyristoylphosphatidylcholine (DMPC) result in the formation of discoidal lipoprotein similar in diameter and conformation to astrocyte secreted human LpE [20, 56].”
From ApoE lipoproteins in the central nervous system under homeostasis and role in Alzheimer’s disease and related disorders (2026) · cites this paper as [56]
Another study incubating discoidal ApoE containing two ApoE protein per particle from 8.7 to 10.8 nm in diameter with LCAT found that they formed spherical particles ~ 10.4 nm in diameter with a predicted 3 ApoE molecules per particle based on the diameter measured by electron microscopy.
“Another study incubating discoidal ApoE containing two ApoE protein per particle from 8.7 to 10.8 nm in diameter with LCAT found that they formed spherical particles ~ 10.4 nm in diameter with a predicted 3 ApoE molecules per particle based on the diameter measured by electron microscopy [56].”
From ApoE lipoproteins in the central nervous system under homeostasis and role in Alzheimer’s disease and related disorders (2026) · cites this paper as [56]
Larger particles can contain a higher stoichiometric ratio of ApoE to lipid, which may influence receptor binding and interaction with enzymes like LCAT.
“Larger particles are also able to contain a higher stoichiometric ratio of ApoE to lipid which may also influence receptor binding and interaction with enzymes like LCAT [56, 118].”
From ApoE lipoproteins in the central nervous system under homeostasis and role in Alzheimer’s disease and related disorders (2026) · cites this paper as [56]
Citations
Cites
Aggerbeck, 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
Flagged first, then by citations
Research works printed but not linked: 38
- Jonas, 1989, J. Biol. Chem., 264, 4818, 10.1016/S0021-9258(18)83664-X · DOI
- Castro, 1988, Biochemistry, 27, 25, 10.1021/bi00401a005 · DOI
- Jonas, 1986, Methods Enzymol., 128, 553, 10.1016/0076-6879(86)28092-1 · DOI
- Wald, 1990, J. Biol. Chem., 265, 20037, 10.1016/S0021-9258(17)45479-2 · DOI
- Jonas, 1990, J. Biol. Chem., 265, 22123, 10.1016/S0021-9258(18)45679-7 · DOI
- Zorich, 1987, Biochim. Biophys. Acta, 919, 181, 10.1016/0005-2760(87)90206-2 · DOI
- Nichols, 1983, Biochim. Biophys. Acta, 750, 353, 10.1016/0005-2760(83)90040-1 · DOI
- Nichols, 1984, Biochim. Biophys. Acta, 793, 325, 10.1016/0005-2760(84)90246-7 · DOI
- Cheung, 1987, J. Lipid Res., 28, 913, 10.1016/S0022-2275(20)38631-4 · DOI
- Boguski, 1986, J. Lipid Res., 27, 1011, 10.1016/S0022-2275(20)38761-7 · DOI
- Li, 1988, J. Lipid Res., 29, 245, 10.1016/S0022-2275(20)38532-1 · DOI
- Brasseur, 1990, Biochim. Biophys. Acta, 1043, 245, 10.1016/0005-2760(90)90023-Q · DOI
- Marcel, 1991, J. Biol. Chem., 266, 3644, 10.1016/S0021-9258(19)67843-9 · DOI
- Luo, 1986, J. Mol. Biol., 187, 325, 10.1016/0022-2836(86)90436-5 · DOI · Paper page
- Karathanasis, 1986, Biochemistry, 25, 3962, 10.1021/bi00361a034 · DOI
- Yokoyama, 1985, J. Biol. Chem., 260, 16375, 10.1016/S0021-9258(17)36247-6 · DOI
- Rifici, 1985, Biochim. Biophys. Acta, 834, 205, 10.1016/0005-2760(85)90157-2 · DOI
- Zorich, 1985, J. Biol. Chem., 260, 8831, 10.1016/S0021-9258(17)39427-9 · DOI · Paper page
- Steinmetz, 1985, J. Biol. Chem., 260, 2258, 10.1016/S0021-9258(18)89547-3 · DOI
- Edelstein, 1972, J. Biol. Chem., 247, 5842, 10.1016/S0021-9258(19)44834-5 · DOI
- Utermann, 1975, Hoppe-Seyler Z. Physiol. Chem., 356, 1113, 10.1515/bchm2.1975.356.2.1113 · DOI
- Steinmetz, 1989, J. Chromatogr., 487, 154, 10.1016/S0378-4347(00)83018-2 · DOI
- Pownall, 1986, Methods Enzymol., 128, 515, 10.1016/0076-6879(86)28089-1 · DOI
- Beaven, 1952, Adv. Protein Chem., 7, 319, 10.1016/S0065-3233(08)60022-4 · DOI
- Staros, 1982, Biochemistry, 21, 3950, 10.1021/bi00260a008 · DOI
- Chen, 1972, Biochemistry, 11, 4120, 10.1021/bi00772a015 · DOI
- Matz, 1982, J. Biol. Chem., 257, 4541, 10.1016/S0021-9258(18)34757-4 · DOI
- Jonas, 1988, J. Lipid Res., 29, 1349, 10.1016/S0022-2275(20)38436-4 · DOI
- Jonas, 1991, Biochim. Biophys. Acta, 1085, 71, 10.1016/0005-2760(91)90233-8 · DOI
- Ritter, 1977, J. Biol. Chem., 252, 1208, 10.1016/S0021-9258(17)40642-9 · DOI
- Weinberg, 1985, J. Biol. Chem., 260, 14279, 10.1016/S0021-9258(17)38714-8 · DOI
- Weinberg, 1990, J. Biol. Chem., 265, 8081, 10.1016/S0021-9258(19)39041-6 · DOI
- Wetterau, 1988, J. Biol. Chem., 263, 6240, 10.1016/S0021-9258(18)68778-2 · DOI · Paper page
- Weinberg, 1985, J. Biol. Chem., 260, 4914, 10.1016/S0021-9258(18)89159-1 · DOI
- Gong, 1989, Biochim. Biophys. Acta, 1006, 317, 10.1016/0005-2760(89)90019-2 · DOI · Paper page
- Dvorin, 1985, J. Lipid Res., 26, 38, 10.1016/S0022-2275(20)34402-3 · DOI
- Weinberg, 1990, J. Biol. Chem., 265, 18372, 10.1016/S0021-9258(17)44762-4 · DOI
- Jonas, 1991, J. Lipid Res., 32, 97, 10.1016/S0022-2275(20)42248-5 · DOI
Cited by
Sorted by citations
Molecular physiology of reverse cholesterol transport.
Fielding, C. J., & Fielding, P. E. (1995) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)39898-9 · Cited by 1,448
Rensen, P. C. N., & van Berkel, T. J. C. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.25.14791 · Cited by 144
Clément-Collin, V., Barbier, A., Dergunov, A. D., Visvikis, A., Siest, G., Desmadril, M., Takahashi, M., & Aggerbeck, L. P. (2006) · Biophysical Chemistry · doi:10.1016/j.bpc.2005.07.009 · Cited by 32
Strickland, M. R., & Holtzman, D. M. (2026) · Molecular Neurodegeneration · doi:10.1186/s13024-026-00970-0
Metadata
- Authors
- Jonas, A., Steinmetz, A., & Churgay, L.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1993-01
- Volume
- 268
- Issue
- 3
- Pages
- 1596-1602
- ISSN
- 0021-9258
- Cited by
- 59
- References
- 1
- 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
