New Insights into the Heparan Sulfate Proteoglycan-binding Activity of Apolipoprotein E
Open accessAbstract
Defective binding of apolipoprotein E (apoE) to heparan sulfate proteoglycans (HSPGs) is associated with increased risk of atherosclerosis due to inefficient clearance of lipoprotein remnants by the liver. The interaction of apoE with HSPGs has also been implicated in the pathogenesis of Alzheimer's disease and may play a role in neuronal repair. To identify which residues in the heparin-binding site of apoE and which structural elements of heparan sulfate interact, we used a variety of approaches, including glycosaminoglycan specificity assays, (13)C nuclear magnetic resonance, and heparin affinity chromatography. The formation of the high affinity complex required Arg-142, Lys-143, Arg-145, Lys-146, and Arg-147 from apoE and N- and 6-O-sulfo groups of the glucosamine units from the heparin fragment. As shown by molecular modeling, using a high affinity binding octasaccharide fragment of heparin, these findings are consistent with a binding mode in which five saccharide residues of fully sulfated heparan sulfate lie in a shallow groove of the alpha-helix that contains the HSPG-binding site (helix 4 of the four-helix bundle of the 22-kDa fragment). This groove is lined with residues Arg-136, Ser-139, His-140, Arg-142, Lys-143, Arg-145, Lys-146, and Arg-147. In the model, all of these residues make direct contact with either the 2-O-sulfo groups of the iduronic acid monosaccharides or the N- and 6-O-sulfo groups of the glucosamine sulfate monosaccharides. This model indicates that apoE has an HSPG-binding site highly complementary to heparan sulfate rich in N- and O-sulfo groups such as that found in the liver and the brain.
Integrity signals
Registry
Cites
Statistics
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?
The interaction of apoE with syndecan occurs through electrostatic interactions between positively charged helix 4 domains of apoE and negatively charged sulfate groups in syndecan HSPG.
“Presumably, the interaction of apoE with syndecan occurs through electrostatic interactions between positively charged helix 4 domains of apoE and negatively charged sulfate groups in syndecan HSPG (Libeu et al., 2001).”
From Apolipoprotein E in Synaptic Plasticity and Alzheimer’s Disease: Potential Cellular and Molecular Mechanisms (2014) · cites this paper as Libeu et al., 2001
ApoE is known to bind to heparan sulfate proteoglycan (HSPG) through its N-terminal domain (142-147 amino acid domain).
“apoE is known to bind to heparan sulfate proteoglycan (HSPG) through its N-terminal domain (142–147 amino acid domain) (Libeu et al., 2001).”
From Apolipoprotein E in Synaptic Plasticity and Alzheimer’s Disease: Potential Cellular and Molecular Mechanisms (2014) · cites this paper as Libeu et al., 2001
APOE4 has increased binding affinity (up to two-fold) for heparin and HSPG over APOE3.
“By contrast, APOE4 has increased binding affinity (up to two-fold) for heparin and HSPG over APOE3 (refs. 32–35).”
From The APOE-R136S mutation protects against APOE4-driven tau pathology, neurodegeneration, and neuroinflammation (2023) · cites this paper as [34]
The 22-kDa domain of lipid-bound apoE3[R145C] has 48% reduced HSPG binding capacity compared to apoE3-22kDa.
“and the 22-kDa domain of lipid-bound apoE3[R145C] has 48% reduced HSPG binding capacity compared to apoE3-22kDa [30], [32].”
From Biophysical Analysis of Apolipoprotein E3 Variants Linked with Development of Type III Hyperlipoproteinemia (2011) · cites this paper as [32]
The receptor-binding sites (AA136-150) for LDLR, LRP1, and HSPGs are located in a region conserved between mouse and human APOE.
“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 [14]
The N-terminal domain of apoE contains a heparin binding site located between residues 136-147, overlapping with the LDLR binding region.
“the N-terminal domain site is located between residues 136–147, overlapping with the LDLR binding region (25, 26)”
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 [26]
Mutation in lysine 146 greatly reduced the favorable free energy for the first binding step of apoE to HS and DS.
“In addition, the mutation in lysine 146 which disrupts direct ionic interaction between basic residues on apoE and sulfate groups on the GAG chain (26) greatly reduced the favorable free energy for the first binding step to HS and DS (Fig. 4B).”
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 [26]
The degree of sulfation in GAG has a major effect on the electrostatic interaction with apoE.
“indicating that the degree of sulfation has a major effect on the electrostatic interaction of GAG with apoE.”
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 [26]
Quantitative information on the interaction of apoE with various GAG molecules is limited.
“quantitative information on the interaction with various GAG molecules is limited (26, 34).”
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 [26]
The contribution of the initial electrostatic interaction to the overall binding is lower for HS and DS than for heparin.
“However, the large decreases in the association rate and the favorable free energy of binding in the first step observed for HS and DS compared to heparin (Fig. 3) indicate that the contribution of the initial electrostatic interaction to the overall binding is lower for HS and DS than for heparin (26).”
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 [26]
Cites
PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT
Lowry, O. H., Rosebrough, N., Farr, A. L., & Randall, R. (1951) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)52451-6 · Cited by 315,771 · see citing works
MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
Kraulis, P. J. (1991) · Journal of Applied Crystallography · doi:10.1107/s0021889891004399 · Cited by 14,011 · see citing works
The Metabolic and Molecular Bases of Inherited Disease
Scriver, R. C. (1995) · Medical Entomology and Zoology · Cited by 12,101 · see citing works
The metabolic and molecular bases of inherited disease
Chen, Y.-T. (2001) · Medical Entomology and Zoology · Cited by 6,928 · see citing works
Apolipoprotein E: Cholesterol Transport Protein with Expanding Role in Cell Biology
Mahley, R. W. (1988) · Science · doi:10.1126/science.3283935 · Cited by 4,028 · see citing works
[26] Raster3D: Photorealistic molecular graphics
Merritt, E. A., & Bacon, D. (1997) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(97)77028-9 · Cited by 3,749 · see citing works
Williams Textbook of Endocrinology
Melmed, S., & Polonsky, K. С. (2016) · Elsevier eBooks · doi:10.1016/c2013-0-15980-6 · Cited by 3,716 · see citing works
Apolipoprotein E: Far More Than a Lipid Transport Protein
Mahley, R. W., & Rall, S. C. (2000) · Annual Review of Genomics and Human Genetics · doi:10.1146/annurev.genom.1.1.507 · Cited by 1,836 · see citing works
Williams Textbook of Endocrinology
Stoffer, S. S. (1999) · JAMA · doi:10.1001/jama.281.9.851 · Cited by 1,260 · see citing works
Apolipoprotein E: Structure-Function Relationships
Weisgraber, K. H. (1994) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60642-7 · Cited by 830 · see citing works
Self-citationHeparin Structure and Interactions with Basic Fibroblast Growth Factor
Faham, S., Hileman, R. E., Fromm, J. R., Linhardt, R. J., & Rees, D. C. (1996) · Science · doi:10.1126/science.271.5252.1116 · Cited by 798 · see citing works
Self-citationMahley, R. W., & Ji, Z.-S. (1999) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)33334-4 · Cited by 693 · see citing works
(1998) · Elsevier eBooks · doi:10.1016/b978-0-12-186060-8.x5000-1 · Cited by 504 · see citing works
Mahley, R. W., Huang, Y., & Rall, S. C. (1999) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)32417-2 · Cited by 447 · see citing works
Purification of antithrombin III by affinity chromatography
Miller-Andersson, M., Borg, H., & Andersson, L. (1974) · Thrombosis Research · doi:10.1016/0049-3848(74)90001-2 · Cited by 423 · see citing works
N.m.r. and molecular-modelling studies of the solution conformation of heparin
Mulloy, B., Forster, M. J., Jones, C., & Davies, D. B. (1993) · Biochemical Journal · doi:10.1042/bj2930849 · Cited by 410 · see citing works
Mahley, R. W., & Huang, Y. (1999) · Current Opinion in Lipidology · doi:10.1097/00041433-199906000-00003 · Cited by 388 · see citing works
Structure of a heparin-linked biologically active dimer of fibroblast growth factor
DiGabriele, A. D., Lax, I., Chen, D. I., Svahn, C. M., Jaye, M., Schlessinger, J., & Hendrickson, W. A. (1998) · Nature · doi:10.1038/31741 · Cited by 353 · see citing works
Holtzman, D. M., Pitas, R. E., Kilbridge, J., Nathan, B., Mahley, R. W., Bu, G., & Schwartz, A. L. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.21.9480 · Cited by 349 · see citing works
The Molecular and Genetic Basis of Neurological Disease
Trojanowski, J. Q. (1993) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-199309000-00013 · Cited by 341 · see citing works
Dong, L. M., Wilson, C., Wardell, M. R., Simmons, T., Mahley, R. W., Weisgraber, K. H., & Agard, D. A. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31797-0 · Cited by 320 · see citing works
Self-citationBellosta, S., Nathan, B. P., Orth, M., Dong, L.-M., Mahley, R. W., & Pitas, R. E. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.45.27063 · Cited by 313 · see citing works
Innerarity, T. L., Pitas, R. E., & Mahley, R. W. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)50713-4 · Cited by 300 · see citing works
Domain Structure of Heparan Sulfates from Bovine Organs
Maccarana, M., Sakura, Y., Tawada, A., Yoshida, K., & Lindahl, U. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.30.17804 · Cited by 284 · see citing works
The receptor-binding domain of human apolipoprotein E. Binding of apolipoprotein E fragments.
Innerarity, T. L., Friedlander, E. J., Rall, S. C., Weisgraber, K. H., & Mahley, R. W. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)44180-9 · Cited by 276 · see citing works
Self-citationLiver heparan sulfate structure. A novel molecular design
Lyon, M., Deakin, J. A., & Gallagher, J. T. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)78112-5 · Cited by 240 · see citing works
Human apolipoprotein E. Determination of the heparin binding sites of apolipoprotein E3.
Weisgraber, K. H., Rall, S. C., Mahley, R. W., Milne, R. W., Marcel, Y. L., & Sparrow, J. T. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)35898-2 · Cited by 240 · see citing works
Self-citationCell-surface heparan sulfate. Mechanisms of proteoglycan-cell association.
Kjellén, L., Oldberg, Å., & Höök, M. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)70479-7 · Cited by 223 · see citing works
The receptor-binding domain of human apolipoprotein E. Monoclonal antibody inhibition of binding.
Weisgraber, K. H., Innerarity, T. L., Harder, K. J., Mahley, R. W., Milne, R. W., Marcel, Y. L., & Sparrow, J. T. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)44181-0 · Cited by 220 · see citing works
Self-citationLalazar, A., Weisgraber, K. H., Rall, S. C., Giladi, H., Innerarity, T. L., Levanon, A. Z., Boyles, J. K., Amit, B., Gorecki, M., & Mahley, R. W. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)68957-4 · Cited by 209 · see citing works
Self-citationDiversity does make a difference: fibroblast growth factor-heparin interactions
Faham, S., Linhardt, R. J., & Rees, D. C. (1998) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(98)80147-4 · Cited by 155 · see citing works
Self-citation[13] Isolation and characterization of apolipoprotein E
Rall, S. C., Weisgraber, K. H., & Mahley, R. W. (1986) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(86)28073-8 · Cited by 150 · see citing works
Self-citationAge-dependent Modulation of Heparan Sulfate Structure and Function
Feyzi, E., Saldeen, T. G. P., Larsson, E., Lindahl, U., & Salmivirta, M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.22.13395 · Cited by 144 · see citing works
Ji, Z. S., Fazio, S., & Mahley, R. W. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36849-7 · Cited by 138 · see citing works
Cell-surface heparan sulfate proteoglycans: dynamic molecules mediating ligand catabolism
Williams, K. J., & Fuki, I. V. (1997) · Current Opinion in Lipidology · doi:10.1097/00041433-199710000-00003 · Cited by 135 · see citing works
Distribution of sulphate and iduronic acid residues in heparin and heparan sulphate
Höök, M., Lindahl, U., & Iverius, P. (1974) · Biochemical Journal · doi:10.1042/bj1370033 · Cited by 130 · see citing works
Novel mechanism for defective receptor binding of apolipoprotein E2 in type III hyperlipoproteinemia
Dong, L., Parkin, S., Trakhanov, S. D., Rupp, B., Simmons, T., Arnold, K. S., Newhouse, Y. M., Innerarity, T. L., & Weisgraber, K. H. (1996) · Nature Structural & Molecular Biology · doi:10.1038/nsb0896-718 · Cited by 129 · see citing works
Self-citationKinnunen, T., Raulo, E., Nolo, R., Maccarana, M., Lindahl, U., & Rauvala, H. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.4.2243 · Cited by 127 · see citing works
Orr, G. A. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)70041-6 · Cited by 122 · see citing works
Reduced Sulfation of Liver Heparan Sulfate in Experimentally Diabetic Rats
Kjellén, L., Bielefeld, D. R., & Höök, M. (1983) · Diabetes · doi:10.2337/diab.32.4.337 · Cited by 112 · see citing works
Parthasarathy, N., Goldberg, I. J., Sivaram, P., Mulloy, B., Flory, D. M., & Wagner, W. D. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31802-1 · Cited by 108 · see citing works
Ebara, T., Conde, K., Kako, Y., Liu, Y., Xu, Y. K., Ramakrishnan, R., Goldberg, I. J., & Shachter, N. S. (2000) · Journal of Clinical Investigation · doi:10.1172/jci8283 · Cited by 103 · see citing works
Interaction of the N-Terminal Domain of Apolipoprotein E4 with Heparin
Dong, J., Peters-Libeu, C. A., Weisgraber, K. H., Segelke, B. W., Rupp, B., Capila, I., Hernáiz, M. J., LeBrun, L. A., & Linhardt, R. J. (2001) · Biochemistry · doi:10.1021/bi002417n · Cited by 99 · see citing works
Self-citation友也, 田., 定也, 美., & 貴史, 伊. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003508200 · Cited by 95 · see citing works
Horie, Y., Fazio, S., Westerlund, J. R., Weisgraber, K. H., & Rall, S. C. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)46040-1 · Cited by 94 · see citing works
Self-citationFunctional Characterization of Apolipoprotein E Isoforms Overexpressed in Escherichia coli
Morrow, J. A., Arnold, K. S., & Weisgraber, K. H. (1999) · Protein Expression and Purification · doi:10.1006/prep.1999.1069 · Cited by 94 · see citing works
Self-citationLund‐Katz, S., Ibdah, J. A., Letizia, J. Y., Thomas, M. T., & Phillips, M. C. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)68319-x · Cited by 77 · see citing works
Self-citationLindahl, B., Westling, C., Giménez‐Gallego, G., Lindahl, U., & Salmivirta, M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.43.30631 · Cited by 70 · see citing works
The Molecular and Genetic Basis of Neurological Disease
Albin, R. L. (1997) · JAMA · doi:10.1001/jama.1997.03550070091049 · Cited by 65 · see citing works
Cell Surface Proteoglycans Modulate Net Synthesis and Secretion of Macrophage Apolipoprotein E
Lucas, M., & Mazzone, T. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.23.13454 · Cited by 63 · see citing works
Effects of Lipid Interaction on the Lysine Microenvironments in Apolipoprotein E
Lund‐Katz, S., Zaiou, M., Wehrli, S. L., Dhanasekaran, P., Baldwin, F., Weisgraber, K. H., & Phillips, M. C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m005265200 · Cited by 54 · see citing works
Self-citationUnger, E., Pettersson, I., Eriksson, U. J., Lindahl, U., & Kjellén, L. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)31496-0 · Cited by 52 · see citing works
Riesenfeld, J., Höök, M., & Lindahl, U. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)86121-5 · Cited by 52 · see citing works
Mann, W. A., Meyer, N., Weber, W. T., Meyer, S., Greten, H., & Beisiegel†, U. (1995) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)39885-0 · Cited by 47 · see citing works
Shuvaev, V. V., Laffont, I., & Siest, G. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)01285-5 · Cited by 27 · see citing works
Minnich, A., Weisgraber, K. H., Newhouse, Y., Dong, L. M., Fortin, L. J., Tremblay, M., & Davignon, J. (1995) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)39754-6 · Cited by 26 · see citing works
Self-citationMärz, W., Hoffmann, M. M., Scharnagl, H., Fisher, E., Chen, M., Nauck, M., Feussner, G., & Wieland, H. (1998) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)33303-4 · Cited by 21 · see citing works
Heparin specifically inhibits binding of apolipoprotein E to amyloid β-peptide
Shuvaev, V. V., & Siest, G. (2000) · Neuroscience Letters · doi:10.1016/s0304-3940(00)00764-3 · Cited by 19 · see citing works
Murata, K., Murata, A., & Yoshida, K. (1997) · Atherosclerosis · doi:10.1016/s0021-9150(97)00049-x · Cited by 14 · see citing works
Conrad, H. E. (1998) · Elsevier eBooks · doi:10.1016/b978-012186060-8/50003-6 · Cited by 11 · see citing works
Cole (2000) · doi:10.1002/1097-0029(20000815)50:4
Flagged first, then by citations
Cited by
Sorted by citations
Survey of the year 2003 commercial optical biosensor literature
Rich, R. L., & Myszka, D. G. (2004) · Journal of Molecular Recognition · doi:10.1002/jmr.726 · Cited by 505 · see citing works
Apolipoprotein E isoforms and lipoprotein metabolism
Phillips, M. C. (2014) · IUBMB Life · doi:10.1002/iub.1314 · Cited by 328 · see citing works
Self-citationTopology of human apolipoprotein E3 uniquely regulates its diverse biological functions
Chen, J., Li, Q., & Wang, J. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1106420108 · Cited by 283 · see citing works
The key role of apolipoprotein E in atherosclerosis
Greenow, K. R., Pearce, N. J., & Ramji, D. P. (2005) · Journal of Molecular Medicine · doi:10.1007/s00109-004-0631-3 · Cited by 236 · see citing works
Stanford, K. I., Bishop, J. R., Foley, E. M., Gonzales, J. C., Niesman, I. R., Witztum, J. L., & Esko, J. D. (2009) · Journal of Clinical Investigation · doi:10.1172/jci38251 · Cited by 226 · see citing works
Heparan sulphate proteoglycans in Alzheimer's disease and amyloid‐related disorders
van Horssen, J., Wesseling, P., van den Heuvel, L. P. J. W., de Waal, R. M. W., & Verbeek, M. M. (2003) · The Lancet Neurology · doi:10.1016/s1474-4422(03)00484-8 · Cited by 226 · see citing works
MacArthur, J. M., Bishop, J. R., Stanford, K. I., Wang, L., Bensadoun, A., Witztum, J. L., & Esko, J. D. (2007) · Journal of Clinical Investigation · doi:10.1172/jci29154 · Cited by 216 · see citing works
Saito, H., Lund‐Katz, S., & Phillips, M. C. (2004) · Progress in Lipid Research · doi:10.1016/j.plipres.2004.05.002 · Cited by 216 · see citing works
Self-citationHeparin-Binding Domains in Vascular Biology
Munoz, E. M., & Linhardt, R. J. (2004) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000137189.22999.3f · Cited by 213 · see citing works
Self-citationHepatitis C Virus Attachment Mediated by Apolipoprotein E Binding to Cell Surface Heparan Sulfate
Jiang, J., Cun, W., Wu, X., Shi, Q., Tang, H., & Luo, G. G. (2012) · Journal of Virology · doi:10.1128/jvi.07222-11 · Cited by 170 · see citing works
Apolipoprotein 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 · see citing works
PLASMODIUMSPOROZOITE MOLECULAR CELL BIOLOGY
Kappe, S. H. I., Buscaglia, C. A., & Nussenzweig, V. (2004) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.20.011603.150935 · Cited by 149 · see citing works
Kim, J., Yoon, H., Basak, J., & Kim, J. (2014) · Molecules and Cells · doi:10.14348/molcells.2014.0248 · Cited by 141 · see citing works
“HSPG can take up extracellular apoE-containing lipoproteins, independent of LDLR and LRP1.”
BackgroundInfluentialAmyloid accomplices and enforcers
Alexandrescu, A. T. (2004) · Protein Science · doi:10.1110/ps.04887005 · Cited by 134 · see citing works
Shi, Q., Jiang, J., & Luo, G. G. (2013) · Journal of Virology · doi:10.1128/jvi.03475-12 · Cited by 126 · see citing works
Update on the molecular biology of dyslipidemias
Ramasamy, I. (2015) · Clinica Chimica Acta · doi:10.1016/j.cca.2015.10.033 · Cited by 126 · see citing works
Vaillant, A. (2016) · Antiviral Research · doi:10.1016/j.antiviral.2016.07.004 · Cited by 125 · see citing works
ApoE genotype, cardiovascular risk and responsiveness to dietary fat manipulation
Minihane, A. M., Jofre‐Monseny, L., Olano-Martin, E., & Rimbach, G. H. (2007) · Proceedings of The Nutrition Society · doi:10.1017/s0029665107005435 · Cited by 125 · see citing works
Nelson, M. R., Liu, P., Agrawal, A., Yip, O., Blumenfeld, J., Traglia, M., Kim, M. J., Koutsodendris, N., Rao, A., Grone, B., et al. (2023) · Nature Neuroscience · doi:10.1038/s41593-023-01480-8 · Cited by 118 · see citing works
Pharmacogenomics in Alzheimer's Disease
Cacabelos, R. (2008) · Methods in molecular biology · doi:10.1007/978-1-59745-205-2_10 · Cited by 109 · see citing works
Sato, Y., Kinami, Y., Hashiba, K., & Harashima, H. (2020) · Journal of Controlled Release · doi:10.1016/j.jconrel.2020.03.006 · Cited by 108 · see citing works
Survey of the year 2001 commercial optical biosensor literature
Rich, R. L., & Myszka, D. G. (2002) · Journal of Molecular Recognition · doi:10.1002/jmr.598 · Cited by 99 · see citing works
Jendresen, C., Årskog, V., Daws, M. R., & Nilsson, L. N. G. (2017) · Journal of Neuroinflammation · doi:10.1186/s12974-017-0835-4 · Cited by 94 · see citing works
Two-step Mechanism of Binding of Apolipoprotein E to Heparin
Futamura, M., Dhanasekaran, P., Handa, T., Phillips, M. C., Lund-Katz, S., & Saito, H. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m411719200 · Cited by 91 · see citing works
Self-citationCharacterization of the Heparin Binding Sites in Human Apolipoprotein E
Saito, H., Dhanasekaran, P., Nguyen, D., Baldwin, F., Weisgraber, K. H., Wehrli, S., Phillips, M. C., & Lund-Katz, S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m213207200 · Cited by 90 · see citing works
Self-citationDietary fats, cerebrovasculature integrity and Alzheimer’s disease risk
Takechi, R., Galloway, S., Pallebage‐Gamarallage, M. M., Lam, V., & Mamo, J. C. L. (2009) · Progress in Lipid Research · doi:10.1016/j.plipres.2009.10.004 · Cited by 88 · see citing works
Brain‐targeted stem cell gene therapy corrects mucopolysaccharidosis type II via multiple mechanisms
Gleitz, H. F. E., Liao, A. Y., Cook, J. R., Rowlston, S., Forte, G. M. A., D’Souza, Z., O’Leary, C., Holley, R. J., & Bigger, B. (2018) · EMBO Molecular Medicine · doi:10.15252/emmm.201708730 · Cited by 85 · see citing works
Lefèvre, M., Felmlee, D. J., Parnot, M., Baumert, T. F., & Schuster, C. (2014) · PLoS ONE · doi:10.1371/journal.pone.0095550 · Cited by 86 · see citing works
Heparan Sulfate 2-O-Sulfotransferase Is Required for Triglyceride-rich Lipoprotein Clearance
Stanford, K. I., Wang, L., Castagnola, J., Song, D., Bishop, J. R., Brown, J. R., Lawrence, R., Bai, X., Habuchi, H., Tanaka, M., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.063701 · Cited by 84 · see citing works
Isolation and characterization of heparan sulfate from various murine tissues
Warda, M., Toida, T., Zhang, F., Sun, P., Munoz, E. M., Xie, J., & Linhardt, R. J. (2006) · Glycoconjugate Journal · doi:10.1007/s10719-006-7668-1 · Cited by 81 · see citing works
Self-citationWilsie, L. C., & Orlando, R. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m208786200 · Cited by 81 · see citing works
Molecular biology of apolipoprotein E
Strittmatter, W. J., & Hill, C. B. (2002) · Current Opinion in Lipidology · doi:10.1097/00041433-200204000-00002 · Cited by 80 · see citing works
Mosquito Heparan Sulfate and Its Potential Role in Malaria Infection and Transmission
Sinnis, P., Coppi, A., Toida, T., Toyoda, H., Kinoshita‐Toyoda, A., Xie, J., Kemp, M. M., & Linhardt, R. J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704698200 · Cited by 76 · see citing works
Self-citationSignaling pathways regulating neuron–glia interaction and their implications in Alzheimer's disease
Lian, H., & Zheng, H. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13424 · Cited by 75 · see citing works
Fu, Y., Zhao, J., Atagi, Y., Nielsen, H. M., Liu, C., Zheng, H., Shinohara, M., Kanekiyo, T., & Bu, G. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0099-y · Cited by 71 · see citing works
Structural characterization of human liver heparan sulfate
Vongchan, P., Warda, M., Toyoda, H., Toida, T., Marks, R. M., & Linhardt, R. J. (2004) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2004.09.007 · Cited by 73 · see citing works
Self-citationThe helix bundle: A reversible lipid binding motif
Narayanaswami, V., Kiss, R. S., & Weers, P. M. M. (2009) · Comparative Biochemistry and Physiology Part A Molecular & Integrative Physiology · doi:10.1016/j.cbpa.2009.09.009 · Cited by 67 · see citing works
González-Martı́nez, D., Hu, Y., & Bouloux, P. M. (2004) · Frontiers in Neuroendocrinology · doi:10.1016/j.yfrne.2004.06.001 · Cited by 65 · see citing works
Hashiba, A., Toyooka, M., Sato, Y., Maeki, M., Tokeshi, M., & Harashima, H. (2020) · Journal of Controlled Release · doi:10.1016/j.jconrel.2020.08.031 · Cited by 66 · see citing works
Elimova, E. C., Kisilevsky, R., Szarek, W. A., & Ancsin, J. B. (2004) · The FASEB Journal · doi:10.1096/fj.03-1436fje · Cited by 66 · see citing works
Molecular Mechanism of Apolipoprotein E Binding to Lipoprotein Particles
Nguyen, D., Dhanasekaran, P., Phillips, M. C., & Lund‐Katz, S. (2009) · Biochemistry · doi:10.1021/bi9000694 · Cited by 63 · see citing works
Self-citationHuman apolipoprotein E promotes hepatitis B virus infection and production
Qiao, L., & Luo, G. G. (2019) · PLoS Pathogens · doi:10.1371/journal.ppat.1007874 · Cited by 64 · see citing works
Elimova, E., Kisilevsky, R., & Ancsin, J. B. (2009) · The FASEB Journal · doi:10.1096/fj.09-134981 · Cited by 59 · see citing works
Yamauchi, Y., Deguchi, N., Takagi, C., Tanaka, M., Dhanasekaran, P., Nakano, M., Handa, T., Phillips, M. C., Lund-Katz, S., & Saito, H. (2008) · Biochemistry · doi:10.1021/bi8003999 · Cited by 53 · see citing works
Self-citationDo infectious agents play a role in dementia?
Dobson, C. B., Wozniak, M. A., & Itzhaki, R. F. (2003) · Trends in Microbiology · doi:10.1016/s0966-842x(03)00146-x · Cited by 56 · see citing works
Genomics of Dementia:APOE- andCYP2D6-Related Pharmacogenetics
Cacabelos, R., Martínez, R., Fernández‐Novoa, L., Carril, J. C., Lombardi, V., Carrera, I., Corzo, L., Tellado, I., Leszek, J., McKay, A., et al. (2012) · International Journal of Alzheimer s Disease · doi:10.1155/2012/518901 · Cited by 55 · see citing works
Receptor-associated Protein Interacts with Amyloid-β Peptide and Promotes Its Cellular Uptake
Kanekiyo, T., & Bu, G. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.015032 · Cited by 54 · see citing works
Heparan sulfate proteoglycans and triglyceride-rich lipoprotein metabolism
Bishop, J. R., Stanford, K. I., & Esko, J. D. (2008) · Current Opinion in Lipidology · doi:10.1097/mol.0b013e3282feec2d · Cited by 52 · see citing works
Functional role of extracellular vesicles and lipoproteins in the tumour microenvironment
Menard, J. A., Cerezo-Magaña, M., & Belting, M. (2017) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2016.0480 · Cited by 50 · see citing works
Alzheimer's Disease: Another Target for Heparin Therapy
Bergamaschini, L. C., Rossi, E., Vergani, C., & Simoni, M. G. D. (2009) · The Scientific World JOURNAL · doi:10.1100/tsw.2009.100 · Cited by 46 · see citing works
Tamamizu‐Kato, S., Wong, J. Y., Jairam, V., Uchida, K., Raussens, V., Kato, H., Ruysschaert, J., & Narayanaswami, V. (2007) · Biochemistry · doi:10.1021/bi700289k · Cited by 46 · see citing works
Hepatic Heparan Sulfate Proteoglycans and Endocytic Clearance of Triglyceride-Rich Lipoproteins
Foley, E. M., & Esko, J. D. (2010) · Progress in molecular biology and translational science · doi:10.1016/s1877-1173(10)93010-x · Cited by 45 · see citing works
Fagan, R. P., Lambert, M. A., & Smith, S. G. J. (2007) · Infection and Immunity · doi:10.1128/iai.01327-07 · Cited by 43 · see citing works
McMillan, I. O., Li, J., & Wang, L. (2023) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00247.2022 · Cited by 42 · see citing works
Heparan Sulfate as a Therapeutic Target in Tauopathies: Insights From Zebrafish
Naini, S. M. A., & Soussi‐Yanicostas, N. (2018) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2018.00163 · Cited by 39 · see citing works
Lund‐Katz, S., Nguyen, D., Dhanasekaran, P., Kono, M., Nickel, M., Saito, H., & Phillips, M. C. (2009) · Journal of Lipid Research · doi:10.1194/jlr.m002055 · Cited by 38 · see citing works
Self-citationYamada, Y., Sato, Y., Nakamura, T., & Harashima, H. (2020) · Journal of Controlled Release · doi:10.1016/j.jconrel.2020.09.007 · Cited by 39 · see citing works
Kato, N., Yamada, S., Suzuki, R., Iida, Y., Matsumoto, M., Fumoto, S., Arima, H., Mukai, H., & Kawakami, S. (2023) · Drug Delivery · doi:10.1080/10717544.2023.2173333 · Cited by 33 · see citing works
Cheung, M. C., & Albers, J. J. (2006) · Journal of Lipid Research · doi:10.1194/jlr.m600042-jlr200 · Cited by 31 · see citing works
Tran, K. M., Kwang, N. E., Butler, C. A., Gomez-Arboledas, A., Kawauchi, S., Mar, C., Chao, D., Barahona, R. A., Da Cunha, C., Tsourmas, K. I., et al. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-024-00793-x · Cited by 28 · see citing works
Sato, Y. (2021) · Chemical and Pharmaceutical Bulletin · doi:10.1248/cpb.c21-00705 · Cited by 28 · see citing works
Heparan sulfates and heparan sulfate binding proteins in sepsis
Liao, Y.-E., Liu, J., & Arnold, K. (2023) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2023.1146685 · Cited by 26 · see citing works
Glycosaminoglycan-Mediated Downstream Signaling of CXCL8 Binding to Endothelial Cells
Derler, R., Gesslbauer, B., Weber, C., Strutzmann, E., Miller, I., & Kungl, A. J. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18122605 · Cited by 25 · see citing works
Tran, T. N., Kosaraju, M. G., Tamamizu‐Kato, S., Akintunde, O., Zheng, Y. Y., Bielicki, J. K., Pinkerton, K. E., Uchida, K., Lee, Y. Y., & Narayanaswami, V. (2013) · Biochemistry · doi:10.1021/bi401404u · Cited by 26 · see citing works
Bång-Rudenstam, A., Cerezo-Magaña, M., & Belting, M. (2019) · Cancer and Metastasis Reviews · doi:10.1007/s10555-019-09786-5 · Cited by 25 · see citing works
Georgiadou, D., Chroni, A., Vezeridis, A., Zannis, V. I., & Stratikos, E. (2011) · PLoS ONE · doi:10.1371/journal.pone.0027037 · Cited by 24 · see citing works
What role for cellular metabolism in the control of hepatitis viruses?
Diaz, O., Vidalain, P., Ramière, C., Lotteau, V., & Perrin‐Cocon, L. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.1033314 · Cited by 22 · see citing works
Apolipoprotein E Recognizes Alzheimer's Disease Associated 3‐O Sulfation of Heparan Sulfate
Mah, D., Zhu, Y., Su, G., Zhao, J., Canning, A., Gibson, J. M., Song, X., Stancanelli, E., Xu, Y., Zhang, F., et al. (2023) · Angewandte Chemie International Edition · doi:10.1002/anie.202212636 · Cited by 23 · see citing works
Self-citationLeupold, E., Nikolenko, H., Beyermann, M., & Dathe, M. (2008) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2008.09.008 · Cited by 22 · see citing works
Zeng, X., Hou, Y., Luo, L., Ren, L., Wang, Y., Jin, X., Deng, L., Gao, Y., Zhang, D., Huang, J., et al. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.148054 · Cited by 23 · see citing works
Apolipoprotein E isoprotein-specific interactions with tissue plasminogen activator
Biehle, S. J., Carrozzella, J. A., Shukla, R., Popplewell, J. F., Swann, M. J., Freeman, N. J., & Clark, J. F. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.04.004 · Cited by 21 · see citing works
The Lipoprotein Transport System in the Pathogenesis of Multiple Myeloma: Advances and Challenges
Lazaris, V., Hatziri, A., Symeonidis, A. S., & Kypreos, K. E. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.638288 · Cited by 18 · see citing works
Structure–function properties of the apoE-dependent COX-2 pathway in vascular smooth muscle cells
Ali, K., Lund‐Katz, S., Lawson, J. A., Phillips, M. C., & Rader, D. J. (2007) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2007.03.038 · Cited by 17 · see citing works
Self-citationCortés, V., Amigo, L., Donoso, K., Valencia, I., Quiñones, V., Zanlungo, S., Brandan, E., & Rigotti, A. (2007) · Liver International · doi:10.1111/j.1478-3231.2007.01442.x · Cited by 17 · see citing works
Anower-E-Khuda, F., Singh, G., Deng, Y., Gordts, P. L. S. M., & Esko, J. D. (2019) · Glycobiology · doi:10.1093/glycob/cwz037 · Cited by 15 · see citing works
The Interplay of Apoes with Syndecans in Influencing Key Cellular Events of Amyloid Pathology
Hudák, A., Jósvay, K., Domonkos, I., Letoha, A., Szilák, L., & Letoha, T. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22137070 · Cited by 14 · see citing works
Rosenmann, H., Meiner, Z., Kahana, E., Aladjem, Z., Friedman, G., Ben‐Yehuda, A., Grenader, T., Wertman, E., & Abramsky, O. (2004) · American Journal of Medical Genetics Part B Neuropsychiatric Genetics · doi:10.1002/ajmg.b.30015 · Cited by 13 · see citing works
Holmes, B. B., Weigel, T. K., Chung, J. M., Kaufman, S. K., Apresa, B. I., Byrnes, J. R., Kumru, K. S., Vaquer‐Alicea, J., Gupta, A., Rose, I. V. L., et al. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-025-00883-4 · Cited by 13 · see citing works
The role of heparin/heparan sulphate in the IFN-γ-led Arena
Xu, K., & Jin, L. (2019) · Biochimie · doi:10.1016/j.biochi.2019.11.018 · Cited by 10 · see citing works
Apolipoprotein E, a Crucial Cellular Protein in the Lifecycle of Hepatitis Viruses
Tréguier, Y., Bull-Maurer, A., & Roingeard, P. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23073676 · Cited by 11 · see citing works
Kuot, A., Ronci, M., Mills, R. A., Klebe, S., Snibson, G. R., Wiffen, S. J., Loh, R. S. K., Corbett, M. A., Zhou, T., Chataway, T., et al. (2019) · Clinical and Experimental Ophthalmology · doi:10.1111/ceo.13569 · Cited by 10 · see citing works
Heparin protects against septic mortality via apoE-antagonism
Chuang, K., Leung, B., Hsu, N. Y.-H., & Harris, H. W. (2011) · The American Journal of Surgery · doi:10.1016/j.amjsurg.2010.10.017 · Cited by 10 · see citing works
Breaking Bruch's: How changes in Bruch's membrane influence retinal homeostasis
Clark, S. J., Curcio, C. A., Dick, A. D., Doyle, S., Edwards, M. M., Flores‐Bellver, M., Hass, D. T., Lennon, R., Toomey, C. B., & Rohrer, B. (2025) · Experimental Eye Research · doi:10.1016/j.exer.2025.110343 · Cited by 10 · see citing works
Lee, S., Grosskopf, I., Choi, S. Y., & Cooper, A. D. (2004) · Journal of Lipid Research · doi:10.1194/jlr.m400284-jlr200 · Cited by 9 · see citing works
Protective Effects of High-Density Lipoprotein on Cancer Risk: Focus on Multiple Myeloma
Allegra, A., Murdaca, G., Mirabile, G., & Gangemi, S. (2024) · Biomedicines · doi:10.3390/biomedicines12030514 · Cited by 8 · see citing works
Recruitment of apolipoprotein E facilitates Herpes simplex virus 1 attachment and release
Liu, L., Bano, F., Conca, D. V., Thorsteinsson, K., Jayaweera, S. W., Avinens, D., Pace, H. P., Lövheim, H., Olofsson, A., & Bally, M. (2025) · npj Viruses · doi:10.1038/s44298-025-00099-9 · Cited by 8 · see citing works
Al‐Horani, R. A., Afosah, D. K., Kar, S., Aliter, K. F., & Mottamal, M. (2023) · RPS Pharmacy and Pharmacology Reports · doi:10.1093/rpsppr/rqad001 · Cited by 7 · see citing works
Expression of human liver HSPGs on acute myeloid leukemia
Vongchan, P., & Linhardt, R. J. (2006) · Clinical Immunology · doi:10.1016/j.clim.2006.08.017 · Cited by 6 · see citing works
Self-citationSyndecan 2 proteoglycan serves as a hepatitis B virus cell attachment receptor
Tripathi, S. K., Li, Y., & Luo, G. G. (2025) · Journal of Virology · doi:10.1128/jvi.00796-25 · Cited by 5 · see citing works
Physiological, Pathophysiological and Therapeutic Roles of Heparin and Heparan Sulfate
Xie, J., Murugesan, S., & Linhardt, R. J. (2008) · Elsevier eBooks · doi:10.1016/b978-0-08-054816-6.00010-0 · Cited by 4 · see citing works
Self-citationVongchan, P., Kothan, S., Wutti-In, Y., & Linhardt, R. J. (2011) · PubMed · Cited by 4 · see citing works
Self-citationAndré, C., Lethier, L., Adotévi, O., & Guillaume, Y. C. (2023) · Analytical Methods · doi:10.1039/d3ay00046j · Cited by 3 · see citing works
Apolipoprotein E Recognizes Alzheimer's Disease Associated 3‐O Sulfation of Heparan Sulfate
Mah, D., Zhu, Y., Su, G., Zhao, J., Canning, A., Gibson, J. M., Song, X., Stancanelli, E., Xu, Y., Zhang, F., et al. (2023) · Angewandte Chemie · doi:10.1002/ange.202212636 · Cited by 3 · see citing works
Self-citationOlivieri, P. H., Hayashi, J. Y., Torquato, R. J. S., Lima, A. F., Pereira, T. P., Lima, I. F., Fonseca, F. L. A., Iwai, L. K., Nader, H. B., Tashima, A. K., et al. (2025) · ACS Nano · doi:10.1021/acsnano.5c19714 · Cited by 2 · see citing works
Mahley, R. W. (2025) · Springer eBooks · doi:10.1007/978-3-031-52641-1_2-1 · Cited by 1 · see citing works
The Structural and Functional Journey of Apolipoprotein A-I Through the Human Body
Powell, S. M., You, Y., Ogbu, C. P., & Melchior, J. (2026) · Current Atherosclerosis Reports · doi:10.1007/s11883-026-01405-3 · Cited by 1 · see citing works
Marcotrigiano, J., & Catanese, M. T. (2016) · Springer eBooks · doi:10.1007/978-4-431-56098-2_3 · Cited by 1 · see citing works
The effects of triglyceride on lysosomal function in macrophage foam cells.
Ullery, J. C. (2009) · Europe PMC (PubMed Central) · Cited by 1 · see citing works
GPR182 is a lipoprotein receptor for dietary fat absorptionPreprint
Sun, Z., Torphy, R. J., Miller, E. N., Darehshouri, A., Vigil, I., Terai, T., Eleanor, E., Sun, Y., Guo, Y., Yee, E. J., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.02.03.634329 · Cited by 1 · see citing works
Apolipoprotein C-I and Apolipoprotein E Production During Adipocyte Differentiation
Nguyen, A. T. (2009) · Library, Museums and Press - UDSpace (University of Delaware)
- Authors
- Libeu, C. P., Lund-Katz, S., Phillips, M. C., Wehrli, S., Hernáiz, M. J., Capila, I., Linhardt, R. J., Raffaı̈, R. L., Newhouse, Y. M., Zhou, F., & Weisgraber, K. H.
- Affiliations
- Gladstone Institutes (US)
- Children's Hospital of Philadelphia (US)
- University of Iowa (US)
- Texas A&M University (US)
- Corresponding author
- Weisgraber, Karl H.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2001-10
- Volume
- 276
- Issue
- 42
- Pages
- 39138-39144
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2106771721
- Cited by
- 113
- References
- 61
- Citations by year
- 2026: 5 · 2025: 12 · 2024: 2 · 2023: 8 · 2022: 4 · 2021: 3 · 2020: 3 · 2019: 5 · 2018: 2 · 2017: 3 · 2016: 3 · 2015: 2 · 2014: 5 · 2013: 2 · 2012: 2
- FWCI
- 2.04
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Heart, Lung, and Blood Institute (HL-41633, P01HL041633, R01HL056083, HL-56083, HL 52622, R01HL052622)
- National Institute of General Medical Sciences (GM38060, R01GM038060)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Proteoglycans and glycosaminoglycans research
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Surgery › Cholesterol and Lipid Metabolism
- Keywords
- apolipoprotein E, heparan sulfate proteoglycans, heparin-binding site, iduronic acid, glucosamine sulfate, atherosclerosis, Alzheimer's disease, lipoprotein clearance, binding site modeling
- MeSH terms
- Animals, Apolipoproteins E, Arginine, Binding Sites, Brain, Cattle, Chromatography, Affinity, Dose-Response Relationship, Drug, Glucosamine, Heparin, Humans, Hydrogen-Ion Concentration, Kinetics, Liver, Lysine, Models, Molecular, Mutation, Magnetic Resonance Spectroscopy, Polysaccharides, Protein Binding, Serine, Time Factors, Streptavidin, Heparan Sulfate Proteoglycans, Biotinylation, Surface Plasmon Resonance
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
