The DOI matches its Crossref record; 87 of the 88 references it cites were found in a registry or an index.
Apolipoprotein E structure: insights into function
Abstract
Human apolipoprotein E (apoE) is a member of the family of soluble apolipoproteins. Through its interaction with members of the low-density lipoprotein receptor family, apoE has a key role in lipid transport both in the plasma and in the central nervous system. Its three common structural isoforms differentially affect the risk of developing atherosclerosis and neurodegenerative disorders, including Alzheimer's disease. Because the function of apoE is dictated by its structure, understanding the structural properties of apoE and its isoforms is required both to determine its role in disease and for the development of therapeutic strategies.
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?
In the citing paper
“Several biophysical studies have shown that apoE displays low thermodynamic stability and significant conformational plasticity, and allelic differences as well as single point mutations have been shown to affect protein conformation and to hinder physiological function”
From Thermodynamic destabilization and aggregation propensity as the mechanism behind the association of apoE3 mutants and lipoprotein glomerulopathy (2018) · cites this paper as [13]
In the citing paper
“Several biophysical studies have shown that apoE displays low thermodynamic stability and significant conformational plasticity, and allelic differences as well as single point mutations have been shown to affect protein conformation and to hinder physiological function”
From Thermodynamic destabilization and aggregation propensity as the mechanism behind the association of apoE3 mutants and lipoprotein glomerulopathy (2018) · cites this paper as [13]
In the citing paper
“Inter-domain interactions within apoE have been hypothesized to underlie key conformational changes related to apoE function [44], [45].”
From Biophysical Analysis of Apolipoprotein E3 Variants Linked with Development of Type III Hyperlipoproteinemia (2011) · cites this paper as [44]
In the citing paper
“Several studies have suggested that the structural and biophysical properties of apoE can dictate the function of the protein and have provided insight into the mechanisms by which apoE is involved in cardiovascular and neurological diseases [42], [43], [44], [45], [46], [47], [48], [49].”
From Biophysical Analysis of Apolipoprotein E3 Variants Linked with Development of Type III Hyperlipoproteinemia (2011) · cites this paper as [44]
In the citing paper
“of the second unfolding transition of apoE3 variant (Table 3) that corresponds to the unfolding of the N-terminal domain where the K146E mutation is located [13], [44], [65].”
From Biophysical Analysis of Apolipoprotein E3 Variants Linked with Development of Type III Hyperlipoproteinemia (2011) · cites this paper as [44]
In the citing paper
“Apo E4 isoform is associated with elevated total and LDL-cholesterol levels, due to the higher affinity of apo E4 for VLDL and LDL”
From Description of a Large Family with Autosomal Dominant Hypercholesterolemia Associated with the APOE p.Leu167del Mutation (2013) · cites this paper as Hatters DM et al. 2006
In the citing paper
“Mutated ApoE2 (Arg158Cys) exhibits only 2% affinity to LDL receptor compared to the wide type ApoE3 isoform [13]”
From A case report of youth-onset lipoprotein glomerulopathy with APOE Chicago mutation (2024) · cites this paper as [13]
In the citing paper
“Biophysical and computational analyses suggest that unfolding of the N-terminal domain constitutes a necessary conformational change for lipid binding and apoE function (19).”
From Molecular Basis for Increased Risk for Late-onset Alzheimer Disease Due to the Naturally Occurring L28P Mutation in Apolipoprotein E4 (2014) · cites this paper as [19]
In the citing paper
“ApoE variants with lower thermodynamic stability and changes in conformational plasticity have been shown to have altered interdomain interactions and defective physiological functions (19, 24 -28).”
From Molecular Basis for Increased Risk for Late-onset Alzheimer Disease Due to the Naturally Occurring L28P Mutation in Apolipoprotein E4 (2014) · cites this paper as [19]
In the citing paper
“First, apoE4 preferentially forms a “molten globule state” that ultimately reduces the in vitro stability of apoE4 relative to the other isoforms.”
From Impact of Apolipoprotein E (ApoE) Polymorphism on Brain ApoE Levels (2008) · cites this paper as Hatters et al., 2006
In the citing paper
“Second, apoE4 forms a unique salt bridge interaction between Arg-61 in the N terminal and Glu-255 in the carboxy-terminal domain.”
From Impact of Apolipoprotein E (ApoE) Polymorphism on Brain ApoE Levels (2008) · cites this paper as Hatters et al., 2006
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 [19]
In the citing paper
“This domain interaction mediated by a salt bridge formation between Arg-61 and Glu-255 is unique to apoE4 (Fig. 1) [15].”
From Apolipoprotein E4, inhibitory network dysfunction, and Alzheimer’s disease (2019) · cites this paper as [15]
Citations
Cites
2 retracted
Ajees, A. A., Anantharamaiah, G. M., Mishra, V., Hussain, M. M., & Murthy, H. M. K. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506877103 · Cited by 204
RetractedKumar, M., Carson, M. A., Hussain, M. M., & Murthy, H. M. K. (2002) · Biochemistry · doi:10.1021/bi026069w · Cited by 33
RetractedThe Metabolic and Molecular Bases of Inherited Disease
Scriver, R. C. (1995) · Medical Entomology and Zoology · Cited by 12,101
Corder, E. H., Saunders, A. M., Strittmatter, W. J., Schmechel, D. E., Gaskell, P. C., Small, G. W., Roses, A. D., Haines, J. L., & Pericak-Vance, M. A. (1993) · Science · doi:10.1126/science.8346443 · Cited by 9,429
The metabolic and molecular bases of inherited disease
Chen, Y.-T. (2001) · Medical Entomology and Zoology · Cited by 6,928
Association of apolipoprotein E allele ϵ4 with late‐onset familial and sporadic Alzheimer's disease
Saunders, A. M., Strittmatter, W. J., Schmechel, D., St. George-Hyslop, P. H., Pericak-Vance, M. A., Joo, S. H., Rosi, B. L., Gusella, J. F., Crapper-MacLachlan, D. R., Alberts, M. J., et al. (1993) · Neurology · doi:10.1212/wnl.43.8.1467 · Cited by 3,786
Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm
Wright, P. E., & Dyson, H. J. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3110 · Cited by 2,968
The plasma lecithin:cholesterol acyltransferase reaction
Glomset, J. A. (1968) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)43114-1 · Cited by 2,396
Strittmatter, W. J., Weisgraber, K. H., Huang, D. Y., Dong, L. M., Salvesen, G. S., Pericak-Vance, M., Schmechel, D., Saunders, A. M., Goldgaber, D., & Roses, A. D. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.17.8098 · Cited by 1,363
Self-citationMolten Globule and Protein Folding
Ptitsyn, O. B. (1995) · Advances in protein chemistry · doi:10.1016/s0065-3233(08)60546-x · Cited by 1,222
Holtzman, D. M., Bales, K. R., Tenkova, T., Fagan, A. M., Parsadanian, M., Sartorius, L. J., Mackey, B., Olney, J., McKeel, D., Wozniak, D., et al. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.050004797 · Cited by 937
The structural basis of protein folding and its links with human disease
Dobson, C. M. (2001) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2000.0758 · Cited by 934
Segrest, J., Jones, M., Loof, H. D., Brouillette, C. G., Venkatachalapathi, Y. V., & Anantharamaiah, G. M. (1992) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)41536-6 · Cited by 868
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-citationWeisgraber, K. H., Rall, S. C., & Mahley, R. W. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)52510-8 · Cited by 777
Self-citationMiyata, M., & Smith, J. D. (1996) · Nature Genetics · doi:10.1038/ng0996-55 · Cited by 735
Three-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., Innerarity, T. L., & Mahley, R. W. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)34954-8 · Cited by 673
Self-citationApolipoprotein E ε4 allele is associated with deposition of amyloid β-protein following head injury
Nicoll, J. A. R., Roberts, G. W., & Graham, D. I. (1995) · Nature Medicine · doi:10.1038/nm0295-135 · Cited by 486
Kowal, R. C., Herz, J., Weisgraber, K. H., Mahley, R. W., Brown, M. S., & Goldstein, J. L. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)87014-4 · Cited by 445
Self-citationCrystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation
Borhani, D. W., Rogers, D. P., Engler, J. A., & Brouillette, C. G. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.23.12291 · Cited by 434
Brecht, W. J., Harris, F. M., Chang, S., Tesseur, I., Yu, G.-Q., Xu, Q., Dee Fish, J., Wyss-Coray, T., Buttini, M., Mucke, L., et al. (2004) · The Journal of Neuroscience · doi:10.1523/jneurosci.4315-03.2004 · Cited by 403
Huang, Y., Liu, X. Q., Wyss-Coray, T., Brecht, W. J., Sanan, D. A., & Mahley, R. W. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.151254698 · Cited by 392
Buttini, M., Orth, M., Bellosta, S., Akeefe, H., Pitas, R. E., Wyss‐Coray, T., Mucke, L., & Mahley, R. W. (1999) · Journal of Neuroscience · doi:10.1523/jneurosci.19-12-04867.1999 · Cited by 363
Harris, F. M., Brecht, W. J., Xu, Q., Tesseur, I., Kekonius, L., Wyss-Coray, T., Fish, J. D., Masliah, E., Hopkins, P. C., Scearce-Levie, K., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1434398100 · Cited by 342
Self-citationDong, 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
Self-citationHuman Apolipoprotein E4 Domain Interaction
Dong, L.-M., & Weisgraber, K. H. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.32.19053 · Cited by 318
Self-citationMorrow, J. A., Segall, M. L., Lund-Katz, S., Phillips, M. C., Knapp, M., Rupp, B., & Weisgraber, K. H. (2000) · Biochemistry · doi:10.1021/bi000099m · Cited by 315
Self-citationWeisgraber, K. H. (1990) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)42621-5 · Cited by 304
Self-citationHuman apolipoprotein E3 in aqueous solution. I. Evidence for two structural domains.
Wetterau, J. R., Aggerbeck, L. P., Rall, S. C., & Weisgraber, K. H. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)68778-2 · Cited by 293
Self-citationThe 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
Self-citationInnerarity, T. L., Pitas, R. E., & Mahley, R. W. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)50713-4 · Cited by 246
Huang, Y., Weisgraber, K. H., Mucke, L., & Mahley, R. W. (2004) · Journal of Molecular Neuroscience · doi:10.1385/jmn:23:3:189 · Cited by 242
Self-citationLalazar (1989) · doi:10.1016/s0021-9258(18)81806-3 · Cited by 238
Weisgraber, K. H., Mahley, R. W., Kowal, R. C., Herz, J., Goldstein, J. L., & Brown, M. S. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)45726-2 · Cited by 235
Self-citationMolecular structure of an apolipoprotein determined at 2.5-.ANG. resolution
Breiter, D. R., Kanost, M. R., Benning, M. M., Wesenberg, G. E., Law, J. H., Wells, M. A., Rayment, I., & Holden, H. M. (1991) · Biochemistry · doi:10.1021/bi00217a002 · Cited by 229
Montine, K. S., Olson, S. J., Amarnath, K., Whetsell, W. O., Graham, D. G., & Montine, T. J. (1997) · Europe PMC (PubMed Central) · Cited by 220
Luc, G., Bard, J., Arveiler, D., Evans, A., Cambou, J., Bingham, A., Amouyel, P., Schaffer, P., Ruidavets, J., & Cambien, F. (1994) · Arteriosclerosis and Thrombosis A Journal of Vascular Biology · doi:10.1161/01.atv.14.9.1412 · Cited by 215
Apolipoprotein E4 Forms a Molten Globule
Morrow, J. A., Hatters, D. M., Lu, B., Höchtl, P., Oberg, K. A., Rupp, B., & Weisgraber, K. H. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204898200 · Cited by 204
Self-citationIntroduction of human apolipoprotein E4 “domain interaction” into mouse apolipoprotein E
Raffaı̈, R. L., Dong, L., Farese, R. V., & Weisgraber, K. H. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.201279298 · Cited by 201
Self-citationJi, Z.-S., Miranda, R. D., Newhouse, Y. M., Weisgraber, K. H., Huang, Y., & Mahley, R. W. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m112109200 · Cited by 177
Self-citationPutting cholesterol in its place: apoE and reverse cholesterol transport
Mahley, R. W. (2006) · Journal of Clinical Investigation · doi:10.1172/jci28632 · Cited by 173
Increased Plasma and Lipoprotein Lipid Peroxidation in apo E-Deficient Mice
Hayek, T., Oiknine, J., Brook, J. G., & Aviram, M. (1994) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1994.1883 · Cited by 171
Gursky, O., & Atkinson, D. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.7.2991 · Cited by 167
Koo, C., Innerarity, T. L., & Mahley, R. W. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38968-8 · Cited by 162
Gianturco, S. H., Gotto, A. M., Hwang, S. L., Karlin, J. B., Lin, A., Prasad, S. C., & Bradley, W. A. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)32655-3 · Cited by 161
Is Alzheimer's disease an apolipoprotein E amyloidosis?
Wisniewski, T., Lalowski, M., Golabek, A., Frangione, B., & Vogel, T. (1995) · The Lancet · doi:10.1016/s0140-6736(95)90701-7 · Cited by 155
Montine, K. S., Reich, E. E., Neely, M. D., Sidell, K. R., Olson, S. J., Markesbery, W. R., & Montine, T. J. (1998) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-199805000-00005 · Cited by 153
Molecular basis of exchangeable apolipoprotein function
Narayanaswami, V., & Ryan, R. O. (2000) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/s1388-1981(99)00176-6 · Cited by 152
Pitas, R. E., Innerarity, T. L., & Mahley, R. W. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)70808-4 · Cited by 138
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
Self-citationReactivity of Apolipoprotein E4 and Amyloid β Peptide
Ji, Z.-S., Müllendorff, K., Cheng, I. H., Miranda, R. D., Huang, Y., & Mahley, R. W. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m506646200 · Cited by 127
Farrer, L. A. (1997) · JAMA · doi:10.1001/jama.1997.03550160069041 · Cited by 124
Behavior of human apolipoprotein E in aqueous solutions and at interfaces.
Yokoyama, S., Kawai, Y., Tajima, S., & Yamamoto, A. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36247-6 · Cited by 114
Lipid Binding-induced Conformational Change in Human Apolipoprotein E
Saito, H., Dhanasekaran, P., Baldwin, F., Weisgraber, K. H., Lund-Katz, S., & Phillips, M. C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106337200 · Cited by 113
Self-citationWang, J., Sykes, B. D., & Ryan, R. O. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.032565999 · Cited by 104
Dolev, I., & Michaelson, D. M. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0404458101 · Cited by 102
Lipid binding-induced conformational changes in the N-terminal domain of human apolipoprotein E
Fisher, C. A., & Ryan, R. O. (1999) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)33343-5 · Cited by 95
Lu, B., Morrow, J. A., & Weisgraber, K. H. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003508200 · Cited by 89
Modulation of Apolipoprotein E Structure by Domain Interaction
Hatters, D. M., Budamagunta, M. S., Voss, J. C., & Weisgraber, K. H. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506044200 · Cited by 88
Self-citationThe Low Density Lipoprotein Receptor Active Conformation of Apolipoprotein E
Raussens, V., Fisher, C. A., Goormaghtigh, E., Ryan, R. O., & Ruysschaert, J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.40.25825 · Cited by 88
The structural basis for amyloid formation by plasma apolipoproteins: a review
Hatters, D. M., & Howlett, G. J. (2002) · European Biophysics Journal · doi:10.1007/s002490100172 · Cited by 86
Self-citationAcharya, P., Segall, M. L., Zaiou, M., Morrow, J., Weisgraber, K. H., Phillips, M. C., Lund-Katz, S., & Snow, J. (2002) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/s1388-1981(02)00263-9 · Cited by 82
Self-citationModel of Biologically Active Apolipoprotein E Bound to Dipalmitoylphosphatidylcholine
Peters-Libeu, C. A., Newhouse, Y., Hatters, D. M., & Weisgraber, K. H. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m510851200 · Cited by 82
Self-citationDavidson, W. S., & Silva, R. G. D. (2005) · Current Opinion in Lipidology · doi:10.1097/01.mol.0000169349.38321.ad · Cited by 80
Xu, Q., Brecht, W. J., Weisgraber, K. H., Mahley, R. W., & Huang, Y. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311256200 · Cited by 80
Self-citationFisher, C. A., Narayanaswami, V., & Ryan, R. O. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002643200 · Cited by 78
Narayanaswami, V., Maiorano, J. N., Dhanasekaran, P., Ryan, R. O., Phillips, M. C., Lund‐Katz, S., & Davidson, W. S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313318200 · Cited by 77
Conformational, thermodynamic, and stability properties of Manduca sexta apolipophorin III.
Ryan, R. O., Oikawa, K., & Kay, C. M. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53884-9 · Cited by 71
Effect of Arginine 172 on the Binding of Apolipoprotein E to the Low Density Lipoprotein Receptor
Morrow, J. A., Arnold, K. S., Dong, J., Balestra, M. E., Innerarity, T. L., & Weisgraber, K. H. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.4.2576 · Cited by 67
Self-citationAmyloid β‐Peptide Effects on Synaptosomes from Apolipoprotein E‐Deficient Mice
Keller, J. N., Lauderback, C. M., Butterfield, D. A., Kindy, M. S., Yu, J., & Markesbery, W. R. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0741579.x · Cited by 63
Increased 3-nitrotyrosine in brains of Apo E-deficient mice
Matthews, R. T., & Beal, M. F. (1996) · Brain Research · doi:10.1016/0006-8993(95)01576-0 · Cited by 57
The Receptor Binding Domain of Apolipoprotein E Is Responsible for Its Antioxidant Activity
Pham, T., Kodvawala, A., & Hui, D. Y. (2005) · Biochemistry · doi:10.1021/bi0472696 · Cited by 52
Krul, E. S., Tikkanen, M. J., & Schonfeld, G. (1988) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)38434-0 · Cited by 50
Modulation of the lipid binding properties of the N‐terminal domain of human apolipoprotein E3
Weers, P. M. M., Narayanaswami, V., & Ryan, R. O. (2001) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2001.02282.x · Cited by 47
Segrest, J. P., Harvey, S. C., & Zannis, V. I. (2000) · Trends in Cardiovascular Medicine · doi:10.1016/s1050-1738(00)00078-5 · Cited by 43
High‐ and low‐temperature unfolding of human high‐density apolipoprotein A‐2
Gursky, O., & Atkinson, D. (1996) · Protein Science · doi:10.1002/pro.5560050913 · Cited by 43
Ishikawa, Y., Fielding, C. J., & Fielding, P. E. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)69131-8 · Cited by 41
Structural Analysis of Lipoprotein E Particles
Schneeweis, L. A., Koppaka, V., Lund-Katz, S., Phillips, M. C., & Axelsen, P. H. (2005) · Biochemistry · doi:10.1021/bi050872j · Cited by 39
Engineering Conformational Destabilization into Mouse Apolipoprotein E
Hatters, D. M., Peters-Libeu, C. A., & Weisgraber, K. H. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503910200 · Cited by 38
Self-citationExamination of Lipid-bound Conformation of Apolipoprotein E4 by Pyrene Excimer Fluorescence
Drury, J., & Narayanaswami, V. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414019200 · Cited by 37
Perugini, M. A., Schuck, P., & Howlett, G. J. (2002) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2002.03319.x · Cited by 35
Orientation and mode of lipid-binding interaction of human apolipoprotein E C-terminal domain
Raussens, V., Drury, J., Forte, T. M., Choy, N., Goormaghtigh, E., Ruysschaert, J., & Narayanaswami, V. (2005) · Biochemical Journal · doi:10.1042/bj20041536 · Cited by 35
Weers, P. M. M., Abdullahi, W. E., Cabrera, J. M., & Hsu, T.-C. (2005) · Biochemistry · doi:10.1021/bi050502v · Cited by 26
Apolipoprotein E-Related Neurotoxicity as a Therapeutic Target for Alzheimer's Disease
Marques, M. A., & Crutcher, K. A. (2003) · Journal of Molecular Neuroscience · doi:10.1385/jmn:20:3:327 · Cited by 17
Newhouse, Y., Peters-Libeu, C., & Weisgraber, K. H. (2005) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s1744309105032410 · Cited by 15
Self-citationReplacement of helix 1′ enhances the lipid binding activity of apoE3 N‐terminal domain
Redmond, K. A., Murphy, C., Narayanaswami, V., Kiss, R. S., Hauser, P. S., Guigard, E., Kay, C. M., & Ryan, R. O. (2006) · FEBS Journal · doi:10.1111/j.1742-4658.2005.05089.x · Cited by 9
Flagged first, then by citations
1 of the 88 references couldn’t be matched to a known paper.
Research works printed but not linked: 1
- Pitas, 1980, Cell surface receptor binding of phospholipid–protein complexes containing different ratios of receptor-active and -inactive E apoprotein, J. Biol. Chem., 255, 5454, 10.1016/S0021-9258(19)70808-4 · DOI · Paper page
Cited by
Sorted by citations
Lipid Droplets and Cellular Lipid Metabolism
Walther, T. C., & Farese, R. V. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061009-102430 · Cited by 1,701
“Apo E binds lipoproteins by opening its four-helix bundle and exposing hydrophobic, amphipathic sequences to the lipid surface (86).”
BackgroundApolipoprotein E and Alzheimer disease: pathobiology and targeting strategies
Yamazaki, Y., Zhao, N., Caulfield, T. R., Liu, C.-C., & Bu, G. (2019) · Nature Reviews Neurology · doi:10.1038/s41582-019-0228-7 · Cited by 1,425
Apolipoprotein E and its receptors in Alzheimer's disease: pathways, pathogenesis and therapy
Bu, G. (2009) · Nature Reviews Neuroscience · doi:10.1038/nrn2620 · Cited by 1,168
“Human APOE contains 299 amino acid residues and has independently folded amino-terminal and carboxy-terminal domains, which are joined together by a flexible hinge regio”
BackgroundMolecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease
Guo, T., Zhang, D., Zeng, Y., Huang, T. Y., Xu, H., & Zhao, Y. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00391-7 · Cited by 994
“ε2 encodes Cys residues at the position 112 and 158, ε3 encodes a Cys residue at position 112 and a Arg residue at position 158, and ε4 comprises Arg residues at both positions [447].”
BackgroundBrasaemle, D. (2007) · Journal of Lipid Research · doi:10.1194/jlr.r700014-jlr200 · Cited by 997
“helices into the acyl chains of the surface phospholipid monolayer of lipoproteins (34, 35).”
Metadata
- Authors
- Hatters, D. M., Peters-Libeu, C. A., & Weisgraber, K. H.
- Affiliations
- Gladstone Institutes (US)
- Corresponding author
- Weisgraber, Karl H.
- ORCID
- Hatters, Danny M.
- Venue
- Trends in Biochemical Sciences
- Publisher
- Elsevier BV
- Published
- 2006-08
- Volume
- 31
- Issue
- 8
- Pages
- 445-454
- ISSN
- 0968-0004 (ISSN-L)
- OpenAlex
- W2051394059
- Cited by
- 583
- References
- 88
- Citations by year
- 2026: 25 · 2025: 32 · 2024: 26 · 2023: 32 · 2022: 34 · 2021: 37 · 2020: 22 · 2019: 21 · 2018: 24 · 2017: 25 · 2016: 32 · 2015: 32 · 2014: 42 · 2013: 24 · 2012: 42
- FWCI
- 2.88
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- Trends in Biochemical Sciences (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute on Aging (R01AG020235, P01AG022074)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Lipoproteins and Cardiovascular Health
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Cholesterol and Lipid Metabolism
- Keywords
- apolipoprotein E, protein structure, APOE isoforms, low-density lipoprotein receptor family, lipid transport, atherosclerosis, Alzheimer's disease, neurodegenerative diseases, central nervous system, treatment options
- MeSH terms
- Animals, Apolipoproteins E, Humans, Models, Molecular, Protein Binding, Protein Folding, Neurodegenerative Diseases, Protein Isoforms, Atherosclerosis
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
