The DOI matches its Crossref record; 48 of the 48 references it cites were found in a registry or an index.
Lipidation of apolipoprotein E influences its isoform-specific interaction with Alzheimer's amyloid β peptides
Open accessAbstract
The inheritance of the apolipoprotein E (apoE) ϵ4 allele is a prevailing risk factor for sporadic and familial Alzheimer's disease (AD). ApoE isoforms bind directly to Alzheimer's amyloid β (Aβ) peptides both in vitro and in vivo. Recent studies suggest that association of apoE with lipids may modulate its interaction with Aβ. We examined the binding of lipid-associated and delipidated apoE3 and apoE4 isoforms to Aβ utilizing a solid-phase binding assay and estimated the dissociation constants for the interaction of various apoE and Aβ species. Using native apoE isoforms from stably transfected RAW 264 and human embryonic kidney 293 cells, apoE3 had greater affinity than apoE4 for both Aβ1-40 and Aβ1-42. Delipidation of apoE decreased its affinity for Aβ peptides by 5-10-fold and abolished the isoform-specificity. Conversely, incorporation of apoE isoforms produced by baculovirus-infected Sf9 cells into reconstituted human high-density-lipoprotein lipoparticles restored the affinity values for Aβ peptides and resulted in preferential binding of apoE3. The data demonstrate that native lipid-associated apoE3 binds to Aβ peptides with 2-3-fold higher affinity than lipid-associated apoE4. Since the isoforms' binding efficiency correlate inversely with the risk of developing late-onset AD, the results suggest a possible involvement of apoE3 in the clearance or routing out of Aβ from the central nervous system as one of the mechanisms underlying the pathology of the disease.
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?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Increased levels of ApoE and lipidation of ApoE increase the intra-and extracellular microglial degradation of Ab 1 -42 by increasing the interaction between ApoE and Ab 1 -42 (15).”
From SUCLG2 identified as both a determinator of CSF Aβ1–42 levels and an attenuator of cognitive decline in Alzheimer's disease (2014) · cites this paper as [15]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Several in vitro studies have demonstrated that lipidated apoE2 and apoE3 bind Aβ with greater affinity compared to apoE4 (39, 51-54).”
From Human ApoE isoforms differentially regulate brain amyloid-β peptide clearance (2011) · cites this paper as [54]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Most studies demonstrate that the efficiency of complex formation between lipidated apoE and Aβ follows the order of apoE2 > apoE3 ≫ apoE4 (Tokuda et al., 2000).”
From The role of apolipoprotein E in Alzheimer's disease (2009) · cites this paper as Tokuda et al., 2000
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“studies have demonstrated that apoE4 does not clear plaques or soluble Aβ as well as apoE3 [45, 46].”
From Inhibition of ACAT as a Therapeutic Target for Alzheimer's Disease Is Independent of ApoE4 Lipidation (2023) · cites this paper as [45]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“High-affinity in vitro binding of A b to a 2M and to lipidated apoE3 and apoE4, and a lower-affinity binding to delipidated apoE isoforms has been well documented (23, 70).”
From Clearance of Alzheimer’s amyloid-β1-40 peptide from brain by LDL receptor–related protein-1 at the blood-brain barrier (2000) · cites this paper as [70]
Experimental — accuracy not yet measured
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
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
Strittmatter, W. J., Saunders, A. M., Schmechel, D., Pericak-Vance, M., Enghild, J., Salvesen, G. S., & Roses, A. D. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.5.1977 · Cited by 4,268
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
Diffusible, nonfibrillar ligands derived from Aβ 1–42 are potent central nervous system neurotoxins
Lambert, M. P., Barlow, A. K., Chromy, B. A., Edwards, C., Freed, R., Liosatos, M., Morgan, T. E., Rozovsky, I., Trommer, B., Viola, K. L., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6448 · Cited by 3,506
Isolation and quantification of soluble Alzheimer's β-peptide from biological fluids
Seubert, P., Vigo-Pelfrey, C., Esch, F., Lee, M., Dovey, H., Davis, D., Sinha, S., Schiossmacher, M., Whaley, J., Swindlehurst, C., et al. (1992) · Nature · doi:10.1038/359325a0 · Cited by 1,731
Schmechel, D. E., Saunders, A. M., Strittmatter, W. J., Crain, B. J., Hulette, C. M., Joo, S. H., Pericak-Vance, M. A., Goldgaber, D., & Roses, A. D. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.20.9649 · Cited by 1,525
Production of the Alzheimer Amyloid β Protein by Normal Proteolytic Processing
Shoji, M., Golde, T. E., Ghiso, J., Cheung, T. T., Estus, S., Shaffer, L. M., Cai, X.-D., McKay, D. M., Tintner, R., Frangione, B., et al. (1992) · Science · doi:10.1126/science.1439760 · Cited by 1,447
Self-citationStrittmatter, 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
Namba, Y., Tomonaga, M., Kawasaki, H., Otomo, E., & Ikeda, K. (1991) · Brain Research · doi:10.1016/0006-8993(91)91092-f · Cited by 1,157
Apolipoprotein E in sporadic Alzheimer's disease: Allelic variation and receptor interactions
William Rebeck, G., Reiter, J. S., Strickland, D. K., & Hyman, B. T. (1993) · Neuron · doi:10.1016/0896-6273(93)90070-8 · Cited by 1,107
Research works printed but not linked: 1
- Rebeck, G. W. and Hyman. B. T. (1999) Lipoprotein receptors in brain. In Clusterin in Normal Brain Functions and during Neurodegeneration (Finch, C. E., ed.), pp. 49-59, R. G. Landes Co., Austin 45
Cited by
Sorted by citations
Items 101–200 of 272
Alzheimer’s Disease Risk Genes and Lipid Regulators
Gaamouch, F. E., Jing, P., Xia, J., & Cai, D. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160169 · Cited by 67
Transcriptional Effects of ApoE4: Relevance to Alzheimer’s Disease
Theendakara, V., Peters-Libeu, C. A., Bredesen, D. E., & Rao, R. V. (2018) · Molecular Neurobiology · doi:10.1007/s12035-017-0757-2 · Cited by 63
Hirsch-Reinshagen, V., & Wellington, C. L. (2007) · Current Opinion in Lipidology · doi:10.1097/mol.0b013e32813aeabf · Cited by 61
Hong-xin, F., Zhang, Y., Liu, T., Zhang, X., & Wu, S. (2017) · Bioscience Biotechnology and Biochemistry · doi:10.1080/09168451.2017.1399788 · Cited by 62
Minh, T. N., Dodacki, A., Alata, W., Calon, F., Nicolic, S., Scherrmann, J., Farinotti, R., & Bourasset, F. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-150350 · Cited by 65
Isoform-specific proteolysis of apolipoprotein-E in the brain
Elliott, D. A., Tsoi, K., Holinkova, S., Chan, S. L., Kim, W. S., Halliday, G. M., Rye, K., & Garner, B. (2009) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2009.02.006 · Cited by 59
Prenatal high‐fat diet alters the cerebrovasculature and clearance of β‐amyloid in adult offspring
Hawkes, C. A., Gentleman, S., Nicoll, J. A. R., & Carare, R. O. (2014) · The Journal of Pathology · doi:10.1002/path.4468 · Cited by 56
Interaction with Amyloid β Peptide Compromises the Lipid Binding Function of Apolipoprotein E
Tamamizu‐Kato, S., Cohen, J. K., Drake, C. B., Kosaraju, M. G., Drury, J., & Narayanaswami, V. (2008) · Biochemistry · doi:10.1021/bi702097s · Cited by 56
The role of ATP-binding cassette subfamily A in the etiology of Alzheimer’s disease
Bossaerts, L., Cacace, R., & Broeckhoven, C. V. (2022) · Molecular Neurodegeneration · doi:10.1186/s13024-022-00536-w · Cited by 56
Dong, H. K., Gim, J., Yeo, S. H., & Kim, H. (2016) · Gene · doi:10.1016/j.gene.2016.10.022 · Cited by 57
Baker-Nigh, A. T., Mawuenyega, K. G., Bollinger, J. G., Ovod, V., Kasten, T., Franklin, E. E., Liao, F., Jiang, H., Holtzman, D., Cairns, N. J., et al. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.721779 · Cited by 54
Emerging role of HDL in brain cholesterol metabolism and neurodegenerative disorders
Turri, M., Marchi, C., Adorni, M. P., Calabresi, L., & Zimetti, F. (2022) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2022.159123 · Cited by 54
Interactions of metals and Apolipoprotein E in Alzheimer’s disease
Xu, H. J., Finkelstein, D. I., & Adlard, P. A. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00121 · Cited by 56
Spagnuolo, M. S., Donizetti, A., Iannotta, L., Aliperti, V., Cupidi, C., Bruni, A. C., & Cigliano, L. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.26480 · Cited by 55
Fanaee‐Danesh, E., Gali, C. C., Tadić, J., Zandl‐Lang, M., Kober, A. C., Agujetas, V. R., de Dios, C., Tam‐Amersdorfer, C., Stracke, A., Albrecher, N. M., et al. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2019.04.019 · Cited by 53
Plasma lipoprotein β-amyloid in subjects with Alzheimer's disease or mild cognitive impairment
Mamo, J. C. L., Jian, L., James, A. P., Flicker, L. A., Esselmann, H., & Wiltfang, J. (2008) · Annals of Clinical Biochemistry International Journal of Laboratory Medicine · doi:10.1258/acb.2008.007214 · Cited by 53
Zhen, J., Huang, X., Halm‐Lutterodt, N. V., Dong, S., Ma, W., Xiao, R., & Yuan, L. (2017) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2017.00248 · Cited by 50
Ramirez, A., van der Flier, W. M., Herold, C., Ramonet, D., Heilmann, S., Lewczuk, P., Popp, J., Lacour, A., Drichel, D., Louwersheimer, E., et al. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu372 · Cited by 49
Cholesterol in mild cognitive impairment and Alzheimer’s disease in a birth cohort over 14 years
Toro, P., Degen, C., Pierer, M., Gustafson, D., Schröder, J., & Schönknecht, P. (2013) · European Archives of Psychiatry and Clinical Neuroscience · doi:10.1007/s00406-013-0468-2 · Cited by 54
Reelin and apoE actions on signal transduction, synaptic function and memory formation
Rogers, J. T., & Weeber, E. J. (2008) · Neuron Glia Biology · doi:10.1017/s1740925x09990184 · Cited by 48
A differential association of Apolipoprotein E isoforms with the amyloid‐β oligomer in solution
Petrlová, J., Hong, H., Bricarello, D. A., Ghimire, H., Lorigan, G. A., Jin, L., & Voss, J. C. (2010) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.22891 · Cited by 51
A Multifaceted Role for apoE in the Clearance of Beta-Amyloid across the Blood-Brain Barrier
Bachmeier, C. J., Paris, D., Beaulieu‐Abdelahad, D., Mouzon, B., MULLAN, M. J., & Crawford, F. (2012) · Neurodegenerative Diseases · doi:10.1159/000337231 · Cited by 53
The potential applications of Apolipoprotein E in personalized medicine
Villeneuve, S., Brisson, D., Marchant, N. L., & Gaudet, D. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00154 · Cited by 50
Amyloid β, Lipid Metabolism, Basal Cholinergic System, and Therapeutics in Alzheimer’s Disease
Campos‐Peña, V., Pichardo-Rojas, P. S., Sánchez-Barbosa, T., Ortíz-Islas, E., Rodríguez-Pérez, C. E., Montes, P., Ramos-Palacios, G., Silva‐Adaya, D., Quintana, R. V., Cerna-Cortés, J. F., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232012092 · Cited by 47
Jones, A., Kulozik, P., Ostertag, A., & Herzig, S. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-0973 · Cited by 47
Alzheimer's disease: brain expression of a metabolic disorder?
Merlo, S., Spampinato, S. F., Canonico, P. L., Copani, A., & Sortino, M. A. (2010) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2010.05.005 · Cited by 50
Serum amyloid A (SAA)-induced remodeling of CSF-HDL
Miida, T., Yamada, T., Seino, U., Ito, M., Fueki, Y., Takahashi, A., Kosuge, K., Soda, S., Hanyu, O., Obayashi, K., et al. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2006.03.013 · Cited by 46
Ayton, S., & Bush, A. I. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2020.101212 · Cited by 45
Wu, C., Zhao, S., & Yu, B. (2014) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/brv.12116 · Cited by 45
ApoE-isoform-dependent cellular uptake of amyloid-β is mediated by lipoprotein receptor LR11/SorLA
Yajima, R., Tokutake, T., Koyama, A., Kasuga, K., Tezuka, T., Nishizawa, M., & Ikeuchi, T. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.11.111 · Cited by 43
Bentley, N. M., LaDu, M. J., Rajan, C., Getz, G. S., & Reardon, C. A. (2002) · Biochemical Journal · doi:10.1042/bj20020207 · Cited by 43
Self-citationLipid-Binding Proteins in Brain Health and Disease
Corraliza-Gómez, M., Sánchez, D., & Ganfornina, M. D. (2019) · Frontiers in Neurology · doi:10.3389/fneur.2019.01152 · Cited by 43
Stratman, N. C., Castle, C. K., Taylor, B. M., Epps, D. E. V., Melchior, G. W., & Carter, D. B. (2005) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2005.06.005 · Cited by 44
Hunter, S., Arendt, T., & Brayne, C. (2013) · Molecular Neurobiology · doi:10.1007/s12035-013-8445-3 · Cited by 41
Chen, Y. L., Wang, L.-Y., Chen, Y., Gao, J. Y., Marshall, C., Cai, Z., Hu, G., & Xiao, M. (2015) · Neuroscience · doi:10.1016/j.neuroscience.2015.12.039 · Cited by 40
The Role of Apolipoprotein E Isoforms in Alzheimer’s Disease
Roda, A. R., Montoliu‐Gaya, L., & Villegas, S. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-180740 · Cited by 41
Raman, S., Brookhouser, N., & Brafman, D. A. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2020.104788 · Cited by 41
Abdelhamid, M., Jung, C., Zhou, C., Abdullah, M., Nakano, M., Wakabayashi, H., Abe, F., & Michikawa, M. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-191181 · Cited by 41
Apolipoprotein E isoform-dependent effects on the processing of Alzheimer's amyloid-β
Chai, A. B., Lam, H. H. J., Kockx, M., & Gelissen, I. C. (2021) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2021.158980 · Cited by 41
Kennedy, R., Cutter, G., & Schneider, L. S. (2013) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2013.03.003 · Cited by 42
The Continuing Failure of Bexarotene in Alzheimer’s Disease Mice
Balducci, C., Paladini, A., Micotti, E., Tolomeo, D., Vitola, P. L., Grigoli, E., Richardson, J. C., & Forloni, G. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-150029 · Cited by 37
Association of ApoE and LRP mRNA levels with dementia and AD neuropathology
Akram, A. M., Schmeidler, J., Katsel, P., Hof, P. R., & Haroutunian, V. H. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.04.010 · Cited by 37
Sawmiller, D. R., Habib, A., Hou, H., Mori, T., Fan, A., Tian, J., Jin, Z., Giunta, B. N., Sanberg, P. R., Mattson, M. P., et al. (2019) · Biological Psychiatry · doi:10.1016/j.biopsych.2019.04.026 · Cited by 38
RetractedThe Impact of Apolipoprotein E (APOE) Epigenetics on Aging and Sporadic Alzheimer’s Disease
Lozupone, M., Dibello, V., Sardone, R., Castellana, F., Zupo, R., Lampignano, L., Bortone, I., Daniele, A., Bellomo, A., Solfrizzi, V., et al. (2023) · Biology · doi:10.3390/biology12121529 · Cited by 39
Brat, D. J., Gearing, M., Goldthwaite, P. T., Wainer, B. H., & Burger, P. C. (2001) · Neuropathology and Applied Neurobiology · doi:10.1046/j.1365-2990.2001.00311.x · Cited by 36
SDS-Stable Complex Formation between Native Apolipoprotein E3 and β-Amyloid Peptides
Munson, G. W., Roher, A. E., Kuo, Y., Gilligan, S. M., Reardon, C. A., Getz, G. S., & LaDu, M. J. (2000) · Biochemistry · doi:10.1021/bi0017475 · Cited by 36
Self-citationLaDu, M. J., Stine, Narita, M., Getz, G. S., Reardon, C. A., & Bu, G. (2006) · Biochemistry · doi:10.1021/bi051765s · Cited by 36
Self-citationExtracellular Proteolysis of Apolipoprotein E (apoE) by Secreted Serine Neuronal Protease
Tamboli, I. Y., Heo, D., & Rebeck, G. W. (2014) · PLoS ONE · doi:10.1371/journal.pone.0093120 · Cited by 35
The Pathological Effects of Circulating Hydrophobic Bile Acids in Alzheimer’s Disease
Ehtezazi, T., Rahman, K., Davies, R., & Leach, A. G. (2023) · Journal of Alzheimer s Disease Reports · doi:10.3233/adr-220071 · Cited by 37
Glöckner, F., Meske, V., & Ohm, T. G. (2002) · Neuroscience · doi:10.1016/s0306-4522(02)00178-1 · Cited by 36
ApoE mimetic peptide decreases Aβ production in vitro and in vivo
Minami, S. S., Cordova, A., Cirrito, J. R., Tesoriero, J. A., Babus, L. W., Davis, G. C., Dakshanamurthy, S., Turner, R. S., Pak, D. T., Rebeck, G. W., et al. (2010) · Molecular Neurodegeneration · doi:10.1186/1750-1326-5-16 · Cited by 34
Ruzali, W. A. W., Kehoe, P. G., & Love, S. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-121336 · Cited by 36
Diet and Age Interactions with Regards to Cholesterol Regulation and Brain Pathogenesis
Uranga, R. M., & Keller, J. N. (2010) · Current Gerontology and Geriatrics Research · doi:10.1155/2010/219683 · Cited by 36
Lane, R. F., Shineman, D. W., Steele, J., Lee, L. H., & Fillit, H. M. (2012) · Advances in pharmacology · doi:10.1016/b978-0-12-394816-8.00007-6 · Cited by 35
Apolipoprotein-E forms dimers in human frontal cortex and hippocampus
Elliott, D. A., Halliday, G. M., & Garner, B. (2010) · BMC Neuroscience · doi:10.1186/1471-2202-11-23 · Cited by 31
Alzheimer's Amyloid-β as a Preventive Antioxidant for Brain Lipoproteins
Kontush, A. (2001) · Cellular and Molecular Neurobiology · doi:10.1023/a:1012629603390 · Cited by 34
Expanding the cerebrospinal fluid endopeptidome
Hansson, K. T., Skillbäck, T. B., Pernevik, E., Kern, S., Portelius, E., Höglund, K., Brinkmalm, G., Holmén‐Larsson, J., Blennow, K., Zetterberg, H., et al. (2017) · PROTEOMICS · doi:10.1002/pmic.201600384 · Cited by 32
Hu, Y., Meuret, C. J., Go, S., Yassine, H. N., & Nedelkov, D. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-200203 · Cited by 33
LaDu, M. J., Munson, G. W., Jungbauer, L., Getz, G. S., Reardon, C. A., Tai, L. M., & Yu, C. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2011.11.005 · Cited by 30
Self-citationSuon, S., Zhao, J. J., Villarreal, S. A., Anumula, N., Liu, M., Carangia, L. M., Renger, J. J., & Zerbinatti, C. (2010) · Molecular Neurodegeneration · doi:10.1186/1750-1326-5-44 · Cited by 31
Zeng, Y., & Han, X. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05481.x · Cited by 29
Are apolipoprotein E fragments a promising new therapeutic target for Alzheimer’s disease?
Vecchio, F. L., Bisceglia, P., Imbimbo, B. P., Lozupone, M., Latino, R. R., Resta, E., Leone, M., Solfrizzi, V., Greco, A., Daniele, A., et al. (2022) · Therapeutic Advances in Chronic Disease · doi:10.1177/20406223221081605 · Cited by 28
Seneviratne, U. I., Huang, Z., Ende, C. W. A., Butler, T. W., Cleary, L., Dresselhaus, E. C., Evrard, E., Fisher, E. L., Green, M. E., Helal, C. J., et al. (2020) · Cell chemical biology · doi:10.1016/j.chembiol.2020.09.002 · Cited by 28
Ringland, C., Schweig, J. E., Paris, D., Shackleton, B., Lynch, C., Eisenbaum, M., MULLAN, M. J., Crawford, F., Abdullah, L. I., & Bachmeier, C. J. (2020) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2020.06.018 · Cited by 27
Hao, J., Zhang, W., Zhang, P., Liu, R., Liu, L., Lei, G., Su, C., Miao, J., & Li, Z. (2010) · Neuropeptides · doi:10.1016/j.npep.2010.03.001 · Cited by 26
Lahdo, R., & Bessueille, L. (2004) · Biochemical Journal · doi:10.1042/bj20040777 · Cited by 26
Class I HDAC inhibition is a novel pathway for regulating astrocytic apoE secretion
Dresselhaus, E., Duerr, J. M., Vincent, F., Sylvain, E. K., Beyna, M., Lanyon, L. F., LaChapelle, E., Pettersson, M., Bales, K. R., & Ramaswamy, G. (2018) · PLOS ONE · doi:10.1371/journal.pone.0194661 · Cited by 25
High-density lipoprotein-related cholesterol metabolism in Alzheimer's disease
Pedrini, S., Chatterjee, P., Hone, E., & Martins, R. N. (2021) · Journal of Neurochemistry · doi:10.1111/jnc.15170 · Cited by 22
Valencia-Olvera, A. C., Balu, D., Faulk, N., Amiridis, A., Wang, Y., Pham, C., Avila-Munoz, E., York, J. M., Thatcher, G. R. J., & LaDu, M. J. (2023) · Neurotherapeutics · doi:10.1007/s13311-023-01375-3 · Cited by 22
Self-citationЛю, Ч., Liu, J., Wang, Y., Xu, S.-F., & Yu, L.-M. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-05629-3 · Cited by 22
Johnson, N. R., Wang, A. C.-J., Coughlan, C. M., Sillau, S., Lucero, E., Viltz, L., Markham, N. E., Allen, C., Dhanasekaran, A. R., Chial, H. J., et al. (2022) · Alzheimer s Research & Therapy · doi:10.1186/s13195-022-01020-9 · Cited by 24
Increase in Cerebrospinal Fluid F2-Isoprostanes is Related to Cognitive Decline in APOE ε4 Carriers
Duits, F. H., Kester, M. I., Scheffer, P. G., Blankenstein, M. A., Scheltens, P., Teunissen, C. E., & van der Flier, W. M. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-122227 · Cited by 22
Phu, M.-J., Hawbecker, S. K., & Narayanaswami, V. (2005) · Journal of Neuroscience Research · doi:10.1002/jnr.20503 · Cited by 21
Hsiao, J.-H. T., Fu, Y., Hill, A. F., Halliday, G. M., & Kim, W. S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0074016 · Cited by 22
Sugano, M., Yamauchi, K., Kawasaki, K., Tozuka, M., Fujita, K., Okumura, N., & Ota, H. (2007) · Clinica Chimica Acta · doi:10.1016/j.cca.2007.10.024 · Cited by 21
Kara, E., Marks, J. D., Roe, A. D., Commins, C., Fan, Z., Calvo-Rodriguez, M., Wegmann, S., Hudry, E., & Hyman, B. T. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra117.001388 · Cited by 20
Evidence that Alzheimer’s Disease Is a Disease of Competitive Synaptic Plasticity Gone Awry
Huang, Z. (2024) · Journal of Alzheimer s Disease · doi:10.3233/jad-240042 · Cited by 20
Apolipoprotein E impairs amyloid‐β fibril elongation and maturation
Islam, T., Gharibyan, A. L., Surano, S., Pettersson, N., Brännström, K., Hedberg, I., Virta, M., Olofsson, L., & Olofsson, A. (2019) · FEBS Journal · doi:10.1111/febs.15075 · Cited by 21
O'Callaghan, P. W., Noborn, F., Sehlin, D., Li, J., Lannfelt, L., Lindahl, U., & Zhang, X. (2014) · Amyloid · doi:10.3109/13506129.2013.879643 · Cited by 20
Amyloid-beta metabolism in age-related neurocardiovascular diseases
Aivalioti, E., Georgiopoulos, G. A., Tual‐Chalot, S., Bampatsias, D., Delialis, D., Sopova, K., Drakos, S. G., Stellos, K., & Stamatelopoulos, K. S. (2024) · European Heart Journal · doi:10.1093/eurheartj/ehae655 · Cited by 20
Potential Therapeutic Implications of Gelsolin in Alzheimer's Disease
Ji, L., Zhao, X., & Hua, Z. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-141548 · Cited by 20
Pedrini, S., Doecke, J. D., Hone, E., Wang, P., Thota, R. N., Bush, A. I., Rowe, C. C., Doré, V., Villemagne, V. L., Ames, D. J., et al. (2022) · Journal of Neurochemistry · doi:10.1111/jnc.15681 · Cited by 20
Differential metabolism of ApoE isoforms in plasma and CSF
Wahrle, S. E., & Holtzman, D. M. (2003) · Experimental Neurology · doi:10.1016/s0014-4886(03)00185-7 · Cited by 19
Westlye, E. T., Hodneland, E., Haász, J., Espeseth, T., Lundervold, A., & Lundervold, A. J. (2012) · NeuroImage · doi:10.1016/j.neuroimage.2012.06.072 · Cited by 20
Lipoproteins produced by ApoE–/– astrocytes infected with adenovirus expressing human ApoE
Peng, D., Song, C., Reardon, C. A., Liao, S., & Getz, G. S. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01950.x · Cited by 19
Bioenergetics and lipid metabolism in Alzheimer's disease: From cell biology to systemic health
Maioli, S., Nalvarte, I., Ankarcrona, M., Schultzberg, M., Zuloaga, K. L., Goikolea, J., Visser, P. J., Strooper, B. D., Winblad, B., Pizzo, P., et al. (2025) · Journal of Internal Medicine · doi:10.1111/joim.70036 · Cited by 19
Cerebrospinal Fluid Proteins as Regulators of Beta‐amyloid Aggregation and Toxicity
Pate, K. M., & Murphy, R. M. (2017) · Israel Journal of Chemistry · doi:10.1002/ijch.201600078 · Cited by 17
Apolipoprotein E-mediated Modulation of ADAM10 in Alzheimer's Disease
Shackleton, B., Crawford, F., & Bachmeier, C. J. (2017) · Current Alzheimer Research · doi:10.2174/1567205014666170203093219 · Cited by 16
Liu, Y., Song, J., Xu, W., Hou, X., Li, J., Yu, J., Tan, L., Chi, S., & Initiative, A. A. D. N. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.633576 · Cited by 16
Prasinou, P., Dafnis, I., Giacometti, G., Ferreri, C., Chroni, A., & Chatgilialoglu, C. (2017) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2017.07.001 · Cited by 15
TGFβ1 enhances formation of cellular Aβ/apoE deposits in vascular myocytes
Mazur‐Kolecka, B., Frackowiak, J., LeVine, H., Haske, T., Evans, L. M., Sukontasup, T., & Golabek, A. A. (2002) · Neurobiology of Aging · doi:10.1016/s0197-4580(02)00095-7 · Cited by 15
Zhang, J., Liu, B., Chen, H., Zhang, L., & Jiang, X. (2024) · International Journal of Nanomedicine · doi:10.2147/ijn.s468695 · Cited by 14
Should the ApoE genotype be a covariate for clinical trials in Alzheimer disease?
Farlow, M. R. (2010) · Alzheimer s Research & Therapy · doi:10.1186/alzrt39 · Cited by 14
Jäkel, L., Biemans, E. A. L. M., Klijn, C. J. M., Kuiperij, H. B., & Verbeek, M. M. (2020) · Molecular Neurobiology · doi:10.1007/s12035-020-01873-x · Cited by 15
Wang, Y., Xue, Y., Wang, S., Huang, J., & Yang, X. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.0c03542 · Cited by 14
Role of A β Transport and Clearance in the Pathogenesis and Treatment of Alzheimer’s Disease
Holtzman, D. M., & Zloković, B. V. (2007) · Springer eBooks · doi:10.1007/978-0-387-35135-3_11 · Cited by 15
The nucleation growth and reversibility of Amyloid-β deposition in vivo
Dolev, I., & Michaelson, D. M. (2006) · Journal of Alzheimer s Disease · doi:10.3233/jad-2006-102-313 · Cited by 13
Meuret, C., Hu, Y.-M., Smadi, S., Bantugan, M. A., Xian, H., Martinez, A. E., Krauss, R., Ma, Q.-L., Nedelkov, D., & Yassine, H. N. (2023) · Alzheimer's Research & Therapy · doi:10.1186/s13195-023-01239-0 · Cited by 12
The combined risk effect among BIN1, CLU, and APOE genes in Alzheimer’s disease
dos Santos, L. R., Almeida, J. F. F., Pimassoni, L. H. S., Morelato, R. L., & Paula, F. (2019) · Genetics and Molecular Biology · doi:10.1590/1678-4685-gmb-2018-0320 · Cited by 12
ApoE: The link between Alzheimer’s-related glucose hypometabolism and Aβ deposition?
Patil, S. P., Ballard, R., Sanchez, S., Osborn, J., & Santangelo, D. (2012) · Medical Hypotheses · doi:10.1016/j.mehy.2012.01.015 · Cited by 13
Metadata
- Authors
- TOKUDA, T., CALERO, M., MATSUBARA, E., VIDAL, R., KUMAR, A., PERMANNE, B., ZLOKOVIC, B., SMITH, J. D., LADU, M. J., ROSTAGNO, A., FRANGIONE, B., & GHISO, J.
- Affiliations
- New York University (US)
- Gunma University (JP)
- Department of Pathology, New York University School of Medicine, 550 First Avenue, New York, NY 10016, U.S.A.
- Department of Neurological Surgery, USC School of Medicine, Los Angeles, CA 90033, U.S.A.
- Rockefeller University (US)
- ENH Research Institute, Evanston, IL 60201, U.S.A.
- Corresponding author
- TOKUDA, Takahiko
- CALERO, Miguel
- KUMAR, Asok
- PERMANNE, Bruno
- ROSTAGNO, Agueda
- FRANGIONE, Blas
- GHISO, Jorge
- ORCID
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 2000-05-23
- Volume
- 348
- Issue
- 2
- Pages
- 359-365
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- PMC
- PMC1221074
- OpenAlex
- W2131975162
- Cited by
- 272
- References
- 47
- Citations by year
- 2026: 10 · 2025: 7 · 2024: 12 · 2023: 6 · 2022: 14 · 2021: 10 · 2020: 15 · 2019: 14 · 2018: 6 · 2017: 13 · 2016: 12 · 2015: 10 · 2014: 20 · 2013: 15 · 2012: 14
- FWCI
- 4.50
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Biochemical Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Institute on Aging (P01AG010491, AG10491, AG05891)
- National Institute of Neurological Disorders and Stroke (NS 38777, R01NS038777)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- apolipoprotein E, APOE3, APOE ε4, Alzheimer's disease, amyloid-beta, lipid modification, delipidation, high-density lipoprotein, amyloid clearance
- MeSH terms
- Animals, Apolipoproteins E, Cell Line, Humans, Kidney, Kinetics, Macrophages, Transfection, Amyloid beta-Peptides, Spodoptera, Protein Isoforms, Mice, Apolipoprotein E3, Apolipoprotein E4
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
