The DOI matches its Crossref record; 39 of the 40 references it cites were found in a registry or an index.
Apolipoprotein E promotes astrocyte colocalization and degradation of deposited amyloid-β peptides
Abstract
We have previously shown that apolipoprotein E (Apoe) promotes the formation of amyloid in brain and that astrocyte-specific expression of APOE markedly affects the deposition of amyloid-beta peptides (Abeta) in a mouse model of Alzheimer disease. Given the capacity of astrocytes to degrade Abeta, we investigated the potential role of Apoe in this astrocyte-mediated degradation. In contrast to cultured adult wild-type mouse astrocytes, adult Apoe(-/-) astrocytes do not degrade Abeta present in Abeta plaque-bearing brain sections in vitro. Coincubation with antibodies to either Apoe or Abeta, or with RAP, an antagonist of the low-density lipoprotein receptor family, effectively blocks Abeta degradation by astrocytes. Phase-contrast and confocal microscopy show that Apoe(-/-) astrocytes do not respond to or internalize Abeta deposits to the same extent as do wild-type astrocytes. Thus, Apoe seems to be important in the degradation and clearance of deposited Abeta species by astrocytes, a process that may be impaired in Alzheimer disease.
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
“Moreover, this plaque-degrading activity in astrocytes was subsequently found to be dependent on apolipoprotein E (apoE) expression (42).”
From Attenuating astrocyte activation accelerates plaque pathogenesis in APP/PS1 mice (2013) · cites this paper as [42]
In the citing paper
“In a mouse model of amyloid deposition, ApoE has been reported to promote the localization of astrocytes to plaques (19).”
From Regulation of astrocyte lipid metabolism and ApoE secretion by the microglial oxysterol, 25-hydroxycholesterol (2023) · cites this paper as [19]
In the citing paper
“Several studies have shown that astrocytes are capable of taking up amyloid peptides (Funato et al., 1998; Matsunaga et al., 2003; Nagele et al., 2003; Lasagna-Reeves and Kayed, 2011), and in vitro this ability was restricted to adult astrocytes (al-Ali and al-Hussain, 1996; Wyss-Coray et al., 2003; Koistinaho et al., 2004; Pihlaja et al., 2008).”
From Mechanisms Underlying the Rapid Peroxisome Proliferator-Activated Receptor-γ-Mediated Amyloid Clearance and Reversal of Cognitive Deficits in a Murine Model of Alzheimer's Disease (2012) · cites this paper as Koistinaho et al., 2004
In the citing paper
“endogenous CNS-derived apoE-containing lipoprotein particles bind to A and promote its clearance and degradation (DeMattos et al., 2004;Koistinaho et al., 2004;Manelli et al., 2004;Stratman et al., 2005;Trommer et al., 2005)”
From Impact of Apolipoprotein E (ApoE) Polymorphism on Brain ApoE Levels (2008) · cites this paper as Koistinaho et al., 2004
In the citing paper
“It has been demonstrated that only mature astrocytes from adult mice, but not neonatal astrocytes, are capable of phagocytosing Aβ plaques (Wyss-Coray et al., 2003;Koistinaho et al., 2004).”
From Cell Adhesion Molecule Protocadherin-γC5 Ameliorates Aβ Plaque Pathogenesis by Modulating Astrocyte Function in Alzheimer's Disease (2025) · cites this paper as Koistinaho et al., 2004
In the citing paper
“It has been reported that the phagocytosis ability of astrocytes is dependent on mouse age.Only mature astrocytes cultured from adult, but not neonatal, mice was able to phagocytose and degrade Aβ, reducing Aβ plaques (Wyss-Coray et al., 2003;Koistinaho et al., 2004).”
From Cell Adhesion Molecule Protocadherin-γC5 Ameliorates Aβ Plaque Pathogenesis by Modulating Astrocyte Function in Alzheimer's Disease (2025) · cites this paper as Koistinaho et al., 2004
In the citing paper
“reactive astrocytes have been reported to phagocytose and degrade Aβ, reducing Aβ plaque burden in the brain (Wyss-Coray et al., 2003;Koistinaho et al., 2004;Kraft et al., 2013;Gomez-Arboledas et al., 2018;Preman et al., 2021)”
From Cell Adhesion Molecule Protocadherin-γC5 Ameliorates Aβ Plaque Pathogenesis by Modulating Astrocyte Function in Alzheimer's Disease (2025) · cites this paper as Koistinaho et al., 2004
In the citing paper
“Two in vitro studies have also demonstrated that apoE can facilitate the cellular degradation of Aβ (Jiang et al., 2008; Koistinaho et al., 2004).”
From The role of apolipoprotein E in Alzheimer's disease (2009) · cites this paper as Koistinaho et al., 2004
In the citing paper
“One common hypothesis states that APOE sequesters soluble Aβ in the extracellular space resulting in cellular uptake and catabolism of this neurotoxic peptide. This hypothesis is supported by many in vitro studies (Koistinaho et al., 2004; Morikawa et al., 2005; Jiang et al., 2008).”
From The Pro-Neurotrophin Receptor Sortilin Is a Major Neuronal Apolipoprotein E Receptor for Catabolism of Amyloid-β Peptide in the Brain (2013) · cites this paper as Koistinaho et al., 2004
In the citing paper
“In the brain, endocytic pathways in glia cells (likely the LDL receptor) and in neurons are implicated in cellular catabolism of APOE/Aβ complexes (Koistinaho et al., 2004; Jiang et al., 2008; Holtzman et al., 2012).”
From The Pro-Neurotrophin Receptor Sortilin Is a Major Neuronal Apolipoprotein E Receptor for Catabolism of Amyloid-β Peptide in the Brain (2013) · cites this paper as Koistinaho et al., 2004
In the citing paper
“In the context of neurodegeneration, astrocytes take up aggregate-prone MAPT/tau, amyloid beta (Aβ) and SNCA (synuclein alpha), and degrade these proteins through autophagy [407–412].”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [407]
Citations
Cites
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
Measurement of co‐localization of objects in dual‐colour confocal images
Manders, E. M. M., Verbeek, F. J., & Aten, J. A. (1993) · Journal of Microscopy · doi:10.1111/j.1365-2818.1993.tb03313.x · Cited by 2,132
Bard, F., Cannon, C., Barbour, R., Burke, R.-L., Games, D., Grajeda, H., Guido, T., Hu, K., Huang, J., Johnson-Wood, K., et al. (2000) · Nature Medicine · doi:10.1038/78682 · Cited by 2,012
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
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
Activation of microglial cells by β-amyloid protein and interferon-γ
Meda, L., Cassatella, M. A., Szendrei, G. I., Otvos, L., Baron, P., Villalba, M., Ferrari, D., & Rossi, F. (1995) · Nature · doi:10.1038/374647a0 · Cited by 1,314
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
Adult mouse astrocytes degrade amyloid-β in vitro and in situ
Wyss-Coray, T., Loike, J. D., Brionne, T. C., Lu, E., Anankov, R., Yan, F., Silverstein, S. C., & Husemann, J. (2003) · Nature Medicine · doi:10.1038/nm838 · Cited by 909
Lack of apolipoprotein E dramatically reduces amyloid β-peptide deposition
Bales, K. R., Verina, T., Dodel, R. C., Du, Y., Altstiel, L., Bender, M., Hyslop, P., Johnstone, E. M., Little, S. P., Cummins, D. J., et al. (1997) · Nature Genetics · doi:10.1038/ng1197-263 · Cited by 830
Self-citationTGF-β1 promotes microglial amyloid-β clearance and reduces plaque burden in transgenic mice
Wyss-Coray, T., Lin, C., Yan, F., Yu, G.-Q., Rohde, M., McConlogue, L., Masliah, E., & Mucke, L. (2001) · Nature Medicine · doi:10.1038/87945 · Cited by 587
Flagged first, then by citations
1 of the 40 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Items 401–500 of 569
Carrera, I., Etcheverrı́a, I., Li, Y., Fernández‐Novoa, L., Lombardi, V., Vigo, C., Palacios, H. H., Benberin, V. V., Cacabelos, R., & Aliev, G. (2013) · BioMed Research International · doi:10.1155/2013/709145 · Cited by 19
Distinct brain regional proteome changes in the rTg‐DI rat model of cerebral amyloid angiopathy
Schrader, J. M., Xu, F., & Nostrand, W. E. V. (2021) · Journal of Neurochemistry · doi:10.1111/jnc.15463 · Cited by 18
Lazo, N. D., Maji, S. K., Fradinger, E. A., Bitan, G., & Teplow, D. B. (2005) · Wiley eBooks · doi:10.1002/9783527619344.ch17 · Cited by 18
Stephen, T., Breningstall, B. M., Suresh, S., McGill, C. J., & Pike, C. J. (2022) · Journal of Neuroinflammation · doi:10.1186/s12974-022-02650-4 · Cited by 17
Molecular Effects of Pteryxin and Scopoletin in the 5xFAD Alzheimer’s Disease Mouse Model
Kiris, İ., Skalicka‐Woźniak, K., Karayel‐Basar, M., Şahin, B., Gürel, B., & Baykal, A. T. (2021) · Current Medicinal Chemistry · doi:10.2174/0929867328666210827152914 · Cited by 17
Patel, A., Vasanthan, V., Fu, W., Fahlman, R. P., MacTavish, D., & Jhamandas, J. H. (2015) · Brain Structure and Function · doi:10.1007/s00429-015-1007-x · Cited by 19
TRPC Channels and Alzheimer’s Disease
Lu, R., Qian, H., & Wang, J. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-94-024-1088-4_7 · Cited by 17
Peng, L., Zhang, Z., Li, Q., Song, Z., Yan, C., & Ling, H. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e39217 · Cited by 18
The Dual Role of Astrocytes in CNS Homeostasis and Dysfunction
Tiwari, A., Rout, S., Deep, P., Sahu, C., & Samal, P. K. (2025) · Neuroglia · doi:10.3390/neuroglia6040038 · Cited by 18
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
Calcium signaling at the interface between astrocytes and brain inflammation
Novakovic, M. M., & Prakriya, M. (2024) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2024.102940 · Cited by 16
Translational considerations for CNS gene therapy
Ryan, D. A., & Federoff, H. J. (2007) · Expert Opinion on Biological Therapy · doi:10.1517/14712598.7.3.305 · Cited by 16
Meyer, P., Savard, M., Poirier, J., Morgan, D., Breitner, J. C. S., & Initiative, A. D. N. (2019) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2019.05.007 · Cited by 15
Serbinek, D., Ullrich, C., Pirchl, M., Hochstrasser, T., Schmidt‐Kastner, R., & Humpel, C. (2010) · Cardiovascular Psychiatry and Neurology · doi:10.1155/2010/106123 · Cited by 15
Ueno, M. (2017) · Rinsho Shinkeigaku · doi:10.5692/clinicalneurol.cn-001004 · Cited by 15
Martínez‐Bonet, M., Muñoz‐Fernández, M. Á., & Álvarez, S. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.26462 · Cited by 15
Brockmann, K., Lerche, S., Dilger, S. S., Stirnkorb, J. G., Apel, A., Hauser, A., Liepelt‐Scarfone, I., Berg, D., Gasser, T., Schulte, C., et al. (2017) · Neurology · doi:10.1212/wnl.0000000000004705 · Cited by 15
Ding, X., Yang, W., Ren, Q., Hu, J., Shen, Y., Han, W., Wang, J., Wang, X., & Wang, H. (2020) · Journal of Neuroinflammation · doi:10.1186/s12974-020-01839-9 · Cited by 14
Multitasking Microglia and Alzheimer’s Disease: Diversity, Tools and Therapeutic Targets
Grubman, A., Kanninen, K. M., & Malm, T. (2016) · Journal of Molecular Neuroscience · doi:10.1007/s12031-016-0825-5 · 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
Reed, A. L., Mitchell, W., Alexandrescu, A. T., & Alder, N. N. (2023) · Frontiers in Physiology · doi:10.3389/fphys.2023.1263420 · Cited by 13
Evaluation of the Therapeutic Effect of Lycoramine on Alzheimer’s Disease in Mouse Model
Kiris, İ., Karayel‐Basar, M., Şahin, B., Gürel, B., Coşkun, J., Mroczek, T., & Baykal, A. T. (2020) · Current Medicinal Chemistry · doi:10.2174/0929867327999201116193126 · Cited by 13
Complementary Distributions of Amyloid-β and Neprilysin in the Brains of Dogs and Cats
Takeuchi, Y., Uetsuka, K., Murayama, M., Kikuta, F., Takashima, A., Doi, K., & Nakayama, H. (2008) · Veterinary Pathology · doi:10.1354/vp.45-4-455 · Cited by 13
Friends Turn Foe—Astrocytes Contribute to Neuronal Damage in NeuroAIDS
Pandey, H. S., & Seth, P. (2019) · Journal of Molecular Neuroscience · doi:10.1007/s12031-019-01357-1 · Cited by 13
Koller, E. J., Cruz, E. G. D. L., Weinrich, M. J., Williams, T., Cruz, P. E., Ryu, D. H., Golde, T. E., Sullivan, P. M., Lewis, J. M., Borchelt, D., et al. (2020) · Molecular Neurobiology · doi:10.1007/s12035-019-01859-4 · Cited by 13
Glial phagocytosis for synapse and toxic proteins in neurodegenerative diseases
Choi, Y., & Chung, W. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-025-00870-9 · Cited by 14
Thumrongsiri, N., Dana, P., Bawab, R., Tanyapanyachon, P., Treetidnipa, C., Saengkrit, N., & Sathornsumetee, S. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.112979 · Cited by 12
Blood–Brain Barrier Transport of Alzheimer’s Amyloid β-Peptide
Nelson, A. R., Sagare, A. P., & Zloković, B. V. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802173-6.00009-5 · Cited by 12
Feng, D. N., Wang, L. N., Hu, A. N., & Zhang, S. (2025) · Journal of Integrative Neuroscience · doi:10.31083/jin45223 · Cited by 11
Amyloid-β deposits in human astrocytes contain truncated and highly resistant proteoforms
Beretta, C., Svensson, E., Dakhel, A., Zyśk, M., Hanrieder, J., Sehlin, D., Michno, W., & Erlandsson, A. (2024) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2024.103916 · Cited by 12
Immune cells in Alzheimer’s disease: insights into pathogenesis and potential therapeutic targets
Fu, X., Cai, H., Quan, S., Ren, Z., Xu, Y., & Jia, L. (2024) · Medical Review · doi:10.1515/mr-2024-0064 · Cited by 10
Protective role of functional food in cognitive deficit in young and senile rats
Attia, H. N., & Ahmed, K. A. (2020) · Behavioural Pharmacology · doi:10.1097/fbp.0000000000000522 · Cited by 11
A Comparative Study on 5hmC Targeting Regulation of Neurons in AD Mice by Several Natural Compounds
Cao, D., Jiang, D., Zhou, D., Yu, H., & Li, J. (2020) · BioMed Research International · doi:10.1155/2020/5016706 · Cited by 11
Shoubridge, A. P., Carpenter, L., Flynn, E. F., Papanicolas, L. E., Collins, J., Gordon, D., Lynn, D. J., Whitehead, C., Leong, L. E. X., Cations, M., et al. (2025) · The Journals of Gerontology Series A · doi:10.1093/gerona/glaf053 · Cited by 10
Apolipoprotein E receptor pathways in Alzheimer disease
Schmidt, V., Carlo, A.-S., & Willnow, T. E. (2014) · WIREs Systems Biology and Medicine · doi:10.1002/wsbm.1262 · Cited by 10
Scuderi, C., & Golini, L. (2021) · Animals · doi:10.3390/ani11092584 · Cited by 14
Moon, S. W., Byun, M. S., Yi, D., Lee, J. H., Jeon, S. Y., Lee, Y., Kee, B. S., & Lee, D. Y. (2018) · The Journals of Gerontology Series A · doi:10.1093/gerona/gly157 · Cited by 10
Wang, K., & Zhang, W. (2021) · Synapse · doi:10.1002/syn.22196 · Cited by 11
Yu, Y., Wang, C., Wang, B., Wang, X., Zhao, Q. S., Yan, Y., & Liu, X. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26157271 · Cited by 9
Chen, K., Padilla, C. G., Kiselyov, K. I., & Kozai, T. D. Y. (2023) · Biomaterials · doi:10.1016/j.biomaterials.2023.122316 · Cited by 9
Alzheimer's Factors in Ischemic Brain Injury
Pluta, R. M., & Jaboski, M. (2012) · InTech eBooks · doi:10.5772/27205 · Cited by 9
Malm, T., Magga, J. M., & Koıstınaho, J. (2012) · Current Translational Geriatrics and Experimental Gerontology Reports · doi:10.1007/s13670-011-0004-z · Cited by 9
Dasadhikari, S., Ghosh, S., Pal, S., Knowles, T. P. J., & Garai, K. (2025) · Communications Chemistry · doi:10.1038/s42004-025-01524-z · Cited by 9
Crompton, L., Llana, O. C., & Caldwell, M. A. (2017) · Brain Pathology · doi:10.1111/bpa.12522 · Cited by 8
Correlation Analysis between External Factors and Students’ Physics Learning Achievement
Karyadi, K., Sinon, I. L. S., Yusuf, I., & Widyaningsih, S. W. (2018) · Scientiae Educatia · doi:10.24235/sc.educatia.v7i1.2415 · Cited by 9
DYRK1A in the physiology and pathology of the neuron-astrocyte axis
Cisternas, P., Kim, J.-Y., Ashfeld, B. L., & Zartman, J. J. (2025) · Frontiers in Neuroscience · doi:10.3389/fnins.2025.1626062 · Cited by 7
Singh, A. S., Naqvi, A. R., & Chanu, M. T. (2026) · Journal of Psychiatric Research · doi:10.1016/j.jpsychires.2026.01.050 · Cited by 7
The Emerging Role of Astrocytic Autophagy in Central Nervous System Disorders
Zhou, Z., Zhou, J., Liao, J., Chen, Z., & Zheng, Y. (2022) · Neurochemical Research · doi:10.1007/s11064-022-03714-w · Cited by 7
Can Astrocytes Be a Target for Precision Medicine?
Allen, C. F., Shaw, P. J., & Ferraiuolo, L. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-60733-7_7 · Cited by 7
Chaplygina, A. V., Zhdanova, D., Kovalev, V. I., Полтавцева, Р. А., Medvinskaya, N. I., & Бобкова, Н. В. (2022) · Journal of Evolutionary Biochemistry and Physiology · doi:10.1134/s0022093022010112 · Cited by 7
Frisardi, V. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-111568 · Cited by 7
Type II nuclear receptors with potential role in Alzheimer disease
Muñoz-Cabrera, J., Adrián, S.-H., & Arboleda, G. (2021) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2020.100940 · Cited by 9
The Essential Role of Astrocytes in Neurodegeneration and Neuroprotection
Couselo, F. L., Saba, J., Carniglia, L., Durand, D., Lasaga, M., & Caruso, C. M. (2023) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/0118715273269881231012062255 · Cited by 6
APOEε4 alters ApoE and Fabp7 in frontal cortex white matter in prodromal Alzheimer's disease
Moreno‐Rodríguez, M., Perez, S. E., Malek‐Ahmadi, M. H., & Mufson, E. J. (2025) · Journal of Neuroinflammation · doi:10.1186/s12974-025-03349-y · Cited by 8
de Lima, I. B. Q., Cardozo, P. L., Fahel, J. S., Lacerda, J. P. S., de Miranda, A. S., Teixeira, A. L., & Ribeiro, F. M. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1283331 · Cited by 6
Zhai, Y., Yamashita, T., Kurata, T., Fukui, Y., Sato, K., Kono, S., Liu, W., Omote, Y., Hishikawa, N., Deguchi, K., et al. (2014) · Journal of Stroke and Cerebrovascular Diseases · doi:10.1016/j.jstrokecerebrovasdis.2014.05.033 · Cited by 6
Cellular prion protein offers neuroprotection in astrocytes submitted to amyloid β oligomer toxicity
Marques, C. M. S., Gomes, R. N., Pedron, T., Batista, B. L., & Cerchiaro, G. (2022) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-022-04631-w · Cited by 6
Kurronen, A., Pihlaja, R., Pollari, E., Kanninen, K. M., Storvik, M., Wong, G., Koistinaho, M., & Koıstınaho, J. (2012) · World Journal of Neuroscience · doi:10.4236/wjns.2012.22009 · Cited by 6
Self-citationNeuroinflammation in Alzheimer's, Parkinson's and Huntington's Diseases
Sastre, M., Katsouri, L., Birch, A. M., Renziehausen, A., Dexter, D. T., Crichton, R. R., & Ward, R. J. (2014) · Wiley eBooks · doi:10.1002/9781118406557.ch6 · Cited by 6
Arndt, H., Bachurski, M., Yuanxiang, P., Franke, K., Wessjohann, L. A., Kreutz, M. R., & Grochowska, K. M. (2024) · Molecular Neurobiology · doi:10.1007/s12035-024-04509-6 · Cited by 5
Peripheral Inflammatory Biomarkers of Alzheimer’s Disease
Hao, J., Guo, Y., Guo, K., & Yang, Q. (2022) · Journal of Alzheimer s Disease · doi:10.3233/jad-215422 · Cited by 5
Role of apoE in conformation-prone diseases and atherosclerosis
Dergunov, A. D. (2006) · Biochemistry (Moscow) · doi:10.1134/s0006297906070029 · Cited by 5
Sun, X., Pan, S., Li, D., Su, M., Zheng, H., Zhang, Y.-W., & Li, Y. (2025) · The Journal of Neuroscience · doi:10.1523/jneurosci.0967-24.2025 · Cited by 4
Sharma, A., Kaur, S., Wani, A., Kour, D., Ali, M., Ali, S. M., Singh, L., Gour, A., Nandi, U., Datt, M., et al. (2024) · Autophagy Reports · doi:10.1080/27694127.2023.2296209 · Cited by 4
Huang, S., Nunez, J., Toresco, D. L., Wen, C., Slotabec, L. A., Wang, H., Zhang, H., Rouhi, N., Adenawoola, M. I., & Li, J. (2025) · The FASEB Journal · doi:10.1096/fj.202402725rr · Cited by 4
Inhibition of Sirt2 Decreases ApoE Secretion in Astrocytes and Microglial Cells
Chen, Y., Zhou, C., Abdelhamid, M., Jung, C., & Michikawa, M. (2023) · The Journal of Biochemistry · doi:10.1093/jb/mvad054 · Cited by 4
Yoon, S., & Kim, Y. (2015) · Global Medical Genetics · doi:10.3934/genet.2015.3.230 · Cited by 5
Modulating Role of TTR in Aβ Toxicity, from Health to Disease
Cardoso, I., Santos, L. M., & Alemi, M. (2016) · InTech eBooks · doi:10.5772/63194 · Cited by 7
Nodule Detection in Postero Anterior Chest Radiographs
Campadelli, P., & Casiraghi, E. (2004) · Lecture notes in computer science · doi:10.1007/978-3-540-30136-3_132 · Cited by 4
Key Enzymes and Proteins in Amyloid-Beta Production and Clearance
Santos, C. R. A., Cardoso, I., & Gonçalves, I. (2011) · InTech eBooks · doi:10.5772/17646 · Cited by 5
Neuroimmune Dynamics in Alzheimer’s Disease Progression
Andrade, V., Guzmán‐Martínez, L., Vergara-Pulgar, K., & Maccioni, R. B. (2017) · InTech eBooks · doi:10.5772/intechopen.68941 · Cited by 4
Wei, H., Zhang, G., Xu, Y., Zhao, A., Zheng, Y., Shao, Y. W., Yang, L., Wang, J., & Jiang, X. (2025) · Phytomedicine · doi:10.1016/j.phymed.2025.157238 · Cited by 3
Yamashita, T., Zhai, Y., Kurata, T., Hishikawa, N., Morimoto, N., Ohta, Y., Deguchi, K., & Abe, K. (2014) · Journal of Stroke and Cerebrovascular Diseases · doi:10.1016/j.jstrokecerebrovasdis.2014.04.010 · Cited by 3
Yamamoto, N., Tokumon, T., Obuchi, A., Kono, M., Saigo, K., Tanida, M., Ikeda‐Matsuo, Y., & Sobue, K. (2022) · Journal of Neurochemistry · doi:10.1111/jnc.15716 · Cited by 5
The contribution of S100B to the glioprotective effects of valproic and arundic acids.
Keshavarz, M., Farrokhi, M. R., Amiri, A., & Hosseini, M. (2019) · PubMed Central · doi:10.22038/ijbms.2019.29852.7204 · Cited by 3
Ethanol Toxicity in the Brain: Alteration of Astroglial Cell Function
Lipnik‐Štangelj, M. (2012) · InTech eBooks · doi:10.5772/31366 · Cited by 3
Astrocyte Responses to Central Nervous System Injury and Disease
Sofroniew, M. V. (2012) · Oxford University Press eBooks · doi:10.1093/med/9780199794591.003.0051 · Cited by 3
BMAL1 in Astrocytes: A Protective Role in Alzheimer’s and Parkinson’s Disease
Brash-Arias, D., García, L. I., Aranda-Abreu, G. E., Toledo‐Cárdenas, M. R., Pérez-Estudillo, C. A., & Chi-Castañeda, D. (2025) · Neuroglia · doi:10.3390/neuroglia6010001 · Cited by 2
Gong, M., Lan, J. X., & Miao, J. (2026) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2026.1908574 · Cited by 3
The Role of Astrocytes in Astrocytes Alzheimer’s Disease
Mavroudis, I. A., Petridis, F., Chatzikonstantinou, S., McKENN, J., Karantali, E., & KAZIS, D. (2020) · Annals of the Academy of Romanian Scientists Series on Biological Sciences · doi:10.56082/annalsarscibio.2020.1.65 · Cited by 2
Reactive Astrogliosis and Neuronal Functions of Astrocytes in Neurological Disorders
Mathure, D. M., Kumar, D., Ranpise, H. A., & Awasthi, R. (2024) · Indian Journal of Pharmaceutical Education and Research · doi:10.5530/ijper.58.2.44 · Cited by 2
Identification of TMED10 as A Regulator for Neuronal Exocytosis of Amyloid Beta 42
Meng, P., Sha, L., Yu, X., Wang, Y., Zhang, E., Meng, K., Li, B., Zhao, Q., & Xu, Q. (2025) · Neuroscience Bulletin · doi:10.1007/s12264-025-01492-3 · Cited by 2
Girardi, C. S., Yi, L., Fitz, N. F., Gelain, D. P., Lefterov, I. M., & Koldamova, R. P. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27052435 · Cited by 2
Cholesterol Trafficking in the Brain
Lütjohann, D., Vanmierlo, T., & Mulder, M. T. (2009) · Springer eBooks · doi:10.1007/978-3-642-00300-4_5 · Cited by 2
Biomarkers of Alzheimer’s disease
Pitt, J. E. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-404630-6.00048-8 · Cited by 2
Astrocytes as Targets for Neurological Gene Therapy
Imura, T., & Sofroniew, M. V. (2006) · CRC Press eBooks · doi:10.3109/9781420016390-8 · Cited by 2
Heat Shock Proteins, a Key Modulator of Neuroinflammation in Alzheimer’s Disease
Panchal, K., Bhatt, V., Raval, M., & Tiwari, A. K. (2020) · Heat shock proteins · doi:10.1007/7515_2020_12 · Cited by 2
Neuron–Astrocyte Interactions in Neuroinflammation
Križ, J. (2013) · Advances in neurobiology · doi:10.1007/978-1-4614-8313-7_5 · Cited by 2
Dabbs, R. A., Wyatt, A. R., Yerbury, J. J., Ecroyd, H. W., & Wilson, M. R. (2010) · Topics in current chemistry · doi:10.1007/128_2010_85 · Cited by 2
S14 TRANSGENIC MICE MODELS FOR ALZHEIMER??S DISEASE
LEUVEN, F. V. (2006) · Behavioural Pharmacology · doi:10.1097/00008877-200609000-00033 · Cited by 2
Fischer, R. (2011) · OPUS Publication Server of the University of Stuttgart (University of Stuttgart) · doi:10.18419/opus-1905 · Cited by 2
Gene Therapy for Neurological Disorders
Malviya, R., Singh, A. K., Goyal, P., & Sundram, S. (2024) · Apple Academic Press eBooks · doi:10.1201/9781003494102 · Cited by 1
Autophagic and Lysosomal Disorders
Chandra, S., & Pahan, K. (2024) · Springer eBooks · doi:10.1007/978-3-031-68237-7_11 · Cited by 1
Zhu, X., Diep, Y. N., Tran, V. T. A., Kang, Y. J., Lee, L. P., & Cho, H. (2025) · BioChip Journal · doi:10.1007/s13206-025-00228-9 · Cited by 1
Sambhariya, W. S., Rickman, C. B., D'Amore, P. A., Corradetti, G., Hageman, G. S., Howell, G. R., Marola, O. J., Phatnani, H. P., Philp, N. J., Sinha, D., et al. (2026) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2026.101449 · Cited by 1
Xie, Y., Tian, J., Li, H., Peng, Y., Li, M., & Wu, Y. H. (2026) · Frontiers in Neuroscience · doi:10.3389/fnins.2026.1771310 · Cited by 1
Effect of acute ischemic stroke in 3xTg-AD mouse model of Alzheimer’s disease
Yadav, S. K., Srivastava, R., Yadawa, A. K., Turro, D. G., & Verma, R. (2026) · Scientific Reports · doi:10.1038/s41598-026-54645-3 · Cited by 1
APP /Aβ Signaling Orchestrates Reactive Astrocyte Networks in Alzheimer's Disease
Jáuregui, G. V., Coomes, S., Emmett, E., Thatcher, A., Oyelakin, N., Čarná, M., Zelinková, J., Novotný, J., Polakova, N., Kuruvilla, T., et al. (2026) · Journal of Neurochemistry · doi:10.1111/jnc.70526 · Cited by 1
Oligodendroglial-Astroglial Cell-Cell Communication in the Central Nervous System
Basu, R., & Sarma, J. D. (2022) · Springer eBooks · doi:10.1007/978-981-16-8313-8_4 · Cited by 1
Role of Reactive Astrocytes in Alzheimer’s Disease
Sarkar, S., Guha, S., & Biswas, S. C. (2022) · Springer eBooks · doi:10.1007/978-981-16-8313-8_9 · Cited by 1
Metadata
- Authors
- Koistinaho, M., Lin, S., Wu, X., Esterman, M., Koger, D., Hanson, J., Higgs, R., Liu, F., Malkani, S., Bales, K. R., & Paul, S. M.
- Affiliations
- Eli Lilly (United States) (US)
- Corresponding author
- Paul, Steven M
- Venue
- Nature Medicine
- Published
- 2004-06-13
- Volume
- 10
- Issue
- 7
- Pages
- 719-726
- ISSN
- 1078-8956 (ISSN-L)
- 1546-170X
- OpenAlex
- W2171311951
- Cited by
- 571
- References
- 40
- Citations by year
- 2026: 13 · 2025: 20 · 2024: 15 · 2023: 20 · 2022: 29 · 2021: 23 · 2020: 34 · 2019: 31 · 2018: 26 · 2017: 29 · 2016: 32 · 2015: 29 · 2014: 36 · 2013: 30 · 2012: 38
- FWCI
- 13.59
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Medicine (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Suomen Kulttuurirahasto
- Saastamoisen säätiö
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- apolipoprotein E, amyloid-beta, astrocytes, amyloid beta degradation, Alzheimer's disease, amyloid plaques, rap, low-density lipoprotein receptor family, ApoE-deficient mice
- MeSH terms
- Animals, Apolipoproteins E, Astrocytes, Cell Aggregation, Cell Survival, Cells, Cultured, Mice, Inbred C57BL, Amyloid beta-Peptides, Low Density Lipoprotein Receptor-Related Protein-1, Mice
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