Alzheimer’s Disease Risk Genes and Mechanisms of Disease Pathogenesis

Karch, Celeste M.; Goate, Alison M.

doi:10.1016/j.biopsych.2014.05.006

Cited by 1,357Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroinflammation and Neurodegeneration Mechanisms

Alzheimer’s Disease Risk Genes and Mechanisms of Disease Pathogenesis

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Karch, Celeste M., Goate, Alison M.·2015·Biological Psychiatry

DOI 10.1016/j.biopsych.2014.05.006PMC PMC4234692

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Abstract

We review the genetic risk factors for late-onset Alzheimer's disease (AD) and their role in AD pathogenesis. More recent advances in understanding of the human genome-technologic advances in methods to analyze millions of polymorphisms in thousands of subjects-have revealed new genes associated with AD risk, including ABCA7, BIN1, CASS4, CD33, CD2AP, CELF1, CLU, CR1, DSG2, EPHA1, FERMT2, HLA-DRB5-DBR1, INPP5D, MS4A, MEF2C, NME8, PICALM, PTK2B, SLC24H4-RIN3, SORL1, and ZCWPW1. Emerging technologies to analyze the entire genome in large data sets have also revealed coding variants that increase AD risk: PLD3 and TREM2. We review the relationship between these AD risk genes and the cellular and neuropathologic features of AD. Understanding the mechanisms underlying the association of these genes with risk for disease will provide the most meaningful targets for therapeutic development to date.

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PSEN1 is the catalytical component of γ-secretase.
“PSEN1 is the catalytical component of 𝛄 -secretase (304).”
From Blood-Brain Barrier: From Physiology to Disease and Back (2019) · cites this paper as [304]
The “APP, PSEN1, and PSEN2” section says PSEN1 and PSEN2 are critical components of the γ-secretase complex. It does not identify PSEN1 specifically as a catalytic component, so that part of the claim is not supported by our copy. (LLM, conf=0.86)
Experimental — accuracy not yet measured
To date, 228 PSEN1 mutations have been identified causing ADAD.
“To date, 228 PSEN1 mutations have been identified causing ADAD (49, 303, 304, 440, 566, 580).”
From Blood-Brain Barrier: From Physiology to Disease and Back (2019) · cites this paper as [304]
The “APP, PSEN1, and PSEN2” section (page unavailable) states that dominantly inherited PSEN1 mutations cause early-onset Alzheimer’s disease. It does not state that 228 such mutations have been identified, so the specific count is unsupported by this source. (LLM, conf=0.88)
Experimental — accuracy not yet measured
Some PSEN1 mutations lead to very early onset ADAD (<35 years of age).
“Some PSEN1 mutations lead to very early onset ADAD ( < 35 yr of age) (177, 304).”
From Blood-Brain Barrier: From Physiology to Disease and Back (2019) · cites this paper as [304]
The “APP, PSEN1, and PSEN2” section (page unavailable) states that dominantly inherited PSEN1 mutations cause early-onset Alzheimer’s disease. It does not specify onset before age 35, so the claim’s age threshold is not supported by this source. (LLM, conf=0.88)
Experimental — accuracy not yet measured
TREM2 loss-of-function impairs microglial protective functions and worsens neuronal dystrophy.
“TREM2 loss‐of‐function impairs microglial protective functions and worsens neuronal dystrophy. 9 , 37 , 38 , 41 , 42 , 61”
From PLCG2 modulates TREM2 expression and signaling in response to Alzheimer's disease pathology (2025) · cites this paper as [9]
The Immune Response > TREM2 section says TREM2 stimulates microglial phagocytosis and suppresses inflammation, supporting its protective role. It reports more extensive brain atrophy in TREM2 mutation carriers with Alzheimer’s disease, but does not establish that loss of function impairs those activities or worsens neuronal dystrophy specifically. (LLM, conf=0.87)
Experimental — accuracy not yet measured
Approximately 40% of the susceptibility genes identified in genetic studies of LOAD are immune- and microglia-related, suggesting that microglia are involved in modulating AD pathology.
“approximately 40% of the susceptibility genes identified in genetic studies of LOAD are immune- and microglia-related, suggesting that microglia are involved in modulating AD pathology [8].”
From PLCG2 is associated with the inflammatory response and is induced by amyloid plaques in Alzheimer’s disease (2022) · cites this paper as [8]
The Immune Response section lists several LOAD risk genes involved in immune pathways, and its CD33 subsection describes microglial involvement in Aβ clearance and plaque burden. Our copy does not state or substantiate the claimed approximately 40% proportion of susceptibility genes. (LLM, conf=0.86)
Experimental — accuracy not yet measured

Genome-wide association studies have identified associations between inflammation- and immune-related variants in genes (such as a missense mutation in TREM2) and increased AD risk.
“In addition, genome-wide association studies have identified associations between inflammation- and immune-related variants in genes (such as a missense mutation in the gene encoding for TREM2, a receptor expressed on microglia) and increased AD risk [36].”
From Cerebrospinal fluid levels of the neurotrophic factor neuroleukin are increased in early Alzheimer’s disease, but not in cerebral amyloid angiopathy (2021) · cites this paper as [36]
The Immune Response section reports GWAS associations for several immune-related genes, and its TREM2 subsection reports that rare missense TREM2 variants increase late-onset AD risk. But the Immune Response section says TREM2 coding variants were identified in sequencing studies, not GWAS; the Emerging Genetics section explicitly distinguishes those methods. (LLM, conf=0.88)
Experimental — accuracy not yet measured
Many AD risk genes are primarily expressed in microglia.
“Most notably, these genetic studies implicate central roles for the innate immune system, with many AD risk genes being primarily expressed in microglia (Efthymiou and Goate, 2017; Karch and Goate, 2015; Lopes et al., 2022).”
From Alzheimer’s genetic risk factor CASS4 controls microglial focal adhesion biology and amyloidosis (2026) · cites this paper as Karch and Goate, 2015
The Immune Response sections identify AD risk genes CD33 and TREM2 as expressed in microglia, and the Emerging Genetics section discusses disrupted microglia-specific networks (page numbers unavailable). The paper does not establish that many AD risk genes are primarily expressed in microglia; it also describes MS4A genes as expressed in myeloid cells and monocytes. (LLM, conf=0.85)
Experimental — accuracy not yet measured
Among the top risk genes for sporadic Alzheimer's disease, APOE, TREM2, APOJ, PICALM, ABCA7, and SORL1 are all directly involved in lipid trafficking or metabolism.
“among the top risk genes for sporadic AD, APOE, TREM2, APOJ, PICALM, ABCA7, and SORL1 are all directly involved in lipid trafficking or metabolism (Karch and Goate, 2015).”
From ApoE4 Impairs Neuron-Astrocyte Coupling of Fatty Acid Metabolism (2021) · cites this paper as Karch and Goate, 2015
The Cholesterol Metabolism section identifies APOE, CLU (APOJ), ABCA7, and SORL1 as involved in cholesterol metabolism or lipid transport; the CLU subsection describes lipid transport, and the SORL1 subsection describes lipoprotein uptake. But the Immune Response > TREM2 subsection describes phagocytosis and inflammation, while Endocytosis > PICALM describes clathrin-mediated trafficking, not direct lipid trafficking or metabolism. The paper therefore does not support saying that all six genes have that direct role. (LLM, conf=0.90)
Experimental — accuracy not yet measured
The main genetic risk factor in sporadic Alzheimer's disease is the APOE gene.
“the main genetic risk factor in SAD is the APOE gene [91,92,93,94].”
From Alzheimer's Disease: Treatment Strategies and Their Limitations. (2022) · cites this paper as [94]
Autosomal-dominant AD is caused by mutations in APP and PSEN1 and PSEN2 genes.
“Autosomal-dominant AD (ADAD) is an inherited form of AD caused by mutations in amyloid precursor protein ( APP ) and presenilin-1 and 2 ( PSEN1; PSEN2 ) genes (49, 177, 303, 304, 580).”
From Blood-Brain Barrier: From Physiology to Disease and Back (2019) · cites this paper as [304]
Genetic studies have identified numerous AD risk variants in immune- and microglial-associated genes.
“Genetic studies have identified numerous AD risk variants in immune‐ and microglial‐associated genes, highlighting the importance of microglia function in disease progression. 3 , 4 , 5 , 6 , 7”
From Alzheimer's disease–associated PLCG2 variants alter microglial state and function in human induced pluripotent stem cell–derived microglia‐like cells (2025) · cites this paper as [5]
HLA-DRB polymorphisms are associated with increased risk of AD.
“Moreover, HLA‐DRB polymorphisms are associated with increased risk of AD 2 , 19 , 20”
From The P522R protective variant of PLCG2 promotes the expression of antigen presentation genes by human microglia in an Alzheimer's disease mouse model (2022) · cites this paper as [2]
Inpp5d is expressed predominantly in microglia in the brain.
“Inpp5d is expressed predominantly in microglia but its function in brain is poorly understood.”
From Loss of Inpp5d has disease‐relevant and sex‐specific effects on glial transcriptomes (2024) · cites this paper as [16]
The Immune Response > CD33 section discusses microglial expression of CD33, not INPP5D. Searches of our full-text copy for INPP5D and SHIP1 found no passage addressing whether INPP5D is expressed predominantly in brain microglia; page numbers were unavailable. (LLM, conf=0.75)
Experimental — accuracy not yet measured
GWAS have identified several single-nucleotide polymorphisms in immune genes as independent risk factors for late-onset AD, directly implicating microglia-mediated mechanisms in sporadic AD progression.
“Likewise, genome-wide association studies (GWAS) have identified several single-nucleotide polymorphisms (SNPs) in immune genes as independent risk factors for LOAD [52–55], directly implicating microglia-mediated mechanisms in sporadic AD progression.”
From Systems-based proteomics to resolve the biology of Alzheimer’s disease beyond amyloid and tau (2021) · cites this paper as [55]

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The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics
Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864 · see citing works
Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy
Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D. (2013) · Neurodegenerative Diseases · doi:10.1159/000337230 · Cited by 10,359 · see citing works
Gene Dose of Apolipoprotein E Type 4 Allele and the Risk of Alzheimer's Disease in Late Onset Families
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 · see citing works
Meta-Analysis of 74,046 Individuals Identifies 11 New Susceptibility Loci for Alzheimer’s Disease
(EADI), E. A. D. I., Lambert, J.-C., (GERAD), G. A. E. R. I. A. D., Alzheimer's Disease Genetic Consortium (ADGC), (CHARGE), C. F. H. A. A. R. I. G. E., Ibrahim-Verbaas, C. A., Harold, D., Naj, A. C., Sims, R., Bellenguez, C., et al. (2013) · Nature Genetics · doi:10.1038/ng.2802 · Cited by 4,336 · see citing works
Self-citation
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
Genome-wide association study identifies variants at CLU and PICALM associated with Alzheimer's disease
Harold, D., Abraham, R., Hollingworth, P., Sims, R., Gerrish, A., Hamshere, M. L., Pahwa, J. S., Moskvina, V., Dowzell, K., Williams, A., et al. (2009) · Nature Genetics · doi:10.1038/ng.440 · Cited by 3,326 · see citing works
Self-citation
TREM2 Variants in Alzheimer's Disease
Guerreiro, R., Wojtas, A., Bras, J., Carrasquillo, M., Rogaeva, E., Majounie, E., Cruchaga, C., Sassi, C., Kauwe, J. S. K., Younkin, S., et al. (2013) · New England Journal of Medicine · doi:10.1056/nejmoa1211851 · Cited by 3,020 · see citing works
Self-citation
Variant of TREM2 Associated with the Risk of Alzheimer's Disease
Jonsson, T., Stefansson, H., Steinberg, S., Jonsdottir, I., Jonsson, P. V., Snaedal, J., Bjornsson, S., Huttenlocher, J., Levey, A. I., Lah, J. J., et al. (2013) · New England Journal of Medicine · doi:10.1056/nejmoa1211103 · Cited by 2,558 · see citing works
Genome-wide association study identifies variants at CLU and CR1 associated with Alzheimer's disease
the European Alzheimer's Disease Initiative Investigators, Lambert, J.-C., Heath, S., Even, G., Campion, D., Sleegers, K., Hiltunen, M., Combarros, O., Zelenika, D., Bullido, M. J., et al. (2009) · Nature Genetics · doi:10.1038/ng.439 · Cited by 2,234 · see citing works
Common variants at ABCA7, MS4A6A/MS4A4E, EPHA1, CD33 and CD2AP are associated with Alzheimer's disease
Initiative, T. A. D. N., Hollingworth, P., CHARGE consortium, EADI1 consortium, Harold, D., Sims, R., Gerrish, A., Lambert, J.-C., Carrasquillo, M. M., Abraham, R., et al. (2011) · Nature Genetics · doi:10.1038/ng.803 · Cited by 1,997 · see citing works
Self-citation
Common variants at MS4A4/MS4A6E, CD2AP, CD33 and EPHA1 are associated with late-onset Alzheimer's disease
Naj, A. C., Jun, G., Beecham, G. W., Wang, L.-S., Vardarajan, B. N., Buros, J., Gallins, P. J., Buxbaum, J. D., Jarvik, G. P., Crane, P. K., et al. (2011) · Nature Genetics · doi:10.1038/ng.801 · Cited by 1,901 · see citing works
Self-citation
A mutation in APP protects against Alzheimer’s disease and age-related cognitive decline
Jonsson, T., Atwal, J. K., Steinberg, S., Snaedal, J., Jonsson, P. V., Bjornsson, S., Stefansson, H., Sulem, P., Gudbjartsson, D., Maloney, J., et al. (2012) · Nature · doi:10.1038/nature11283 · Cited by 1,738 · see citing works
The role of apolipoprotein E in Alzheimer's disease
Kim, J., Basak, J. M., & Holtzman, D. M. (2009) · Neuron · doi:10.1016/j.neuron.2009.06.026 · Cited by 1,661 · see citing works
Integrated Systems Approach Identifies Genetic Nodes and Networks in Late-Onset Alzheimer’s Disease
Zhang, B., Gaiteri, C., Bodea, L.-G., Wang, Z., McElwee, J., Podtelezhnikov, A. A., Zhang, C., Xie, T., Tran, L., Dobrin, R., et al. (2013) · Cell · doi:10.1016/j.cell.2013.03.030 · Cited by 1,657 · see citing works
Alzheimer’s Disease: The Challenge of the Second Century
Holtzman, D. M., Morris, J. C., & Goate, A. M. (2011) · Science Translational Medicine · doi:10.1126/scitranslmed.3002369 · Cited by 1,424 · see citing works
Self-citation
Binding of human apolipoprotein E to synthetic amyloid beta peptide: isoform-specific effects and implications for late-onset Alzheimer disease.
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 · see citing works
Human ApoE isoforms differentially regulate brain amyloid-β peptide clearance
Castellano, J. M., Kim, J., Stewart, F. R., Jiang, H., DeMattos, R. B., Patterson, B. W., Fagan, A. M., Morris, J. C., Mawuenyega, K. G., Cruchaga, C., et al. (2011) · Science Translational Medicine · doi:10.1126/scitranslmed.3002156 · Cited by 1,227 · cited 2× · see citing works
“The SNP rs9331888 is associated with expression of an alternative splice variant (36), whereas rs9331888 and rs11136000 are associated with plasma clusterin levels (47–49).”
Self-citation
The neuronal sortilin-related receptor SORL1 is genetically associated with Alzheimer disease
Rogaeva, E., Meng, Y., Lee, J. H., Gu, Y., Kawarai, T., Zou, F., Katayama, T., Baldwin, C. T., Cheng, R., Hasegawa, H., et al. (2007) · Nature Genetics · doi:10.1038/ng1943 · Cited by 1,167 · see citing works
Amyloid Precursor Protein Trafficking, Processing, and Function
Thinakaran, G., & Koo, E. H. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r800019200 · Cited by 1,141 · see citing works
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 · see citing works
The Alzheimer's Disease Neuroimaging Initiative: A review of papers published since its inception
Weiner, M. W., Veitch, D. P., Aisen, P. S. S., Beckett, L. A., Cairns, N. J., Green, R. C., Harvey, D. J., Jack, C. R., Jagust, W. J., Liu, E., et al. (2013) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2013.05.1769 · Cited by 1,010 · see citing works
Alzheimer’s Disease Risk Gene CD33 Inhibits Microglial Uptake of Amyloid Beta
Griciuc, A., Serrano-Pozo, A., Parrado, A. R., Lesinski, A. N., Asselin, C. N., Mullin, K., Hooli, B., Choi, S. H., Hyman, B. T., & Tanzi, R. E. (2013) · Neuron · doi:10.1016/j.neuron.2013.04.014 · Cited by 1,004 · see citing works
Apolipoprotein E isoform-dependent amyloid deposition and neuritic degeneration in a mouse model of Alzheimer's disease
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 · see citing works
Oncogenic BRAF Induces Senescence and Apoptosis through Pathways Mediated by the Secreted Protein IGFBP7
Wajapeyee, N., Serra, R. W., Zhu, X., Mahalingam, M., & Green, M. R. (2008) · Cell · doi:10.1016/j.cell.2007.12.032 · Cited by 903 · see citing works
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 · see citing works
APOE predicts amyloid‐beta but not tau Alzheimer pathology in cognitively normal aging
Morris, J. C., Roe, C. M., Xiong, C., Fagan, A. M., Goate, A. M., Holtzman, D. M., & Mintun, M. A. (2010) · Annals of Neurology · doi:10.1002/ana.21843 · Cited by 830 · see citing works
Self-citation
Evidence for excitoprotective and intraneuronal calcium-regulating roles for secreted forms of the β-amyloid precursor protein
Mattson, M. P., Cheng, B., Culwell, A. R., Esch, F. S., Lieberburg, I. M., & Rydel, R. E. (1993) · Neuron · doi:10.1016/0896-6273(93)90315-i · Cited by 795 · see citing works
Fibrillar amyloid-β burden in cognitively normal people at 3 levels of genetic risk for Alzheimer's disease
Reiman, E. M., Chen, K., Liu, X., Bandy, D., Yu, M., Lee, W., Ayutyanont, N., Keppler, J., Reeder, S. A., Langbaum, J. B. S., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900345106 · Cited by 785 · see citing works
A Novel Adaptor Protein Orchestrates Receptor Patterning and Cytoskeletal Polarity in T-Cell Contacts
Dustin, M. L., Olszowy, M. W., Holdorf, A. D., Li, J., Bromley, S. K., Desai, N. N., Widder, P., Rosenberger, F., van der Merwe, P. A., Allen, P. M., et al. (1998) · Cell · doi:10.1016/s0092-8674(00)81608-6 · Cited by 710 · see citing works
TREMs in the immune system and beyond
Colonna, M. (2003) · Nature Reviews Immunology · doi:10.1038/nri1106 · Cited by 701 · see citing works
Mutations in Two Genes Encoding Different Subunits of a Receptor Signaling Complex Result in an Identical Disease Phenotype
Paloneva, J., Manninen, T., Christman, G., Hovanes, K., Mandelin, J., Adolfsson, R., Bianchin, M., Bird, T., Miranda, R., Salmaggi, A., et al. (2002) · The American Journal of Human Genetics · doi:10.1086/342259 · Cited by 683 · see citing works
Iron-Export Ferroxidase Activity of β-Amyloid Precursor Protein Is Inhibited by Zinc in Alzheimer's Disease
Duce, J. A., Tsatsanis, A., Cater, M. A., James, S., Robb, E. L., Wikhe, K., Leong, S. L., Perez, K. A., Johanssen, T., Greenough, M. A., et al. (2010) · Cell · doi:10.1016/j.cell.2010.08.014 · Cited by 682 · see citing works
ADAM10 is the physiologically relevant, constitutive α‐secretase of the amyloid precursor protein in primary neurons
Kuhn, P., Wang, H., Dislich, B., Colombo, A., Zeitschel, U., Ellwart, J. W., Kremmer, E., Roßner, S., & Lichtenthaler, S. F. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.167 · Cited by 621 · cited 1× · see citing works
“org/journ in ADAM10, the major α-secretase involved in shedding of the APP ectodomain (30), cosegregate in seven LOAD families (8,31).”
ApoE influences amyloid-β (Aβ) clearance despite minimal apoE/Aβ association in physiological conditions
Verghese, P. B., Castellano, J. M., Garai, K., Wang, Y., Jiang, H., Shah, A., Bu, G., Frieden, C., & Holtzman, D. M. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1220484110 · Cited by 556 · see citing works
Genome-wide Association Analysis Reveals Putative Alzheimer's Disease Susceptibility Loci in Addition to APOE
Bertram, L., Lange, C., Mullin, K., Parkinson, M., Hsiao, M., Hogan, M. F., Schjeide, B. M. M., Hooli, B., DiVito, J., Ionita, I., et al. (2008) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2008.10.008 · Cited by 511 · see citing works
Clusterin
Jones, S. (2002) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(01)00155-8 · Cited by 488 · see citing works
Rare coding variants in the phospholipase D3 gene confer risk for Alzheimer’s disease
Cruchaga, C., Karch, C. M., Jin, S. C., Benitez, B. A., Cai, Y., Guerreiro, R., Harari, O., Norton, J., Budde, J., Bertelsen, S., et al. (2014) · Nature · doi:10.1038/nature12825 · Cited by 461 · see citing works
Self-citation
ApoE and Clusterin Cooperatively Suppress Aβ Levels and Deposition
DeMattos, R. B., Cirrito, J. R., Parsadanian, M., May, P. C., O'Dell, M. A., Taylor, J. W., Harmony, J. A. K., Aronow, B. J., Bales, K. R., Paul, S. M., et al. (2004) · Neuron · doi:10.1016/s0896-6273(03)00850-x · Cited by 459 · see citing works
Immunoglobulins and complement factors in senile plaques: An immunoperoxidase study
Eikelenboom, P., & Stam, F. C. (1982) · Acta Neuropathologica · doi:10.1007/bf00685397 · Cited by 454 · see citing works
Synaptic Vesicle Size and Number Are Regulated by a Clathrin Adaptor Protein Required for Endocytosis
Zhang, B., Koh, Y. H., Beckstead, R. B., Budnik, V., Ganetzky, B., & Bellen, H. J. (1998) · Neuron · doi:10.1016/s0896-6273(00)80664-9 · Cited by 434 · see citing works
Increased expression of BIN1 mediates Alzheimer genetic risk by modulating tau pathology
GERAD consortium, Chapuis, J., Hansmannel, F., Gistelinck, M., Mounier, A., Van Cauwenberghe, C., Kolen, K. V., Geller, F., Sottejeau, Y., Harold, D., et al. (2013) · Molecular Psychiatry · doi:10.1038/mp.2013.1 · Cited by 407 · see citing works
Association of plasma clusterin concentration with severity, pathology, and progression in Alzheimer disease
Thambisetty, M., Simmons, A., Velayudhan, L., Hye, A., Campbell, J., Zhang, Y., Wahlund, L.-O., Westman, E., Kinsey, A., Güntert, A., et al. (2010) · Archives of General Psychiatry · doi:10.1001/archgenpsychiatry.2010.78 · Cited by 405 · see citing works
TREM2 in neurodegeneration: evidence for association of the p.R47H variant with frontotemporal dementia and Parkinson’s disease
Rayaprolu, S., Mullen, B., Baker, M., Lynch, T., Finger, E., Seeley, W. W., Hatanpaa, K. J., Lomen-Hoerth, C., Kertesz, A., Bigio, E. H., et al. (2013) · Molecular Neurodegeneration · doi:10.1186/1750-1326-8-19 · Cited by 404 · see citing works
Inhibition of Osf2/Cbfa1 expression and terminal osteoblast differentiation by PPAR?2
Lecka‐Czernik, B., Gubrij, I. B., Moerman, E. J., Kajkenova, O., Lipschitz, D. A., Manolagas, S. C., & Jilka, R. L. (1999) · Journal of Cellular Biochemistry · doi:10.1002/(sici)1097-4644(19990901)74:3 · Cited by 403 · see citing works
The Secreted β-Amyloid Precursor Protein Ectodomain APPsα Is Sufficient to Rescue the Anatomical, Behavioral, and Electrophysiological Abnormalities of APP-Deficient Mice
Ring, S., Weyer, S. W., Kilian, S. B., Waldron, E., Pietrzik, C. U., Filippov, M. A., Herms, J., Buchholz, C., Eckman, C. B., Korte, M., et al. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.1026-07.2007 · Cited by 390 · see citing works
Activation of the classical complement pathway in brain tissue of Alzheimer patients
McGeer, P. L., Akiyama, H., Itagaki, S., & McGeer, E. G. (1989) · Neuroscience Letters · doi:10.1016/0304-3940(89)90843-4 · Cited by 383 · see citing works
GWAS of Cerebrospinal Fluid Tau Levels Identifies Risk Variants for Alzheimer’s Disease
Cruchaga, C., Kauwe, J. S. K., Harari, O., Jin, S. C., Cai, Y., Karch, C. M., Benitez, B. A., Jeng, A. T., Skorupa, T., Carrell, D., et al. (2013) · Neuron · doi:10.1016/j.neuron.2013.02.026 · Cited by 383 · see citing works
Self-citation
Functional Links Between Aβ Toxicity, Endocytic Trafficking, and Alzheimer’s Disease Risk Factors in Yeast
Treusch, S., Hamamichi, S., Goodman, J. L., Matlack, K. E. S., Chung, C. Y., Baru, V., Shulman, J. M., Parrado, A., Bevis, B. J., Valastyan, J. S., et al. (2011) · Science · doi:10.1126/science.1213210 · Cited by 379 · see citing works
Using Exome Sequencing to Reveal Mutations in TREM2 Presenting as a Frontotemporal Dementia–like Syndrome Without Bone Involvement
Guerreiro, R. J., Lohmann, E., Brás, J. M., Gibbs, J. R., Rohrer, J. D., Gurunlian, N., Dursun, B., Bilgic, B., Hanagasi, H., Gurvit, H., et al. (2013) · JAMA Neurology · doi:10.1001/jamaneurol.2013.579 · Cited by 374 · cited 2× · see citing works
“TREM2 R47H is also associated with increased risk for Parkinson’s disease, frontotemporal dementia, and amyotrophic lateral sclerosis (96,97,102,103).”
Clusterin promotes amyloid plaque formation and is critical for neuritic toxicity in a mouse model of Alzheimer's disease
DeMattos, R. B., O'dell, M. A., Parsadanian, M., Taylor, J. W., Harmony, J. A. K., Bales, K. R., Paul, S. M., Aronow, B. J., & Holtzman, D. M. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.162228299 · Cited by 359 · see citing works
Clusterin (apoJ) Alters the Aggregation of Amyloid β-Peptide (Aβ1-42) and Forms Slowly Sedimenting Aβ Complexes That Cause Oxidative Stress
Oda, T., Wals, P., Osterburg, H. H., Johnson, S. A., Pasinetti, G. M., Morgan, T. E., Rozovsky, I., Stine, W. B., Snyder, S. W., Holzman, T. F., et al. (1995) · Experimental Neurology · doi:10.1006/exnr.1995.1080 · Cited by 352 · see citing works
Dynamics of gene expression for a hippocampal glycoprotein elevated in Alzheimer's disease and in response to experimental lesions in rat
May, P. C., Lampert-Etchells, M., Johnson, S. A., Poirier, J., Masters, J. N., & Finch, C. E. (1990) · Neuron · doi:10.1016/0896-6273(90)90342-d · Cited by 339 · see citing works
Phospholipase D
McDermott, M. I., Wakelam, M. J. O., & Morris, A. J. (2004) · Biochemistry and Cell Biology · doi:10.1139/o03-079 · Cited by 333 · see citing works
Expression of Novel Alzheimer’s Disease Risk Genes in Control and Alzheimer’s Disease Brains
Karch, C. M., Jeng, A. T., Nowotny, P., Cady, J., Cruchaga, C., & Goate, A. M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0050976 · Cited by 328 · see citing works
Self-citation
Rare variants in APP, PSEN1 and PSEN2 increase risk for AD in late-onset Alzheimer’s disease families
Cruchaga, C., Chakraverty, S., Mayo, K., Vallania, F. L. M., Mitra, R. D., Faber, K., Williamson, J., Bird, T., Diaz-Arrastia, R., Foroud, T. M., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0031039 · Cited by 320 · see citing works
Self-citation
Loss of apolipoprotein E receptor LR11 in Alzheimer disease
Scherzer, C. R., Offe, K., Gearing, M., Rees, H. D., Fang, G., Heilman, C. J., Schaller, C., Bujo, H., Levey, A. I., & Lah, J. J. (2004) · Archives of Neurology · doi:10.1001/archneur.61.8.1200 · Cited by 316 · see citing works
Sequential Proteolytic Processing of the Triggering Receptor Expressed on Myeloid Cells-2 (TREM2) Protein by Ectodomain Shedding and γ-Secretase-dependent Intramembranous Cleavage
Wunderlich, P., Glebov, K., Kemmerling, N., Tien, N. T., Neumann, H., & Walter, J. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.517540 · Cited by 296 · see citing works
Human and Murine ApoE Markedly Alters Aβ Metabolism before and after Plaque Formation in a Mouse Model of Alzheimer's Disease
Fagan, A. M., Watson, M., Parsadanian, M., Bales, K. R., Paul, S. M., & Holtzman, D. M. (2002) · Neurobiology of Disease · doi:10.1006/nbdi.2002.0483 · Cited by 290 · see citing works
The genetic architecture of Alzheimer's disease: beyond APP, PSENs and APOE
Guerreiro, R. J., Gustafson, D. R., & Hardy, J. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2010.03.025 · Cited by 285 · see citing works
The Lipoprotein Receptor LR11 Regulates Amyloid β Production and Amyloid Precursor Protein Traffic in Endosomal Compartments
Offe, K., Dodson, S. E., Shoemaker, J. T., Fritz, J. J., Gearing, M., Levey, A. I., & Lah, J. J. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.4946-05.2006 · Cited by 279 · see citing works
Human Apolipoprotein E4 Alters the Amyloid-β 40:42 Ratio and Promotes the Formation of Cerebral Amyloid Angiopathy in an Amyloid Precursor Protein Transgenic Model
Fryer, J. D., Simmons, K., Parsadanian, M., Bales, K. R., Paul, S. M., Sullivan, P. M., & Holtzman, D. M. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.5170-04.2005 · Cited by 278 · see citing works
TREM2Variant p.R47H as a Risk Factor for Sporadic Amyotrophic Lateral Sclerosis
Cady, J., Koval, E. D., Benitez, B. A., Zaidman, C., Jockel-Balsarotti, J., Allred, P., Baloh, R. H., Ravits, J., Simpson, E., Appel, S. H., et al. (2014) · JAMA Neurology · doi:10.1001/jamaneurol.2013.6237 · Cited by 262 · see citing works
Self-citation
CD33 Alzheimer’s risk-altering polymorphism, CD33 expression, and exon 2 splicing
Malik, M., Simpson, J. F., Parikh, I., Wilfred, B. R., Fardo, D. W., Nelson, P. T., & Estus, S. (2013) · The Journal of Neuroscience · doi:10.1523/jneurosci.1224-13.2013 · Cited by 262 · see citing works
TREM2and Neurodegenerative Disease
Reitz, C., & Mayeux, R. P. (2013) · New England Journal of Medicine · doi:10.1056/nejmc1306509 · Cited by 254 · see citing works
The amphiphysin family of proteins and their role in endocytosis at the synapse
Wigge, P., & McMahon, H. T. (1998) · Trends in Neurosciences · doi:10.1016/s0166-2236(98)01264-8 · Cited by 247 · see citing works
Role of ATP‐binding cassette transporters in brain lipid transport and neurological disease
Kim, W. S., Weickert, C. S., & Garner, B. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.05099.x · Cited by 237 · see citing works
Decreased Synaptic Vesicle Recycling Efficiency and Cognitive Deficits in Amphiphysin 1 Knockout Mice
Paolo, G. D., Sankaranarayanan, S., Wenk, M. R., DANIELL, L. W., Perucco, E., Caldarone, B. J., Flavell, R. A., Picciotto, M. R., Ryan, T. A., Cremona, O., et al. (2002) · Neuron · doi:10.1016/s0896-6273(02)00601-3 · Cited by 235 · see citing works
Evidence for impaired amyloid β clearance in Alzheimer's disease
Wildsmith, K. R., Holley, M., Savage, J. C., Skerrett, R., & Landreth, G. E. (2013) · Alzheimer s Research & Therapy · doi:10.1186/alzrt187 · Cited by 234 · see citing works
Potential late-onset Alzheimer's disease-associated mutations in the ADAM10 gene attenuate α-secretase activity
Kim, M., Suh, J., Romano, D., Truong, M. H., Mullin, K., Hooli, B., Norton, D., Tesco, G., Elliott, K., Wagner, S. L., et al. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp323 · Cited by 234 · see citing works
Adaptor complex AP2/PICALM, through interaction with LC3, targets Alzheimer's APP-CTF for terminal degradation via autophagy
Tian, Y., Chang, J. C., Fan, E. Y., Flajolet, M., & Greengard, P. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1315110110 · Cited by 233 · see citing works
Genetic Variation and Neuroimaging Measures in Alzheimer Disease
Biffi, A. (2010) · Archives of Neurology · doi:10.1001/archneurol.2010.108 · Cited by 222 · see citing works
Plasma clusterin and the risk of Alzheimer disease
Schrijvers, E. M. C. (2011) · JAMA · doi:10.1001/jama.2011.381 · Cited by 220 · see citing works
The BAR Domain Proteins: Molding Membranes in Fission, Fusion, and Phagy
Ren, G., Vajjhala, P., Lee, J. S., Winsor, B., & Munn, A. (2006) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.70.1.37-120.2006 · Cited by 219 · see citing works
AMPH-1/Amphiphysin/Bin1 functions with RME-1/Ehd1 in endocytic recycling
Pant, S., Sharma, M., Patel, K., Caplan, S., Carr, C. M., & Grant, B. D. (2009) · Nature Cell Biology · doi:10.1038/ncb1986 · Cited by 218 · see citing works
ADAM10 Missense Mutations Potentiate β-Amyloid Accumulation by Impairing Prodomain Chaperone Function
Suh, J., Choi, S. H., Romano, D. M., Gannon, M. A., Lesinski, A. N., Kim, D. Y., & Tanzi, R. E. (2013) · Neuron · doi:10.1016/j.neuron.2013.08.035 · Cited by 217 · see citing works
Neuronal expression of mRNAs for complement proteins of the classical pathway in Alzheimer brain.
Shen, Y., Li, R.-N., Mcgeer, E., & McGeer, P. (1997) · Brain Research · doi:10.1016/s0006-8993(97)00850-0 · Cited by 213 · see citing works
ATP-binding cassette transporter A7 enhances phagocytosis of apoptotic cells and associated ERK signaling in macrophages
Jehle, A. W., Gardai, S. J., Li, S., Linsel‐Nitschke, P., Morimoto, K., Janssen, W. J., Vandivier, R. W., Wang, N., Greenberg, S., Dale, B. M., et al. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200601030 · Cited by 213 · see citing works
Deletion ofAbca7Increases Cerebral Amyloid-β Accumulation in the J20 Mouse Model of Alzheimer's Disease
Kim, W. S., Li, H., Ruberu, K. R., Chan, S. L., Elliott, D. A., Low, J. K., Cheng, D., Karl, T., & Garner, B. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.4165-12.2013 · Cited by 209 · see citing works
Characterization of Apolipoprotein J-Alzheimer's Aβ Interaction
Matsubara, E., Frangione, B., & Ghiso, J. A. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.13.7563 · Cited by 195 · see citing works
Synapse development and plasticity: roles of ephrin/Eph receptor signaling
Lai, K., & Ip, N. Y. (2009) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2009.04.009 · Cited by 191 · see citing works
Apolipoprotein J and Alzheimer's amyloid β solubility
Matsubara, E., Soto, C. A., Governale, S., Frangione, B., & Ghiso, J. A. (1996) · Biochemical Journal · doi:10.1042/bj3160671 · Cited by 190 · see citing works
Candidate Blood Proteome Markers of Alzheimer's Disease Onset and Progression: A Systematic Review and Replication Study
Kiddle, S. J., Sattlecker, M., Proitsi, P., Simmons, A., Westman, E., Bazenet, C. E., Nelson, S. K., Williams, S., Hodges, A., Johnston, C., et al. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-130380 · Cited by 187 · see citing works
Complement activation by neurofibrillary tangles in Alzheimer's disease
Shen, Y., Lue, L.-F., Yang, L.-B., Roher, A., Kuo, Y.-M., Strohmeyer, R., Goux, W. J., Lee, V., Johnson, G. V. W., Webster, S. D., et al. (2001) · Neuroscience Letters · doi:10.1016/s0304-3940(01)01842-0 · Cited by 185 · see citing works
Multiple Amphiphysin II Splice Variants Display Differential Clathrin Binding: Identification of Two Distinct Clathrin‐Binding Sites
Ramjaun, A. R., & McPherson, P. S. (1998) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1998.70062369.x · Cited by 183 · see citing works
SorLA/LR11 regulates processing of amyloid precursor protein via interaction with adaptors GGA and PACS-1
Schmidt, V., Sporbert, A., Rohe, M., Reimer, T., Rehm, A., Andersen, O. M., & Willnow, T. E. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705073200 · Cited by 181 · see citing works
Interaction of the Cytosolic Domains of sorLA/LR11 with the Amyloid Precursor Protein (APP) and β-Secretase β-Site APP-Cleaving Enzyme
Spoelgen, R., Arnim, C. A. F. V., Thomas, A. V., Peltan, I. D., Koker, M., Deng, A., Irizarry, M. C., Andersen, O. M., Willnow, T. E., & Hyman, B. T. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.3882-05.2006 · Cited by 181 · see citing works
Phospholipase D2 Ablation Ameliorates Alzheimer's Disease-Linked Synaptic Dysfunction and Cognitive Deficits
Oliveira, T. G., Chan, R., Tian, H., Laredo, M., Shui, G., Staniszewski, A., Zhang, H., Wang, L., Kim, T., Duff, K., et al. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.3317-10.2010 · Cited by 179 · see citing works
Peripheral clearance of amyloid β peptide by complement C3-dependent adherence to erythrocytes
Rogers, J., Li, R., Mastroeni, D., Grover, A., Leonard, B., Ahern, G., Cao, P., Kolody, H., Vedders, L., Kolb, W. P., et al. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.09.043 · Cited by 175 · see citing works
Role of Phosphatidylinositol Clathrin Assembly Lymphoid-Myeloid Leukemia (PICALM) in Intracellular Amyloid Precursor Protein (APP) Processing and Amyloid Plaque Pathogenesis
Xiao, Q., Gil, S.-C., Yan, P., Wang, Y., Han, S., Gonzales, E., Perez, R., Cirrito, J. R., & Lee, J.-M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.338376 · Cited by 166 · see citing works
Protein traffic in the yeast endocytic and vacuolar protein sorting pathways
Wendland, B., Emr, S. D., & Riezman, H. (1998) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(98)80067-7 · Cited by 164 · see citing works
Novel late-onset Alzheimer disease loci variants associate with brain gene expression
Allen, M., Zou, F., Chai, H. S., Younkin, C. S., Crook, J. E., Pankratz, V. S., Carrasquillo, M. M., Rowley, C. N., Nair, A., Middha, S., et al. (2012) · Neurology · doi:10.1212/wnl.0b013e3182605801 · Cited by 164 · see citing works
TREM2 R47H Variant as a Risk Factor for Early-Onset Alzheimer's Disease
Pottier, C. P., collaborators, G., Wallon, D., Rousseau, S., Rovelet‐Lecrux, A., Richard, A., Rollin‐Sillaire, A., Frébourg, T., Campion, D., & Hannequin, D. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-122311 · Cited by 162 · see citing works
Quantitation of ATP-binding cassette subfamily-A transporter gene expression in primary human brain cells
Kim, W., Guillemin, G., Glaros, E., Lim, C. K., & Garner, B. (2006) · NeuroReport · doi:10.1097/01.wnr.0000221833.41340.cd · Cited by 158 · see citing works
Genetic Susceptibility for Alzheimer Disease Neuritic Plaque Pathology
Shulman, J. M., Chen, K., Keenan, B. T., Chibnik, L. B., Fleisher, A., Thiyyagura, P., Roontiva, A., Aubin, C., Patsopoulos, N. A., Corneveaux, J. J., et al. (2013) · JAMA Neurology · doi:10.1001/jamaneurol.2013.2815 · Cited by 156 · see citing works
LR11/SorLA Expression Is Reduced in Sporadic Alzheimer Disease but not in Familial Alzheimer Disease
Dodson, S. E., Gearing, M., Lippa, C. F., Montine, T. J., Levey, A. I., & Lah, J. J. (2006) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/01.jnen.0000228205.19915.20 · Cited by 154 · see citing works
Neurons express proteins of the classical complement pathway in Alzheimer disease.
Terai, K., Walker, D., Mcgeer, E., & McGeer, P. (1997) · Brain Research · doi:10.1016/s0006-8993(97)00849-4 · Cited by 149 · see citing works
Aspartate residue 7 in amyloid β-protein is critical for classical complement pathway activation: Implications for Alzheimer's disease pathogenesis
Velázquez, P., Cribbs, D. H., Poulos, T. L., & Tenner, A. J. (1997) · Nature Medicine · doi:10.1038/nm0197-77 · Cited by 147 · see citing works
Variants in triggering receptor expressed on myeloid cells 2 are associated with both behavioral variant frontotemporal lobar degeneration and Alzheimer's disease
Giraldo, M., Lopera, F., Siniard, A. L., Corneveaux, J. J., Schrauwen, I., Carvajal, J., Muñoz, C., Ramirez-Restrepo, M., Gaiteri, C., Myers, A. J., et al. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.02.016 · Cited by 147 · see citing works
Evidence for CALM in Directing VAMP2 Trafficking
Harel, A., Wu, F., Mattson, M. P., Morris, C. M., & Yao, P. J. (2008) · Traffic · doi:10.1111/j.1600-0854.2007.00694.x · Cited by 144 · see citing works
Loss of LR11/SORLA Enhances Early Pathology in a Mouse Model of Amyloidosis: Evidence for a Proximal Role in Alzheimer's Disease
Dodson, S. E., Andersen, O. M., Karmali, V., Fritz, J. J., Cheng, D., Peng, J., Levey, A. I., Willnow, T. E., & Lah, J. J. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.4582-08.2008 · Cited by 141 · see citing works
CD2AP/CMS Regulates Endosome Morphology and Traffic to the Degradative Pathway Through its Interaction with Rab4 and c‐Cbl
Cormont, M., Metón, I., Mari, M. C., Monzo, P., Keslair, F., Gaskin, C., McGraw, T. E., & MARCHAND‐BRUSTEL, Y. L. (2003) · Traffic · doi:10.1034/j.1600-0854.2003.40205.x · Cited by 138 · see citing works
Abca7 Null Mice Retain Normal Macrophage Phosphatidylcholine and Cholesterol Efflux Activity despite Alterations in Adipose Mass and Serum Cholesterol Levels
Kim, W. S., Fitzgerald, M. L., Kang, K., Okuhira, K., Bell, S. A., Manning, J. J., Koehn, S. L., Lu, N., Moore, K. J., & Freeman, M. W. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m412602200 · Cited by 137 · see citing works
ATP‐binding cassette transporter A7 regulates processing of amyloid precursor protein in vitro
Chan, S. L., Kim, W. S., Kwok, J. B., Hill, A. F., Cappai, R., Rye, K., & Garner, B. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05433.x · Cited by 133 · see citing works
SNPs Associated with Cerebrospinal Fluid Phospho-Tau Levels Influence Rate of Decline in Alzheimer's Disease
Cruchaga, C., Kauwe, J. S. K., Mayo, K., Spiegel, N., Bertelsen, S., Nowotny, P., Shah, A. R., Abraham, R., Hollingworth, P., Harold, D., et al. (2010) · PLoS Genetics · doi:10.1371/journal.pgen.1001101 · Cited by 128 · see citing works
Self-citation
Distinct Endocytic Mechanisms of CD22 (Siglec-2) and Siglec-F Reflect Roles in Cell Signaling and Innate Immunity
Tateno, H., Li, H., Schur, M. J., Bovin, N. V., Crocker, P. R., Wakarchuk, W. W., & Paulson, J. C. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00383-07 · Cited by 123 · see citing works
Expression of the complement classical pathway by human glioma in culture. A model for complement expression by nerve cells.
Gasque, P., Ischenko, A. M., Legoedec, J., Mauger, C., Schouft, M., & Fontaine, M. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)74572-4 · Cited by 117 · see citing works
Microglial activatory (immunoreceptor tyrosine‐based activation motif)‐ and inhibitory (immunoreceptor tyrosine‐based inhibition motif)‐signaling receptors for recognition of the neuronal glycocalyx
Linnartz‐Gerlach, B., & Neumann, H. (2012) · Glia · doi:10.1002/glia.22359 · Cited by 117 · see citing works
Distribution and Expression of Picalm in Alzheimer Disease
Baig, S., Joseph, S. A., Tayler, H., Abraham, R., Owen, M. J., Williams, J., Kehoe, P. G., & Love, S. (2010) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3181f52e01 · Cited by 115 · see citing works
SnapShot: genetics of Alzheimer's disease.
Guerreiro, R., Bras, J., & Hardy, J. (2013) · Cell · doi:10.1016/j.cell.2013.10.037 · Cited by 114 · see citing works
Presenilin-1 uses phospholipase D1 as a negative regulator of β-amyloid formation
Cai, D., Netzer, W. J., Zhong, M., Lin, Y., Du, G., Frohman, M. A., Foster, D. A., Sisodia, S. S., Xu, H., Gorelick, F. S., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0510708103 · Cited by 111 · see citing works
Phospholipase D1 corrects impaired βAPP trafficking and neurite outgrowth in familial Alzheimer’s disease-linked presenilin-1 mutant neurons
Cai, D., Zhong, M., Wang, R., Netzer, W. J., Shields, D., Zheng, H., Sisodia, S. S., Foster, D. A., Gorelick, F. S., Xu, H., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0510710103 · Cited by 109 · see citing works
EphA1 interacts with integrin-linked kinase and regulates cell morphology and motility
Yamazaki, T., Masuda, J., Omori, T., Usui, R., Akiyama, H., & Maru, Y. (2008) · Journal of Cell Science · doi:10.1242/jcs.036467 · Cited by 107 · see citing works
Pooled-DNA sequencing identifies novel causative variants in PSEN1, GRN and MAPT in a clinical early-onset and familial Alzheimer's disease Ibero-American cohort
Jin, S. C., Pástor, P., Cooper, B., Cervantes, S., Benítez, B. A., Razquín, C., Goate, A., Ibero-American Alzheimer Disease Genetics Group Researchers, & Cruchaga, C. (2012) · Alzheimer s Research & Therapy · doi:10.1186/alzrt137 · Cited by 106 · see citing works
Self-citation
ABCA7 expression is associated with Alzheimer's disease polymorphism and disease status
Vasquez, J. B., Fardo, D. W., & Estus, S. (2013) · Neuroscience Letters · doi:10.1016/j.neulet.2013.09.058 · Cited by 101 · see citing works
Clathrin interacts specifically with amphiphysin and is displaced by dynamin 1
McMahon, H. T., Wigge, P., & Smith, C. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00928-9 · Cited by 97 · see citing works
Neuronal LR11/sorLA expression is reduced in mild cognitive impairment
Sager, K. L., Wuu, J., Leurgans, S. E., Rees, H. D., Gearing, M., Mufson, E. J., Levey, A. I., & Lah, J. J. (2007) · Annals of Neurology · doi:10.1002/ana.21190 · Cited by 96 · see citing works
Expression of complement messenger RNAs and proteins by human oligodendroglial cells
Hosokawa, M., Klegeris, A., Maguire, J. A., & McGeer, P. L. (2003) · Glia · doi:10.1002/glia.10234 · Cited by 95 · see citing works
Variation in MAPT is associated with cerebrospinal fluid tau levels in the presence of amyloid-beta deposition
Kauwe, J. S. K., Cruchaga, C., Mayo, K., Fenoglio, C., Bertelsen, S. E., Nowotny, P., Galimberti, D., Scarpini, E. A., Morris, J. C., Fagan, A. M., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0801227105 · Cited by 89 · see citing works
Self-citation
Comparative Proteomic Analysis of Brains of Naturally Aging Mice
Yang, S., Liu, T., Li, S., Zhang, X., Ding, Q., Que, H., Yan, X., Wei, K., & Liu, S. (2008) · Neuroscience · doi:10.1016/j.neuroscience.2008.04.012 · Cited by 82 · see citing works
The structure, genetic polymorphisms, expression and biological functions of complement receptor type 1 (CR1/CD35)
Liu, D., & Zhong-xiang, N. (2009) · Immunopharmacology and Immunotoxicology · doi:10.3109/08923970902845768 · Cited by 79 · see citing works
Functional Screening of Alzheimer Pathology Genome-wide Association Signals in Drosophila
Shulman, J. M., Chipendo, P. I., Chibnik, L. B., Aubin, C., Tran, D., Keenan, B. T., Kramer, P. L., Schneider, J. A., Bennett, D., Feany, M. Β., et al. (2011) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2011.01.006 · Cited by 77 · see citing works
The potential role of sialoadhesin as a macrophage recognition molecule in health and disease
Crocker, P. R., Hartnell, A., Munday, J. R., et al. (1997) · Glycoconjugate Journal · doi:10.1023/a:1018588526788 · Cited by 74 · see citing works
Roles of ATP-Binding Cassette Transporter A7 in Cholesterol Homeostasis and Host Defense System
Tanaka, N., Abe-Dohmae, S., Iwamoto, N., & Yokoyama, S. (2011) · Journal of Atherosclerosis and Thrombosis · doi:10.5551/jat.6726 · Cited by 73 · see citing works
ASSOCIATION BETWEEN GENETIC VARIANTS IN SORL1 AND AUTOPSY-CONFIRMED ALZHEIMER DISEASE
Lee, J. H., Cheng, R., Honig, L. S., Vonsattel, J.-P., Clark, L. N., & Mayeux, R. P. (2007) · Neurology · doi:10.1212/01.wnl.0000280581.39755.89 · Cited by 73 · see citing works
Posttranscriptional regulation of human ABCA7 and its function for the apoA-I-dependent lipid release
Ikeda, Y., Abe-Dohmae, S., Munehira, Y., Aoki, R., Kawamoto, S., Furuya, A., Shitara, K., Amachi, T., Kioka, N., Matsuo, M., et al. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2003.10.002 · Cited by 72 · see citing works
Fine Mapping of Genetic Variants in BIN1, CLU, CR1 and PICALM for Association with Cerebrospinal Fluid Biomarkers for Alzheimer's Disease
Kauwe, J. S. K., Cruchaga, C., Karch, C. M. M., Sadler, B. E., Lee, M., Mayo, K., Latu, W., Su'a, M., Fagan, A. M., Holtzman, D. M., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0015918 · Cited by 72 · see citing works
Self-citation
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Howie, D., Nolan, K. F., Daley, S. R., Butterfield, E., Adams, E., Rueda, H. G., Thompson, C., Saunders, N. J. S. G., Cobbold, S. P., Tone, Y., et al. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0901070 · Cited by 72 · see citing works
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Zuccolo, J., Bau, J. A., Childs, S. J., Goss, G. G., Sensen, C. W., & Deans, J. P. (2010) · PLoS ONE · doi:10.1371/journal.pone.0009369 · Cited by 71 · see citing works
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Tsutsui, K., Maeda, Y., Tsutsui, K., Seki, S., & Tokunaga, A. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.6927 · Cited by 68 · see citing works
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Szymanski, M., Wang, R., Bassett, S. S., & Avramopoulos, D. (2011) · Translational Psychiatry · doi:10.1038/tp.2011.17 · Cited by 68 · see citing works
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Benítez, B. A., Karch, C. M. M., Cai, Y., Jin, S. C., Cooper, B., Carrell, D., Bertelsen, S. E., Chibnik, L. B., Schneider, J. A., Bennett, D., et al. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003685 · Cited by 64 · see citing works
Self-citation
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Wixler, V., Laplantine, E., Geerts, D., Sonnenberg, A., Petersohn, D., Eckes, B., Paulsson, M., & Aumailley, M. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00151-9 · Cited by 63 · see citing works
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Meunier, B., Quaranta, M., Daviet, L., Hatzoglou, A., & Leprince, C. (2008) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2008.08.006 · Cited by 59 · see citing works
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Sakamoto, A., Sugamoto, Y., Tokunaga, Y., et al. (2011) · Journal of International Medical Research · doi:10.1177/147323001103900220 · Cited by 54 · see citing works
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Xing, Y.-Y., Yu, J., Cui, W., Zhong, X.-L., Wu, Z., Zhang, Q., & Tan, L. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-111844 · Cited by 53 · see citing works
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Rizzi, F., Caccamo, A. E., Belloni, L., & Bettuzzi, S. (2009) · Journal of Cellular Physiology · doi:10.1002/jcp.21671 · Cited by 49 · see citing works
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Self-citation
Disruption of ephrin-A/EphA binding alters synaptogenesis and neural connectivity in the hippocampus
Martı́nez, A., Otal, R., Sieber, B.-A., Ibáñez, C. F., & Soriano, E. (2005) · Neuroscience · doi:10.1016/j.neuroscience.2005.06.052 · Cited by 41 · see citing works
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Munck, A., Böhm, C., Seibel, N. M., Hosseini, Z. H., & Hampe, W. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2005.04601.x · Cited by 35 · see citing works
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Schifferli, J. A., & Paccaud, J. (2017) · Complement and Inflammation · doi:10.1159/000463068 · Cited by 26 · see citing works
Relationship between Immune Complex Binding and Release and the Quantitative Expression of the Complement Receptor, Type 1 (CR1, CD35) on Human Erythrocytes
Gibson, N. C., & Waxman, F. J. (1994) · Clinical Immunology and Immunopathology · doi:10.1006/clin.1994.1017 · Cited by 19 · see citing works
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Bazenet, C. E., Kiddle, S. J., Sattlecker, M., Proitsi, P., Simmons, A., Westman, E., Nelson, S., Sterling, D., Williams, S., Hodges, A., et al. (2013) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2013.08.178 · Cited by 14 · see citing works
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[98]Bertram L Parrado AR Tanzi RE TREM2 and neurodegenerative disease. N Engl J Med 2013 369 1565 24131185
[99]Benitez BA Cruchaga C TREM2 and neurodegenerative disease. N Engl J Med 2013 369 1567 1568 24131187 PMC4380008
[101]Guerreiro R Hardy J TREM2 and neurodegenerative disease. N Engl J Med 2013 369 1569 1570 24143816
[104]Rajagopalan P Hibar DP Thompson PM TREM2 and neurodegenerative disease. N Engl J Med 2013 369 1565 1567 24131186 PMC4024453

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Howard, R., Zubko, O., Bradley, R., Harper, E., Pank, L., O’Brien, J., Fox, C., Tabet, N., Livingston, G., Bentham, P., et al. (2020) · JAMA Neurology · doi:10.1001/jamaneurol.2019.3762 · Cited by 194 · see citing works
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Lall, D., & Baloh, R. H. (2017) · Journal of Clinical Investigation · doi:10.1172/jci90607 · Cited by 175 · see citing works
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Self-citation
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Hung, C. O. Y., & Livesey, F. J. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.11.095 · Cited by 159 · see citing works
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Herbert, J., & Lucassen, P. J. (2016) · Frontiers in Neuroendocrinology · doi:10.1016/j.yfrne.2015.12.001 · Cited by 150 · see citing works
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McKenzie, A. T., Moyon, S., Wang, M., Katsyv, I., Song, W.-M., Zhou, X., Dammer, E. B., Duong, D. M., Aaker, J., Zhao, Y., et al. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0219-3 · Cited by 154 · see citing works
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Walker, K. A., Chen, J., Shi, L., Yang, Y., Fornage, M., Zhou, L., Schlosser, P., Surapaneni, A., Grams, M. E., Duggan, M. R., et al. (2023) · Science Translational Medicine · doi:10.1126/scitranslmed.adf5681 · Cited by 148 · see citing works
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Arber, C., Lovejoy, C., & Wray, S. (2017) · Alzheimer's Research & Therapy · doi:10.1186/s13195-017-0268-4 · Cited by 143 · see citing works
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Steiner, H., Fukumori, A., Tagami, S., & Okochi, M. (2018) · Cell Stress · doi:10.15698/cst2018.11.162 · Cited by 133 · see citing works
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Baligács, N., Albertini, G., Borrie, S. C., Serneels, L., Pridans, C., Balusu, S., & De Strooper, B. (2024) · Nature Communications · doi:10.1038/s41467-024-54779-w · Cited by 123 · see citing works
Systems-based proteomics to resolve the biology of Alzheimer’s disease beyond amyloid and tau
Rayaprolu, S., Higginbotham, L., Bagchi, P., Watson, C. M., Zhang, T., Levey, A. I., Rangaraju, S., & Seyfried, N. T. (2021) · Neuropsychopharmacology · doi:10.1038/s41386-020-00840-3 · Cited by 118 · see citing works
CX3CR1 deficiency aggravates amyloid driven neuronal pathology and cognitive decline in Alzheimer’s disease
Puntambekar, S. S., Moutinho, M., Lin, P. B.-C., Jadhav, V., Tumbleson-Brink, D., Balaji, A., Benito, M. A., Xu, G., Oblak, A., Lasagna-Reeves, C. A., et al. (2022) · Molecular Neurodegeneration · doi:10.1186/s13024-022-00545-9 · Cited by 113 · see citing works
The BIN1 rs744373 SNP is associated with increased tau-PET levels and impaired memory
Franzmeier, N., Rubinski, A., Neitzel, J., Ewers, M., (ADNI), T. A. D. N. I., Weiner, M. W., Aisen, P., Petersen, R., Jack, C. R., Jagust, W., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-09564-5 · Cited by 109 · see citing works
Early intraneuronal amyloid triggers neuron-derived inflammatory signaling in APP transgenic rats and human brain
Welikovitch, L. A., Do Carmo, S., Maglóczky, Z., Malcolm, J. C., Lőke, J., Klein, W. L., Freund, T., & Cuello, A. C. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1914593117 · Cited by 116 · see citing works
Chronic cerebral hypoperfusion enhances Tau hyperphosphorylation and reduces autophagy in Alzheimer’s disease mice
Qiu, L., Ng, G., Tan, E. K., Liao, P., Kandiah, N., & Zeng, L. (2016) · Scientific Reports · doi:10.1038/srep23964 · Cited by 115 · see citing works
APOE genotype and sex affect microglial interactions with plaques in Alzheimer’s disease mice
Stephen, T. L., Cacciottolo, M., Balu, D., Morgan, T. E., LaDu, M. J., Finch, C. E., & Pike, C. J. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0729-z · Cited by 115 · see citing works
TREM2 ectodomain and its soluble form in Alzheimer’s disease
Yang, J., Fu, Z., Zhang, X., Xiong, M., Meng, L., & Zhang, Z. (2020) · Journal of Neuroinflammation · doi:10.1186/s12974-020-01878-2 · Cited by 113 · see citing works
PICALM and Alzheimer’s Disease: An Update and Perspectives
Ando, K., Nagaraj, S., Küçükali, F., de Fisenne, M.-A., Kosa, A.-C., Doeraene, E., Lopez Gutierrez, L., Brion, J.-P., & Leroy, K. (2022) · Cells · doi:10.3390/cells11243994 · Cited by 104 · see citing works
Linkage, whole genome sequence, and biological data implicate variants in RAB10 in Alzheimer’s disease resilience
Initiative, F. T. A. D. N., Ridge, P. G., Karch, C. M., Hsu, S., Arano, I., Teerlink, C. C., Ebbert, M. T. W., Gonzalez Murcia, J. D., Farnham, J. M., Damato, A. R., et al. (2017) · Genome Medicine · doi:10.1186/s13073-017-0486-1 · Cited by 83 · see citing works
Self-citation
Fine-mapping of the human leukocyte antigen locus as a risk factor for Alzheimer disease: A case–control study
Steele, N. Z. R., Carr, J. S., Bonham, L. W., Geier, E. G., Damotte, V., Miller, Z. A., Desikan, R. S., Boehme, K. L., Mukherjee, S., Crane, P. K., et al. (2017) · PLOS Medicine · doi:10.1371/journal.pmed.1002272 · Cited by 91 · see citing works
PLCG2 is associated with the inflammatory response and is induced by amyloid plaques in Alzheimer’s disease
Tsai, A. P., Dong, C., Lin, P. B.-C., Messenger, E. J., Casali, B. T., Moutinho, M., Liu, Y., Oblak, A. L., Lamb, B. T., Landreth, G. E., et al. (2022) · Genome Medicine · doi:10.1186/s13073-022-01022-0 · Cited by 92 · see citing works
Genome-wide RNAseq study of the molecular mechanisms underlying microglia activation in response to pathological tau perturbation in the rTg4510 tau transgenic animal model
Wang, H., Li, Y., Ryder, J. W., Hole, J. T., Ebert, P. J., Airey, D. C., Qian, H.-R., Logsdon, B., Fisher, A., Ahmed, Z., et al. (2018) · Molecular Neurodegeneration · doi:10.1186/s13024-018-0296-y · Cited by 83 · see citing works
Prevalence of the apolipoprotein E ε4 allele in amyloid β positive subjects across the spectrum of Alzheimer's disease
Mattsson, N., Groot, C., Jansen, W. J., Landau, S. M., Villemagne, V. L., Engelborghs, S., Mintun, M. M., Lleo, A., Molinuevo, J. L., Jagust, W. J., et al. (2018) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2018.02.009 · Cited by 88 · see citing works
Dendritic Spines: Mediators of Cognitive Resilience in Aging and Alzheimer’s Disease
Walker, C. K., & Herskowitz, J. H. (2021) · The Neuroscientist · doi:10.1177/1073858420945964 · Cited by 86 · see citing works
The Transcriptional Landscape of Microglial Genes in Aging and Neurodegenerative Disease
Bonham, L. W., Sirkis, D. W., & Yokoyama, J. S. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.01170 · Cited by 83 · see citing works
Identification of Conserved Proteomic Networks in Neurodegenerative Dementia
Swarup, V., Chang, T. S., Duong, D. M., Dammer, E. B., Dai, J., Lah, J. J., Johnson, E. C. B., Seyfried, N. T., Levey, A. I., & Geschwind, D. H. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.107807 · Cited by 78 · see citing works
Identification of conserved proteomic networks in neurodegenerative dementia
Swarup, V., Chang, T. S., Duong, D. M., Dammer, E. B., Lah, J. J., Johnson, E. E. C. B., Seyfried, N. T., Levey, A. I., & Geschwind, D. H. (2019) · doi:10.1101/825802 · Cited by 78 · see citing works
A novel role for the late-onset Alzheimer’s disease (LOAD)-associated protein Bin1 in regulating postsynaptic trafficking and glutamatergic signaling
Schürmann, B., Bermingham, D. P., Kopeikina, K. J., Myczek, K., Yoon, S., Horan, K. E., Kelly, C. J., Martin-de-Saavedra, M. D., Forrest, M. P., Fawcett-Patel, J. M., et al. (2020) · Molecular Psychiatry · doi:10.1038/s41380-019-0407-3 · Cited by 72 · see citing works
Astrocyte-secreted glypican-4 drives APOE4-dependent tau hyperphosphorylation
Saroja, S. R., Gorbachev, K., Julia, T., Goate, A. M., & Pereira, A. C. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2108870119 · Cited by 75 · see citing works
Self-citation
Differential default mode network trajectories in asymptomatic individuals at risk for Alzheimer’s disease
Chiesa, P. A., Cavedo, E., Vergallo, A., Lista, S., Potier, M., Habert, M., Dubois, B., Thiebaut de Schotten, M., Hampel, H., and the INSIGHT‐preAD study group, et al. (2019) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2019.03.006 · Cited by 66 · see citing works
Microglia: Friend and foe in tauopathy
Odfalk, K. F., Bieniek, K. F., & Hopp, S. C. (2022) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2022.102306 · Cited by 60 · see citing works
The contribution of altered neuronal autophagy to neurodegeneration
Filippone, A., Esposito, E., Mannino, D., Lyssenko, N., & Praticò, D. (2022) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2022.108178 · Cited by 55 · see citing works
A multifactorial model of pathology for age of onset heterogeneity in familial Alzheimer’s disease
Sepulveda-Falla, D., Chavez-Gutierrez, L., Portelius, E., Vélez, J. I., Dujardin, S., Barrera-Ocampo, A., Dinkel, F., Hagel, C., Puig, B., Mastronardi, C., et al. (2021) · Acta Neuropathologica · doi:10.1007/s00401-020-02249-0 · Cited by 54 · see citing works
Functional genomics and the future of iPSCs in disease modeling
Brooks, I. R., Garrone, C. M., Kerins, C., Kiar, C. S., Syntaka, S., Xu, J. Z., Spagnoli, F. M., & Watt, F. M. (2022) · Stem Cell Reports · doi:10.1016/j.stemcr.2022.03.019 · Cited by 54 · see citing works
INPP5D deficiency attenuates amyloid pathology in a mouse model of Alzheimer's disease
Lin, P. B., Tsai, A. P., Soni, D., Lee‐Gosselin, A., Moutinho, M., Puntambekar, S. S., Landreth, G. E., Lamb, B. T., & Oblak, A. L. (2023) · Alzheimer's & Dementia · doi:10.1002/alz.12849 · Cited by 54 · see citing works
The P522R protective variant of PLCG2 promotes the expression of antigen presentation genes by human microglia in an Alzheimer's disease mouse model
Claes, C., England, W. E., Danhash, E. P., Kiani Shabestari, S., Jairaman, A., Chadarevian, J. P., Hasselmann, J., Tsai, A. P., Coburn, M. A., Sanchez, J., et al. (2022) · Alzheimer's & Dementia · doi:10.1002/alz.12577 · Cited by 52 · see citing works
A human brain vascular atlas reveals diverse cell mediators of Alzheimer’s disease risk
Yang, A. C., Vest, R. T., Kern, F., Lee, D. P., Maat, C. A., Losada, P. M., Chen, M. B., Agam, M., Schaum, N., Khoury, N., et al. (2021) · doi:10.1101/2021.04.26.441262 · Cited by 48 · see citing works
Cytosolic calcium: Judge, jury and executioner of neurodegeneration in Alzheimer's disease and beyond
Webber, E. K., Fivaz, M., Stutzmann, G. E., & Griffioen, G. (2023) · Alzheimer's & Dementia · doi:10.1002/alz.13065 · Cited by 50 · see citing works
Sex-Specific Cross Tissue Meta-Analysis Identifies Immune Dysregulation in Women With Alzheimer’s Disease
Paranjpe, M. D., Belonwu, S., Wang, J. K., Oskotsky, T., Gupta, A., Taubes, A., Zalocusky, K. A., Paranjpe, I., Glicksberg, B. S., Huang, Y., et al. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.735611 · Cited by 49 · see citing works
Current Anti-Amyloid-β Therapy for Alzheimer’s Disease Treatment: From Clinical Research to Nanomedicine
Zhao, Z., Liu, Y., Ruan, S., & Hu, Y. (2023) · International Journal of Nanomedicine · doi:10.2147/ijn.s444115 · Cited by 49 · see citing works
TREM2 splice isoforms generate soluble TREM2 species that disrupt long-term potentiation
Moutinho, M., Coronel, I., Tsai, A. P., Di Prisco, G. V., Pennington, T., Atwood, B. K., Puntambekar, S. S., Smith, D. C., Martinez, P., Han, S., et al. (2023) · Genome Medicine · doi:10.1186/s13073-023-01160-z · Cited by 42 · see citing works
“The triggering receptor expressed in myeloid cell 2 (TREM2) is among these immune genes, as its genetic variants, such as R47H or H157Y, confer a significantly increased risk of LOAD [5–8].”
Background
Gene Therapy Strategies for Alzheimer's Disease: An Overview
Alves, S., Fol, R., & Cartier, N. (2016) · Human Gene Therapy · doi:10.1089/hum.2016.017 · Cited by 45 · see citing works
Neuroprotective Roles of the Reverse Transsulfuration Pathway in Alzheimer’s Disease
Paul, B. D. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.659402 · Cited by 42 · see citing works
β‐Glucan attenuates cognitive impairment of <scp>APP</scp>/<scp>PS1</scp> mice via regulating intestinal flora and its metabolites
Zhang, Q., Zhao, W., Hou, Y., Song, X., Yu, H., Tan, J., Zhou, Y., & Zhang, H. (2023) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.14132 · Cited by 40 · see citing works
COVID-19 as a Risk Factor for Alzheimer’s Disease
Golzari-Sorkheh, M., Weaver, D. F., & Reed, M. A. (2023) · Journal of Alzheimer's Disease · doi:10.3233/jad-220800 · Cited by 39 · see citing works
Identification of novel diagnostic panel for mild cognitive impairment and Alzheimer’s disease: findings based on urine proteomics and machine learning
Wang, Y., Sun, Y., Wang, Y., Jia, S., Qiao, Y., Zhou, Z., Shao, W., Zhang, X., Guo, J., Zhang, B., et al. (2023) · Alzheimer's Research & Therapy · doi:10.1186/s13195-023-01324-4 · Cited by 34 · see citing works
“Besides, PLD3 was suggested to be the gene that increases AD risk [45–47] and was downregulated in AD brains which might participate in AD pathogenesis through amyloid precursor protein (APP) processing [48, 49].”
Background
Microglial cGAS Deletion Preserves Intercellular Communication and Alleviates Amyloid‐β‐Induced Pathogenesis of Alzheimer's Disease
He, S., Li, X., Mittra, N., Bhattacharjee, A., Wang, H., Song, S., Zhao, S., Liu, F., & Han, X. (2025) · Advanced Science · doi:10.1002/advs.202410910 · Cited by 34 · see citing works
Current therapeutics for Alzheimer’s disease and clinical trials
Xiao, D., & Zhang, C. (2024) · Exploration of Neuroscience · doi:10.37349/en.2024.00048 · Cited by 30 · see citing works
Insulin‐like growth factor‐2 is a promising candidate for the treatment and prevention of Alzheimer's disease
Fitzgerald, G. S., Chuchta, T. G., & McNay, E. C. (2023) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.14160 · Cited by 22 · see citing works
Protective ApoE variants support neuronal function by effluxing oxidized phospholipids
Ralhan, I., Do, A. D., Bae, J.-Y., Feringa, F. M., Cai, W., Chang, J., Chik, K., Lee, N. Y. J., Gerry, C. J., van der Kant, R., et al. (2026) · Neuron · doi:10.1016/j.neuron.2025.10.040 · Cited by 23 · see citing works
Microbial infection promotes amyloid pathology in a mouse model of Alzheimer’s disease via modulating γ-secretase
Zhao, M., Ma, G., Yan, X., Li, X., Wang, E., Xu, X.-X., Zhao, J.-B., Ma, X., & Zeng, J. (2024) · Molecular Psychiatry · doi:10.1038/s41380-024-02428-5 · Cited by 21 · see citing works
A microglia clonal inflammatory disorder in Alzheimer’s disease
Vicario, R., Fragkogianni, S., Weber, L., Lazarov, T., Hu, Y., Hayashi, S. Y., Craddock, B., Socci, N. D., Alberdi, A., Baako, A., et al. (2025) · eLife · doi:10.7554/elife.96519.3 · Cited by 21 · see citing works
Quantitative genetics validates previous genetic variants and identifies novel genetic players influencing Alzheimer’s disease cerebrospinal fluid biomarkers
Ramos de Matos, M., Ferreira, C., Herukka, S.-K., Soininen, H., Janeiro, A., Santana, I., Baldeiras, I., Almeida, M. R., Lleó, A., Dols-Icardo, O., et al. (2018) · Journal of Alzheimer's Disease · doi:10.3233/jad-180512 · Cited by 18 · see citing works

Lessons and implications from association studies and post-GWAS analyses of cervical cancer
Chen, D., & Gyllensten, U. B. (2014) · Trends in Genetics · doi:10.1016/j.tig.2014.10.005 · Cited by 53 · see citing works
Gene and Pathway-Based Analysis: Second Wave of Genome-wide Association Studies
Peng, G., Luo, L., Siu, H., Zhu, Y., Hu, P., Hong, S., Zhao, J., Zhou, X., Reveille, J. D., Li, J., et al. (2008) · European Journal of Human Genetics · doi:10.1038/ejhg.2009.115 · Cited by 236 · see citing works
Genome-wide association studies in aging-related processes such as diabetes mellitus, atherosclerosis and cancer
Kronenberg, F. (2007) · Experimental Gerontology · doi:10.1016/j.exger.2007.09.005 · Cited by 44 · see citing works
GWAS summary-based pathway analysis correcting for the genetic confounding impact of environmental exposures
Fan, Q., Zhang, F., Wang, W., Xu, J., Hao, J., He, A., Wen, Y. F., Li, P., Liang, X., Du, Y., et al. (2017) · Briefings in Bioinformatics · doi:10.1093/bib/bbx025 · Cited by 4 · see citing works
Progress of genome‐wide association studies of ankylosing spondylitis
Li, Z., & Brown, M. A. (2017) · Clinical & Translational Immunology · doi:10.1038/cti.2017.49 · Cited by 53 · see citing works

Authors: Karch, C. M., & Goate, A. M.
Affiliations: Washington University in St. Louis (US)
Corresponding author: Goate, Alison M.
ORCID: Karch, Celeste M.
Goate, Alison M.
Venue: Biological Psychiatry
Publisher: Elsevier BV
Published: 2015-01
Volume: 77
Issue: 1
Pages: 43-51
ISSN: 0006-3223 (ISSN-L)
DOI: 10.1016/j.biopsych.2014.05.006
PMC: PMC4234692
OpenAlex: W1999794509
Cited by: 1,357
References: 149
Citations by year: 2026: 80 · 2025: 136 · 2024: 130 · 2023: 132 · 2022: 151 · 2021: 153 · 2020: 146 · 2019: 117 · 2018: 94 · 2017: 94 · 2016: 74 · 2015: 44 · 2014: 5
FWCI: 8.50
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Biological Psychiatry (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: Wellcome Trust (503147, G0801418)
National Institute on Aging (K01AG046374, R01AG035083, P50AG005681, U01AG032438)
Topics: Health Sciences › Medicine › Physiology › 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: Alzheimer's disease, late-onset Alzheimer's disease, genetic risk factors, susceptibility genes, Alzheimer's disease pathogenesis, single nucleotide polymorphisms, ABCA7, BIN1, SORL1, TREM2, PLD3, CD33, PICALM, clusterin, neuropathology, therapeutic target
MeSH terms: Alzheimer Disease, Cholesterol, Endocytosis, Humans, Phenotype, Risk Factors, Amyloid beta-Protein Precursor, Genetic Predisposition to Disease, Presenilin-1, Presenilin-2, Genome-Wide Association Study

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Alzheimer’s Disease Risk Genes and Mechanisms of Disease Pathogenesis

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