A split-luciferase complementation, real-time reporting assay enables monitoring of the disease-associated transmembrane protein TREM2 in live cells

<i>TREM2</i> 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

Variant of <i>TREM2</i> 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

TREM2 Lipid Sensing Sustains the Microglial Response in an Alzheimer’s Disease Model

Wang, Y., Cella, M., Mallinson, K., Ulrich, J. D., Young, K. L., Robinette, M. L., Gilfillan, S., Krishnan, G. M., Sudhakar, S., Zinselmeyer, B. H., et al. (2015) · Cell · doi:10.1016/j.cell.2015.01.049 · Cited by 1,736 · see citing works

Identification of a factor that links apoptotic cells to phagocytes

Hanayama, R., Tanaka, M., Miwa, K., Shinohara, A., Iwamatsu, A., & Nagata, S. (2002) · Nature · doi:10.1038/417182a · Cited by 1,401 · see citing works

Clearance of apoptotic neurons without inflammation by microglial triggering receptor expressed on myeloid cells-2

Takahashi, K., Rochford, C. D. P., & Neumann, H. (2005) · The Journal of Experimental Medicine · doi:10.1084/jem.20041611 · Cited by 1,124 · see citing works

TREM2 Binds to Apolipoproteins, Including APOE and CLU/APOJ, and Thereby Facilitates Uptake of Amyloid-Beta by Microglia

Yeh, F. L., Wang, Y., Tom, I., Gonzalez, L. C., & Sheng, M. (2016) · Neuron · doi:10.1016/j.neuron.2016.06.015 · Cited by 943 · see citing works

TREM2 Haplodeficiency in Mice and Humans Impairs the Microglia Barrier Function Leading to Decreased Amyloid Compaction and Severe Axonal Dystrophy

Yuan, P., Condello, C., Keene, C. D., Wang, Y., Bird, T. D., Paul, S. M., Luo, W., Colonna, M., Baddeley, D., & Grutzendler, J. (2016) · Neuron · doi:10.1016/j.neuron.2016.05.003 · Cited by 817 · see citing works

TREM2 mutations implicated in neurodegeneration impair cell surface transport and phagocytosis

Kleinberger, G., Yamanishi, Y., Suárez-Calvet, M., Czirr, E., Lohmann, E., Cuyvers, E., Struyfs, H., Pettkus, N., Wenninger-Weinzierl, A., Mazaheri, F., et al. (2014) · Science Translational Medicine · doi:10.1126/scitranslmed.3009093 · Cited by 798 · 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

Cutting Edge: TREM-2 Attenuates Macrophage Activation

Turnbull, I. R., Gilfillan, S., Cella, M., Aoshi, T., Miller, M., Piccio, L., Hernandez, M., & Colonna, M. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.6.3520 · Cited by 688 · 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

TREM2 deficiency eliminates TREM2+ inflammatory macrophages and ameliorates pathology in Alzheimer’s disease mouse models

Jay, T. R., Miller, C. M., Cheng, P. J., Graham, L. C., Bemiller, S., Broihier, M. L., Xu, G., Margevicius, D., Karlo, J. C., Sousa, G. L., et al. (2015) · Journal of Experimental Medicine · doi:10.1084/jem.20142322 · Cited by 682 · cited 3× · see citing works

Apolipoprotein E Is a Ligand for Triggering Receptor Expressed on Myeloid Cells 2 (TREM2)

Atagi, Y., Liu, C.-C., Painter, M. M., Chen, X.-F., Verbeeck, C., Zheng, H., Li, X., Rademakers, R., Kang, S. S., Xu, H., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.679043 · Cited by 587 · see citing works

The TREM receptor family and signal integration

Klesney‐Tait, J., Turnbull, I. R., & Colonna, M. (2006) · Nature Immunology · doi:10.1038/ni1411 · Cited by 586 · see citing works

A role for TREM2 ligands in the phagocytosis of apoptotic neuronal cells by microglia

Hsieh, C. L., Koike, M., Spusta, S. C., Niemi, E. C., Yenari, M., Nakamura, M. C., & Seaman, W. E. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06042.x · Cited by 475 · see citing works

A DAP12-mediated pathway regulates expression of CC chemokine receptor 7 and maturation of human dendritic cells

Bouchon, A., Hernández-Munain, C., Cella, M., & Colonna, M. (2001) · The Journal of Experimental Medicine · doi:10.1084/jem.194.8.1111 · Cited by 460 · see citing works

Cutting Edge: Inhibition of TLR and FcR Responses in Macrophages by Triggering Receptor Expressed on Myeloid Cells (TREM)-2 and DAP12

Hamerman, J. A., Jarjoura, J. R., Humphrey, M. B., Nakamura, M. C., Seaman, W. E., & Lanier, L. L. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.4.2051 · Cited by 440 · see citing works

TREM2-Transduced Myeloid Precursors Mediate Nervous Tissue Debris Clearance and Facilitate Recovery in an Animal Model of Multiple Sclerosis

Takahashi, K., Prinz, M., Stagi, M., Chechneva, O., & Neumann, H. (2007) · PLoS Medicine · doi:10.1371/journal.pmed.0040124 · Cited by 414 · see citing works

TREM2- and DAP12-dependent activation of PI3K requires DAP10 and is inhibited by SHIP1

Peng, Q., Malhotra, S., Torchia, J. A., Kerr, W. G., Coggeshall, K. M., & Humphrey, M. B. (2010) · Science Signaling · doi:10.1126/scisignal.2000500 · Cited by 413 · 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

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 · see citing works

Role of the cytoskeleton during leukocyte responses

Vicente‐Manzanares, M., & Sánchez‐Madrid, F. (2004) · Nature reviews. Immunology · doi:10.1038/nri1268 · Cited by 360 · see citing works

Heterogeneous expression of the triggering receptor expressed on myeloid cells‐2 on adult murine microglia

Schmid, C. D., Sautkulis, L. N., Danielson, P. E., Cooper, J., Hasel, K. W., Hilbush, B. S., Sutcliffe, J. G., & Carson, M. J. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.01243.x · Cited by 351 · see citing works

TAM receptors, Gas6, and protein S: roles in inflammation and hemostasis

van der Meer, J. H. M., van der Poll, T., & Veer, C. V. ′. (2014) · Blood · doi:10.1182/blood-2013-09-528752 · Cited by 341 · see citing works

Cerebrospinal fluid soluble TREM2 is higher in Alzheimer disease and associated with mutation status

Piccio, L., Deming, Y., Del-Águila, J. L., Ghezzi, L., Holtzman, D. M., Fagan, A. M., Fenoglio, C., Galimberti, D., Borroni, B., & Cruchaga, C. (2016) · Acta Neuropathologica · doi:10.1007/s00401-016-1533-5 · Cited by 337 · see citing works

Upregulation of TREM2 Ameliorates Neuropathology and Rescues Spatial Cognitive Impairment in a Transgenic Mouse Model of Alzheimer’s Disease

Jiang, T., Tan, L., Zhu, X.-C., Zhang, Q.-Q., Cao, L., Tan, M.-S., Gu, L.-Z., Wang, H.-F., Ding, Z.-Z., Zhang, Y.-D., et al. (2014) · Neuropsychopharmacology · doi:10.1038/npp.2014.164 · Cited by 320 · see citing works

Monitoring Protein−Protein Interactions Using Split Synthetic Renilla Luciferase Protein-Fragment-Assisted Complementation

Paulmurugan, R., & Gambhir, S. S. (2003) · Analytical Chemistry · doi:10.1021/ac020731c · Cited by 318 · see citing works

Enhanced Toll-like receptor responses in the absence of signaling adaptor DAP12

Hamerman, J. A., Tchao, N. K., Lowell, C. A., & Lanier, L. L. (2005) · Nature Immunology · doi:10.1038/ni1204 · Cited by 318 · see citing works

Increased cerebrospinal fluid soluble TREM2 concentration in Alzheimer’s disease

Heslegrave, A., Heywood, W., Paterson, R., Magdalinou, N., Svensson, J., Johansson, P., Öhrfelt, A., Blennow, K., Hardy, J., Schott, J., et al. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0071-x · Cited by 303 · see citing works

Alzheimer's disease‐associated TREM2 variants exhibit either decreased or increased ligand‐dependent activation

Song, W., Hooli, B., Mullin, K., Jin, S. C., Cella, M., Ulland, T. K., Wang, Y., Tanzi, R. E., & Colonna, M. (2017) · Alzheimer's &amp; Dementia · doi:10.1016/j.jalz.2016.07.004 · Cited by 297 · see citing works

Differential TAM receptor–ligand–phospholipid interactions delimit differential TAM bioactivities

Lew, E. D., Oh, J., Burrola, P., Lax, I., Zagórska, A., Través, P. G., Schlessinger, J., & Lemke, G. (2014) · eLife · doi:10.7554/elife.03385 · Cited by 271 · see citing works

<i>TREM2</i>Variant 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

TREM2 is upregulated in amyloid plaque-associated microglia in aged APP23 transgenic mice

Frank, S., Burbach, G. J., Bonin, M., Walter, M., Streit, W., Bechmann, I., & Deller, T. (2008) · Glia · doi:10.1002/glia.20710 · Cited by 247 · see citing works

TREM-2 (triggering receptor expressed on myeloid cells 2) is a phagocytic receptor for bacteria

N’Diaye, E.-N., Branda, C., Branda, S. S., Nevarez, L., Colonna, M., Lowell, C. A., Hamerman, J. A., & Seaman, W. E. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200808080 · Cited by 242 · see citing works

Receptor Tyrosine Kinases, TYRO3, AXL, and MER, Demonstrate Distinct Patterns and Complex Regulation of Ligand-induced Activation

Tsou, W., Nguyen, K.-Q. N., Calarese, D. A., Garforth, S., Lewis-Antes, A., Sv, S., Almo, S. C., Birge, R. B., & Kotenko, S. V. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.569020 · Cited by 237 · see citing works

Purification and properties of Renilla reniformis luciferase

Matthews, J. C., Hori, K., & Cormier, M. J. (1977) · Biochemistry · doi:10.1021/bi00620a014 · Cited by 224 · see citing works

Investigating the role of rare heterozygous TREM2 variants in Alzheimer's disease and frontotemporal dementia.

Cuyvers, E., Bettens, K., Philtjens, S., Langenhove, T. V., Gijselinck, I., van der Zee, J., Engelborghs, S., Vandenbulcke, M., Dongen, J. V., Geerts, N., et al. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.09.009 · Cited by 191 · see citing works

Heterozygous TREM2 mutations in frontotemporal dementia

Borroni, B., Ferrari, F., Galimberti, D., Nacmias, B., Barone, C., Bagnoli, S., Fenoglio, C., Piaceri, I., Archetti, S., Bonvicini, C., et al. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.09.017 · Cited by 173 · see citing works

Distribution and signaling of TREM2/DAP12, the receptor system mutated in human polycystic lipomembraneous osteodysplasia with sclerosing leukoencephalopathy dementia

Sessa, G., Podini, P., Mariani, M., Meroni, A., Spreafico, R., Sinigaglia, F., Colonna, M., Panina, P., & Meldolesi, J. (2004) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2004.03729.x · Cited by 165 · see citing works

MFG-E8 Regulates Microglial Phagocytosis of Apoptotic Neurons

Fuller, A. D., & Eldik, L. J. V. (2008) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-008-9118-2 · Cited by 155 · see citing works

TECHNICAL ADVANCE: Split luciferase complementation assay to study protein–protein interactions in Arabidopsis protoplasts

Fujikawa, Y., & Kato, N. (2007) · The Plant Journal · doi:10.1111/j.1365-313x.2007.03214.x · Cited by 152 · see citing works

Nasu–Hakola Disease (Polycystic Lipomembranous Osteodysplasia with Sclerosing Leukoencephalopathy—PLOSL): A Dementia Associated with Bone Cystic Lesions. From Clinical to Genetic and Molecular Aspects

Bianchin, M., Capella, H., Chaves, D. L., Steindel, M., Grisard, E., Ganev, G. G., da Silva, J. P., Schaeffer, E., Poffo, M. A., Walz, R., et al. (2004) · Cellular and molecular neurobiology · doi:10.1023/b:cemn.0000012721.08168.ee · Cited by 147 · see citing works

Mechanisms of neurofibrillary degeneration and the formation of neurofibrillary tangles

Iqbal, K., Alonso, A. D. C., Gong, C., Khatoon, S., Pei, J. ‐., Wang, J. Z., & Grundke, I. (1998) · Journal of neural transmission. Supplementum · doi:10.1007/978-3-7091-6467-9_15 · Cited by 140 · see citing works

Dual Induction of TREM2 and Tolerance-Related Transcript, Tmem176b, in Amyloid Transgenic Mice: Implications for Vaccine-Based Therapies for Alzheimer’s Disease

Melchior, B., Garcia, A., Hsiung, B., Lo, K. M., Doose, J. M., Thrash, J. C., Stalder, A. K., Staufenbiel, M., Neumann, H., & Carson, M. J. (2010) · ASN NEURO · doi:10.1042/an20100010 · Cited by 133 · see citing works

DAP12 stabilizes the C-terminal fragment of the triggering receptor expressed on myeloid cells-2 (TREM2) and protects against LPS-induced pro-inflammatory response

Zhong, L., Chen, X.-F., Zhang, Z.-L., Wang, Z., Shi, X.-Z., Xu, K., Zhang, Y.-W., Xu, H., & Bu, G. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.645986 · Cited by 133 · see citing works

Heterogeneity of presenile dementia with bone cysts (Nasu–Hakola disease)

Kondo, T., Takahashi, K., Kohara, N., Takahashi, Y., Hayashi, S., Takahashi, H., Matsuo, H., Yamazaki, M., Inoue, K., Miyamoto, K., et al. (2002) · Neurology · doi:10.1212/wnl.59.7.1105 · Cited by 106 · see citing works

A signal-switch hypothesis for cross-regulation of cytokine and TLR signalling pathways

Ivashkiv, L. B. (2008) · Nature reviews. Immunology · doi:10.1038/nri2396 · Cited by 80 · see citing works

Essential Role of MFG-E8 for Phagocytic Properties of Microglial Cells

Liu, Y., Yang, X., Guo, C., Nie, P., Liu, Y., & Ma, J. (2013) · PLoS ONE · doi:10.1371/journal.pone.0055754 · Cited by 40 · see citing works

Mechanisms of Function of Tapasin, a Critical Major Histocompatibility Complex Class I Assembly Factor

Rizvi, S. M., & Raghavan, M. (2009) · Traffic · doi:10.1111/j.1600-0854.2009.01025.x · Cited by 37 · see citing works

Application of a split luciferase complementation assay for the detection of viral protein–protein interactions

Deng, Q., Wang, D., Xiang, X., Gao, X., Hardwidge, P. R., Kaushik, R. S., Wolff, T., Chakravarty, S., & Li, F. (2011) · Journal of Virological Methods · doi:10.1016/j.jviromet.2011.04.028 · Cited by 25 · see citing works

[Pustular psoriasis (Zumbusch) treated with 8-methoxypsoralen phototherapy (author's transl)].

Mizuno, N., Uematsu, S., & Ono, M. (1975) · PubMed · Cited by 2 · see citing works

Untitled work

Daws (2001) · doi:10.1002/1521-4141(200103)31:3

TREM2 in Neurodegenerative Diseases

Jay, T. R., von Saucken, V. E., & Landreth, G. E. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0197-5 · Cited by 427 · see citing works

Gene expression and functional deficits underlie TREM2-knockout microglia responses in human models of Alzheimer’s disease

McQuade, A., Kang, Y. J., Hasselmann, J., Jairaman, A., Sotelo, A., Coburn, M., Shabestari, S. K., Chadarevian, J. P., Fote, G., Tu, C. H., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-19227-5 · Cited by 361 · see citing works

Plaque-associated human microglia accumulate lipid droplets in a chimeric model of Alzheimer’s disease

Claes, C., Danhash, E. P., Hasselmann, J., Chadarevian, J. P., Shabestari, S. K., England, W. E., Lim, T. E., Hidalgo, J. L. S., Spitale, R. C., Davtyan, H., et al. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00473-0 · Cited by 197 · see citing works

Metabolons, enzyme–enzyme assemblies that mediate substrate channeling, and their roles in plant metabolism

Zhang, Y., & Fernie, A. R. (2020) · Plant Communications · doi:10.1016/j.xplc.2020.100081 · Cited by 163 · see citing works

Alzheimer's Disease: The Role of Microglia in Brain Homeostasis and Proteopathy

Clayton, K. A., Enoo, A. A. V., & Ikezu, T. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00680 · Cited by 132 · see citing works

Distinct Signaling Pathways Regulate TREM2 Phagocytic and NFκB Antagonistic Activities

Yao, H., Coppola, K., Schweig, J. E., Crawford, F., Mullan, M., & Paris, D. (2019) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00457 · Cited by 110 · see citing works

Human stem cell–derived monocytes and microglia‐like cells reveal impaired amyloid plaque clearance upon heterozygous or homozygous loss of TREM2

Claes, C., Daele, J. V. D., Boon, R., Schouteden, S., Colombo, A. V., Monasor, L. S., Fiers, M. W. E. J., Ordovás, L., Nami, F., Bohrmann, B., et al. (2018) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2018.09.006 · Cited by 81 · see citing works

Triggering receptor expressed on myeloid cells 2 (TREM2): a potential therapeutic target for Alzheimer disease?

Deming, Y. K., Li, Z., Benítez, B. A., & Cruchaga, C. (2018) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2018.1486823 · Cited by 48 · see citing works

Coelenterazine-Dependent Luciferases as a Powerful Analytical Tool for Research and Biomedical Applications

Krasitskaya, V. V., Bashmakova, E. E., & Frank, L. A. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21207465 · Cited by 42 · see citing works

PLCγ2 regulates TREM2 signalling and integrin-mediated adhesion and migration of human iPSC-derived macrophages

Obst, J., Hall-Roberts, H. L., Smith, T. B., Kreuzer, M., Magno, L., Di Daniel, E., Davis, J. B., & Mead, E. (2021) · Scientific Reports · doi:10.1038/s41598-021-96144-7 · Cited by 36 · see citing works

Reduced TREM2 activation in microglia of patients with Alzheimer's disease

Okuzono, Y., Sakuma, H., Miyakawa, S., Ifuku, M., Lee, J. H., Das, D., Banerjee, A., Zhao, Y., Yamamoto, K., Ando, T., et al. (2021) · FEBS Open Bio · doi:10.1002/2211-5463.13300 · Cited by 31 · see citing works

Roles of TREM2 in Alzheimer’s disease

Qi, X., Zhu, K., Ke, W., Wang, J., Mao, S., & Chen, G. (2025) · Translational Neurodegeneration · doi:10.1186/s40035-025-00515-3 · Cited by 36 · see citing works

Stable and Temporary Enzyme Complexes and Metabolons Involved in Energy and Redox Metabolism

Zhang, Y., & Fernie, A. R. (2020) · Antioxidants and Redox Signaling · doi:10.1089/ars.2019.7981 · Cited by 20 · see citing works

MEK1/2 activity modulates TREM2 cell surface recruitment

Schapansky, J., Grinberg, Y. Y., Osiecki, D. M., Freeman, E. A., Walker, S. G., Karran, E. H., Gopalakrishnan, S. M., & Talanian, R. V. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.014352 · Cited by 14 · see citing works

Selenoprotein P is a target for regulating extracellular vesicle biogenesis and secretion from activated microglia in vivo

Bodart‐Santos, V., Ruan, Z., Melvin, B. C., Pandey, I., Ikezu, S., & Ikezu, T. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.115025 · Cited by 12 · see citing works

Characterization of covalent inhibitors that disrupt the interaction between the tandem SH2 domains of SYK and FCER1G phospho-ITAM

Bashore, F. M., Katis, V. L., Du, Y., Sikdar, A., Wang, D., Bradshaw, W. J., Rygiel, K. A., Leisner, T. M., Chalk, R., Mishra, S., et al. (2024) · PLoS ONE · doi:10.1371/journal.pone.0293548 · Cited by 12 · see citing works

Development of In Vitro and In Vivo Evaluation Systems for Vitamin D Derivatives and Their Application to Drug Discovery

Yasuda, K., Nishikawa, M., Mano, H., Takano, M., Kittaka, A., Ikushiro, S., & Sakaki, T. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222111839 · Cited by 7 · see citing works

Choroidal Neovascularization Is Suppressed With Activation of TREM2 in Mononuclear Phagocytes—Brief Report

Yagi, H., Boeck, M., Neilsen, K., Yang, J., Ko, M.-J., Tomita, Y., Negishi, K., Fu, Z., Sun, Y., & Smith, L. (2025) · Arteriosclerosis, Thrombosis and Vascular Biology · doi:10.1161/atvbaha.124.321809 · Cited by 6 · see citing works

Biophysical characterization of TREM2 missense variants implicated in neurodegenerative disease

Pillai, J. P., Sung, K., Shi, L. Z., & Wu, C. (2025) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2025.07.003 · Cited by 2 · see citing works

Evaluating the pathogenicity, stability, and stereochemical effects of variants of unknown significance in TREM2 using orthogonal structural analysesPreprint

Pillai, J. P., Sung, K., Shi, L. Z., & Wu, C. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.05.25.656054

Additional file 3 of Plaque-associated human microglia accumulate lipid droplets in a chimeric model of Alzheimer’s disease

Claes, C., Danhash, E., Hasselmann, J., Chadarevian, J. P., Shabestari, S. K., England, W., Lim, T. E., Hidalgo, J. L. S., Spitale, R. C., Davtyan, H., et al. (2021) · Figshare · doi:10.6084/m9.figshare.15047551

ARID5A RNA-binding coordinates microglial defense and ferroptosis in iPSC-derived models

Schafer, D. M., Blue, S. M., Xu, S., Mizrahi, O., Gosztyla, M. L., Street, L., Rothamel, K. L., Kopalle, H., Landry, S. B., Rosales, E. K. F., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-76131-0

A reporter cell system for the triggering receptor expressed on myeloid cells 2 reveals differential effects of disease‐associated variants on receptor signaling and activation by antibodies against the stalk region

Ibach, M., Mathews, M., Linnartz‐Gerlach, B., Theil, S., Kumar, S., Feederle, R., Brüstle, O., Neumann, H., & Walter, J. (2020) · Glia · doi:10.1002/glia.23953 · Cited by 24 · see citing works

A reporter cell system for TREM2 reveals differential effects of disease-associated variants on receptor signaling and activation by antibodies against the stalk region

Ibach, M. (2021) · bonndoc (University of Bonn)

TREM2 T204A mutation enhances the ability of microglia to clear Aβ and promotes the activation of the TREM2-DAP12-SYK signaling pathway

NIU Qi, W. Q. (2026) · DOAJ (DOAJ: Directory of Open Access Journals) · doi:10.16352/j.issn.1001-6325.2026.08.1036

Soluble TREM2: Innocent bystander or active player in neurological diseases?

Filipello, F., Goldsbury, C., You, S. F., Locca, A., Karch, C. M., & Piccio, L. (2022) · Neurobiology of Disease · doi:10.1016/j.nbd.2022.105630 · Cited by 134 · see citing works

Biophysical analysis of TREM2 interactions reveals a shared binding site for Alzheimer’s disease ligands apoE and oligomeric amyloid beta

Greven, J. A., Song, J. H., Kober, D. L., Alexander‐Brett, J. M., Gross, M. L., & Brett, T. J. (2022) · Alzheimer s & Dementia · doi:10.1002/alz.067634