Pattern Recognition by TREM-2: Binding of Anionic Ligands

In Vitro Cultivation of Human Tumors: Establishment of Cell Lines Derived From a Series of Solid Tumors2

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Pattern Recognition Receptors

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Mutations in Two Genes Encoding Different Subunits of a Receptor Signaling Complex Result in an Identical Disease Phenotype

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The human TREM gene cluster at 6p21.1 encodes both activating and inhibitory single IgV domain receptors and includes NKp44

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The NKp46 Receptor Contributes to NK Cell Lysis of Mononuclear Phagocytes Infected with an Intracellular Bacterium

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Mouse Ly-49D Recognizes H-2Dd and Activates Natural Killer Cell Cytotoxicity

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Involvement of natural cytotoxicity receptors in human natural killer cell-mediated lysis of neuroblastoma and glioblastoma cell lines

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Establishment and characterization of five cell lines derived from human malignant gliomas

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Initial characterization of TREM-like transcript (TLT)-1: a putative inhibitory receptor within the TREM cluster.

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Arginine Residues in Domain V Have a Central Role for Bacteria-Binding Activity of Macrophage Scavenger Receptor MARCO

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Secretory phospholipases A2 induce cytokine release from blood and synovial fluid monocytes

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Functional Changes in Scavenger Receptor Binding Conformation Are Induced by Charge Mutants Spanning the Entire Collagen Domain

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Hold Tight (but Not Too Tight) to Get It Right

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N-linked carbohydrates in tyrosinase are required for its recognition by human MHC class II-restricted CD4+ T cells

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Crystallization and preliminary crystallographic characterization of the extracellular Ig-like domain of human natural killer cell activating receptor NKp44

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The three dimensional structure of NK cell receptor Nkp44, a triggering partner in natural cytotoxicity

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Untitled work

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

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

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Systemic infections and inflammation affect chronic neurodegeneration

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TREM2-mediated early microglial response limits diffusion and toxicity of amyloid plaques

Wang, Y., Ulland, T. K., Ulrich, J. D., Song, W., Tzaferis, J. A., Hole, J. T., Yuan, P., Mahan, T. E., Shi, Y., Gilfillan, S., et al. (2016) · Journal of Experimental Medicine · doi:10.1084/jem.20151948 · Cited by 840 · see citing works

CNS immune privilege: hiding in plain sight

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TREM2 — a key player in microglial biology and Alzheimer disease

Ulland, T. K., & Colonna, M. (2018) · Nature Reviews Neurology · doi:10.1038/s41582-018-0072-1 · Cited by 735 · 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

The Microglial Innate Immune Receptor TREM2 Is Required for Synapse Elimination and Normal Brain Connectivity

Filipello, F., Morini, R., Corradini, I., Zerbi, V., Canzi, A., Michalski, B., Erreni, M., Markicevic, M., Starvaggi-Cucuzza, C., Otero, K., et al. (2018) · Immunity · doi:10.1016/j.immuni.2018.04.016 · Cited by 695 · see citing works

Macrophages in health and disease

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The TREM receptor family and signal integration

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

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Janus-faced microglia: beneficial and detrimental consequences of microglial phagocytosis

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Inflammation: the link between comorbidities, genetics, and Alzheimer’s disease

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TREM2 sustains microglial expansion during aging and response to demyelination

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New insights into the role of TREM2 in Alzheimer’s disease

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

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The endotoxin hypothesis of neurodegeneration

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TREM2, microglia, and neurodegenerative diseases

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

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Macrophages and the Recovery from Acute and Chronic Inflammation

Hamidzadeh, K., Christensen, S. M., Dalby, E., Chandrasekaran, P., & Mosser, D. M. (2016) · Annual Review of Physiology · doi:10.1146/annurev-physiol-022516-034348 · Cited by 439 · see citing works

TREM and TREM-like receptors in inflammation and disease

Ford, J. W., & McVicar, D. W. (2009) · Current Opinion in Immunology · doi:10.1016/j.coi.2009.01.009 · Cited by 434 · see citing works

TREM2 in Neurodegenerative Diseases

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TREM2 variants: new keys to decipher Alzheimer disease pathogenesis

Colonna, M., & Wang, Y. (2016) · Nature Reviews Neuroscience · doi:10.1038/nrn.2016.7 · Cited by 418 · see citing works

Regulation of microglial activation in stroke

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The amyloid cascade hypothesis: are we poised for success or failure?

Karran, E., & De Strooper, B. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13632 · Cited by 402 · see citing works

The biology of TREM receptors

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TREM2 activation on microglia promotes myelin debris clearance and remyelination in a model of multiple sclerosis

Cignarella, F., Filipello, F., Bollman, B., Cantoni, C., Locca, A., Mikesell, R., Manis, M., Ibrahim, A., Deng, L., Benitez, B. A., et al. (2020) · Acta Neuropathologica · doi:10.1007/s00401-020-02193-z · Cited by 392 · see citing works

Microglial Activation in Stroke: Therapeutic Targets

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Triggering receptor expressed on myeloid cells 2 (TREM2) deficiency attenuates phagocytic activities of microglia and exacerbates ischemic damage in experimental stroke

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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

Immune Signaling in Neurodegeneration

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Elucidating the Role of TREM2 in Alzheimer’s Disease

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DAP10‐ and DAP12‐associated receptors in innate immunity

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

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The Triggering Receptor Expressed on Myeloid Cells 2 Binds Apolipoprotein E

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The cellular response in neuroinflammation: The role of leukocytes, microglia and astrocytes in neuronal death and survival

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TREM2 regulates microglial cell activation in response to demyelination in vivo

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Blockade of TREM‐2 exacerbates experimental autoimmune encephalomyelitis

Piccio, L., Buonsanti, C., Mariani, M., Cella, M., Gilfillan, S., Cross, A. H., Colonna, M., & Panina‐Bordignon, P. (2007) · European Journal of Immunology · doi:10.1002/eji.200636837 · Cited by 284 · see citing works

TREM2-Ligand Interactions in Health and Disease

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Clearance of cerebral Aβ in Alzheimer’s disease: reassessing the role of microglia and monocytes

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Activating and inhibitory functions of DAP12

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Microglia and Aging: The Role of the TREM2–DAP12 and CX3CL1-CX3CR1 Axes

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TREM2 macrophages drive NK cell paucity and dysfunction in lung cancer

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The FTD‐like syndrome causing TREM2 T66M mutation impairs microglia function, brain perfusion, and glucose metabolism

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

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Role of ITAM‐containing adapter proteins and their receptors in the immune system and bone

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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

Neurodegenerative disease mutations in TREM2 reveal a functional surface and distinct loss-of-function mechanisms

Kober, D. L., Alexander-Brett, J. M., Karch, C. M., Cruchaga, C., Colonna, M., Holtzman, M. J., & Brett, T. J. (2016) · eLife · doi:10.7554/elife.20391 · Cited by 238 · see citing works

Macrophage subsets in atherosclerosis as defined by single‐cell technologies

Willemsen, L., & de Winther, M. P. J. (2020) · The Journal of Pathology · doi:10.1002/path.5392 · Cited by 228 · see citing works

The Link between Oxidative Stress, Mitochondrial Dysfunction and Neuroinflammation in the Pathophysiology of Alzheimer’s Disease: Therapeutic Implications and Future Perspectives

Jurcău, M. C., Andronie-Cioara, F. L., Jurcău, A., Marcu, F., Ţiț, D. M., Pașcalău, N., & Nistor-Cseppentö, D. C. (2022) · Antioxidants · doi:10.3390/antiox11112167 · Cited by 226 · see citing works

TREM2, microglia, and Alzheimer’s disease.

Qin, Q., Teng, Z., Liu, C., Li, Q., Yin, Y., & Tang, Y. (2021) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2021.111438 · Cited by 219 · see citing works

Amyloid-beta modulates microglial responses by binding to the triggering receptor expressed on myeloid cells 2 (TREM2)

Zhong, L., Wang, Z., Wang, D., Wang, Z., Martens, Y. A., Wu, L., Xu, Y., Wang, K., Li, J., Huang, R., et al. (2018) · Molecular Neurodegeneration · doi:10.1186/s13024-018-0247-7 · Cited by 217 · see citing works

Mycobacterium tuberculosis Inhibits Macrophage Responses to IFN-γ through Myeloid Differentiation Factor 88-Dependent and -Independent Mechanisms

Fortune, S. M., Solache, A., Jaeger, A., Hill, P. J., Belisle, J. T., Bloom, B. R., Rubin, E. J., & Ernst, J. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.172.10.6272 · Cited by 205 · see citing works

From expression to signaling: Roles of TREM-1 and TREM-2 in innate immunity and bacterial infection

Sharif, O., & Knapp, S. (2008) · Immunobiology · doi:10.1016/j.imbio.2008.07.008 · Cited by 196 · see citing works

Functional Studies of Missense TREM2 Mutations in Human Stem Cell-Derived Microglia

Brownjohn, P. W., Smith, J., Solanki, R., Lohmann, E., Houlden, H., Hardy, J., Dietmann, S., & Livesey, F. J. (2018) · Stem Cell Reports · doi:10.1016/j.stemcr.2018.03.003 · Cited by 193 · see citing works

Immune Surveillance of the CNS following Infection and Injury

Russo, M. V., & McGavern, D. B. (2015) · Trends in Immunology · doi:10.1016/j.it.2015.08.002 · Cited by 191 · see citing works

The Role of APOE and TREM2 in Alzheimer′s Disease—Current Understanding and Perspectives

Wolfe, C. M., Fitz, N. F., Nam, K. N., Lefterov, I. M., & Koldamova, R. P. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms20010081 · Cited by 192 · see citing works

Insights into TREM2 biology by network analysis of human brain gene expression data

Forabosco, P., Ramasamy, A., Trabzuni, D., Walker, R., Smith, C., Bras, J., Levine, A. P., Hardy, J., Pocock, J. M., Guerreiro, R., et al. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.05.001 · Cited by 180 · see citing works

Innate Immune Responses to TREM-1 Activation: Overlap, Divergence, and Positive and Negative Cross-Talk with Bacterial Lipopolysaccharide

Dower, K., Ellis, D. K., Saraf, K. A., Jelinsky, S. A., & Lin, L. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.180.5.3520 · Cited by 175 · see citing works

ADAM17 is the main sheddase for the generation of human triggering receptor expressed in myeloid cells (hTREM2) ectodomain and cleaves TREM2 after Histidine 157

Feuerbach, D., Schindler, P. A., Barske, C., Joller, S., Beng-Louka, E., Worringer, K. A., Kommineni, S., Kaykas, A., Ho, D. J., Ye, C., et al. (2017) · Neuroscience Letters · doi:10.1016/j.neulet.2017.09.034 · Cited by 172 · see citing works

Identification of a common gene signature for type II cytokine–associated myeloid cells elicited in vivo in different pathologic conditions

Ghassabeh, G. H., BAETSELIER, P. D., Brys, L., Noël, W., Ginderachter, J. A. V., Meerschaut, S., Beschin, A., Brombacher, F., & Raes, G. (2006) · Blood · doi:10.1182/blood-2005-04-1485 · Cited by 175 · see citing works

TREM-2, triggering receptor expressed on myeloid cell-2, negatively regulates TLR responses in dendritic cells

Ito, H., & Hamerman, J. A. (2012) · European Journal of Immunology · doi:10.1002/eji.201141679 · Cited by 173 · see citing works

TREM2 in CNS homeostasis and neurodegenerative disease

Painter, M. M., Atagi, Y., Liu, C.-C., Rademakers, R., Xu, H., Fryer, J. D., & Bu, G. (2015) · Molecular Neurodegeneration · doi:10.1186/s13024-015-0040-9 · Cited by 169 · 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

Specific lipid recognition is a general feature of CD300 and TREM molecules

Cannon, J. P., O’Driscoll, M., & Litman, G. W. (2011) · Immunogenetics · doi:10.1007/s00251-011-0562-4 · Cited by 162 · see citing works

TREM2, a DAP12-associated receptor, regulates osteoclast differentiation and function

Humphrey, M. B., Daws, M. R., Spusta, S. C., Niemi, E. C., Torchia, J. A., Lanier, L. L., Seaman, W. E., & Nakamura, M. C. (2006) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.051016 · Cited by 162 · see citing works

Human Induced Pluripotent Stem Cell-Derived Microglia-Like Cells Harboring TREM2 Missense Mutations Show Specific Deficits in Phagocytosis

Garcia-Reitboeck, P., Phillips, A., Piers, T. M., Villegas-Llerena, C., Butler, M., Mallach, A., Rodrigues, C., Arber, C. E., Heslegrave, A., Zetterberg, H., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.07.094 · Cited by 162 · see citing works

Acute injury in the peripheral nervous system triggers an alternative macrophage response

Ydens, E., Cauwels, A., Asselbergh, B., Goethals, S., Peeraer, L., Lornet, G., Almeida-Souza, L., Ginderachter, J. A. V., Timmerman, V., & Janssens, S. (2012) · Journal of Neuroinflammation · doi:10.1186/1742-2094-9-176 · Cited by 163 · see citing works

Microglial TYROBP/DAP12 in Alzheimer's Disease: Transduction of Physiological and Pathological Signals Across TREM2

Haure-Mirande, J.-V., Audrain, M., Ehrlich, M. E., & Gandy, S. (2022) · Molecular Neurodegeneration · doi:10.1186/s13024-022-00552-w · Cited by 159 · see citing works

The surface‐exposed chaperone, Hsp60, is an agonist of the microglial TREM2 receptor

Stefano, L., Racchetti, G., Bianco, F., Passini, N., Gupta, R. S., Panina‐Bordignon, P., & Meldolesi, J. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06130.x · Cited by 150 · see citing works

The role of the microglia in acute CNS injury

Kawabori, M., & Yenari, M. A. (2014) · Metabolic Brain Disease · doi:10.1007/s11011-014-9531-6 · Cited by 138 · see citing works

Myelin as an inflammatory mediator: Myelin interactions with complement, macrophages, and microglia in spinal cord injury

Kopper, T. J., & Gensel, J. C. (2017) · Journal of Neuroscience Research · doi:10.1002/jnr.24114 · Cited by 141 · see citing works

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

The endotoxin hypothesis of Alzheimer’s disease

Brown, G. C., & Heneka, M. T. (2024) · Molecular Neurodegeneration · doi:10.1186/s13024-024-00722-y · Cited by 140 · see citing works

The expanding roles of ITAM adapters FcRγ and DAP12 in myeloid cells

Hamerman, J. A., Ni, M., Killebrew, J. R., Chu, C., & Lowell, C. A. (2009) · Immunological Reviews · doi:10.1111/j.1600-065x.2009.00841.x · Cited by 128 · see citing works

Triggering receptor expressed on myeloid cells-1 (TREM-1) amplifies the signals induced by the NACHT-LRR (NLR) pattern recognition receptors

Netea, M. G., Azam, T., Ferwerda, G., Girardin, S. E., Kim, S.-H., & Dinarello, C. A. (2006) · Journal of Leukocyte Biology · doi:10.1189/jlb.1205758 · Cited by 129 · see citing works

Factors and signals that govern the migration of dendritic cells via lymphatics: recent advances

Randolph, G. J., Sánchez‐Schmitz, G., & Angeli, V. (2004) · Springer Seminars in Immunopathology · doi:10.1007/s00281-004-0168-0 · Cited by 124 · see citing works

The Early Events That Initiate β-Amyloid Aggregation in Alzheimer’s Disease

Zhang, X., Fu, Z., Meng, L., He, M., & Zhang, Z. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00359 · Cited by 122 · see citing works

The Signaling Adapter Protein DAP12 Regulates Multinucleation During Osteoclast Development

Humphrey, M. B., Ogasawara, K., Yao, W., Spusta, S. C., Daws, M. R., Lane, N. E., Lanier, L. L., & Nakamura, M. C. (2004) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.0301234 · Cited by 123 · see citing works

Mechanisms and Potential Therapeutic Applications of Microglial Activation after Brain Injury

Kim, J. Y., Kim, N., & Yenari, M. A. (2014) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.12360 · Cited by 119 · see citing works

An in-depth comparison of the porcine, murine and human inflammasomes; lessons from the porcine genome and transcriptome

Dawson, H. D., Smith, A. D., Chen, C. T., & Urban, J. F. (2016) · Veterinary Microbiology · doi:10.1016/j.vetmic.2016.05.013 · Cited by 119 · see citing works

Essential Role of DAP12 Signaling in Macrophage Programming into a Fusion-Competent State

Helming, L., Tomasello, E., Kyriakides, T. R., Martinez, F. O., Takai, T., Gordon, S., & Vivier, E. (2008) · Science Signaling · doi:10.1126/scisignal.1159665 · Cited by 116 · 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

Aminophospholipids are signal-transducing TREM2 ligands on apoptotic cells

Shirotani, K., Hori, Y., Yoshizaki, R., Higuchi, E., Colonna, M., Saito, T., Hashimoto, S., Saito, T., Saido, T. C., & Iwata, N. (2019) · Scientific Reports · doi:10.1038/s41598-019-43535-6 · Cited by 116 · see citing works

Cerebrospinal fluid sTREM2 levels are associated with gray matter volume increases and reduced diffusivity in early Alzheimer's disease

Gispert, J. D., Suárez‐Calvet, M., Monté, G. C., Tucholka, A., Falcón, C., Rojas, S., Rami, L., Sánchez‐Valle, R., Lladó, A., Kleinberger, G., et al. (2016) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2016.06.005 · Cited by 114 · see citing works

Neutrophil-specific deletion of Syk kinase results in reduced host defense to bacterial infection

Ziffle, J. V., & Lowell, C. A. (2009) · Blood · doi:10.1182/blood-2009-05-220806 · Cited by 115 · see citing works

A Rose by Any Other Name? The Potential Consequences of Microglial Heterogeneity During CNS Health and Disease

Carson, M. J., Bilousova, T. V., Puntambekar, S. S., Melchior, B., Doose, J. M., & Ethell, I. M. (2007) · Neurotherapeutics · doi:10.1016/j.nurt.2007.07.002 · Cited by 113 · 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

Microglia and inflammation: conspiracy, controversy or control?

Fernandes, A. M. A., Miller‐Fleming, L., & Pais, T. F. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1670-8 · Cited by 110 · see citing works

New Insights into Neuroinflammation Involved in Pathogenic Mechanism of Alzheimer’s Disease and Its Potential for Therapeutic Intervention

Li, T., Lu, L., Pember, E., Li, X., Zhang, B., & Zhu, Z. (2022) · Cells · doi:10.3390/cells11121925 · Cited by 109 · see citing works

Microglia in Alzheimer’s disease: A target for immunotherapy

Wang, S., & Colonna, M. (2019) · Journal of Leukocyte Biology · doi:10.1002/jlb.mr0818-319r · Cited by 104 · see citing works

TREM2 triggers microglial density and age-related neuronal loss

Linnartz‐Gerlach, B., Bodea, L., Klaus, C., Ginolhac, A., Halder, R., Sinkkonen, L., Walter, J., Colonna, M., & Neumann, H. (2019) · Glia · doi:10.1002/glia.23563 · Cited by 104 · see citing works

Structure, expression pattern and biological activity of molecular complex TREM-2/DAP12

Paradowska-Gorycka, A., & Jurkowska, M. (2013) · Human Immunology · doi:10.1016/j.humimm.2013.02.003 · Cited by 103 · see citing works

Developmental Regulation of TREM2 and DAP12 Expression in the Murine CNS: Implications for Nasu-Hakola Disease

Thrash, J. C., Torbett, B. E., & Carson, M. J. (2008) · Neurochemical Research · doi:10.1007/s11064-008-9657-1 · Cited by 103 · see citing works

TREM2 in Alzheimer’s Disease: Microglial Survival and Energy Metabolism

Zheng, H., Cheng, B., Li, Y., Li, X., Chen, X., & Zhang, Y.-W. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00395 · Cited by 94 · see citing works

The Alzheimer’s disease risk factors apolipoprotein E and TREM2 are linked in a receptor signaling pathway

Jendresen, C., Årskog, V., Daws, M. R., & Nilsson, L. N. G. (2017) · Journal of Neuroinflammation · doi:10.1186/s12974-017-0835-4 · Cited by 94 · see citing works

TREM2 is a receptor for non-glycosylated mycolic acids of mycobacteria that limits anti-mycobacterial macrophage activation

Iizasa, E., Chuma, Y., Uematsu, T., Kubota, M., Kawaguchi, H., Umemura, M., Toyonaga, K., Kiyohara, H., Yano, I., Colonna, M., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-22620-3 · Cited by 92 · see citing works

OSCAR is an FcRγ-associated receptor that is expressed by myeloid cells and is involved in antigen presentation and activation of human dendritic cells

Merck, E., Gaillard, C., Gorman, D. M., Montero‐Julian, F. A., Durand, I., Zurawski, S., Ménétrier‐Caux, C., Carra, G., Lebecque, S., Trinchieri, G., et al. (2004) · Blood · doi:10.1182/blood-2004-03-0850 · Cited by 92 · see citing works

A Comprehensive Review of Immunoreceptor Regulation of Osteoclasts

Humphrey, M. B., & Nakamura, M. C. (2015) · Clinical Reviews in Allergy & Immunology · doi:10.1007/s12016-015-8521-8 · Cited by 93 · see citing works

TREM2 suppresses the proinflammatory response to facilitate PRRSV infection via PI3K/NF-κB signaling

Zhu, Z., Zhang, X., Dong, W., Wang, X., he, S. T., Zhang, H., Wang, X., Wei, R., Chen, Y., Liu, X., et al. (2020) · PLoS Pathogens · doi:10.1371/journal.ppat.1008543 · Cited by 91 · see citing works

Profiling Carbohydrate-Receptor Interaction with Recombinant Innate Immunity Receptor-Fc Fusion Proteins

Hsu, T.-L., Cheng, S., Yang, W., Chin, S.-W., Chen, B.-H., Huang, M., Hsieh, S.-L., & Wong, C. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.065961 · Cited by 90 · see citing works

Extracellular domain of TREM2 possess two distinct ligand recognition sites: Insights from machine-learning guided docking and all-atoms molecular dynamics simulations

Mishra, S., Swain, P. S., Pati, S., & Dehury, B. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e41414 · Cited by 14 · see citing works

Protein recognition is chiefly mediated by the CDR2 region in TREM2 - an in silico characterization.

Dantas, P. H. D. S., Matos, A. O., Colmenares, M. T. C., Costa, V., Felice, A. G., Neto, J. R., Soares, S., Silva-Sales, M., Neves, B., & Sales-Campos, H. (2025) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2025.109058 · Cited by 4 · see citing works

From expression to signaling: Roles of TREM-1 and TREM-2 in innate immunity and bacterial infection

Sharif, O., & Knapp, S. (2008) · Immunobiology · doi:10.1016/j.imbio.2008.07.008 · Cited by 196 · see citing works

The role of Triggering Receptor expressed on myeloid Cells-2 in bacterial lung infections

Gawish, R. (2010) · University of Vienna · doi:10.25365/thesis.12865

Cutting Edge: Identification of Neutrophil PGLYRP1 as a Ligand for TREM-1

Read, C. B., Kuijper, J. L., Hjorth, S. A., Heipel, M., Tang, X., Fleetwood, A. J., Dantzler, J. L., Grell, S. N., Kastrup, J., Wang, C., et al. (2015) · The Journal of Immunology · doi:10.4049/jimmunol.1402303 · Cited by 158 · see citing works