The DOI matches its Crossref record; 155 of the 161 references it cites were found in a registry or an index.
TREM2-Ligand Interactions in Health and Disease
Open accessAbstract
The protein triggering receptor expressed on myeloid cells-2 (TREM2) is an immunomodulatory receptor with a central role in myeloid cell activation and survival. In recent years, the importance of TREM2 has been highlighted by the identification of coding variants that increase risk for Alzheimer's disease and other neurodegenerative diseases. Animal studies have further shown the importance of TREM2 in neurodegenerative and other inflammatory disease models including chronic obstructive pulmonary disease, multiple sclerosis, and stroke. A mechanistic understanding of TREM2 function remains elusive, however, due in part to the absence of conclusive information regarding the identity of endogenous TREM2 ligands. While many TREM2 ligands have been proposed, their physiological role and mechanism of engagement remain to be determined. In this review, we highlight the suggested roles of TREM2 in these diseases and the recent advances in our understanding of TREM2 and discuss putative TREM2-ligand interactions and their potential roles in signaling during health and disease. We develop a model based on the TREM2 structure to explain how different TREM2 ligands might interact with the receptor and how disease risk variants may alter ligand interactions. Finally, we propose future experimental directions to establish the role and importance of these different interactions on TREM2 function.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“TREM2 binds lipids exposed on the surface of apoptotic cells [49, 50], as well as ApoE [51] and lipidated Amyloid beta (Aβ) [52].”
From TREM2/PLCγ2 signalling in immune cells: function, structural insight, and potential therapeutic modulation (2021) · cites this paper as [52]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“TREM2 associates with the immunoreceptor tyrosine-based activation motif (ITAM)–containing adaptor protein DAP12 to induce signal transduction, including recruitment and activation of spleen tyrosine kinase (SYK) and calcium flux24,25.”
From PLCγ2 regulates TREM2 signalling and integrin-mediated adhesion and migration of human iPSC-derived macrophages (2021) · cites this paper as [24]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Complement and microglia mediate early synapse loss in Alzheimer mouse models
Hong, S., Beja-Glasser, V. F., Nfonoyim, B. M., Frouin, A., Li, S., Ramakrishnan, S., Merry, K. M., Shi, Q., Rosenthal, A., Barres, B. A., et al. (2016) · Science · doi:10.1126/science.aad8373 · Cited by 3,343
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 · cited 15×
“Although there have been reports of TREM2 detection on non-myeloid/microglial cells in the CNS [4, 36], these cases have largely used immunostaining methods to identify neuronal expression of TREM2, which may identify sTREM2 produced by microglia that is released and bound to neurons which express a TREM2 ligand [26,…”
BackgroundInfluentialVariant 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 · cited 5×
“The importance of TREM2 is highlighted by genetic studies linking TREM2 variants to various neurodegenerative diseases, including Alzheimer’s disease (AD) [4, 5].”
BackgroundInfluentialIdentification of a unique TGF-β–dependent molecular and functional signature in microglia
Butovsky, O., Jedrychowski, M. P., Moore, C. S., Cialic, R., Lanser, A. J., Gabriely, G., Koeglsperger, T., Dake, B., Wu, P. M., Doykan, C. E., et al. (2014) · Nature Neuroscience · doi:10.1038/nn.3599 · Cited by 2,543
The structural basis of lipopolysaccharide recognition by the TLR4–MD-2 complex
Park, B. S., Song, D. H., Kim, H. M., Choi, B., Lee, H., & Lee, J. (2009) · Nature · doi:10.1038/nature07830 · Cited by 2,438
How neuroinflammation contributes to neurodegeneration
Ransohoff, R. M. (2016) · Science · doi:10.1126/science.aag2590 · Cited by 1,967 · cited 2×
“This creates a vicious cycle where microglia are exposed to stimuli, and although they may first respond with phagocytic and less inflammatory results [58], they will fail to resolve the plaques and create an inflammatory milieu that is primed to additional inflammation with subsequent insults until the microglia even…”
BackgroundTREM2 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 · cited 7×
“TREM2 inhibits inflammatory cytokine production in cultured microglia following exposure to apoptotic neurons [142], and Trem2-deficient and haploinsufficient microglia have impaired microgliosis and don’t properly respond to plaques [30, 42, 45, 47, 143] (Fig.”
BackgroundResultInfluentialNeuroinflammation in Alzheimer's disease: current evidence and future directions
Calsolaro, V., & Edison, P. (2016) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2016.02.010 · Cited by 1,726 · cited 2×
“This creates a vicious cycle where microglia are exposed to stimuli, and although they may first respond with phagocytic and less inflammatory results [58], they will fail to resolve the plaques and create an inflammatory milieu that is primed to additional inflammation with subsequent insults until the microglia even…”
BackgroundIntegrated 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 · cited 4×
“A uthor M anuscript A uthor M anuscript A uthor M anuscript A uthor M anuscript CL cardiolipin COPD chronic obstructive pulmonary disease CS Chondroitin sulfate CSF-1R Colony stimulating factor 1 receptor DAG diacylglycerol DAMPs Damage-associated molecular patters DAP12 DNAX-activation protein 12 DC Dendritic cell EL…”
BackgroundInfluentialThe microglial sensome revealed by direct RNA sequencing
Hickman, S. E., Kingery, N. D., Ohsumi, T. K., Borowsky, M. L., Wang, L.-C., Means, T. K., & El Khoury, J. (2013) · Nature Neuroscience · doi:10.1038/nn.3554 · Cited by 1,511 · cited 1×
“RNA expression analyses have confirmed Trem2 is expressed selectively on microglia in the brain [40, 41], and parabiosis experiments show these microglia are most likely resident microglia and not infiltrating monocytes [42], although this is still controversial [43].”
Background
Flagged first, then by citations
6 of the 161 references couldn’t be matched to a known paper.
Research works printed but not linked: 5
- Soragna, 2003, An Italian family affected by Nasu–Hakola disease with a novel genetic mutation in the TREM2 gene, J. Neurol. Neurosurg. Psychiatry, 74, 825, 10.1136/jnnp.74.6.825-a · DOI · Paper page
- Pimplikar, 2014, Neuroinflammation in Alzheimer's disease: from pathogenesis to a therapeutic target, J. Clin. Immunol., 34, 64, 10.1007/s10875-014-0032-5 · DOI
- Correale, 2013, Bacterial sensor triggering receptor expressed on myeloid cells-2 regulates the mucosal inflammatory response, Gastroenterology, 144, 346, 10.1053/j.gastro.2012.10.040 · DOI
- Sharif, 2014, The triggering receptor expressed on myeloid cells 2 inhibits complement component 1q effector mechanisms and exerts detrimental effects during pneumococcal pneumonia, PLoS Pathog., 10, e1004167, 10.1371/journal.ppat.1004167 · DOI
- Murphy, 2007, Structural and functional basis of CXCL12 (stromal cell-derived factor-1 alpha) binding to heparin, J. Biol. Chem., 282, 10,018, 10.1074/jbc.M608796200 · DOI
Cited by
Sorted by citations
Items 201–241 of 241
Fuchs, N., Gaamouch, F. E., Nada, H., Cho, S., & Gabr, M. (2026) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2026.118612 · Cited by 2
Zhong, Z., Ulmschneider, M. B., & Lorenz, C. D. (2025) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.5c01891 · Cited by 2
Birts, C. N., & Wilton, D. C. (2023) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2023.166837 · Cited by 3
“In fact, TREM2 is now a major focus in understanding the accumulation of amyloid β in the nervous system [35 – 38].”
InfluentialFruhwürth, S., Reinert, L. S., Öberg, C., Sakr, M., Henricsson, M., Zetterberg, H., & Paludan, S. R. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.03.16.532882 · Cited by 2
“Interestingly, it has been reported that for instance DNA, different lipids, and complex carbohydrates, which are present on viral particles and stressed cells, have been reported as TREM2 agonists (19).”
BackgroundTREM2 as a Prognostic Biomarker for Osteosarcoma Microenvironment Remodeling
Shen, Z. Z., Chen, Z.-Y., Ji, Y., Jiang, H., Zhu, Z.-P., Yuan, H., Li, B., Xu, W., & Xiao, J. (2023) · Journal of Oncology · doi:10.1155/2023/3677789 · Cited by 3
“Several researchers identifed the TREM2 receptor as a dominating signaling hub of pathology-induced immunity, which can sense tissue damage and activate robust remodeling immunity as responding to it [11].”
BackgroundBastelica, P., Reboussin, É., Przegralek, L., Darche, M., Buffault, J., Goazigo, A. R.-L., Labbé, A., Parsadaniantz, S. M., & Baudouin, C. (2026) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2026.119648 · Cited by 1
Microglial ITAM & ITIM Signaling in Neurodegenerative Disease and Brain Aging
Mangalmurti, A., Bonheur, A., & Lukens, J. R. (2026) · Journal of Molecular Biology · doi:10.1016/j.jmb.2026.169910 · Cited by 1
Song, P., Qi, P., Jin, X., Li, B., Wang, R., Jiang, J., Shen, J., Ni, J., Chen, C., Ge, X., et al. (2026) · Cellular and Molecular Gastroenterology and Hepatology · doi:10.1016/j.jcmgh.2026.101819 · Cited by 1
“17,37 It recognizes a diverse array of ligands, including anionic phospholipids, glycolipids, lipoproteins (such as apolipoprotein E), and damage-associated molecular patterns released during tissue injury.”
Cao, P., Zhang, J., Shen, Y., Xing, Z., Han, F., Chen, X., & Jiang, N. (2026) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.5c03239 · Cited by 1
Li, P. P., Sun, Z., Chen, Y., Fang, Z., Yu, D., Wang, L., 任延波, & Gong, P. (2026) · Molecular Neurobiology · doi:10.1007/s12035-026-05764-5
“Given that TREM-1 and TREM-2 share similar structures and partially overlapping ligands [25] and considering that eCIRP binds to TREM-1 to amplify inflammation, we hypothesized that eCIRP might also bind to TREM-2.”
InfluentialPierro, E. W., Garcia, G., Sanchez, V., González-Ericsson, P., Fingleton, B., Hasty, A. H., & Rexer, B. (2025) · Scientific Reports · doi:10.1038/s41598-025-22614-x · Cited by 1
“TREM2 is a transmembrane protein of the immunoglobulin superfamily that is expressed on cells of the monocyte-macrophage lineage 7 .”
Boreland, A. J., Abbo, Y., Li, X., Stillitano, A. C., Zhang, S., Duan, J., Pang, Z. P., & Hart, R. P. (2025) · Alcohol · doi:10.1016/j.alcohol.2025.10.006 · Cited by 8
Banerjee, S., & Sil, P. C. (2025) · Archives of Toxicology · doi:10.1007/s00204-025-04181-2 · Cited by 1
“Microglia infiltrate and degrades the aggregated proteins thereby helping clearance (Kober and Brett 2017).”
Kwak, C. S., Finan, G. M., Park, Y. R., Garg, A., Harari, O., Mun, J. Y., Rhee, H., & Kim, T. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.03.21.533722 · Cited by 1
Neuron-derived Thioredoxin-80: a novel regulator of type-I interferon response in microgliaPreprint
Goikolea, J., Roussarie, J.-P., Gereñu, G., Loera‐Valencia, R., Latorre‐Leal, M., Cedazo-Mı́nguez, Á., Rodriguez‐Rodriguez, P., & Maioli, S. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.03.09.483648 · Cited by 1
“Trem2 is a transmembrane receptor that plays an essential role in microglia activation (3, 4) and its genetic variants have been associated with AD (5).”
BackgroundTakahashi, K. (2018) · Clinical and Experimental Neuroimmunology · doi:10.1111/cen3.12479 · Cited by 1
TREM2 Signaling and Alzheimer’s Disease: Experimental Modulators, Progress, and Challenges
Sayegh, M., Azarfar, K., Reyna, E. M., Kennedy, J. M., Sabbagh, M. N., & Decourt, B. (2026) · Drug Design Development and Therapy · doi:10.2147/dddt.s611558
“41 Early pre-clinical studies demonstrated that TREM2 recognizes DNA, anionic and zwitterionic lipids, including phosphatidylserine, phosphatidylethanolamine, and sphingomyelin, which are exposed on the surface of apoptotic neurons and damaged sphingomyelin.”
Dysfunction of lipid metabolism and lysosomal capacity: at the core of microglial aging?
Šimončičová, E., & Tremblay, M. (2026) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2026.1884230
“Its activation promotes adaptor protein DAP12 (TYROBP) phosphorylation and initiation of downstream signaling pathways supporting phagocytosis, metabolism, cell survival and regulation of inflammatory activity (Feiten et al., 2026; Kober and Brett, 2017).”
Yu, X., Ren, Q., Gao, Y., Xie, S., Dang, R., Meng, J., Su, Z., Li, M., Ao, Y., Liu, A., et al. (2026) · Cell Reports · doi:10.1016/j.celrep.2026.118063
Dynamic Crosstalk Between TREM2+ Macrophages and the MASLD Hepatic Microenvironment
Li, X., Yu, C., Mao, A., Peng, Y., Yiyang, H., & Zhao, Y. (2026) · Biomedicines · doi:10.3390/biomedicines14102167
“TREM2 contains a single extracellular V-type immunoglobulin domain, a short juxtamembrane region, one transmembrane helix, and a short cytoplasmic tail that lacks intrinsic signaling motifs [16,17].”
TREM2-directed therapy in Alzheimer’s disease: from therapeutic window to clinical translation
Kuang, Q., Li, S., Huang, W., Kuang, N., Liu, T., Huang, N., Luo, Y., & Huang, J. (2026) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2026.1938062
“For instance, they might preferentially activate the SYK pathway without adequately engaging the PI3K-Akt or PLC γ 2 branches, thereby inducing dysfunctional microglial responses (Peng et al., 2010; Kober and Brett, 2017).”
Mirizio, E., Werner, G., Hutchins, T., Sanyal, A., Esencan, D., Tabib, T., Chen, W., Lafyatis, R., Jacobe, H., & Torok, K. (2026) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2026.06.1297
He, Z., Feng, J., Yan, R., Wu, P., Zhu, B., Li, H., Yang, T., Lu, Y., He, B., Ma, X., et al. (2026) · Molecular Biology Reports · doi:10.1007/s11033-026-12622-z
“Trem2 is an immunoregulatory receptor mainly expressed on the surface of myeloid cells and is involved in multiple processes, including phagocytic clearance, lipid metabolism, cell survival, and inflammatory regulation [9 ].”
Hossain, M. M., Adhikari, J., Fardous, J., Ahmed, S., Ferdous, M. T., & Shibly, A. Z. (2026) · Next research. · doi:10.1016/j.nexres.2026.102314
Bile acid retention in efferocytic macrophages shapes their inflammatory status during cholangitis
Jawazneh, A. A., Liebold, I., Leyk, S., Lanzloth, C., Brackrock, V., López-López, T., Graute, S., Aranda-Pardos, I., Hamley, M., Bahn, J., et al. (2026) · The Journal of Experimental Medicine · doi:10.1084/jem.20242079
“…uptake affects phagocytic receptor downstream signaling events, as, for instance, the activation of DNAX-activation protein 12 in the case of TREM2 engagement (Kober and Brett, 2017), with TREM2 being described to be involved in uptake of dying hepatocytes (Wang et al., 2023; Liebold et al., 2023).”
Oloruntimehin, E. S., & Malogolovkin, A. S. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27135668
TREM2 drives monocyte-derived macrophage responses to Cryptococcus neoformansPreprint
Abass, A., Ricafrente, A., Trivedi, A., Vichaidit, A., Arshakyan, A., Acharya, S., & Heung, L. J. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.06.10.731331
“TREM2 is a promiscuous receptor that binds to an equally wide variety of endogenous and exogenous ligands (12, 43).”
InfluentialLietzke, E. E., Saeb, D., Aldrich, E. C., de Menezes, R. F., Bruce, K. D., & Sprenger, K. G. (2026) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2026.06.002 · Cited by 1
Deng, W., Chen, Y., Liu, S., Liu, S., Zhang, K., Wang, D., Yu, Z., Zhao, W., Xu, Y., Wang, X., et al. (2026) · Immunity & Inflammation · doi:10.1007/s44466-026-00041-5 · Cited by 1
“TREM2 contains an extracellular V-type immunoglobulin domain and features a pronounced basic patch on its surface, which facilitates the interaction with an extensive array of potential TREM2 ligands [63].”
The human and murine immune systems: regulated by dichotomous molecules
Silva, R. C. M. C. (2026) · International Immunopharmacology · doi:10.1016/j.intimp.2026.116329
TREM2: A Potential Target for the Targeted Therapy of Metabolic Diseases
Li, Y., Liu, S. Q., Chu, C., & Yang, J. (2026) · Mediators of Inflammation · doi:10.1155/mi/6210178
InCytokine, an Open-Source Software, Reveals a TREM2 Variant-Specific Cytokine Signature
Jha, D. K., Ancona, M., Oplt, F., Farmer, S. L., Vagenknecht, M., Vázquez-Otero, A., Prazdnyk, I., Soukup, J., Mathew, R. S., Peterson, V. M., et al. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27031137
“This observation aligns with recent structural studies indicating that TREM2 R47H disrupts ligand binding while potentially altering downstream signaling in complex ways [66,67].”
Teles, R. M. B., Benabdessalem, C., Perrie, J., Wei, C.-F., West, J., Silva, B. J. D. A., Andrade, P. R., Mansky, L. A., Divakar, P., Fischbacher, L. A., et al. (2025) · bioRxiv · doi:10.1101/2025.07.15.664002
“TREM2 is a receptor protein activated by a wide array of biological molecules, including bacterial products, DNA, lipoproteins, and phospholipids 34 , including M. tuberculosis mycolic acids 35,36 .”
Zhong, Z., Ulmschneider, M. B., & Lorenz, C. D. (2025) · bioRxiv · doi:10.1101/2025.06.26.661739
“…range of ligands such as phospholipids, sulfatides, bacterial lipopolysaccharide (LPS) and DNA (Wang et al. 2015; Cannon et al. 2012; Daws et al. 2003; Kawabori et al. 2015), and the nature of these interactions can differentially modulate its signalling strength and outcome (Kober and Brett 2017).”
Understanding Granulomas : A Comprehensive Guide
Nakamizo, S. (2024) · The Nishinihon Journal of Dermatology · doi:10.2336/nishinihonhifu.86.558
Pierro, E. W., Cottam, M., An, H., Lehmann, B. D., Pietenpol, J., Wellen, K., Makowski, L., Rathmell, J., Fingleton, B., & Hasty, A. H. (2024) · bioRxiv · doi:10.1101/2024.09.25.614811
“TREM2 is a transmembrane receptor of the immunoglobulin superfamily that binds a plethora of ligands including bacterial products, DNA, lipoproteins, and phospholipids 13 .”
BackgroundZhong, Z., Ulmschneider, M. B., & Lorenz, C. D. (2024) · bioRxiv · doi:10.1101/2024.03.08.584168
“11 The TREM2 pathway is first triggered when the N-terminus of TREM2 binds to ligands in the extracellular domain, which activates downstream pathways that involve a stable interaction between TREM2 and DAP10/12.”
BackgroundUpregulation of Trem2 expression occurs exclusively on microglial contact with plaquesPreprint
Wood, J. I., Wong, E., Joghee, R., Balbaa, A., Vitanova, K. S., VanSchoiack, A., Phelan, S.-L. J., Launchbury, F., Desai, S., Tripathi, T., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.01.26.477873
“A possible candidate would be a phospholipid, such as phosphoserine that has been suggested to be an “eat me” signals on damaged synapses (Kober and Brett, 2017; Scott-Hewitt et al., 2020).”
BackgroundMicroglia, TREM2, and Therapeutic Methods of Alzheimer’s Disease
Xu, S., Ji, Y., Sha, T., & Li, H. (2021) · IntechOpen eBooks · doi:10.5772/intechopen.100203
“TREM2 was thought to bind a wide range of molecules [60], and the interaction with different ligands can regulate the signal intensity and direction of TREM2 in turn [61].”
BackgroundHall-Roberts, H., Obst, J., Smith, T. B., Daniel, E. D., Mead, E. J., James, W., Davis, J. B., & Cowley, S. (2020) · doi:10.21203/rs.3.rs-16214/v1
“36 37 Figure 4 Syk activation during contact with dead SH-SY5Ys is blunted in TREM2 KO pMac, but not R47H TREM2 pMac.”
BackgroundInfluentialSuandika, M., Handayani, R., & Muti, R. T. (2025) · BIO Web of Conferences · doi:10.1051/bioconf/202515201002
“However, unlike TLRs, the signaling pathway of TREM2 is still poorly understood although it appears to induce ERK1/2 phosphorilation and F-actin reorganization [31].”
Metadata
- Authors
- Kober, D. L., & Brett, T. J.
- Affiliations
- Washington University in St. Louis (US)
- Corresponding author
- Brett, Tom J.
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 2017-06
- Volume
- 429
- Issue
- 11
- Pages
- 1607-1629
- ISSN
- 0022-2836 (ISSN-L)
- PMC
- PMC5485854
- OpenAlex
- W2606080622
- Cited by
- 284
- References
- 161
- Citations by year
- 2026: 28 · 2025: 50 · 2024: 39 · 2023: 56 · 2022: 24 · 2021: 39 · 2020: 19 · 2019: 14 · 2018: 11 · 2017: 4
- FWCI
- 1.27
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute on Aging (P50AG005681)
- National Heart, Lung, and Blood Institute (R01HL119813)
- National Institute of General Medical Sciences (T32GM007067)
- Topics
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Life Sciences › Immunology and Microbiology › Immunology › Inflammation biomarkers and pathways
- Life Sciences › Immunology and Microbiology › Immunology › Phagocytosis and Immune Regulation
- Keywords
- TREM2, myeloid cell activation, Alzheimer's disease, neurodegenerative diseases, chronic obstructive pulmonary disease, multiple sclerosis, stroke, receptor signaling, inflammatory diseases
- MeSH terms
- Animals, Disease Models, Animal, Health, Humans, Membrane Glycoproteins, Protein Binding, Receptors, Immunologic, Neurodegenerative Diseases
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
