The Chemokine-like Receptor 1 Deficiency Improves Cognitive Deficits of AD Mice and Attenuates Tau Hyperphosphorylation via Regulating Tau Seeding
Open accessAbstract
Pathologic features of Alzheimer9s disease (AD) include accumulation of amyloid β (Aβ) and hyperphosphorylated tau protein. We have shown previously that the chemokine-like receptor 1 (CMKLR1) is a functional receptor for Aβ, and CMKLR1 contributes to the uptake of Aβ. However, it is unclear whether CMKLR1 ameliorates or aggravates the process of AD. Here, we show that deletion of the gene coding for CMKLR1 significantly increased Aβ deposits in brains of both male and female amyloid β precursor protein/presenilin-1 mice. However, it markedly decreased the mortality of these mice. Behavioral studies found that CMKLR1 deficiency improved cognitive impairment of male and female amyloid β precursor protein/presenilin-1 mice and intracerebroventricular-streptozotocin injection AD mice. We further explored the effect of CMKLR1 on tau pathology. We found that CMKLR1 deficiency or inhibition attenuated the hyperphosphorylation of tau in brains of AD mice in vivo and in the neuronal cells in vitro. The expression of CMKLR1 on the neurons affected tau phosphorylation by participating in tau seeding. Together, these results uncover a novel mechanism of CMKLR1 in the pathologic process of AD and suggest that inhibiting the promotion effect of CMKLR1 on tau seeding may provide a new strategy for the treatment of AD. SIGNIFICANCE STATEMENT Evidence suggests that inflammation is involved in the pathologic progression of AD. The chemokine-like receptor 1 (CMKLR1), belonging to the family of GPCRs, is able to bind and uptake amyloid β. We show here, for the first time, that, although CMKLR1 deficiency increased amyloid β deposits in AD mice, it reduced the mortality and improved the cognitive deficits of AD mice. We furthermore show that CMKLR1 deficiency or inhibition attenuated tau hyperphosphorylation in brains of AD model mice in vivo and in neuronal cells in vitro. Finally, we first discovered that the expression of CMKLR1 on neurons affected tau phosphorylation by participating in tau seeding. These findings suggest that inhibition of CMKLR1 may provide a new strategy for the treatment of AD.
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Increasing evidence demonstrates that cognitive dysfunction and disease severity are more related to tau pathology.
“Increasing evidence demonstrates that the cognitive dysfunction and severity of the disease are more related to tau pathology [11–14].”
From Tau and neuroinflammation in Alzheimer’s disease: interplay mechanisms and clinical translation (2023) · cites this paper as [14]
Tau pathology is more associated with cognitive dysfunction than Aβ pathology, making tau a potential therapeutic target.
“Tau has received increasing attention as a potential therapeutic target, since evidence indicates that tau pathology is more associated with cognitive dysfunction.”
From Tau and neuroinflammation in Alzheimer’s disease: interplay mechanisms and clinical translation (2023) · cites this paper as [14]
CMKLR1 deletion increases Aβ plaques in the AD mouse brain but reduces mortality and cognitive deficits of AD mice and attenuates tau hyperphosphorylation.
“Our recent study identified that CMKLR1 deletion increases Aβ plaques in the AD mouse brain but reduces mortality and cognitive deficits of AD mice and attenuates tau hyperphosphorylation [14].”
From Tau and neuroinflammation in Alzheimer’s disease: interplay mechanisms and clinical translation (2023) · cites this paper as [14]
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Zhang, Y., Xu, N., Ding, Y. P., Doycheva, D. M., Zhang, Y., Li, Q., Flores, J. J., Haghighiabyaneh, M., Tang, J., & Zhang, J. H. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-1374-y · Cited by 69 · see citing works
Self-citationRetractedPlace navigation impaired in rats with hippocampal lesions
Morris, R. G. M., Garrud, P., Rawlins, J. N. P., & O'Keefe, J. (1982) · Nature · doi:10.1038/297681a0 · Cited by 6,340 · see citing works
Neuroinflammation in Alzheimer's disease
Heneka, M. T., Carson, M. J., Khoury, J. E., Landreth, G. E., Brosseron, F., Feinstein, D. L., Jacobs, A. H., Wyss-Coray, T., Vitorica, J., Ransohoff, R. M., et al. (2015) · The Lancet Neurology · doi:10.1016/s1474-4422(15)70016-5 · Cited by 6,226 · see citing works
Zhang, Y., Chen, K., Sloan, S. A., Bennett, M. L., Scholze, A. R., O'Keeffe, S., Phatnani, H. P., Guarnieri, P., Caneda, C., Ruderisch, N., et al. (2014) · The Journal of Neuroscience · doi:10.1523/jneurosci.1860-14.2014 · Cited by 4,875 · see citing works
Self-citationZhang, Y., Sloan, S. A., Clarke, L. E., Caneda, C., Plaza, C. A., Blumenthal, P. D., Vogel, H., Steinberg, G. K., Edwards, M. S. B., Li, G., et al. (2016) · Neuron · doi:10.1016/j.neuron.2015.11.013 · Cited by 2,295 · see citing works
Self-citationDepletion of microglia and inhibition of exosome synthesis halt tau propagation
Asai, H., Ikezu, S., Tsunoda, S., Medalla, M., Luebke, J., Haydar, T., Wolozin, B., Butovsky, O., Kügler, S., & Ikezu, T. (2015) · Nature Neuroscience · doi:10.1038/nn.4132 · Cited by 1,591 · see citing works
Wyss-Coray (2006) · doi:10.1038/nm1484 · Cited by 1,284 · see citing works
Tau in Alzheimer Disease and Related Tauopathies
Iqbal, K., Liu, F., Gong, C., & Grundke, I. (2010) · Current Alzheimer Research · doi:10.2174/156720510793611592 · Cited by 1,122 · see citing works
El Khoury, J., Toft, M., Hickman, S. E., Means, T. K., Terada, K., Geula, C., & Luster, A. D. (2007) · Nature Medicine · doi:10.1038/nm1555 · Cited by 915 · see citing works
Wittamer, V., Franssen, J.-D., Vulcano, M., Mirjolet, J.-F., Le Poul, E., Migeotte, I., Brézillon, S., Tyldesley, R., Blanpain, C., Detheux, M., et al. (2003) · The Journal of Experimental Medicine · doi:10.1084/jem.20030382 · Cited by 888 · see citing works
Astrocyte function from information processing to cognition and cognitive impairment
Santello, M., Toni, N., & Volterra, A. (2019) · Nature Neuroscience · doi:10.1038/s41593-018-0325-8 · Cited by 737 · see citing works
Characterization of the Drosophila melanogaster genome at the nuclear lamina
Pickersgill, H., Kalverda, B., de Wit, E., Talhout, W., Fornerod, M., & van Steensel, B. (2006) · Nature Genetics · doi:10.1038/ng1852 · Cited by 656 · see citing works
Maphis, N., Xu, G., Kokiko-Cochran, O. N., Jiang, S., Cardona, A., Ransohoff, R. M., Lamb, B. T., & Bhaskar, K. (2015) · Brain · doi:10.1093/brain/awv081 · Cited by 595 · see citing works
Saito, K., Elce, J. S., Hamos, J. E., & Nixon, R. A. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.7.2628 · Cited by 579 · see citing works
Yanamandra, K., Kfoury, N., Jiang, H., Mahan, T. E., Ma, S., Maloney, S. E., Wozniak, D. F., Diamond, M. I., & Holtzman, D. M. (2013) · Neuron · doi:10.1016/j.neuron.2013.07.046 · Cited by 574 · see citing works
Schweers, O., Schönbrunn, E., Marx, A., & Mandelkow�, E. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)51080-8 · Cited by 569 · see citing works
Mechanisms of Aβ Clearance and Degradation by Glial Cells
Ries, M., & Sastre, M. (2016) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2016.00160 · Cited by 527 · see citing works
DeVos, S. L., Miller, R. L., Schoch, K. M., Holmes, B. B., Kebodeaux, C. S., Wegener, A. J., Chen, G., Shen, T., Tran, H., Nichols, B., et al. (2017) · Science Translational Medicine · doi:10.1126/scitranslmed.aag0481 · Cited by 516 · see citing works
Microglia and Astrocytes in Alzheimer's Disease: Implications for Therapy
Fakhoury, M. (2017) · Current Neuropharmacology · doi:10.2174/1570159x15666170720095240 · Cited by 482 · see citing works
Heparan sulfate proteoglycan as a cell-surface endocytosis receptor
Christianson, H. C., & Belting, M. (2014) · Matrix Biology · doi:10.1016/j.matbio.2013.10.004 · Cited by 429 · see citing works
Synthetic chemerin-derived peptides suppress inflammation through ChemR23
Cash, J. L., Hart, R., Russ, A., Dixon, J. P. C., Colledge, W. H., Doran, J., Hendrick, A. G., Carlton, M. B. L., & Greaves, D. R. (2008) · The Journal of Experimental Medicine · doi:10.1084/jem.20071601 · Cited by 372 · see citing works
Takeda, S., Wegmann, S., Cho, H., DeVos, S. L., Commins, C., Roe, A. D., Nicholls, S. B., Carlson, G. A., Pitstick, R., Nobuhara, C. K., et al. (2015) · Nature Communications · doi:10.1038/ncomms9490 · Cited by 371 · see citing works
Yang, T., Li, S., Xu, H., Walsh, D. M., & Selkoe, D. J. (2017) · The Journal of Neuroscience · doi:10.1523/jneurosci.1698-16.2016 · Cited by 347 · see citing works
Inhibition of Stat3‐mediated astrogliosis ameliorates pathology in an Alzheimer's disease model
Reichenbach, N., Delekate, A., Plescher, M., Schmitt, F., Krauss, S., Blank, N., Halle, A., & Petzold, G. C. (2019) · EMBO Molecular Medicine · doi:10.15252/emmm.201809665 · Cited by 343 · see citing works
TREM2 function impedes tau seeding in neuritic plaques
Leyns, C. E. G., Gratuze, M., Narasimhan, S., Jain, N., Koscal, L. J., Jiang, H., Manis, M., Colonna, M., Lee, V. M. Y., Ulrich, J. D., et al. (2019) · Nature Neuroscience · doi:10.1038/s41593-019-0433-0 · Cited by 332 · see citing works
GSK3: a possible link between beta amyloid peptide and tau protein
Hernández, F., Gómez de Barreda, E., Fuster-Matanzo, A., Lucas, J. J., & Avila, J. (2010) · Experimental Neurology · doi:10.1016/j.expneurol.2009.09.011 · Cited by 327 · see citing works
Tau Oligomers: Cytotoxicity, Propagation, and Mitochondrial Damage
Shafiei, S. S., Guerrero-Muñoz, M. J., & Castillo-Carranza, D. L. (2017) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2017.00083 · Cited by 314 · see citing works
Takashima, A., Honda, T., Yasutake, K., Michel, G., Murayama, O., Murayama, M., Ishiguro, K., & Yamaguchi, H. (1998) · Neuroscience Research · doi:10.1016/s0168-0102(98)00061-3 · Cited by 287 · see citing works
Chen, Y., Liang, Z., Blanchard, J., Dai, C., Sun, S., Lee, M. H., Grundke, I., Iqbal, K., Liu, F., & Gong, C. (2012) · Molecular Neurobiology · doi:10.1007/s12035-012-8375-5 · Cited by 286 · see citing works
Self-citationSynaptic Tau Seeding Precedes Tau Pathology in Human Alzheimer’s Disease Brain
DeVos, S. L., Corjuc, B. T., Oakley, D. H., Nobuhara, C. K., Bannon, R. N., Chase, A., Commins, C., Gonzalez, J. A., Dooley, P. M., Frosch, M. P., et al. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00267 · Cited by 285 · see citing works
Tracy, T. E., Sohn, P. D., Minami, S. S., Wang, C., Min, S.-W., Li, Y., Zhou, Y., Le, D., Lo, I., Ponnusamy, R., et al. (2016) · Neuron · doi:10.1016/j.neuron.2016.03.005 · Cited by 277 · see citing works
Amyloid β42Activates a G-Protein-Coupled Chemoattractant Receptor, FPR-Like-1
Le, Y., Gong, W., Tiffany, H. L., Tumanov, A. V., Nedospasov, S. A., Shen, W., Dunlop, N. M., Gao, J., Murphy, P. M., Oppenheim, J. J., et al. (2001) · Journal of Neuroscience · doi:10.1523/jneurosci.21-02-j0003.2001 · Cited by 272 · see citing works
Loss of Bin1 Promotes the Propagation of Tau Pathology
Calafate, S., Flavin, W., Verstreken, P., & Moechars, D. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.09.063 · Cited by 265 · see citing works
Microglial Aβ Receptors in Alzheimer’s Disease
Yu, Y., & Ye, R. D. (2015) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-014-0101-6 · Cited by 247 · see citing works
Self-citationSynaptogyrin-3 Mediates Presynaptic Dysfunction Induced by Tau
McInnes, J., Wierda, K., Snellinx, A., Bounti, L., Wang, Y.-C., Stancu, I.-C., Apóstolo, N., Gevaert, K., Dewachter, I., Spires-Jones, T. L., et al. (2018) · Neuron · doi:10.1016/j.neuron.2018.01.022 · Cited by 242 · see citing works
Absence of CX3CR1 impairs the internalization of Tau by microglia
Bolós, M., Llorens-Martín, M., Perea, J. R., Jurado-Arjona, J., Rábano, A., Hernández, F., & Avila, J. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0200-1 · Cited by 231 · see citing works
Frenkel, D., Wilkinson, K., Zhao, L., Hickman, S. E., Means, T. K., Puckett, L., Farfara, D., Kingery, N. D., Weiner, H. L., & El Khoury, J. (2013) · Nature Communications · doi:10.1038/ncomms3030 · Cited by 214 · see citing works
Characterization of human circulating TIG2 as a ligand for the orphan receptor ChemR23
Meder, W., Wendland, M., Busmann, A., Kutzleb, C., Spodsberg, N., John, H., Richter, R., Schleuder, D., Meyer, M., & Forssmann, W. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)01312-7 · Cited by 205 · see citing works
Pathways by Which Aβ Facilitates Tau Pathology
Blurton-Jones, M. M., & LaFerla, F. M. (2006) · Current Alzheimer Research · doi:10.2174/156720506779025242 · Cited by 195 · see citing works
Kennedy, A. J., & Davenport, A. P. (2017) · Pharmacological Reviews · doi:10.1124/pr.116.013177 · Cited by 175 · see citing works
Truncation and Activation of Calcineurin A by Calpain I in Alzheimer Disease Brain
Liu, F., Grundke, I., Iqbal, K., Oda, Y., Tomizawa, K., & Gong, C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m507475200 · Cited by 171 · see citing works
Propagation of Tau via Extracellular Vesicles
Pérez, M., Avila, J., & Hernández, F. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00698 · Cited by 118 · see citing works
Feng, Y., Xia, Y., Yu, G., Shu, X., Ge, H., Zeng, K., Wang, J., & Wang, X. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12285 · Cited by 103 · see citing works
p35/Cdk5 pathway mediates soluble amyloid‐β peptide‐induced tau phosphorylation in vitro
Town, T., Zolton, J., Shaffner, R., Schnell, B., Crescentini, R. M., Wu, Y., Zeng, J., DelleDonne, A., Obregon, D. F., Tan, J., et al. (2002) · Journal of Neuroscience Research · doi:10.1002/jnr.10299 · Cited by 102 · see citing works
Dai, C.-L., Hu, W., Tung, Y. C., Liu, F., Gong, C.-X., & Iqbal, K. (2018) · Alzheimer's Research & Therapy · doi:10.1186/s13195-018-0341-7 · Cited by 99 · see citing works
TIA1 regulates the generation and response to toxic tau oligomers
Jiang, L., Ash, P. E. A., Maziuk, B. F., Ballance, H. I., Boudeau, S., Abdullatif, A. A., Orlando, M., Petrucelli, L., Ikezu, T., & Wolozin, B. L. (2018) · Acta Neuropathologica · doi:10.1007/s00401-018-1937-5 · Cited by 99 · see citing works
Lee, H. J., Ryu, J. M., Jung, Y., Lee, S.-J., Kim, J. Y., Lee, S.-H., Hwang, I., Seong, J., & Han, H. (2016) · Scientific Reports · doi:10.1038/srep36746 · Cited by 75 · see citing works
Targeting Insulin Signaling for the Treatment of Alzheimer's Disease
Chen, Y., Zhang, J., Zhang, B., & Gong, C. (2015) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026615666150813142423 · Cited by 59 · see citing works
Self-citationLi, S.-Q., Yu, Y., Han, J.-Z., Wang, D., Liu, J., Qian, F., Fan, G.-H., Bucala, R., & Ye, R. D. (2015) · Journal of Neuroinflammation · doi:10.1186/s12974-015-0396-3 · Cited by 59 · see citing works
Self-citationThe Chemerin Receptor CMKLR1 is a Functional Receptor for Amyloid-β Peptide
Lei, P., Yu, Y., Liu, J., Li, S., He, H., Cheng, N., & Ye, R. D. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-141227 · Cited by 59 · see citing works
Self-citationNeves, K. B., Cat, A. N. D., Alves-Lopes, R., Harvey, K. Y., da Costa, R. M., Lobato, N. S., Montezano, A. C., de Oliveira, A. M., Touyz, R. M., & Tostes, R. C. (2018) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00285.2018 · Cited by 53 · see citing works
Tau secretion is correlated to an increase of Golgi dynamics
Mohamed, N., Desjardins, A., & Leclerc, N. M. (2017) · PLoS ONE · doi:10.1371/journal.pone.0178288 · Cited by 50 · see citing works
Amyloid-β Modulates Both AβPP and Tau Phosphorylation
Oliveira, J. M., Henriques, A. G., Martins, F., Rebelo, S., & Silva, O. A. B. D. C. E. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-142664 · Cited by 47 · see citing works
High-glucose induces tau hyperphosphorylation through activation of TLR9-P38MAPK pathway
Sun, Y., Xiao, Q., Luo, C., Zhao, Y., Pu, D., Zhao, K., Chen, J., Wang, M., & Liao, Z. (2017) · Experimental Cell Research · doi:10.1016/j.yexcr.2017.07.032 · Cited by 45 · see citing works
CCR2/CCL2-mediated inflammation protects photoreceptor cells from amyloid-β-induced apoptosis
Bruban, J., Maoui, A., Chalour, N., An, N., Jonet, L., Feumi, C., Tréton, J., Sennlaub, F., Béhar‐Cohen, F., Mascarelli, F., et al. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.01.004 · Cited by 28 · see citing works
Nie, S., Li, X., Tang, C., Min, F.-Y., Shi, X., Wu, L., Zhou, S., Chen, Z., Wu, J., Song, T., et al. (2018) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2018.03.023 · Cited by 26 · see citing works
Zhang, H., Wang, D., Gong, P., Lin, A., Zhang, Y., Ye, R. D., & Yu, Y. (2019) · Journal of Alzheimer's Disease · doi:10.3233/jad-180823 · Cited by 26 · see citing works
Self-citationHigh-yield purification of fetal tau preserving its structure and phosphorylation pattern
Ivanovova, N. P., Handzusova, M., Hanes, J., Kontseková, E., & Novák, M. (2008) · Journal of Immunological Methods · doi:10.1016/j.jim.2008.07.014 · Cited by 10 · see citing works
Yang, T., Li, S., Xu, H., Walsh, D. M., & Selkoe, D. J. (2017) · Journal of Neuroscience · doi:10.1523/jneurosci.1698-16.2017 · Cited by 7 · see citing works
Ye, R. D. (2016) · The FASEB Journal · doi:10.1096/fasebj.30.1_supplement.707.7 · Cited by 1 · see citing works
Self-citation
Flagged first, then by citations
Cited by
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Chen, Y., & Yu, Y. (2023) · Journal of Neuroinflammation · doi:10.1186/s12974-023-02853-3 · Cited by 516 · see citing works
“Our recent study identified that CMKLR1 deletion increases Aβ plaques in the AD mouse brain but reduces mortality and cognitive deficits of AD mice and attenuates tau hyperphosphorylation [14].”
BackgroundSelf-citationZhang, J., Liu, L., Zhang, Y., Yuan, Y., Miao, Z., Lu, K., Zhang, X., Ni, R., Zhang, H., Zhao, Y., et al. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102554 · Cited by 58 · see citing works
Self-citationZhang, H., Xue, K., Li, W., Yang, X., Gou, Y., Su, X., Qian, F., & Sun, L. (2024) · Nature Communications · doi:10.1038/s41467-023-44168-0 · Cited by 31 · see citing works
Self-citationHuang, X., Wang, Y., & Xiang, Y. (2022) · EBioMedicine · doi:10.1016/j.ebiom.2022.104263 · Cited by 31 · see citing works
Gong, P., Chen, Y.-Q., Lin, A.-H., Zhang, H.-B., Zhang, Y., Ye, R. D., & Yu, Y. (2020) · Alzheimer's Research & Therapy · doi:10.1186/s13195-020-00714-2 · Cited by 29 · see citing works
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Yun, H., Dumbell, R., Hanna, K., Bowen, J., McLean, S. L., Kantamneni, S., Pors, K., Wu, Q., & Helfer, G. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.897105 · Cited by 29 · see citing works
Liu, L., Zhang, J., Lu, K., Zhang, Y., Xiaofeng, X., Deng, J., Zhang, X., Zhang, H., Zhao, Y., & Wang, X. (2024) · Journal of Translational Medicine · doi:10.1186/s12967-023-04813-0 · Cited by 27 · see citing works
Self-citationChen, Y., Liu, Z., Gong, P., Zhang, H., Chen, Y., Yao, S., Li, W., Zhang, Y., & Yu, Y. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23169041 · Cited by 25 · see citing works
Self-citationThe Hidden Role of Non-Canonical Amyloid β Isoforms in Alzheimer’s Disease
Busch, L., Eggert, S., Endres, K., & Bufe, B. (2022) · Cells · doi:10.3390/cells11213421 · Cited by 19 · see citing works
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Skv, M., Abraham, S. M., Eshwari, O., Golla, K., Jhelum, P., Maity, S., & Komal, P. (2024) · Molecular Neurobiology · doi:10.1007/s12035-024-03989-w · Cited by 18 · see citing works
Cheng, Z.-Y., Hu, Y., Xia, Q.-P., Wang, C., & He, L. (2021) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2021.07.015 · Cited by 13 · see citing works
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Rosal, A. E., Martin, S. L., & Strafella, A. P. (2025) · Frontiers in Neuroscience · doi:10.3389/fnins.2025.1515374 · Cited by 10 · see citing works
Zheng, J., Wang, H., Wu, W., Wang, L., Qin, M., Zhu, L., Liu, Z., Chen, Y., & Yu, Y. (2025) · Journal of Neuroinflammation · doi:10.1186/s12974-025-03408-4 · Cited by 11 · see citing works
Self-citationLiu, Z., Chen, Y., Chen, Y., Zheng, J., Wu, W., Wang, L., Wang, H., & Yu, Y. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25084324 · Cited by 7 · see citing works
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Liu, C., Wang, Q., Xin, J., Liu, Y., Zeng, F., Chen, D., Li, H.-Y., Yi, X., Zeng, G., Wang, Y., et al. (2023) · Journal of Alzheimer s Disease · doi:10.3233/jad-220860 · Cited by 2 · see citing works
Self-citationChinnathambi, S., Rangappa, N., Velmurugan, G., & Chandrashekar, M. (2025) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2025.10.018 · Cited by 1 · see citing works
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- Authors
- Zhang, H., Lin, A., Gong, P., Chen, Y., Ye, R. D., Qian, F., Zhang, Y., & Yu, Y.
- Affiliations
- Shanghai Jiao Tong University (CN)
- Chinese University of Hong Kong (HK)
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2020-08-12
- Volume
- 40
- Issue
- 36
- Pages
- 6991-7007
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC7470913
- OpenAlex
- W3048952353
- Cited by
- 24
- References
- 60
- Citations by year
- 2026: 3 · 2025: 5 · 2024: 5 · 2023: 2 · 2022: 5 · 2021: 2 · 2020: 2
- FWCI
- 1.65
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Neuroscience (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Natural Science Foundation of China (81571027, 81870835)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- CMKLR1, Alzheimer's disease, amyloid-beta, tau hyperphosphorylation, tau seeding, cognitive impairment, G protein-coupled receptors, amyloid-beta uptake, neuroinflammation, therapeutic target
- MeSH terms
- Alzheimer Disease, Animals, Cells, Cultured, Cognition, Female, Male, Mice, Inbred C57BL, Neurons, Phosphorylation, Amyloid beta-Protein Precursor, tau Proteins, Gene Deletion, Receptors, Chemokine, Cell Line, Tumor, Mice, Presenilin-1
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 ›
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