The DOI matches its Crossref record; 194 of the 194 references it cites were found in a registry or an index.
The SYK tyrosine kinase: a crucial player in diverse biological functions
Open accessAbstract
Spleen tyrosine kinase (SYK) is known to have a crucial role in adaptive immune receptor signalling. However, recent reports indicate that SYK also mediates other, unexpectedly diverse biological functions, including cellular adhesion, innate immune recognition, osteoclast maturation, platelet activation and vascular development. SYK is activated by C-type lectins and integrins, and activates new targets, including the CARD9-BCL-10-MALT1 pathway and the NLRP3 inflammasome. Studies using Drosophila melanogaster suggest that there is an evolutionarily ancient origin of SYK-mediated signalling. Moreover, SYK has a crucial role in autoimmune diseases and haematological malignancies. This Review summarizes our current understanding of the diverse functions of SYK and how this is being translated for therapeutic purposes.
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 cited source says what the claim attributes to it.
In the citing paper
“SYK is perhaps best known for the critical role that it plays in mounting protective antifungal immune responses downstream of C-type lectin (CLEC) receptors expressed on innate immune cells (Lionakis et al., 2017; Mocsai et al., 2010).”
From SYK coordinates neuroprotective microglial responses in neurodegenerative disease (2022) · cites this paper as Mocsai et al., 2010
In the citing paper
“However, recent studies indicate that it is also involved in innate immunity and non-immune functions.”
From The Role of Reactive Species on Innate Immunity (2022) · cites this paper as [96]
In the citing paper
“Upon ITAM phosphorylation, the SYK tyrosine kinase is recruited to the receptor and its activation leads to downstream phosphorylation events including activation of SHP-1 and RAC (11, 12)”
From Macrophage defense mechanisms against intracellular bacteria (2015) · cites this paper as [11]
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
Mizgerd, J. P., Kubo, H., Kutkoski, G. J., Bhagwan, S. D., Scharffetter-Kochanek, K., Beaudet, A. L., & Doerschuk, C. M. (1997) · The Journal of Experimental Medicine · doi:10.1084/jem.186.8.1357 · Cited by 7,332
The Inflammasomes: Guardians of the Body
Martinon, F., Mayor, A., & Tschopp, J. (2009) · Annual Review of Immunology · doi:10.1146/annurev.immunol.021908.132715 · Cited by 2,436
Chronic active B-cell-receptor signalling in diffuse large B-cell lymphoma
Davis, R. E., Ngo, V. N., Lenz, G., Tolar, P., Young, R. M., Romesser, P. B., Kohlhammer, H., Lamy, L., Zhao, H., Yang, Y., et al. (2010) · Nature · doi:10.1038/nature08638 · Cited by 1,651
Signalling through C-type lectin receptors: shaping immune responses
Geijtenbeek, T. B. H., & Gringhuis, S. I. (2009) · Nature reviews. Immunology · doi:10.1038/nri2569 · Cited by 1,449
Reth, M. G. (1989) · Nature · doi:10.1038/338383b0 · Cited by 1,430
Daëron, M. (1997) · Annual Review of Immunology · doi:10.1146/annurev.immunol.15.1.203 · Cited by 1,227
LeibundGut-Landmann, S., Groß, O., Robinson, M. J., Osorio, F., Slack, E. C., Tsoni, S. V., Schweighoffer, E., Tybulewicz, V., Brown, G. D., Ruland, J., et al. (2007) · Nature Immunology · doi:10.1038/ni1460 · Cited by 1,191
Self-citationDectin-1: a signalling non-TLR pattern-recognition receptor
Brown, G. D. (2006) · Nature Reviews Immunology · doi:10.1038/nri1745 · Cited by 1,158
Syk kinase signalling couples to the Nlrp3 inflammasome for anti-fungal host defence
Groß, O., Poeck, H., Bscheider, M., Dostert, C., Hannesschläger, N., Endres, S., Hartmann, G., Tardivel, A., Schweighoffer, E., Tybulewicz, V. L. J., et al. (2009) · Nature · doi:10.1038/nature07965 · Cited by 947
Self-citationRogers, N. C., Slack, E. M. C., Edwards, A. D., Nolte, M. A., Schulz, O., Schweighoffer, E., Williams, D. L., Gordon, S., Tybulewicz, V. L. J., Brown, G. D., et al. (2005) · Immunity · doi:10.1016/j.immuni.2005.03.004 · Cited by 897
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Items 801–900 of 1,003
Progress in the development of kinase inhibitors for treating asthma and COPD
McClean, N., Hasday, J. D., & Shapiro, P. (2023) · Advances in pharmacology · doi:10.1016/bs.apha.2023.04.004 · Cited by 10
Cui, B., Wang, Y., Zhao, Z., Lü, F., Jiao, Y., Li, H., Feng, J., Tang, W., Lu, T., & Chen, Y. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115597 · Cited by 10
Wu, J., Yan, J., Hua, Z., Jia, J., Zhou, Z., Zhang, J., Li, J., & Zhang, J. (2023) · Genomics · doi:10.1016/j.ygeno.2023.110701 · Cited by 10
Geyer, C. E., Chen, H., Bye, A. P., Manz, X. D., Guerra, D., Caniels, T. G., Bijl, T. P. L., Griffith, G. R., Hoepel, W., de Taeye, S. W., et al. (2023) · Life Science Alliance · doi:10.26508/lsa.202302106 · Cited by 10
Samanta, S., Sk, M. F., Koirala, S., & Kar, P. (2023) · SAR and QSAR in environmental research · doi:10.1080/1062936x.2023.2266364 · Cited by 10
Danishuddin, M., Malik, M. Z., Kashif, M., Haque, S., & Kim, J. J. (2024) · SAR and QSAR in environmental research · doi:10.1080/1062936x.2024.2345618 · Cited by 10
., G. X., Liu, W., Lian, Z., Xie, D., Yuan, G., Ye, J., Lin, Z., Wang, W., Zeng, J., Shen, H., et al. (2021) · Biochemical Pharmacology · doi:10.1016/j.bcp.2021.114579 · Cited by 10
Martin, P. D., Cheung, S. Y. A., Yen, M., Han, D., & Gillen, M. S. (2015) · European Journal of Clinical Pharmacology · doi:10.1007/s00228-015-1961-5 · Cited by 10
The protein-tyrosine kinase Syk interacts with the C-terminal region of tensin2
Moon, K., Zhang, X., Zhou, Q., & Geahlen, R. (2011) · Biochimica et Biophysica Acta · doi:10.1016/j.bbamcr.2011.10.001 · Cited by 10
Bruton's tyrosine kinase inhibitors
Ysebaert, L., & Michallet, A. (2014) · Current Opinion in Oncology · doi:10.1097/cco.0000000000000114 · Cited by 10
Ryu, J., Woo, J., Shin, J., Ryoo, H., Kim, Y., & Lee, C. (2014) · Medicine · doi:10.1097/md.0000000000000281 · Cited by 10
Arsenic inhibits mast cell degranulation via suppression of early tyrosine phosphorylation events
Shim, J., Kennedy, R. H., Weatherly, L. M., Hutchinson, L. M., Pelletier, J. H., Hashmi, H. N., Blais, K., Velez, A., & Gosse, J. A. (2016) · Journal of Applied Toxicology · doi:10.1002/jat.3300 · Cited by 10
Role of Malt1 protease activity in pathogenesis of inflammatory disorders mediated by FcγR signaling
Nakamura, Y., Yokoyama, K., Igaki, K., & Tsuchimori, N. (2018) · International Immunopharmacology · doi:10.1016/j.intimp.2018.01.028 · Cited by 10
Park, S., Jang, J., & Moon, E. (2018) · Free Radical Research · doi:10.1080/10715762.2018.1505044 · Cited by 10
Wen, Y., & Shi, Y. (2019) · Current topics in microbiology and immunology · doi:10.1007/82_2019_153 · Cited by 10
Tartey, S., Gurung, P., Karki, R., Burton, A. R., Hertzog, P. J., & Kanneganti, T. (2020) · Cellular and Molecular Immunology · doi:10.1038/s41423-020-0398-7 · Cited by 10
The Serine/Threonine Protein Phosphatase 2A (PP2A) Regulates Syk Activity in Human Platelets
Makhoul, S., Kumm, E. J., Zhang, P., Walter, U., & Jurk, K. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21238939 · Cited by 10
Thiriet, M. (2012) · Biomathematical and biomechanical modeling of the circulatory and ventilatory systems · doi:10.1007/978-1-4614-4370-4_2 · Cited by 9
Chomyk, A., Kucinski, R., Kim, J., Christie, E., Cyncynatus, K., Gossman, Z., Chen, Z., Richardson, B., Cameron, M., Turner, T., et al. (2024) · Annals of Neurology · doi:10.1002/ana.26877 · Cited by 9
Targeting B Cells and Plasma Cells in Glomerular Disease
Ahmad, S. B., & Jefferson, J. A. (2025) · Journal of the American Society of Nephrology · doi:10.1681/asn.0000000772 · Cited by 10
3‐aminopyrazolopyrazine derivatives as spleen tyrosine kinase inhibitors
Shen, J., Li, X., Zhang, Z., Luo, J., Long, H., Tu, Z., Zhou, X., Ding, K., & Lu, X. (2016) · Chemical Biology & Drug Design · doi:10.1111/cbdd.12798 · Cited by 9
Serafin, V., Porcù, E., Cortese, G., Mariotto, E., Veltri, G., Bresolin, S., Basso, G., & Accordi, B. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20246175 · Cited by 9
Strand Displacement in Coiled‐Coil Structures: Controlled Induction and Reversal of Proximity
Gröger, K., Gavins, G. C., & Seitz, O. (2017) · Angewandte Chemie · doi:10.1002/ange.201705339 · Cited by 9
Wu, L., Xiao, F., Sun, J.-Y., Li, F., Chen, Y.-J., Chen, J., Zhang, J., Qian, L., & Wang, R. (2022) · Frontiers in Genetics · doi:10.3389/fgene.2022.971808 · Cited by 9
Activating FcγR function depends on endosomal-signaling platforms
Benadda, S., Nugue, M., Koumantou, D., Bens, M., Luca, M. D., Pellé, O., Monteiro, R. C., Evnouchidou, I., & Saveanu, L. (2023) · iScience · doi:10.1016/j.isci.2023.107055 · Cited by 9
PHGDH/SYK: a hub integrating anti-fungal immunity and serine metabolism
Chen, A., Zhang, X., Hu, D., Sun, X., Gu, Y., Zhou, Y., Su, C., Liu, S., Zhang, C., Wu, Q., et al. (2024) · Cell Death and Differentiation · doi:10.1038/s41418-024-01374-7 · Cited by 9
Graham, M., Abram, C. L., Hu, Y., & Lowell, C. A. (2013) · PLoS ONE · doi:10.1371/journal.pone.0077542 · Cited by 9
Protein-Protein Interaction Analysis Highlights Additional Loci of Interest for Multiple Sclerosis
Ragnedda, G., Disanto, G., Giovannoni, G., Ebers, G. C., Sotgiu, S., & Ramagopalan, S. V. (2012) · PLoS ONE · doi:10.1371/journal.pone.0046730 · Cited by 9
Matsuda, Y., Wang, X., Oishi, H., Guan, Z., Saito, M., Liu, M., Keshavjee, S. H., & Chow, C. (2015) · American Journal of Transplantation · doi:10.1111/ajt.13442 · Cited by 9
Sanches, R. C. O., Souza, C. D. L. R., & Oliveira, S. C. (2020) · Microbes and Infection · doi:10.1016/j.micinf.2020.08.001 · Cited by 9
Tung, M., Tsai, K., Fung, K.-M., Don, M., & Tseng, T. (2021) · RSC Advances · doi:10.1039/d0ra08769f · Cited by 9
Loss of NF1 in Melanoma Confers Sensitivity to SYK Kinase Inhibition
Abecunas, C., Whitehead, C. E., Ziemke, E. K., Baumann, D. G., Frankowski-McGregor, C. L., Sebolt, J. S., & Fallahi‐Sichani, M. (2022) · Cancer Research · doi:10.1158/0008-5472.can-22-0883 · Cited by 9
ABATACEPT FOR RHEUMATOID ARTHRITIS: A NOVEL FORMULATION, NEW MECHANISMS, NEW POSSIBILITIES
Nasonov, E. L. (2015) · Rheumatology Science and Practice · doi:10.14412/1995-4484-2015-522-541 · Cited by 9
Barrera‐Vargas, A., Gómez‐Martín, D., & Alcocer-Varela, J. C. (2014) · Human Immunology · doi:10.1016/j.humimm.2014.08.207 · Cited by 9
Liu, C., Su, P., Li, R., Zhang, Q., Zhu, T., Liu, X., & Li, Q. (2015) · Development Genes and Evolution · doi:10.1007/s00427-015-0492-5 · Cited by 9
Orally bioavailable Syk inhibitors with activity in a rat PK/PD model
Thoma, G., Veenstra, S. J., Strang, R. S., Blanz, J., Vangrevelinghe, E., Berghausen, J., Lee, C. C., & Zerwes, H. (2015) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2015.08.037 · Cited by 9
Dasgupta, N., Thakur, B. K., Ta, A., Dutta, P., & Das, S. (2016) · Journal of Cellular Biochemistry · doi:10.1002/jcb.25625 · Cited by 9
Novel therapeutic targets in Waldenstrom macroglobulinemia
Paulus, A., Ailawadhi, S., & Chanan-Khan, A. A. (2016) · Best Practice & Research Clinical Haematology · doi:10.1016/j.beha.2016.08.020 · Cited by 9
Non-receptor Tyrosine Kinases Role and Significance in Hematological Malignancies
Azevedo, A. P., Silva, S., & Rueff, J. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.84873 · Cited by 9
Tyrosine phosphorylation modulates cell surface expression of chloride cotransporters NKCC2 and KCC3
Loureiro, C. A., Barros, P., Matos, P., & Jordan, P. (2019) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2019.05.022 · Cited by 9
Tempest-Roe, S., Prendecki, M. F., McAdoo, S. P., Clarke, C., Tanna, A., Turner‐Stokes, T., Masuda, E. S., Willicombe, M. K., Cook, H. T., Roufosse, C. A., et al. (2022) · Scientific Reports · doi:10.1038/s41598-022-06413-2 · Cited by 9
van Buijtenen, E., Janssen, W., Vink, P. M., Habraken, M., Wingens, L., van Elsas, A., Huck, W. T. S., van Buggenum, J. A. G. L., & van Eenennaam, H. (2023) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2023.100492 · Cited by 10
Singh, R. (2016) · FEBS Open Bio · doi:10.1002/2211-5463.12149 · Cited by 9
Liang, K., Ma, N., Luo, S., Niu, W., Wang, Y., & Bu, P. (2019) · Medical Science Monitor · doi:10.12659/msm.913543 · Cited by 9
Chen, L., Zhu, F., Gao, X., Yang, Y., Jin, G., Zhou, Y., Dong, G., & Zhou, G. (2025) · International Immunopharmacology · doi:10.1016/j.intimp.2025.114122 · Cited by 8
Yuasa‐Kawada, J., Kinoshita-Kawada, M., Hiramoto, M., Yamagishi, S., Mishima, T., Yasunaga, S., Tsuboi, Y., Hattori, N., & Wu, J. Y. (2025) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-24-01330 · Cited by 10
SARS-CoV-2 Immune Complex–Mediated Neutrophil Activation
Allen, K. C., Warner, S., Teague, H., Ramos-Benítez, M. J., Miao, R., Tian, X., Reger, R. N., Burbelo, P. D., Pang, C. W. (., Kanthi, Y. M., et al. (2025) · Open Forum Infectious Diseases · doi:10.1093/ofid/ofaf199 · Cited by 8
Nguyen, J. M. H., Zolg, S., Geiss‐Friedlander, R., & Gorrell, M. D. (2025) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-025-05719-4 · Cited by 8
Cytoplasmic Protein Tyrosine Kinases
Thiriet, M. (2012) · Biomathematical and biomechanical modeling of the circulatory and ventilatory systems · doi:10.1007/978-1-4614-4370-4_4 · Cited by 8
Tseng, Y., Braun, A., Chang, J. P., Chiang, M.-L., Tseng, C., & Chen, W. (2018) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2018.12.016 · Cited by 8
Buffard, M., Naldi, A., Freiss, G., Deckert, M., Radulescu, O., Coopman, P. J., & Larive, R. M. (2021) · Biomolecules · doi:10.3390/biom11020308 · Cited by 8
Xu, J., Ma, J., Zeng, Y., Si, H., Wu, Y., Zhang, S., & Shen, B. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.941398 · Cited by 8
Németh, T., Balogh, L., Káposztás, E., Szilveszter, K. P., & Mócsai, A. (2023) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2022.12.016 · Cited by 8
Self-citationGuillet, E., Brun, É., Férard, C., Hardonnière, K., Nabhan, M., Legrand, F., Pallardy, M. J., & Biola‐Vidamment, A. (2023) · Particle and Fibre Toxicology · doi:10.1186/s12989-023-00527-9 · Cited by 8
Ferguson, R., Chat, V., Morales, L. J., Simpson, D., Monson, K. R., Cohen, E., Zusin, S., Madonna, G., Capone, M., Simeone, E., et al. (2023) · European Journal of Cancer · doi:10.1016/j.ejca.2023.05.011 · Cited by 8
GM-CSF receptor/SYK/JNK/FOXO1/CD11c signaling promotes atherosclerosis
Tsukui, D., Kimura, Y., & Kono, H. (2023) · iScience · doi:10.1016/j.isci.2023.107293 · Cited by 8
Liu, Y., Kim, J. H., Lim, H. K., Huang, L., Choi, W., Kopalli, S. R., Lee, S., Lee, B.-H., Lee, J. H., Ju, Y., et al. (2024) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2024.118386 · Cited by 8
Kim, J. G., Kim, M., Hong, B., Choe, Y., Kim, J., Lee, N., You, S., Lee, S.-I., & Kim, W. (2024) · Clinical Immunology · doi:10.1016/j.clim.2024.110425 · Cited by 8
Fargier, G., Favard, C., Parmeggiani, A., Sahuquet, A., Mérezègue, F., Morel, A., Denis, M., Molinari, N., Mangeat, P. H., Coopman, P. J., et al. (2012) · The FASEB Journal · doi:10.1096/fj.11-202465 · Cited by 8
Borna, Š., Fabišik, M., Ilievová, K., Dvoracek, T., & Brdička, T. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.013552 · Cited by 8
Bailey, E. M., Choudhury, A., Vuppula, H., Ortiz, D. F., Schaeck, J. J., Manning, A. M., Bosques, C. J., & Hoppe, A. D. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2020.617767 · Cited by 8
Nahm, J. H., Lee, H. S., Kim, H., Yim, S. Y., Shin, J., Yoo, J. E., Ahn, S. H., Choi, J. S., Lee, J., & Park, Y. N. (2021) · Liver International · doi:10.1111/liv.14835 · Cited by 8
De novo identification of maximally deregulated subnetworks based on multi-omics data with DeRegNet
Winkler, S., Winkler, I., Figaschewski, M., Tiede, T., Nordheim, A., & Kohlbacher, O. (2022) · BMC Bioinformatics · doi:10.1186/s12859-022-04670-6 · Cited by 8
Co-localization of Fibronectin Receptors LILRB4/gp49B and Integrin on Dendritic Cell Surface
Takahashi, N., Itoi, S., Su, M., Endo, S., & Takai, T. (2022) · The Tohoku Journal of Experimental Medicine · doi:10.1620/tjem.2022.j014 · Cited by 8
Denis, V., Cassagnard, N., Rio, M. D., Cornillot, E., Bec, N., Larroque, C., Jeanson, L., Jarlier, M., Combès, E., Robert, B., et al. (2022) · PLoS ONE · doi:10.1371/journal.pone.0274390 · Cited by 8
Wang, J., Wu, Y., Hu, H., Wang, W., Lü, Y., Mao, H.-M., Liu, X., Liu, Z., & Chen, B.-G. (2011) · Cellular Immunology · doi:10.1016/j.cellimm.2011.09.009 · Cited by 8
Spleen tyrosine kinase suppresses osteoblastic differentiation through MAPK and PKCα
Yoshida, K., Higuchi, C., Nakura, A., & Yoshikawa, H. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.07.023 · Cited by 8
Han, D., Zhang, M., Ma, J., Hong, J., Chen, C., Zhang, B., Huang, L., Lv, W., Yin, L., Zhang, A., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0046560 · Cited by 8
Kim, E., Son, Y., Yang, Y., Shen, T., Kim, I., Aravinthan, A., Kim, J., & Cho, J. Y. (2016) · Molecules · doi:10.3390/molecules21040508 · Cited by 8
Wang, G., Kuai, D., Yang, Y., Yang, G., Wei, Z., & Zhao, W. (2017) · Molecular Medicine Reports · doi:10.3892/mmr.2017.6273 · Cited by 8
Updates of cancer hallmarks in patients with inborn errors of immunity
Wang, Y., & Abolhassani, H. (2022) · Current Opinion in Allergy and Clinical Immunology · doi:10.1097/aci.0000000000000863 · Cited by 8
An inhibitor of spleen tyrosine kinase suppresses experimental crescentic glomerulonephritis
Han, Y., Ma, F. Y., Paolo, J. A. D., & Nikolic‐Paterson, D. J. (2018) · International Journal of Immunopathology and Pharmacology · doi:10.1177/2058738418783404 · Cited by 8
SYK Inhibition Potentiates the Effect of Chemotherapeutic Drugs on Neuroblastoma Cells In Vitro
Tümmler, C., Dumitriu, G., Wickström, M., Coopman, P. J., Valkov, A. Y., Kogner, P., Johnsen, J. I., Moens, U. L., & Sveinbjørnsson, B. (2019) · Cancers · doi:10.3390/cancers11020202 · Cited by 8
Lu, X. (2023) · Elsevier eBooks · doi:10.1016/b978-0-443-18611-0.00012-7 · Cited by 7
Elias, E. E., Lau, A. N., Belay, S. G., Derakhshani, A., Andonegui, G., Jenne, C. N., Dufour, A., Bracey, N. A., Chun, J., & Muruve, D. A. (2025) · JCI Insight · doi:10.1172/jci.insight.189601 · Cited by 7
Guanosine Triphosphatases and Their Regulators
Thiriet, M. (2012) · Biomathematical and biomechanical modeling of the circulatory and ventilatory systems · doi:10.1007/978-1-4614-4370-4_9 · Cited by 7
Hao, Y., Tang, X., Xing, J., Sheng, X., Chi, H., & Zhan, W. (2022) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2022.09.054 · Cited by 7
Treatment of congenital thrombocytopenia and decreased collagen reactivity in G6b-B–deficient mice
Mazharian, A., Maître, B., Bornert, A., Hennequin, D., Lourenco‐Rodrigues, M., Geer, M. J., Smith, C. W., Heising, S., Walter, M., Montel, F., et al. (2022) · Blood Advances · doi:10.1182/bloodadvances.2022008873 · Cited by 7
Osmanoğlu, Ö., Gupta, S. K., Almasi, A., Yagci, S., Srivastava, M., Araujo, G. H. M., Nagy, Z., Balkenhol, J., & Dandekar, T. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1285345 · Cited by 7
Role of non-receptor tyrosine kinases in epilepsy: significance and potential as therapeutic targets
Shanker, O. R., Kumar, S., Banerjee, J., Tripathi, M., Chandra, P. S., & Dixit, A. B. (2024) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2024.2343952 · Cited by 7
Animal models of studying the pathogenesis of multi-organ tissue damage in lupus
Wang, X., & Deng, G. (2024) · Clinical Immunology · doi:10.1016/j.clim.2024.110231 · Cited by 8
Syk inhibitors reduce tau protein phosphorylation and oligomerization
Yamaguchi, T., Hamano, T., Sada, K., Asano, R., Kanaan, N. M., Sasaki, H., Yen, S.-H. C., Kitazaki, Y., Endo, Y., Enomoto, S., et al. (2024) · Neurobiology of Disease · doi:10.1016/j.nbd.2024.106656 · Cited by 7
Single cell spatial profiling of FFPE splenic tissue from a humanized mouse model of HIV infection
Wu, G., Keller, S. H., Sardo, L., Magliaro, B. C., Zuck, P. D., Balibar, C. J., Williams, C., Pan, L., Gregory, M., Ton, K., et al. (2024) · Biomarker Research · doi:10.1186/s40364-024-00658-x · Cited by 7
Li, C., Zhang, H., Liu, Y., Zhang, T., & Gu, F. (2025) · Scientific Reports · doi:10.1038/s41598-025-02447-4 · Cited by 7
do Nascimento, E. F., Batista, P. V. C., Cunha, C. S., Lacerda, L. R. A., de Moura, V. C., Oliveira, T. D. Q., Filho, A. J. M. C., de Rezende, P. H. F., Macêdo, D. S., & Vasconcelos, S. M. M. (2025) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5c00221 · Cited by 7
A SYK/SHC1 pathway regulates the amount of CFTR in the plasma membrane
Loureiro, C. A., Pinto, F. R., Barros, P., Matos, P., & Jordan, P. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03448-4 · Cited by 7
Novel potent and selective pyrazolylpyrimidine-based SYK inhibitors
Barlaam, B. C., Boiko, S., Boyd, S., Dry, H., Gingipalli, L., Ikeda, T. P., Johnson, T., Kawatkar, S. P., Lorthioir, O., Pike, A., et al. (2020) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2020.127523 · Cited by 7
Mice with Established Diabetes Show Increased Susceptibility to Renal Ischemia/Reperfusion Injury
Grynberg, K., Tian, L., Tesch, G. H., Ozols, E., Mulley, W. R., Nikolic‐Paterson, D. J., & Ma, F. Y. (2021) · American Journal Of Pathology · doi:10.1016/j.ajpath.2021.12.003 · Cited by 7
Sender, S., Sultan, A. W., Palmer, D. H., Koczan, D., Sekora, A., Beck, J., Schütz, E., Taher, L., Brenig, B., Fuellen, G., et al. (2022) · Cancers · doi:10.3390/cancers14194691 · Cited by 7
Ullah, I., Barrie, U., Kernen, R. M., Mamula, E. T., Khuong, F. T. H., Booshehri, L. M., Rhodes, E. L., Bradford, J. M., Datta, A., & Wetzel, D. M. (2023) · Journal of Cell Science · doi:10.1242/jcs.260809 · Cited by 7
Expanding Our Knowledge of Molecular Pathogenesis in Histiocytoses
Crowley, H. M., Georgantzoglou, N., Tse, J. Y., Williams, E. A., Mata, D. A., Martin, S. S., Guitart, J., Bridge, J. A., & Linos, K. D. (2023) · The American Journal of Surgical Pathology · doi:10.1097/pas.0000000000002102 · Cited by 7
Controling the cytoskeleton during CEACAM3-mediated phagocytosis
Kuiper, J. W., Gregg, H. L., Schüber, M., Klein, J., & Hauck, C. R. (2024) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2024.151384 · Cited by 7
Qiao, J., Arthur, J. F., Collecutt, M. F., Shen, Y., Mu, F., Berndt, M. C., Davis, A. K., Andrews, R. K., & Gardiner, E. E. (2012) · Acta Haematologica · doi:10.1159/000340048 · Cited by 7
Kim, D. K., Lee, J. H., Kim, J. W., Kim, H. S., Kim, A., Kim, B. K., Yi, K. Y., Park, H.-J., Park, D. K., & Choi, W. S. (2011) · Journal of Pharmacological Sciences · doi:10.1254/jphs.10300fp · Cited by 7
Chen, J.-S., Chang, L.-C., Huang, S.-J., & Cheng, C. (2014) · BioMed Research International · doi:10.1155/2014/814869 · Cited by 7
Systems‐level analysis of clinically different phenotypes of juvenile nasopharyngeal angiofibromas
Renkonen, S., Kankainen, M., Hagström, J., Haglund, C. H., Monni, O. M., & Mäkitie, A. A. (2012) · The Laryngoscope · doi:10.1002/lary.23592 · Cited by 7
Syk Inhibition Induces Platelet Dependent Peri-islet Hemorrhage in the Rat Pancreas
Long, A. J., Sampson, E. R., McCarthy, R. W., Harris, C. M., Barnard, M. R., Shi, D., Conlon, D., Caldwell, R. G., Honor, D. J., Wishart, N., et al. (2016) · Toxicologic Pathology · doi:10.1177/0192623316654015 · Cited by 7
Pathogen-Sensing by Mincle: Function and Molecular Aspects
Nagata, M., Omahdi, Z., & Yamasaki, S. (2016) · Springer eBooks · doi:10.1007/978-4-431-56015-9_2 · Cited by 7
Spleen Tyrosine Kinase Inhibition Modulates p53 Activity
Althubiti, M. (2017) · Journal of Cell Death · doi:10.1177/1179066017731564 · Cited by 7
Tyrosine kinase inhibitors for the treatment of rheumatoid arthritis: phase I to Ⅱ clinical trials
Wu, J., Zhu, Z., Yu, Q., & Ding, C. (2019) · Expert Opinion on Investigational Drugs · doi:10.1080/13543784.2019.1692812 · Cited by 7
Metadata
- Authors
- Mócsai, A., Ruland, J., & Tybulewicz, V. L. J.
- Affiliations
- Semmelweis University (HU)
- TUM Klinikum (DE)
- National Institute for Medical Research (GB)
- Corresponding author
- Mócsai, Attila
- Venue
- Nature Reviews Immunology
- Published
- 2010-05-14
- Volume
- 10
- Issue
- 6
- Pages
- 387-402
- ISSN
- 1474-1733 (ISSN-L)
- 1474-1741
- PMC
- PMC4782221
- OpenAlex
- W2017341404
- Cited by
- 1,368
- References
- 194
- Citations by year
- 2026: 71 · 2025: 94 · 2024: 107 · 2023: 111 · 2022: 99 · 2021: 100 · 2020: 78 · 2019: 76 · 2018: 75 · 2017: 87 · 2016: 78 · 2015: 70 · 2014: 87 · 2013: 78 · 2012: 84
- FWCI
- 6.12
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Nature reviews. Immunology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Site cant be reached (submittedVersion)
- Funders
- Wellcome Trust (087782)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Life Sciences › Immunology and Microbiology › Immunology › Cytokine Signaling Pathways and Interactions
- Keywords
- Syk, innate immune recognition, C-type lectin, integrins, NLRP3 inflammasome, osteoclast maturation, bone metabolism, platelet activation, vascular development, cell adhesion, autoimmune disease, B-cell lymphoma, therapeutic target, Drosophila melanogaster
- MeSH terms
- Syk Kinase, Animals, Cell Adhesion, Humans, Protein-Tyrosine Kinases, Receptors, Immunologic, Signal Transduction, Cell Lineage, Intracellular Signaling Peptides and Proteins
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