The DOI matches its Crossref record; 53 of the 54 references it cites were found in a registry or an index.
Phospholipase Cγ2 Is Essential in the Functions of B Cell and Several Fc Receptors
Open accessAbstract
Many receptors activate phospholipase Cgamma1 or -gamma2. To assess the role of PLCgamma2, we derived enzyme-deficient mice. The mice are viable but have decreased mature B cells, a block in pro-B cell differentiation, and B1 B cell deficiency. IgM receptor-induced Ca2+ flux and proliferation to B cell mitogens are absent. IgM, IgG2a, and IgG3 levels are reduced, and T cell-independent antibody production is absent. The similarity to Btk- or Blnk-deficient mice demonstrates that PLCgamma2 is downstream in Btk/Blnk signaling. FcRgamma signaling is also defective, resulting in a loss of collagen-induced platelet aggregation, mast cell FcepsilonR function, and NK cell FcgammaRIII and 2B4 function. The results define a signal transduction pathway broadly utilized by immunoglobulin superfamily receptors.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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?
In the citing paper
“In fact, a previous study reported marked decreases in the most mature B cell population in Plcg2 deficient mice(30).”
From Multi-omics analyses reveal novel effects of PLCγ2 deficiency in the mouse brain (2023) · cites this paper as [30]
In the citing paper
“Previous studies have reported internal hemorrhaging during development in other Plcg2 deficient mouse models (29, 30), which have been proposed to be caused by rupture of blood-filled fragile lymphatic vessels by mechanical stress or pressure of the blood flow (29).”
From Multi-omics analyses reveal novel effects of PLCγ2 deficiency in the mouse brain (2023) · cites this paper as [30]
In the citing paper
“PLCγ2 is primarily expressed in lymphoid tissue (bone marrow, thymus, spleen and lymph nodes), where it functions immediately downstream of the B-cell receptor (BCR) and other ITAM-coupled receptors [22–24].”
From PLCγ2 deficiency compromises systemic immune tolerance and erodes myelin homeostasis while enhancing oxidative metabolism in the mouse brain (2026) · cites this paper as [22]
In the citing paper
“In peripheral immune cells, PLCγ2 has been implicated in signaling pathways downstream of the B cell receptor, and it is thought to modulate the functions of macrophages, platelets, mast cells, neutrophils, and NK cells through the Fc receptor [14].”
From Alzheimer’s disease phospholipase C-gamma-2 (PLCG2) protective variant is a functional hypermorph (2019) · cites this paper as [14]
In the citing paper
“In different models of PLCG2 depletion, homozygous knockout embryos were found to have significant subcutaneous hemorrhaging, suggesting impacted vascular development and bleeding that may underlie embryonic death and reduced frequencies at weaning.”
From PLCG2 modulates TREM2 expression and signaling in response to Alzheimer's disease pathology (2025) · cites this paper as [19]
In the citing paper
“PLCγ2, highly expressed in hematopoietic cells, has the key role in signalling downstream of ITAM-associated receptors; for example, it controls multiple functions of B cells, and several types of innate immune cells in response to stimulation of the B-cell antigen receptor (BCR) and Fc receptors (FcRs), respectively [41,42].”
From Phosphatidylinositol(4,5)bisphosphate: diverse functions at the plasma membrane (2020) · cites this paper as [41]
In the citing paper
“Unlike the germline deletion of PLCγ2 that results in embryonic lethality, mice lacking PLCγ2 enzymatic activity were viable, but with profound defects in B cell development and function. These mice exhibited reduced mature B cells, disrupted differentiation of pro-B cells, and a lack of B1 B cells (24).”
From The role of PLCγ2 in immunological disorders, cancer, and neurodegeneration (2021) · cites this paper as [24]
In the citing paper
“Indeed, PLCγ2-deficient and inducible PLCγ2−/− mice have been widely shown to lack the ability to respond to antigens (24, 26, 27, 28).”
From The role of PLCγ2 in immunological disorders, cancer, and neurodegeneration (2021) · cites this paper as [24]
In the citing paper
“Inducible KO mice showed T cell development and T cell receptor (TCR)-mediated proliferation were normal in the absence of PLCγ2 (24, 26), with development instead depending on the closely related family member PLCγ1 (60).”
From The role of PLCγ2 in immunological disorders, cancer, and neurodegeneration (2021) · cites this paper as [24]
In the citing paper
“On the other hand, PLCγ2 is more broadly present in myeloid cells [5, 25, 26], neutrophils [25, 27], mast cells [25], NK cells [5, 25], B-cells and platelets [5, 28, 29]”
From TREM2/PLCγ2 signalling in immune cells: function, structural insight, and potential therapeutic modulation (2021) · cites this paper as [5]
In the citing paper
“These proteins are critical for the proper maturation, maintenance and function of a range of immune and hematopoietic-lineage cells [5, 23].”
From TREM2/PLCγ2 signalling in immune cells: function, structural insight, and potential therapeutic modulation (2021) · cites this paper as [5]
In the citing paper
“PLCγ2 is expressed in cells of the hematopoietic lineage [5].”
From TREM2/PLCγ2 signalling in immune cells: function, structural insight, and potential therapeutic modulation (2021) · cites this paper as [5]
In the citing paper
“In these cells, PLCγ2, downstream of B-cell receptor and Fc receptor signalling, regulates calcium-dependent functions supporting immune and inflammatory responses [5, 28].”
From TREM2/PLCγ2 signalling in immune cells: function, structural insight, and potential therapeutic modulation (2021) · cites this paper as [5]
In the citing paper
“the deficits in B-cell development and function are the more pronounced effects described to date”
From TREM2/PLCγ2 signalling in immune cells: function, structural insight, and potential therapeutic modulation (2021) · cites this paper as [5]
In the citing paper
“PLCγ2-deficient mice are viable, but exhibit haemorrhaging in various organs in addition to severe immunodeficiency [5]”
From TREM2/PLCγ2 signalling in immune cells: function, structural insight, and potential therapeutic modulation (2021) · cites this paper as [5]
In the citing paper
“These include completely ablated calcium responses downstream of the B-cell receptor, affecting the ability to respond to stimuli, and reduced antibody production [5]”
From TREM2/PLCγ2 signalling in immune cells: function, structural insight, and potential therapeutic modulation (2021) · cites this paper as [5]
In the citing paper
“In both humans and mice, PLCγ2 loss, as well as strong GOF, mostly results in detrimental and sometimes overlapping phenotypes, as largely described for the peripheral immune system [5, 25]”
From TREM2/PLCγ2 signalling in immune cells: function, structural insight, and potential therapeutic modulation (2021) · cites this paper as [5]
Citations
Cites
Signal transduction by lymphocyte antigen receptors
Weiss, A., & Littman, D. R. (1994) · Cell · doi:10.1016/0092-8674(94)90334-4 · Cited by 2,076
Lymphocyte responses and cytokines
Paul, W. E., & Seder, R. A. (1994) · Cell · doi:10.1016/0092-8674(94)90332-8 · Cited by 1,832
Regulation of Phosphoinositide-Specific Phospholipase C
Rhee, S. G. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.281 · Cited by 1,628
Vetrie, D. L. P., Vořechovský, I., Sideras, P., Holland, J., Davies, A. F., Flinter, F. A., Hammarström, L. L. G., Kinnon, C., Levinsky, R. J., Bobrow, M., et al. (1993) · Nature · doi:10.1038/361226a0 · Cited by 1,465
Deficient expression of a B cell cytoplasmic tyrosine kinase in human X-linked agammaglobulinemia
Tsukada, S., Saffran, D. C., Rawlings, D. J., Parolini, O., Allen, R. C., Klisak, I. J., Sparkes, R. S., Kubagawa, H., Mohandas, T. K., Quan, S. G., et al. (1993) · Cell · doi:10.1016/0092-8674(93)90667-f · Cited by 1,326
Signalling through the lipid products of phosphoinositide-3-OH kinase
Toker, A., & Cantley, L. C. (1997) · Nature · doi:10.1038/42648 · Cited by 1,306
Teglund, S., McKay, C., Schuetz, E. G., van Deursen, J. M., Stravopodis, D. J., Wang, D., Brown, M. P., Bodner, S. M., Grosveld, G. C., & Ihle, J. N. (1998) · Cell · doi:10.1016/s0092-8674(00)81444-0 · Cited by 1,266
Self-citationRothe, J., Lesslauer, W., Loetscher, H., Lang, Y., Koebel, P., Köntgen, F., Althage, A., Zinkernagel, R. M., Steinmetz, M., & Bluethmann, H. (1993) · Nature · doi:10.1038/364798a0 · Cited by 1,246
Daëron, M. (1997) · Annual Review of Immunology · doi:10.1146/annurev.immunol.15.1.203 · Cited by 1,227
Ihle, J. N. (1995) · Nature · doi:10.1038/377591a0 · Cited by 1,201
Self-citation
Cited by
Sorted by citations
Items 301–400 of 476
Btk and phospholipase Cγ2 can function independently during B cell development
Halcomb, K. E., Contreras, C. M., Hinman, R. M., Coursey, T. G., Wright, H. L., & Satterthwaite, A. B. (2007) · European Journal of Immunology · doi:10.1002/eji.200636451 · Cited by 21
Platelet-associated IgAs and impaired GPVI responses in platelets lacking WIP
Falet, H., Marchetti, M. P., Hoffmeister, K. M., Massaad, M. J., Geha, R. S., & Hartwig, J. H. (2009) · Blood · doi:10.1182/blood-2009-02-202721 · Cited by 21
Multitasking of Ig-α and Ig-β to Regulate B Cell Antigen Receptor Function
Wienands, J., & Engels, N. (2001) · International Reviews of Immunology · doi:10.3109/08830180109045585 · Cited by 21
Chattopadhyay, A., & Carpenter, G. F. (2002) · Journal of Cell Science · doi:10.1242/jcs.115.10.2233 · Cited by 21
Hoover, C., Kondo, Y., Shao, B., McDaniel, J. M., Lee, R. H., McGee, S., Whiteheart, S. W., Bergmeier, W., McEver, R. P., & Xia, L. (2021) · Blood · doi:10.1182/blood.2020010310 · Cited by 20
Pone, E. J., Lam, T., Lou, Z., Wang, R., Chen, Y., Liu, D., Edinger, A. L., Xu, Z., & Casali, P. (2015) · The Journal of Immunology · doi:10.4049/jimmunol.1401896 · Cited by 20
Rothstein, T. L., & Guo, B.-C. (2009) · Journal of Internal Medicine · doi:10.1111/j.1365-2796.2009.02103.x · Cited by 21
Inui, S., Maeda, K., Hua, D. R., Yamashita, T., Yamamoto, H., Miyamoto, E., Aizawa, S., & Sakaguchi, N. (2002) · International Immunology · doi:10.1093/intimm/14.2.177 · Cited by 19
Erythropoietin receptor Y479 couples to ERK1/2 activation via recruitment of phospholipase Cγ
Halupa, A., Chohan, M., Stickle, N. H., Beattie, B. K., Miller, B. A., & Barber, D. L. (2005) · Experimental Cell Research · doi:10.1016/j.yexcr.2005.04.030 · Cited by 21
Pyfrom, S., Quinn, C. C., Dorando, H. K., Luo, H., & Payton, J. E. (2020) · The Journal of Immunology · doi:10.4049/jimmunol.2000088 · Cited by 19
Hughan, S. C., & Watson, S. P. (2007) · Journal of Thrombosis and Haemostasis · doi:10.1111/j.1538-7836.2007.02307.x · Cited by 19
Regulation of Phospholipase C‐γ2 Networks in B Lymphocytes
Hikida, M., & Kurosaki, T. (2005) · Advances in immunology · doi:10.1016/s0065-2776(05)88003-4 · Cited by 20
Yamasaki, S., Ishikawa, E., Sakuma, M., Kanagawa, O., Cheng, A. M., MALISSEN, B., & Saito, T. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.02109-06 · Cited by 19
The inositol 5-phosphatase INPP5B regulates B cell receptor clustering and signaling
Droubi, A., Wallis, C., Anderson, K. E., Rahman, S., Sa, A. D., Rahman, T., Stephens, L., Hawkins, P. T., & Lowe, M. (2022) · The Journal of Cell Biology · doi:10.1083/jcb.202112018 · Cited by 19
Phosphoproteomic analyses reveal that galectin-1 augments the dynamics of B-cell receptor signaling
Tsai, C., Wu, H., Su, T.-H., Kuo, C., Huang, H., Chung, C., Chen, C.-S., Khoo, K., Chen, Y., & Lin, K. (2014) · Journal of Proteomics · doi:10.1016/j.jprot.2014.03.031 · Cited by 18
The role of the adapter molecule SLP-76 in platelet function
Judd, B. A., & Koretzky, G. A. (2001) · Oncogene · doi:10.1038/sj.onc.1204772 · Cited by 18
2B4 utilizes ITAM-containing receptor complexes to initiate intracellular signaling and cytolysis
Bida, A. T., Neff, J., Dick, C. J., Schoon, R. A., Brickshawana, A., Chini, C. C. S., & Billadeau, D. D. (2011) · Molecular Immunology · doi:10.1016/j.molimm.2011.02.008 · Cited by 17
Yu, M., Chen, Y., He, Y., Podd, A., Fu, G., Wright, J. A., Kleiman, E., Khan, W. N., Wen, R., & Wang, D. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1102952 · Cited by 17
Self-citationLiao, H., Ji, Q., & Carpenter, G. F. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c100030200 · Cited by 17
Abraham, R. T. (2000) · Immunologic Research · doi:10.1385/ir:22:2-3:95 · Cited by 17
PLCG2 modulates TREM2 expression and signaling in response to Alzheimer's disease pathology
Messenger, E. J., Baar, S. A., Bedford, L. M., Tsai, A. P., Lin, P. B., Ferguson, C. A., Xu, G., Wallace, A., Landreth, G. E., Lamb, B. T., et al. (2025) · Alzheimer's & Dementia · doi:10.1002/alz.70231 · Cited by 16
Ishijima, Y., Ohmori, S., Uenishi, A., & Ohneda, K. (2012) · Genes to Cells · doi:10.1111/j.1365-2443.2012.01588.x · Cited by 16
Cepeda, V., Cofré, C., González, R., MacKenzie, S. A., & Vidal, R. (2011) · Aquaculture · doi:10.1016/j.aquaculture.2011.04.045 · Cited by 16
Chen, X., Lv, Q., Ma, J., & Liu, Y. (2018) · Cell Proliferation · doi:10.1111/cpr.12437 · Cited by 16
Sasanuma, H., Tatsuno, A., Hidano, S., Ohshima, K., Matsuzaki, Y., Hayashi, K., Lowell, C., Kitamura, D., & Goitsuka, R. (2006) · Blood · doi:10.1182/blood-2005-10-4102 · Cited by 17
Kim, J. K., Seo, Y., Park, S., Park, S., Lim, S., Lee, S., Kwon, O., Seo, J. K., Choi, U.-K., Ryu, S. H., et al. (2014) · Biochemistry and Cell Biology · doi:10.1139/bcb-2014-0055 · Cited by 16
The role of phospholipase Cγ1 in breast cancer and its clinical significance
Emmanouilidi, A., Lattanzio, R., Sala, G., Piantelli, M., & Falasca, M. (2017) · Future Oncology · doi:10.2217/fon-2017-0125 · Cited by 16
In Vivo Models for the Evaluation of Antithrombotics and Thrombolytics
Mousa, S. A. (2010) · Methods in molecular biology · doi:10.1007/978-1-60761-803-4_2 · Cited by 15
Kurosaki, T., & Okada, T. (2001) · International Reviews of Immunology · doi:10.3109/08830180109045586 · Cited by 15
Phospholipase Cγ2 contributes to stable thrombus formation on VWF
Rathore, V., Wang, D., Newman, D. K., & Newman, P. J. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.07.048 · Cited by 15
Self-citationKang, H. K., Lee, H. Y., Lee, Y.-N., Jo, E., Kim, J. I., Kim, G., Park, Y. M., Min, D. S., Yano, A., Kwak, J., et al. (2004) · International Immunopharmacology · doi:10.1016/j.intimp.2004.04.001 · Cited by 15
Carriers of the p.P522R variant in PLCγ2 have a slightly more responsive immune system
Diks, A. M., Teodosio, C., de Mooij, B., Groenland, R. J., Naber, B. A. E., de Laat, I. F., Vloemans, S. A., Rohde, S., de Jonge, M. I., Lorenz, L., et al. (2023) · Molecular Neurodegeneration · doi:10.1186/s13024-023-00604-9 · Cited by 14
Nepal, R. M., Tong, L., Kolaj, B., Edelmann, W., & Martín, A. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0905965106 · Cited by 14
Yamamoto, M. P. (2004) · International Immunology · doi:10.1093/intimm/dxh116 · Cited by 13
Wolf, C., & Quinn, P. J. (2004) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-1-4757-5806-1_10 · Cited by 16
Pearce, A. C., Wonerow, P., MARSHALL, S. J., Frampton, J., Gartner, T. K., & Watson, S. P. (2004) · Biochemical Journal · doi:10.1042/bj20031298 · Cited by 14
Proximal B cell receptor signaling pathways
Skaggs, B. J., & Clark, M. R. (2004) · Signal Transduction · doi:10.1002/sita.200400034 · Cited by 14
Small Interfering RNA Screen for Phosphatases Involved in IgE-Mediated Mast Cell Degranulation
Zhang, J., Mendoza, M., Guiraldelli, M. F., Barbu, E. A., & Siraganian, R. P. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.0904169 · Cited by 13
Impact of Hemostasis on the Lymphatic System in Development and Disease
Tsukiji, N., & Suzuki‐Inoue, K. (2023) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.123.318824 · Cited by 13
Abdoul‐Azize, S., Hami, R., Riou, G., Derambure, C., Charbonnier, C., Vannier, J., Guzmán, M. L., Schneider, P., & Boyer, O. (2024) · Nature Communications · doi:10.1038/s41467-024-48818-9 · Cited by 14
PKCη directs induction of IRF-4 expression and Ig κ gene rearrangement in pre-BCR signaling pathway
Oda, A., Ono, T., Yamamoto, M., Goitsuka, R., & Kitamura, D. (2008) · International Immunology · doi:10.1093/intimm/dxn101 · Cited by 13
Zheng, Y., Adams, T. L., Zhi, H., Yu, M., Wen, R., Newman, P. J., Wang, D., & Newman, D. K. (2015) · PLoS ONE · doi:10.1371/journal.pone.0119739 · Cited by 13
Self-citationNeves, G. W. P., Curty, N., Kubitschek-Barreira, P. H., Fontaine, T., Souza, G. H. M. F., Cunha, M. L., Goldman, G. H., Beauvais, A., Latgé, J., & Lopes-Bezerra, L. M. (2016) · Journal of Proteomics · doi:10.1016/j.jprot.2016.06.015 · Cited by 13
Synergistic activation of PKD by the B cell antigen receptor and CD19 requires PI3K, Vav1 and PLCγ
Vigorito, E., Kövesdi, D., & Turner, M. (2005) · Cellular Signalling · doi:10.1016/j.cellsig.2005.11.008 · Cited by 13
Actors of the tyrosine kinase receptor downstream signaling pathways in amphioxus
Bertrand, S., Campo‐Paysaa, F., Camasses, A., García‐Fernàndez, J., & Escrivá, H. (2009) · Evolution & Development · doi:10.1111/j.1525-142x.2008.00299.x · Cited by 13
Tec kinase pathways in lymphocyte development and transformation
Pillai, S. S., & Moran, S. T. (2002) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/s0304-419x(02)00041-0 · Cited by 13
Dai, X., Chen, Y., Schuman, J., Hua, Z., Adamson, J. W., Wen, R., & Wang, D. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.1.88-99.2006 · Cited by 13
Self-citationEvaluation of the physiological significance of botrocetin/ von Willebrand factor in vitro signaling
Liu, J., Joglekar, M., Ware, J. L., Fitzgerald, M. E. C., Lowell, C. A., Berndt, M. C., & Gartner, T. K. (2008) · Journal of Thrombosis and Haemostasis · doi:10.1111/j.1538-7836.2008.03135.x · Cited by 12
Human PLCG2 haploinsufficiency results in a novel natural killer cell immunodeficiency
Alinger, J. B., Mace, E. M., Porter, J. R., Mah-Som, A. Y., Daugherty, A. L., Li, S., Throm, A. A., Pingel, J. T., Saucier, N., Yao, A., et al. (2023) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2023.09.002 · Cited by 11
Phospholipases in Health and Disease
Yang, Y. R., Jang, H., Ryu, S. H., & Suh, P. (2014) · Springer eBooks · doi:10.1007/978-1-4939-0464-8_1 · Cited by 12
Simonowski, A., Wilhelm, T., Habib, P., Zorn, C. N., & Huber, M. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2019.118622 · Cited by 12
Phospholipase Cγ2 Dosage Is Critical for B Cell Development in the Absence of Adaptor Protein BLNK
Xu, S., Huo, J., Chew, W.-K., Hikida, M., Kurosaki, T., & Lam, K.-P. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.176.8.4690 · Cited by 12
de Diego, R. P., López‐Granados, E., Rivera, J., Ferreira, A., Fontán, G., Bravo, J., Rodríguez, M. C. G., & Bolland, S. M. (2008) · Clinical & Experimental Immunology · doi:10.1111/j.1365-2249.2008.03589.x · Cited by 12
Abe, K., Wechs, S., Kalaydjiev, S., Franz, T. J., Busch, D. H., Fuchs, H., Soewarto, D., Behrendt, H., Wagner, S., Jakob, T., et al. (2007) · Rheumatology · doi:10.1093/rheumatology/kem358 · Cited by 11
A hypomorphic IgH‐chain allele affects development of B‐cell subsets and favours receptor editing
Brenner, S., Drewel, D., Steinbart, T., Weisel, F. J., Haertel, E., Pötzsch, S., Welzel, H., Brandl, A., Yu, P., Mudde, G. C., et al. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.168 · Cited by 10
Phospholipase Cγ2 Is Essential for Experimental Models of Epidermolysis Bullosa Acquisita
Szilveszter, K. P., Vikár, S., Horváth, Á. I., Helyes, Z., Sárdy, M., & Mócsai, A. (2021) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2021.09.019 · Cited by 10
Futosi, K., Kása, O., Szilveszter, K. P., & Mócsai, A. (2021) · Arthritis & Rheumatology · doi:10.1002/art.41704 · Cited by 10
Park, H. S., Oh, A., Keum, C., Lee, J., Lee, J. K., Son, B. R., Shin, K. S., & Hahn, Y. (2021) · European Journal of Medical Genetics · doi:10.1016/j.ejmg.2021.104387 · Cited by 9
Novel Platelet and Vascular Roles for Immunoreceptor Signaling
Samaha, F. F., & Kahn, M. L. (2006) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000248734.89782.37 · Cited by 10
Dearden-Badet, M.-T., & Mouchiroud, G. (2005) · Cellular Signalling · doi:10.1016/j.cellsig.2005.03.018 · Cited by 10
Zhu, Z., Yu, Y., Wang, B., Ding, M., Tian, Y., Jiang, R., Sun, G., Han, R., Kang, X., Yan, F., et al. (2023) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2023.105094 · Cited by 9
Phospholipase Cδ4: from genome structure to physiological function
Fukami, K., Inoue, T., Kurokawa, M., Fissore, R. A., Nakao, K., Nagano, K., Nakamura, Y., Takenaka, K., Yoshida, N., Mikoshiba, K., et al. (2003) · Advances in Enzyme Regulation · doi:10.1016/s0065-2571(02)00029-8 · Cited by 9
The Roles of LAT in Platelet Signaling Induced by Collagen, TxA2, or ADP
Cho, M. J., Pestina, T. I., Steward, S. A., Jackson, C. W., & Gartner, T. K. (2002) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2002.6738 · Cited by 8
Self-citationThe Role of Platelets in Angiogenesis
Battinelli, E. M. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-813456-6.00024-2 · Cited by 11
Phospholipase C-γ Contains Introns Shared by src Homology 2 Domains in Many Unrelated Proteins
Manning, C. M., Mathews, W. R., Fico, L. P., & Thackeray, J. R. (2003) · Genetics · doi:10.1093/genetics/164.2.433 · Cited by 8
Rivera‐Aguilar, V., Querejeta, E., Luna, R. A. J., Reyna-Garfias, H., Ponce‐Franco, D., Milliar-Garcia, A., QUINONESCARDENAS, A., Pacheco‐Yépez, J., & Campos‐Rodríguez, R. (2008) · Immunology Letters · doi:10.1016/j.imlet.2008.06.006 · Cited by 7
Magnesium and the Immune Response
Schmitz, C., & Perraud, A. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802168-2.00026-9 · Cited by 7
Paroha, R., Chourasia, R., Rai, R., Kumar, A., Vyas, A. K., Chaurasiya, S. K., & Singh, A. K. (2020) · Microbiology and Immunology · doi:10.1111/1348-0421.12839 · Cited by 7
Mankidy, R., Hastings, J., & Thackeray, J. R. (2003) · Genetics · doi:10.1093/genetics/164.2.553 · Cited by 7
Langan, S. A., Navarro‐Núñez, L., Watson, S. P., & Nash, G. B. (2017) · Platelets · doi:10.1080/09537104.2017.1336210 · Cited by 7
Yao, Y., Huang, W., Li, X., Li, X., Qian, J., Han, H., Sun, H., An, X., Lu, L., & Zhao, H. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.00965 · Cited by 7
Activation of Phospholipase C 2 by Tyrosine Phosphorylation
Özdener, F., Dangelmaier, C., Ashby, B., & Kunapuli, S. P. (2002) · Cited by 8
Herzog, S., Storch, B., & Jumaa, H. (2006) · Immunologic Research · doi:10.1385/ir:34:2:143 · Cited by 6
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
Teh, C. E., Horikawa, K., Arnold, C. N., Beutler, B., Kucharska, E. M., Vinuesa, C. G., Bertram, E. M., Goodnow, C. C., & Enders, A. (2013) · Genes and Immunity · doi:10.1038/gene.2013.11 · Cited by 6
Variations in the human phospholipase Cγ2 gene in patients with B-cell defects of unknown etiology
Wang, D., Boylin, E. C., Minegishi, Y., Wen, R., Smith, E. C. I., Ihle, J., & Conley, M. (2001) · Immunogenetics · doi:10.1007/s002510100356 · Cited by 6
Self-citationUse of Toll-Like Receptor (TLR) Ligation to Characterize Human Regulatory B-Cells Subsets
Chayé, M. A. M., Tontini, C., Ozir‐Fazalalikhan, A., Voskamp, A. L., & Smits, H. H. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1237-8_13 · Cited by 6
Whyburn, L. R. (2003) · International Immunology · doi:10.1093/intimm/dxg034 · Cited by 6
Santos, E. W., Dias, C. C., Fock, R. A., Paredes‐Gamero, E. J., Zheng, Y., Wang, Y.-X., & Borelli, P. (2023) · Nutrition Research · doi:10.1016/j.nutres.2023.05.006 · Cited by 5
Functions of IgM fc receptor (FcµR) related to autoimmunity
Kubagawa, H., Aliabadi, P. M., Al‐Qaisi, K., Jani, P. K., Honjo, K., Izui, S., Radbruch, A., & Melchers, F. (2024) · Autoimmunity · doi:10.1080/08916934.2024.2323563 · Cited by 5
Ichise, H., Ichise, T., & Yoshida, N. (2016) · PLoS ONE · doi:10.1371/journal.pone.0150521 · Cited by 5
Rip, J., Hendriks, R. W., & Corneth, O. B. J. (2021) · BIO-PROTOCOL · doi:10.21769/bioprotoc.3902 · Cited by 5
Jr.Devi, G. (2013) · Colloquium Series on Neuropeptides · doi:10.4199/c00082ed1v01y201304npe004 · Cited by 5
BCR activation of PI3K is Vav-independent in murine B cells
Vigorito, E., Clayton, E., & Turner, M. (2004) · Biochemical Society Transactions · doi:10.1042/bst0320781 · Cited by 5
Multi-omics analyses reveal novel effects of PLCγ2 deficiency in the mouse brain
Hopp, S. C., Rogers, J. G., Smith, S., Campos, G., Miller, H., Barannikov, S., Kuri, E. G., Wang, H., Han, X., Bieniek, K. F., et al. (2023) · doi:10.1101/2023.12.06.570499 · Cited by 4
“Previous studies have reported internal hemorrhaging during development in other Plcg2 deficient mouse models (29, 30), which have been proposed to be caused by rupture of blood-filled fragile lymphatic vessels by mechanical stress or pressure of the blood flow (29).”
BackgroundCARD19, a Novel Regulator of the TAK1/NF-κB Pathway in Self-Reactive B Cells
Zheng, Y., Yu, M., Chen, Y., Xue, L., Zhu, W., Fu, G., Morris, S. W., Wen, R., & Wang, D. (2023) · The Journal of Immunology · doi:10.4049/jimmunol.2200639 · Cited by 4
Self-citationCarr, A. J., Hajicek, N., Tsai, A. P., Acharya, P. P., Hardy, P. B., Meyer, E. G., Wyss‐Coray, T., Pearce, K. H., Sondek, J., & Zhang, Q. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.108356 · Cited by 5
Type II phosphatidylinositol 4-kinases interact with FcεRIγ subunit in RBL-2H3 cells
Bojjireddy, N., Sinha, R. K., & Subrahmanyam, G. (2014) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-014-1970-1 · Cited by 4
The intracellular action of sphingosine 1-phosphate in GPVI-mediated Ca2+ mobilization in platelets
Ohmori, T., Yatomi, Y., Osada, M., & Ozaki, Y. (2004) · Thrombosis Research · doi:10.1016/j.thromres.2004.10.008 · Cited by 4
Early Events in B Lymphocyte Activation
Bondada, S., Troyer, A., & Chelvarajan, R. L. (2003) · Current Protocols in Immunology · doi:10.1002/0471142735.im0309s57 · Cited by 4
Defects in B Cell Survival and Activation
Yong, P. F. K., Dziadzio, M., & Grimbacher, B. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-374279-7.18014-2 · Cited by 4
NFKB-Dependent Signaling Pathways
Li, X. (2005) · Oxidative stress and disease · doi:10.1201/9781420028362.ch1 · Cited by 4
Wang, Q., Tao, C., Wu, Y., Anderson, K. E., Makrides, N., Hannan, A., Peregrin, J., Lin, C., Ding, Z., Li, W., et al. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.116046 · Cited by 5
Multi-functional platelets: translating biological functions into therapeutic applications
Zou, C., Deng, Y.-T., Lin, X.-R., & Xie, H.-Q. (2025) · Vessel Plus · doi:10.20517/2574-1209.2025.114 · Cited by 4
Targeting NKG2D/NKG2DL axis in cancer immunotherapy: mechanisms and therapeutic applications
Wei, H., Xiang, L., Zhou, Y., Huang, Y., Liu, L., & Cao, D. (2026) · Journal of Translational Medicine · doi:10.1186/s12967-025-07650-5 · Cited by 6
Meng, L., Yang, Y., He, S., Chen, H., Zhan, Y., Yang, R., Li, Z., Zhu, J., Zhou, J., Li, Y., et al. (2024) · BMC Medicine · doi:10.1186/s12916-024-03611-9 · Cited by 3
Self-nonself Recognition through B-Cell Antigen Receptor
Kitamura, D. (2008) · Springer eBooks · doi:10.1007/978-4-431-73884-8_4 · Cited by 2
Moran, S. T., Cariappa, A., Liu, H., Boboilă, C., Shi, H. N., Holland, P. M., Peschon, J. J., & Pillai, S. S. (2005) · Molecular Immunology · doi:10.1016/j.molimm.2005.09.009 · Cited by 3
Liao, H., & Carpenter, G. F. (2010) · Elsevier eBooks · doi:10.1016/b978-0-12-374145-5.00110-8 · Cited by 3
Everett, K. L., & Katan, M. (2016) · Encyclopedia of Cell Biology · doi:10.1016/b978-0-12-394447-4.30017-7 · Cited by 3
Metadata
- Authors
- Wang, D., Feng, J., Wen, R., Marine, J.-C., Sangster, M. Y., Parganas, E., Hoffmeyer, A., Jackson, C. W., Cleveland, J. L., Murray, P. J., & Ihle, J. N.
- Affiliations
- St. Jude Children's Research Hospital (US)
- Corresponding author
- Ihle, James N.
- ORCID
- Venue
- Immunity
- Publisher
- Elsevier BV
- Published
- 2000-07
- Volume
- 13
- Issue
- 1
- Pages
- 25-35
- ISSN
- 1074-7613 (ISSN-L)
- OpenAlex
- W2039490597
- Cited by
- 475
- References
- 54
- Citations by year
- 2026: 7 · 2025: 8 · 2024: 5 · 2023: 12 · 2022: 4 · 2021: 13 · 2020: 11 · 2019: 10 · 2018: 6 · 2017: 10 · 2016: 12 · 2015: 16 · 2014: 12 · 2013: 14 · 2012: 16
- FWCI
- 12.85
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Immunity (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Heart, Lung, and Blood Institute (P01HL053749, P01HL53749)
- National Cancer Institute (CA21765, P30CA021765)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01-DK42932, R01DK042932)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › T-cell and B-cell Immunology
- Life Sciences › Immunology and Microbiology › Immunology › Immunodeficiency and Autoimmune Disorders
- Life Sciences › Immunology and Microbiology › Immunology › Monoclonal and Polyclonal Antibodies Research
- Keywords
- PLCγ2, B cell development, calcium flux, BTK signaling, 2B4, immunoglobulin superfamily receptors, platelet aggregation
- MeSH terms
- Agammaglobulinaemia Tyrosine Kinase, Animals, B-Lymphocytes, Blood Platelets, Carrier Proteins, Hematopoiesis, Isoenzymes, Mice, Inbred C57BL, Type C Phospholipases, Phosphoproteins, Protein-Tyrosine Kinases, Receptors, Antigen, B-Cell, Receptors, IgG, Mice, Knockout, Adaptor Proteins, Signal Transducing, Mice, Phospholipase C gamma
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
