Dysfunction of phospholipase Cγ in immune disorders and cancer
Abstract
The surge in genetic and genomic investigations over the past 5 years has resulted in many discoveries of causative variants relevant to disease pathophysiology. Although phospholipase C (PLC) enzymes have long been recognized as important components in intracellular signal transmission, it is only recently that this approach highlighted their role in disease development through gain-of-function mutations. In this review we describe the new findings that link the PLCγ family to immune disorders and cancer, and illustrate further efforts to elucidate the molecular mechanisms that underpin their dysfunction.
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
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 protective variant P522R is located within a region of the enzyme that has a regulatory function.
“The protective variant P522R is certainly located within a region of the enzyme that has a regulatory function (Fig. 4d, [7])”
From Alzheimer’s disease phospholipase C-gamma-2 (PLCG2) protective variant is a functional hypermorph (2019) · cites this paper as [7]
Box 1 (p. 17) describes the PLCγ-specific array as involved in interactions with regulatory proteins, and the Figures (p. 16) describe regulatory interactions involving its domains. Our copy does not mention P522R or locate that variant within the array, so it supports the region’s regulatory role but not the claimed location of P522R. (LLM, conf=0.78)
Experimental — accuracy not yet measuredAberrant functions of different PLCs and PI3Ks in disease development are well established.
“Although not covered in this review, the importance of aberrant functions of different PLCs and PI3Ks in disease development is well established and continues to expand [11,62,67,72,134–138].”
From Phosphatidylinositol(4,5)bisphosphate: diverse functions at the plasma membrane (2020) · cites this paper as [137]
The section “Mutations in PLCγ enzymes and disease development” (p. 3) links aberrant PLCγ function to immune disorders and cancer, supporting the PLC portion of the claim. The paper does not substantiate the claim about PI3Ks in disease development; its focus is PLCγ enzymes. (LLM, conf=0.88)
Experimental — accuracy not yet measuredPLCγ2 is a main effector downstream of TREM2 and is an intracellular lipase recruited to the membrane upon activation.
“A main effector downstream of TREM2, PLCγ2 is an intracellular lipase recruited to the membrane upon activation [3, 4].”
From TREM2/PLCγ2 signalling in immune cells: function, structural insight, and potential therapeutic modulation (2021) · cites this paper as [3]
The introduction (p. 2) describes PLCγ2 as a signaling enzyme activated by immune-cell receptors, and Box 1 (p. 18) describes its recruitment to a signaling scaffold and activation as a phospholipase. The cited passages do not identify TREM2 as an upstream receptor or establish PLCγ2 as a main effector downstream of it. Box 1 says Btk—not PLCγ2—is recruited to the membrane environment, so the specific membrane-recruitment claim is not established here. (LLM, conf=0.86)
Experimental — accuracy not yet measuredThe majority of hypermorphic variants (S707Y, Y495C, D993G) have been identified in the context of APLAID disorders, and in some mouse models with autoinflammatory phenotypes.
“the majority of hypermorphic variants (S707Y, Y495C, D993G) have been identified in the context of APLAID disorders, and in some mouse models with autoinflammatory phenotypes [3, 109, 110]”
From TREM2/PLCγ2 signalling in immune cells: function, structural insight, and potential therapeutic modulation (2021) · cites this paper as [3]
The immune-diseases section (pp. 3–4) identifies S707Y in APLAID and describes gain-of-function PLCγ2 mutations in autoinflammatory mouse strains. The structural section (pp. 8–9) places Y495C in ALI14 mice; the table (p. 20) lists D993G in ALI5 mice, although the main text calls that substitution D993L. The copy does not establish that a majority of hypermorphic variants occur in these contexts, and it does not place Y495C or D993G in APLAID patients. (LLM, conf=0.86)
Experimental — accuracy not yet measuredPLCγ2 is present in circulating monocytes, platelets and B-cells, amongst other immune cells.
“PLCγ2 is present in circulating monocytes, platelets and B-cells, amongst other immune cells (see sections above, [3, 130])”
From TREM2/PLCγ2 signalling in immune cells: function, structural insight, and potential therapeutic modulation (2021) · cites this paper as [3]
The introduction (p. 2) says PLCγ2 is predominantly expressed in haematopoietic cells and is activated by B-cell receptors, supporting the B-cell and broader immune-cell portions of the claim. Our copy does not specifically establish its presence in circulating monocytes or platelets; the platelet mention found in the references (p. 14) concerns a PLC inhibitor, not PLCγ2 expression. (LLM, conf=0.84)
Experimental — accuracy not yet measured
PLCγ2 shares high structural and mechanistic overlap with PLCγ1.
“PLCγ2 shares high structural and mechanistic overlap with the other member of the PLCγ family, PLCγ1 [7].”
From Alzheimer’s disease phospholipase C-gamma-2 (PLCG2) protective variant is a functional hypermorph (2019) · cites this paper as [7]
Other mutations in PLCG2 that lead to immune dysfunction are known to be activating.
“Other mutations in PLCG2 that lead to immune dysfunction are known to be activating [7].”
From Alzheimer’s disease phospholipase C-gamma-2 (PLCG2) protective variant is a functional hypermorph (2019) · cites this paper as [7]
PLCγ2 expression is largely restricted to hematopoietic cells and regulates specific responses downstream of several immune receptors.
“While PLCγ1 is ubiquitously expressed and regulates growth factor signalling in a variety of cell types, expression of PLCγ2 is largely restricted to hematopoietic cells, and regulates specific responses downstream of several immune receptors8.”
From PLCγ2 regulates TREM2 signalling and integrin-mediated adhesion and migration of human iPSC-derived macrophages (2021) · cites this paper as [8]
Variants of TREM2 and PLCG2 are known to cause diseases such as Nasu-Hakola disease (TREM2) and PLCγ2-associated antibody deficiency (PLAID) or autoinflammation and PLAID (APLAID).
“with variants of these genes known to cause diseases such as Nasu-Hakola disease (TREM2) [22], and PLCγ2-associated antibody deficiency (PLAID), or autoinflammation and PLAID (APLAID) [3].”
From TREM2/PLCγ2 signalling in immune cells: function, structural insight, and potential therapeutic modulation (2021) · cites this paper as [3]
PLAID-affected individuals have reduced PLCγ2-mediated signal transduction at physiological temperatures, despite constitutive enzyme activation.
“PLAID-affected individuals have reduced PLCγ2-mediated signal transduction at physiological temperatures, despite constitutive enzyme activation [3, 113]”
From TREM2/PLCγ2 signalling in immune cells: function, structural insight, and potential therapeutic modulation (2021) · cites this paper as [3]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Phosphoinositides: Tiny Lipids With Giant Impact on Cell Regulation
Balla, T. (2013) · Physiological Reviews · doi:10.1152/physrev.00028.2012 · Cited by 1,638 · see citing works
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 · see citing works
Frequent somatic mutations of GNAQ in uveal melanoma and blue naevi
Raamsdonk, C. D. V., Bezrookove, V., Green, G., Bauer, J. M., Gaugler, L., O’Brien, J. M., Simpson, E. M., Barsh, G. S., & Bastian, B. C. (2008) · Nature · doi:10.1038/nature07586 · Cited by 1,626 · see citing works
Resistance Mechanisms for the Bruton's Tyrosine Kinase Inhibitor Ibrutinib
Woyach, J. A., Furman, R. R., Liu, T.-M., Ozer, H. G., Zapatka, M., Ruppert, A. S., Xue, L., Li, D. H.-H., Steggerda, S. M., Versele, M., et al. (2014) · New England Journal of Medicine · doi:10.1056/nejmoa1400029 · Cited by 1,275 · see citing works
Initial impact of the sequencing of the human genome
Lander, E. S. (2011) · Nature · doi:10.1038/nature09792 · Cited by 1,044 · see citing works
Structure, function, and control of phosphoinositide-specific phospholipase C.
Rebecchi, M., & Pentyala, S. (2000) · Physiological Reviews · doi:10.1152/physrev.2000.80.4.1291 · Cited by 978 · see citing works
Kim, H.-K., Kim, J., Zilberstein, A., Margolis, B. L., Kim, J. G., Schlessinger, J., & Rhee, S. G. (1991) · Cell · doi:10.1016/0092-8674(91)90461-7 · Cited by 570 · see citing works
Kadamur, G., & Ross, E. M. (2013) · Annual Review of Physiology · doi:10.1146/annurev-physiol-030212-183750 · Cited by 529 · see citing works
Multiple roles of phosphoinositide-specific phospholipase C isozymes
Suh, P.-G., Park, J.-I., Manzoli, L., Cocco, L., Peak, J. C., Katan, M., Fukami, K., Kataoka, T., Yun, S.-U., & Ryu, S.-H. (2008) · BMB Reports · doi:10.5483/bmbrep.2008.41.6.415 · Cited by 501 · see citing works
Self-citationCold Urticaria, Immunodeficiency, and Autoimmunity Related to <i>PLCG2</i> Deletions
Ombrello, M. J., Remmers, E. F., Sun, G., Freeman, A. F., Datta, S., Torabi-Parizi, P., Subramanian, N., Bunney, T. D., Baxendale, R. W., Martins, M. S., et al. (2012) · New England Journal of Medicine · doi:10.1056/nejmoa1102140 · Cited by 425 · see citing works
Self-citationPhosphoinositide signalling in cancer: beyond PI3K and PTEN
Bunney, T. D., & Katan, M. (2010) · Nature Reviews Cancer · doi:10.1038/nrc2842 · Cited by 400 · see citing works
Self-citationZhou, Q., Lee, G.-S., Brady, J., Datta, S., Katan, M., Sheikh, A., Martins, M. S., Bunney, T. D., Santich, B. H., Moir, S., et al. (2012) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2012.08.006 · Cited by 374 · see citing works
Self-citationRecurrent PTPRB and PLCG1 mutations in angiosarcoma
Behjati, S., Tarpey, P. S., Sheldon, H., Martincorena, I., Loo, P. V., Gundem, G., Wedge, D. C., Ramakrishna, M., Cooke, S. L., Pillay, N., et al. (2014) · Nature Genetics · doi:10.1038/ng.2921 · Cited by 307 · see citing works
Self-citationPLCG1 mutations in cutaneous T-cell lymphomas
Vaqué, J. P., Gómez-López, G., Monsálvez, V., Varela, I., Martínez, N., Pérez, C., Domínguez, O., Graña, O., Rodríguez-Peralto, J. L., Rodríguez-Pinilla, S. M., et al. (2014) · Blood · doi:10.1182/blood-2013-05-504308 · Cited by 229 · see citing works
The Phospholipase C Isozymes and Their Regulation
Gresset, A., Sondek, J., & Harden, T. K. (2012) · Subcellular Biochemistry · doi:10.1007/978-94-007-3012-0_3 · Cited by 196 · see citing works
PLC regulation: emerging pictures for molecular mechanisms
Bunney, T. D., & Katan, M. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.08.003 · Cited by 182 · see citing works
Self-citationYu, P., Constien, R., Dear, N., Katan, M., Hanke, P., Bunney, T. D., Kunder, S., Quintanilla-Martinez, L., Huffstadt, U., Schröder, A., et al. (2005) · Immunity · doi:10.1016/j.immuni.2005.01.018 · Cited by 177 · see citing works
Self-citationBae, J. H., Lew, E. D., Yuzawa, S., Tomé, F., Lax, I., & Schlessinger, J. (2009) · Cell · doi:10.1016/j.cell.2009.05.028 · Cited by 158 · see citing works
Structural and Mechanistic Insights into Ras Association Domains of Phospholipase C Epsilon
Bunney, T. D., Harris, R., Gandarillas, N. L., Josephs, M. B., Roe, S. M., Sorli, S., Paterson, H. F., Rodrigues‐Lima, F., Esposito, D., Ponting, C. P., et al. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.01.008 · Cited by 134 · see citing works
Self-citationHeinz, D. W., Essen, L., & Williams, R. L. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1490 · Cited by 118 · see citing works
Mechanism of Phosphorylation-induced Activation of Phospholipase C-γ Isozymes
Gresset, A., Hicks, S. N., Harden, T. K., & Sondek, J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.166512 · Cited by 110 · see citing works
Poulin, B., Sekiya, F., & Rhee, S. G. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0409590102 · Cited by 108 · see citing works
The physiological roles of primary phospholipase C.
Yang, Y., Follo, M., Cocco, L., & Suh, P. (2013) · Advances in Biological Regulation · doi:10.1016/j.jbior.2013.08.003 · Cited by 93 · see citing works
Fu, L., Qin, Y., Xie, D., Hu, L., Kwong, D. L. �., Srivastava, G., Tsao, S. W., & Guan, X. (2007) · Cancer Research · doi:10.1158/0008-5472.can-07-2411 · Cited by 90 · see citing works
Bunney, T. D., Esposito, D., Mas-Droux, C., Lamber, E., Baxendale, R. W., Martins, M., Cole, A., Svergun, D., Driscoll, P. C., & Katan, M. (2012) · Structure · doi:10.1016/j.str.2012.09.005 · Cited by 88 · see citing works
Self-citationRole of phospholipase C in cell invasion and metastasis
Lattanzio, R., Piantelli, M., & Falasca, M. (2013) · Advances in Biological Regulation · doi:10.1016/j.jbior.2013.07.006 · Cited by 81 · see citing works
Isozyme-specific stimulation of phospholipase C-γ2 by Rac GTPases
Piechulek, T., Rehlen, T., Walliser, C., Vatter, P., Moepps, B., & Gierschik, P. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m509396200 · Cited by 80 · see citing works
Direct Activation of Human Phospholipase C by Its Well Known Inhibitor U73122
Klein, R. R., Bourdon, D., Costales, C., Wagner, C. D., White, W. L., Williams, J. D., Hicks, S. N., Sondek, J., & Thakker, D. R. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.191783 · Cited by 78 · see citing works
Hu, X., Zhang, F. B., Fan, Y. C., Shu, X. S., Wong, A., Zhou, W., Shi, Q. L., Tang, H. M., Fu, L., Guan, X. Y., et al. (2009) · Oncogene · doi:10.1038/onc.2009.92 · Cited by 73 · see citing works
Bunney, T. D., Opaleye, O., Roe, S. M., Vatter, P., Baxendale, R. W., Walliser, C., Everett, K. L., Josephs, M. B., Christow, C., Rodrigues-Lima, F., et al. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.02.023 · Cited by 72 · see citing works
Self-citationMechanism of Activation and Inactivation of Gq/Phospholipase C-β Signaling Nodes
Harden, T. K., Waldo, G. L., Hicks, S. N., & Sondek, J. (2011) · Chemical Reviews · doi:10.1021/cr200209p · Cited by 68 · see citing works
Toward the mechanism of phosphoinositide-specific phospholipases C
Bruzik, K. S., & Tsai, M. (1994) · Bioorganic & Medicinal Chemistry · doi:10.1016/s0968-0896(00)82002-7 · Cited by 67 · see citing works
Danielsen, S. A., Cekaite, L., Ågesen, T. H., Sveen, A., Nesbakken, A., Thiis‐Evensen, E., Skotheim, R. I., Lind, G. E., & Lothe, R. A. (2011) · PLoS ONE · doi:10.1371/journal.pone.0024419 · Cited by 66 · see citing works
Phospholipase C epsilon plays a suppressive role in incidence of colorectal cancer
Wang, X., Zhou, C., Qiu, G., Yang, Y., Yan, D., Xing, T., Fan, J., Tang, H., & Peng, Z. (2011) · Medical Oncology · doi:10.1007/s12032-011-9981-1 · Cited by 65 · see citing works
Characterization of Phospholipase Cγ Enzymes with Gain-of-Function Mutations
Everett, K. L., Bunney, T. D., Yoon, Y., Rodrigues-Lima, F., Harris, R., Driscoll, P. C., Abe, K., Fuchs, H., Hrabé de Angelis, M., Yu, P., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.019265 · Cited by 63 · see citing works
Self-citationThe identification of novel PLC-γ inhibitors using virtual high throughput screening
Reynisson, J., Court, W. J., O’Neill, C., Day, J. E. H., Patterson, L., McDonald, E., Workman, P., Katan, M., & Eccles, S. A. (2009) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2009.02.049 · Cited by 58 · see citing works
Self-citationBerven, L. A., & Barritt, G. J. (1995) · Biochemical Pharmacology · doi:10.1016/0006-2952(95)00050-a · Cited by 58 · see citing works
Tumor suppressor role of phospholipase Cε in Ras-triggered cancers
Martins, M., McCarthy, A., Baxendale, R. W., Guichard, S., Magno, L., Kessaris, N., El-Bahrawy, M. A., Yu, P., & Katan, M. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1311500111 · Cited by 51 · see citing works
Self-citationAbe, K., Fuchs, H., Boersma, A., Hans, W., Yu, P., Kalaydjiev, S., Klaften, M., Adler, T., Calzada‐Wack, J., Mossbrugger, I., et al. (2011) · Arthritis & Rheumatism · doi:10.1002/art.30280 · Cited by 46 · see citing works
Self-citationEvidence for separate effects of U73122 on phospholipase C and calcium channels in human platelets
Pulcinelli, F. M., Gresele, P., Bonuglia, M., & Gazzaniga, P. P. (1998) · Biochemical Pharmacology · doi:10.1016/s0006-2952(98)00146-4 · Cited by 42 · see citing works
Feißt, C., Albert, D., Steinhilber, D., & Werz, O. (2005) · Molecular Pharmacology · doi:10.1124/mol.105.011007 · Cited by 42 · see citing works
Autoinhibition and Phosphorylation-Induced Activation of Phospholipase C-γ Isozymes
Hajicek, N., Charpentier, T. H., Rush, J. R., Harden, T. K., & Sondek, J. (2013) · Biochemistry · doi:10.1021/bi400433b · Cited by 41 · see citing works
Diverse cellular and physiological roles of phospholipase C-γ1
Yang, Y. R., Choi, J. H., Chang, J., Kwon, H. M., Jang, H., Ryu, S. H., & Suh, P. (2011) · Advances in Biological Regulation · doi:10.1016/j.advenzreg.2011.09.017 · Cited by 39 · see citing works
Small Molecule Inhibitors of Phospholipase C from a Novel High-throughput Screen*
Huang, W., Barrett, M. O., Hajicek, N., Hicks, S. C., Harden, T. K., Sondek, J., & Zhang, Q. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.422501 · Cited by 39 · see citing works
Wang, J. P. (1996) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/bf00167177 · Cited by 37 · see citing works
Burgdorf, C., Schäfer, U., Richardt, G., & Kurz, T. (2010) · Journal of Cardiovascular Pharmacology · doi:10.1097/fjc.0b013e3181d8bec5 · Cited by 37 · see citing works
Intramolecular Regulation of Phospholipase C-γ1 by Its C-Terminal Src Homology 2 Domain
DeBell, K. E., Graham, L. J., Reischl, I. G., Serrano, C. J., Bonvini, E., & Rellahan, B. L. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01400-06 · Cited by 36 · see citing works
A Fluorogenic, Small Molecule Reporter for Mammalian Phospholipase C Isozymes
Huang, W., Hicks, S. N., Sondek, J., & Zhang, Q. (2010) · ACS Chemical Biology · doi:10.1021/cb100308n · Cited by 33 · see citing works
Strike a pose: Gαq complexes at the membrane
Lyon, A. M., Taylor, V. G., & Tesmer, J. J. G. (2013) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2013.10.008 · Cited by 30 · see citing works
Membrane Environment Exerts an Important Influence on Rac-Mediated Activation of Phospholipase Cγ2
Everett, K. L., Buehler, A., Bunney, T. D., Margineanu, A., Baxendale, R. W., Vatter, P., Retlich, M., Walliser, C., Manning, H. B., Neil, M. A. A., et al. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.01408-10 · Cited by 25 · see citing works
Self-citationGenetics, genomics, and their relevance to pathology and therapy
Ombrello, M. J., Sikora, K. A., & Kastner, D. L. (2014) · Best Practice & Research Clinical Rheumatology · doi:10.1016/j.berh.2014.05.001 · Cited by 24 · see citing works
Synthesis and Evaluation of Fluorogenic Substrates for Phospholipase D and Phospholipase C
Rose, T. M., & Prestwich, G. D. (2006) · Organic Letters · doi:10.1021/ol060773d · Cited by 24 · see citing works
The PI‐PLC inhibitor U‐73122 is a potent inhibitor of the SERCA pump in smooth muscle
Hollywood, M. A., Sergeant, G. P., Thornbury, K. D., & McHale, N. G. (2010) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2010.00795.x · Cited by 22 · see citing works
Rukavishnikov, A. V., Zaikova, T. O., Birrell, G. B., Keana, J. F. W., & Griffith, O. H. (1999) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(99)00166-3 · Cited by 19 · see citing works
Phosphorothiolate Analogues of Phosphatidylinositols as Assay Substrates for Phospholipase C
Liu, Y., Mihai, C., Kubiak, R. J., Rebecchi, M. J., & Bruzik, K. S. (2007) · ChemBioChem · doi:10.1002/cbic.200700061 · Cited by 14 · see citing works
Auto-inhibition and phosphorylation-induced activation of PLC-gamma isozymes
Hajicek, N., & Sondek, J. (2013) · Worldwide Protein Data Bank · doi:10.2210/pdb4k44/pdb · Cited by 11 · see citing works
Wang, X., Barrett, M. O., Sondek, J., Harden, T. K., & Zhang, Q. (2012) · Biochemistry · doi:10.1021/bi300637h · Cited by 8 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Comprehensive review of targeted therapy for colorectal cancer
Xie, Y.-H., Chen, Y.-X., & Fang, J.-Y. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-0116-z · Cited by 1,687 · see citing works
Integrated molecular analysis of adult T cell leukemia/lymphoma
Kataoka, K., Nagata, Y., Kitanaka, A., Shiraishi, Y., Shimamura, T., Yasunaga, J., Totoki, Y., Chiba, K., Sato‐Otsubo, A., Nagae, G., et al. (2015) · Nature Genetics · doi:10.1038/ng.3415 · Cited by 819 · see citing works
The Inositol Trisphosphate/Calcium Signaling Pathway in Health and Disease
Berridge, M. J. (2016) · Physiological Reviews · doi:10.1152/physrev.00006.2016 · Cited by 757 · see citing works
Neutrophils as emerging therapeutic targets
Németh, T., Sperandio, M., & Mócsai, A. (2020) · Nature Reviews Drug Discovery · doi:10.1038/s41573-019-0054-z · Cited by 657 · see citing works
Lipid metabolism in cancer progression and therapeutic strategies
Fu, Y., Zou, T., Shen, X., Nelson, P. J., Li, J., Wu, C., Yang, J., Zheng, Y., Bruns, C. J., Zhao, Y., et al. (2020) · MedComm · doi:10.1002/mco2.27 · Cited by 406 · see citing works
Protein kinase D at the Golgi controls NLRP3 inflammasome activation
Zhang, Z., Mészáros, G., He, W., Xu, Y., Magliarelli, H. D. F., Mailly, L., Mihlan, M., Liu, Y., Gámez, M. P., Goginashvili, A., et al. (2017) · The Journal of Experimental Medicine · doi:10.1084/jem.20162040 · Cited by 279 · see citing works
Phosphatidylinositol(4,5)bisphosphate: diverse functions at the plasma membrane
Katan, M., & Cockcroft, S. (2020) · Essays in Biochemistry · doi:10.1042/ebc20200041 · Cited by 176 · see citing works
Self-citationAlzheimer’s disease phospholipase C-gamma-2 (PLCG2) protective variant is a functional hypermorph
Magno, L., Lessard, C. B., Martins, M., Lang, V., Cruz, P., Asi, Y., Katan, M., Bilsland, J., Lashley, T., Chakrabarty, P., et al. (2019) · Alzheimer's Research & Therapy · doi:10.1186/s13195-019-0469-0 · Cited by 143 · see citing works
Self-citationProtective genes and pathways in Alzheimer’s disease: moving towards precision interventions
Seto, M., Weiner, R. L., Dumitrescu, L., & Hohman, T. J. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00452-5 · Cited by 135 · see citing works
DESGESCO (Dementia Genetics Spanish Consortium), E. (. D. E. D. B., van der Lee, S. J., biobank), E. (. D. E. D., IFGC (International FTD-Genomics Consortium), I. (. I. P. D. G. C., IPDGC (The International Parkinson Disease Genomics Consortium), Dementia), R.-F. (. A. M. F. I. F.-T., (NBB), N. B. B., The GIFT (Genetic Investigation in Frontotemporal Dementia and Alzheimer’s Disease) Study Group, Conway, O. J., Jansen, I., et al. (2019) · Acta Neuropathologica · doi:10.1007/s00401-019-02026-8 · Cited by 120 · see citing works
Bill, C., & Vines, C. (2019) · Advances in Experimental Medicine and Biology · doi:10.1007/978-3-030-12457-1_9 · Cited by 107 · see citing works
The role of the immune system in Alzheimer’s disease
Wu, K., Zhang, Y.-R., Huang, Y., Dong, Q., Tan, L., & Yu, J. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101409 · Cited by 116 · see citing works
The role of PLCγ2 in immunological disorders, cancer, and neurodegeneration
Jackson, J. T., Mulazzani, E., Nutt, S. L., & Masters, S. L. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100905 · Cited by 113 · see citing works
“PLCγ2 was first cloned in a functional form, including the promoter region, in the hematopoietic Raji cell line (4).”
BackgroundCandidate driver genes involved in genome maintenance and DNA repair in Sézary syndrome
Woollard, W. J., Pullabhatla, V., Lorenc, A., Patel, V. M., Butler, R. M., Bayega, A., Begum, N., Bakr, F. S., Dedhia, K., Fisher, J. N. B., et al. (2016) · Blood · doi:10.1182/blood-2016-02-699843 · Cited by 108 · see citing works
Hajicek, N., Keith, N. C., Siraliev-Perez, E., Temple, B. R., Huang, W., Zhang, Q., Harden, T. K., & Sondek, J. (2019) · eLife · doi:10.7554/elife.51700 · Cited by 89 · see citing works
Phosphoinositide-Dependent Signaling in Cancer: A Focus on Phospholipase C Isozymes
Obeng, E. O., Rusciano, I., Marvi, M. V., Fazio, A., Ratti, S., Follo, M. Y., Xian, J., Manzoli, L., Billi, A. M., Mongiorgi, S., et al. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21072581 · Cited by 85 · see citing works
Novel PLCG2 Mutation in a Patient With APLAID and Cutis Laxa
Neves, J. F., Doffinger, R., Barcena-Morales, G., Martins, C., Papapietro, O., Plagnol, V., Curtis, J., Martins, M., Kumararatne, D., Cordeiro, A. I., et al. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.02863 · Cited by 79 · see citing works
Self-citationThe Role of Phospholipase C Signaling in Macrophage-Mediated Inflammatory Response
Zhu, L., Jones, C., & Zhang, G. (2018) · Journal of Immunology Research · doi:10.1155/2018/5201759 · Cited by 74 · see citing works
Jones, D., Woyach, J. A., Zhao, W., Caruthers, S., Tu, H., Coleman, J., Byrd, J. C., Johnson, A. J., & Lozanski, G. (2017) · Leukemia · doi:10.1038/leu.2017.110 · Cited by 71 · see citing works
Campomanes, P., Zoni, V., & Vanni, S. (2019) · Communications Chemistry · doi:10.1038/s42004-019-0175-7 · Cited by 66 · see citing works
Magno, L., Bunney, T. D., Mead, E., Svensson, F., & Bictash, M. N. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00436-5 · Cited by 64 · see citing works
Self-citationHajicek, N., & Sondek, J. (2019) · Worldwide Protein Data Bank · doi:10.2210/pdb6pbc/pdb · Cited by 58 · see citing works
Martín-Nalda, A., Fortuny, C., Rey, L., Bunney, T. D., Alsina, L., Esteve-Solé, A., Bull, D., Anton, M. C., Basagaña, M., Casals, F., et al. (2020) · Journal of Clinical Immunology · doi:10.1007/s10875-020-00794-7 · Cited by 56 · see citing works
Self-citationClaes, C., England, W. E., Danhash, E. P., Kiani Shabestari, S., Jairaman, A., Chadarevian, J. P., Hasselmann, J., Tsai, A. P., Coburn, M. A., Sanchez, J., et al. (2022) · Alzheimer's & Dementia · doi:10.1002/alz.12577 · Cited by 52 · see citing works
Cognitively healthy centenarians are genetically protected against Alzheimer's disease
Tesi, N., van der Lee, S., Hulsman, M., van Schoor, N. M., Huisman, M., Pijnenburg, Y., van der Flier, W. M., Reinders, M., & Holstege, H. (2024) · Alzheimer's & Dementia · doi:10.1002/alz.13810 · Cited by 52 · see citing works
Mandal, S., Bandyopadhyay, S., Tyagi, K., & Roy, A. (2021) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2021.188619 · Cited by 50 · see citing works
Emerging roles of PLCγ1 in endothelial biology
Chen, D.-Y., & Simons, M. (2021) · Science Signaling · doi:10.1126/scisignal.abc6612 · Cited by 34 · see citing works
Liu, Y., Bunney, T. D., Khosa, S., Macé, K., Beckenbauer, K., Askwith, T., Maslen, S., Stubbs, C., de Oliveira, T. M., Sader, K., et al. (2020) · EBioMedicine · doi:10.1016/j.ebiom.2019.102607 · Cited by 42 · see citing works
Self-citationCXCL8 and the peritoneal metastasis of ovarian and gastric cancer
Fu, X., Wang, Q., Du, H., & Hao, H. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1159061 · Cited by 41 · see citing works
Maguire, E., Menzies, G. E., Phillips, T., Sasner, M., Williams, H. M., Czubala, M. A., Evans, N., Cope, E. L., Sims, R., Howell, G. R., et al. (2021) · The EMBO Journal · doi:10.15252/embj.2020105603 · Cited by 41 · see citing works
Gao, C., Shen, X., Tan, Y., & Chen, S. (2022) · Journal of Neuroinflammation · doi:10.1186/s12974-022-02580-1 · Cited by 43 · see citing works
A Systematic Compilation of Human SH3 Domains: A Versatile Superfamily in Cellular Signaling
Mehrabipour, M., Jasemi, N. S. K., Dvorský, R., & Ahmadian, M. R. (2023) · Cells · doi:10.3390/cells12162054 · Cited by 39 · see citing works
Regulation and physiological functions of mammalian phospholipase C
Nakamura, Y., & Fukami, K. (2017) · Journal of Biochemistry · doi:10.1093/jb/mvw094 · Cited by 122 · see citing works
A gain-of-function variation in PLCG1 causes a new immune dysregulation disease
Tao, P., Han, X., Wang, Q., Wang, S., Zhang, J., Liu, L., Fan, X., Liu, C., Liu, M., Guo, L., et al. (2023) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2023.06.020 · Cited by 38 · see citing works
Obst, J., Hall-Roberts, H. L., Smith, T. B., Kreuzer, M., Magno, L., Di Daniel, E., Davis, J. B., & Mead, E. (2021) · Scientific Reports · doi:10.1038/s41598-021-96144-7 · Cited by 36 · see citing works
Holme, M. N., Rashid, M. H., Thomas, M. R., Barriga, H. M. G., Herpoldt, K., Heenan, R. K., Dreiss, C. A., Bañuelos, J. L., Xie, H., Yarovsky, I., et al. (2018) · ACS Central Science · doi:10.1021/acscentsci.8b00286 · Cited by 36 · see citing works
Kim, K., Kim, Y., Rivard, C. J., Kim, D., & Park, K.-S. (2020) · Cancer Research · doi:10.1158/0008-5472.can-20-1453 · Cited by 35 · see citing works
Wist, M., Meier, L., Gutman, O., Haas, J., Endres, S., Zhou, Y., Rösler, R., Wiese, S., Stilgenbauer, S., Hobeika, E., et al. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.011946 · Cited by 34 · see citing works
Patel, V. M., Flanagan, C. E., Martins, M., Jones, C. L., Butler, R. M., Woollard, W. J., Bakr, F. S., Yoxall, A., Begum, N., Katan, M., et al. (2019) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2019.07.693 · Cited by 31 · see citing works
Self-citationPLCγ1 suppression promotes the adaptation of KRAS-mutant lung adenocarcinomas to hypoxia
Saliakoura, M., Sebastiano, M. R., Pozzato, C., Heidel, F. H., Schnoeder, T. M., Prince, S. S., Bubendorf, L., Pinton, P., Schmid, R. A., Baumgartner, J., et al. (2020) · Nature Cell Biology · doi:10.1038/s41556-020-00592-8 · Cited by 31 · see citing works
Gramolelli, S., Weidner-Glunde, M., Abere, B., Viejo‐Borbolla, A., Bala, K., Rückert, J., Kremmer, E., & Schulz, T. F. (2015) · PLoS Pathogens · doi:10.1371/journal.ppat.1005105 · Cited by 30 · see citing works
Angiotensin Converting Enzyme Regulates Cell Proliferation and Migration
de Alvarenga, É. C., Fonseca, M. D. C., Carvalho, C. C., Florentino, R. M., França, A., Matias, E., Guimarães, P. B., Batista, C., Freire, V. N., Carmona, A. K., et al. (2016) · PLoS ONE · doi:10.1371/journal.pone.0165371 · Cited by 30 · see citing works
Biochemistry of Autoinflammatory Diseases: Catalyzing Monogenic Disease
Beck, D. B., & Aksentijevich, I. A. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.00101 · Cited by 29 · see citing works
Phospholipase Cγ2 regulates endocannabinoid and eicosanoid networks in innate immune cells
Jing, H., Reed, A., Ulanovskaya, O. A., Grigoleit, J.-S., Herbst, D. M., Henry, C. L., Li, H., Barbas, S., Germain, J., Masuda, K., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2112971118 · Cited by 24 · see citing works
Xu, X., & Jin, T. (2015) · Journal of Immunology Research · doi:10.1155/2015/817604 · Cited by 26 · see citing works
Fong, W., Sánchez‐Ferrer, A., Rappolt, M., Boyd, B. J., & Mezzenga, R. (2019) · Langmuir · doi:10.1021/acs.langmuir.9b02288 · Cited by 22 · see citing works
Indole-3-Carbinol and Its Derivatives as Neuroprotective Modulators
Singh, A. A., Yadav, D., Khan, F., & Song, M. (2024) · Brain Sciences · doi:10.3390/brainsci14070674 · Cited by 22 · see citing works
Oncogenic role of phospholipase C‐γ1 in progression of hepatocellular carcinoma
Tang, W., Zhou, Y., Sun, D., Dong, L., Xia, J., & Yang, B. (2019) · Hepatology Research · doi:10.1111/hepr.13309 · Cited by 22 · see citing works
Le Huray, K. I. P., Bunney, T. D., Pinotsis, N., Kalli, A. C., & Katan, M. (2022) · Science Advances · doi:10.1126/sciadv.abp9688 · Cited by 21 · see citing works
Self-citationCoordinated loss of microRNA group causes defenseless signaling in malignant lymphoma
Yamagishi, M., Katano, H., Hishima, T., Shimoyama, T., Ota, Y., Nakano, K., Ishida, T., Okada, S., & Watanabe, T. (2015) · Scientific Reports · doi:10.1038/srep17868 · Cited by 21 · see citing works
Ren, Y., Li, H., Yao, J., Tan, Y., Pan, L., Peng, T., Zhao, L., Zhang, G., Yue, J., Hu, X., et al. (2020) · Journal of Proteomics · doi:10.1016/j.jprot.2020.103691 · Cited by 20 · see citing works
Puig, S., Xue, X., Salisbury, R. B., Shelton, M. A., Kim, S.-M., Hildebrand, M. A., Glausier, J. R., Freyberg, Z., Tseng, G. C., Yocum, A. K., et al. (2023) · Molecular Psychiatry · doi:10.1038/s41380-023-02241-6 · Cited by 19 · see citing works
Phosphorylation of PLCγ1 by EphA2 Receptor Tyrosine Kinase Promotes Tumor Growth in Lung Cancer
Song, W., Kim, L. C., Han, W., Hou, Y., Edwards, D. N., Wang, S., Blackwell, T. S., Cheng, F., Brantley‐Sieders, D. M., & Chen, J. (2020) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-20-0075 · Cited by 18 · see citing works
Dynamics of allosteric regulation of the phospholipase C-γ isozymes upon recruitment to membranes
Siraliev-Perez, E., Stariha, J. T., Hoffmann, R. M., Temple, B. R., Zhang, Q., Hajicek, N., Jenkins, M. L., Burke, J. E., & Sondek, J. (2022) · eLife · doi:10.7554/elife.77809 · Cited by 18 · see citing works
Li, K., Ran, B., Wang, Y., Liu, L., & Li, W. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.999061 · Cited by 18 · see citing works
Demin, K. A., Krotova, N. A., Ilyin, N. P., Galstyan, D. S., Kolesnikova, T. O., Strekalova, T. V., de Abreu, M. S., Petersen, E. V., Zabegalov, K. N., & Kalueff, A. V. (2022) · Scientific Reports · doi:10.1038/s41598-022-22688-x · Cited by 19 · see citing works
Yang, Z., Kim, S., Mahajan, S., Zamani, A., & Faccio, R. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.764928 · Cited by 17 · see citing works
Li, Z., Liu, Y., Yi, H., Cai, T., & Wei, Y. (2022) · Frontiers in Genetics · doi:10.3389/fgene.2022.947747 · Cited by 16 · see citing works
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 15 · see citing works
Inositide-dependent signaling pathways as new therapeutic targets in myelodysplastic syndromes
Mongiorgi, S., Finelli, C., Yang, Y. R., Clissa, C., McCubrey, J. A., Billi, A. M., Manzoli, L., Suh, P., Cocco, L., & Follo, M. Y. (2015) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2016.1125885 · Cited by 15 · see citing works
Easter, M., Garth, J. M., Harris, E. S., Shei, R., Helton, E. S., Wei, Y., Denson, R. S., Zaharias, R. S., Rowe, S. M., Geraghty, P. M., et al. (2020) · Frontiers in Medicine · doi:10.3389/fmed.2020.00317 · Cited by 14 · see citing works
Construction of an Immunogenomic Risk Score for Prognostication in Colon Cancer
Zhang, H., Qin, C., Gan, H., Guo, X., & Zhang, L. (2020) · Frontiers in Genetics · doi:10.3389/fgene.2020.00499 · Cited by 13 · see citing works
Mu, T., Hu, H., Ma, Y., Yang, C., Feng, X., Wang, Y., Liu, J., Yu, B., Zhang, J., & Gu, Y. (2022) · Animal Genetics · doi:10.1111/age.13249 · Cited by 12 · see citing works
Reduced PLCG1 expression is associated with inferior survival for myelodysplastic syndromes
Shiseki, M., Ishii, M., Miyazaki, M., Osanai, S., Wang, Y., Yoshinaga, K., Mori, N., & Tanaka, J. (2019) · Cancer Medicine · doi:10.1002/cam4.2717 · Cited by 12 · see citing works
Prawiro, C., Bunney, T. D., Kampyli, C., Yaguchi, H., Katan, M., & Bangham, C. R. M. (2022) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2022.166601 · Cited by 11 · see citing works
Self-citationDynamic Allostery in PLCγ1 and Its Modulation by a Cancer Mutation Revealed by MD Simulation and NMR
Koss, H., Bunney, T. D., Esposito, D., Martins, M., Katan, M., & Driscoll, P. C. (2018) · Biophysical Journal · doi:10.1016/j.bpj.2018.05.031 · Cited by 10 · see citing works
Self-citationTime-resolved FRET reports FGFR1 dimerization and formation of a complex with its effector PLCγ1
Perdios, L., Bunney, T. D., Warren, S. C., Dunsby, C. W., French, P. M. W., Tate, E. W., & Katan, M. (2015) · Advances in Biological Regulation · doi:10.1016/j.jbior.2015.09.002 · Cited by 9 · see citing works
Self-citationGuo, J., Xia, T.-Y., Deng, S.-H., Xue, W., Cui, B., & Liu, Y. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.668888 · Cited by 9 · see citing works
Zazzo, A. D., Tahvildari, M., Florakis, G. J., & Dana, R. (2016) · Cornea · doi:10.1097/ico.0000000000000951 · Cited by 9 · see citing works
Characterisation of molecular mechanisms for PLCγ2 disease-linked variants
Bunney, T. D., Kampyli, C., Gregory, A., & Katan, M. (2024) · Advances in Biological Regulation · doi:10.1016/j.jbior.2024.101053 · Cited by 8 · see citing works
Self-citationShin, Y.-C., Plummer-Medeiros, A. M., Mungenast, A., Choi, H.-W., TenDyke, K., Zhu, X., Shepard, J., Sanders, K., Zhuang, N., Hu, L., et al. (2024) · Science Advances · doi:10.1126/sciadv.adn6037 · Cited by 7 · see citing works
Phospholipase C-γ as a Potential Therapeutic Target for Graves’ Orbitopathy
Roh, T. H., Chae, M. K., Ko, J., Kikkawa, D. O., Jang, S. Y., & Yoon, J. S. (2023) · Endocrinology and Metabolism · doi:10.3803/enm.2023.1780 · Cited by 7 · see citing works
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 · see citing works
Nosbisch, J. L., Bear, J. E., & Haugh, J. M. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.101886 · Cited by 7 · see citing works
Okada, M., Nakagawa-Saito, Y., Mitobe, Y., Sugai, A., Togashi, K., Suzuki, S., & Kitanaka, C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23158785 · Cited by 7 · see citing works
APLAID complicated with arrhythmogenic dilated cardiomyopathy caused by a novel PLCG2 variant
Wang, T., Wang, X., Teng, Y., Wu, L., Zhu, F. Y., Ma, D., Wang, H., & Liu, X. (2024) · Immunologic Research · doi:10.1007/s12026-024-09455-y · Cited by 7 · see citing works
Fluorogenic XY-69 in Lipid Vesicles for Measuring Activity of Phospholipase C Isozymes
Carr, A. J., Siraliev-Perez, E., Huang, W., Sondek, J., & Zhang, Q. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1142-5_17 · Cited by 7 · see citing works
Tripathi, N., Vetrivel, I., Télétchéa, S., Jean, M., Legembre, P., & Laurent, A. D. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20194721 · Cited by 7 · see citing works
Tesi, N., van der Lee, S. J., Hulsman, M., van Schoor, N. M., Huisman, M. A., Pijnenburg, Y. A. L., van der Flier, W. M., Reinders, M. J. T., & Holstege, H. H. (2023) · medRxiv · doi:10.1101/2023.05.16.23290049 · Cited by 7 · see citing works
A PI(4,5)P2‐derived “gasoline engine model” for the sustained B cell receptor activation
Xu, C., Wan, Z., Shaheen, S., Wang, J., Yang, Z., & Liu, W. (2019) · Immunological Reviews · doi:10.1111/imr.12775 · Cited by 6 · see citing works
Perestrelo, R., Petković, M., & Silva, C. L. (2021) · Metabolites · doi:10.3390/metabo11010032 · Cited by 6 · see citing works
Xu, X., Wen, X., Bhimani, S., Moosa, A., Parsons, D., Ha, H., & Jin, T. (2023) · Journal of Leukocyte Biology · doi:10.1093/jleuko/qiad043 · Cited by 6 · see citing works
Samarina, N., Ssebyatika, G. L., Tikla, T., Waldmann, J.-Y., Abere, B., Nanna, V., Marasco, M., Carlomagno, T., Krey, T., & Schulz, T. F. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009635 · Cited by 6 · see citing works
T Cell Receptor Pathway Mutations in Mature T Cell Lymphomas
Zhang, Y., Cheng, K., & Choi, J. (2023) · Journal of Immunology · doi:10.4049/jimmunol.2200682 · Cited by 4 · see citing works
Hamdi, M., Al-Matwi, M. A., Elghoul, N., Al-Kuwari, H., Sayed, T. S., Riguene, E., & Nomikos, M. (2025) · Medicina · doi:10.3390/medicina61061054 · Cited by 5 · see citing works
Faecal Proteomics and Functional Analysis of Equine Melanocytic Neoplasm in Grey Horses
Tesena, P., Kingkaw, A., Phaonakrop, N., Roytrakul, S., Limudomporn, P., Vongsangnak, W., & Kovitvadhi, A. (2022) · Veterinary Sciences · doi:10.3390/vetsci9020094 · Cited by 5 · see citing works
Mondejar, R., Pérez, C., Onaindía, A., Martı́nez, N., González‐Rincón, J., Pisonero, H., Vaque, J. P., Cereceda, L., Santibáñez, M., Sánchez‐Beato, M., et al. (2017) · PLoS ONE · doi:10.1371/journal.pone.0177524 · Cited by 5 · see citing works
Chen, X.-G., Zhu, X.-M., Wei, Z., & Lv, Q.-X. (2019) · Journal of Cellular Biochemistry · doi:10.1002/jcb.29294 · Cited by 3 · see citing works
Dumková, J., Vaškovicová, N., Kristeková, D., Vrlíková, L., Faruzelová, A., Jedličková, A., Tatíčková, M., Alexa, L., Coufalík, P., Bahelková, M., et al. (2025) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2025.139181 · Cited by 4 · see citing works
Xu, X., Kim, W. S., Lee, A. M., & Jin, T. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1633390 · Cited by 4 · see citing works
Phosphoinositide-specific phospholipase C enzymes: Recent advances in a long journey
Macrae, C., Lalović, D., Bunney, T. D., & Katan, M. (2025) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2025.159627 · Cited by 4 · see citing works
Self-citationExposed: The Many and Varied Roles of Phospholipase C γ SH2 Domains
Driscoll, P. C. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2015.06.002 · Cited by 4 · see citing works
Editorial: Microglia and peripheral immune cells in aging and neurodegenerative diseases
Qiu, Y., Shen, X., & Xu, H. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1178496 · Cited by 4 · see citing works
Maguire, E., Menzies, G. E., Phillips, T., Sasner, M., Williams, H. M., Czubala, M. A., Evans, N., Cope, E. L., Sims, R., Howell, G. R., et al. (2020) · doi:10.1101/2020.04.27.059600 · Cited by 4 · see citing works
Puig, S., Xue, X., Salisbury, R. B., Shelton, M. A., Kim, S.-M., Hildebrand, M. A., Glausier, J. R., Freyberg, Z., Tseng, G. C., Yocum, A. K., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.04.07.536056 · Cited by 3 · see citing works
Visvanathan, R., Utsuki, T., Beck, D. E., Clayton, B., Lendy, E. K., Sun, K.-L., Liu, Y., Hering, K. W., Mesecar, A. D., Zhang, Z., et al. (2024) · PLoS ONE · doi:10.1371/journal.pone.0299541 · Cited by 2 · see citing works
Resveratrol alleviates stress-associated bursal injury in chickens: a transcriptomic analysis
Laghari, F., Zhang, H., He, C., Gong, H., Zhang, J., Chang, Q., Bao, J., & Zhang, R. (2025) · British Poultry Science · doi:10.1080/00071668.2025.2512376 · Cited by 2 · see citing works
Chen, X., Zhu, X., Wei, Z., & Lv, Q. (2020) · Cytology and Genetics · doi:10.3103/s009545272006002x · Cited by 2 · see citing works
Biochemical mechanisms in the regulation of phospholipases
Adefegha, S. A., Molehin, O. R., & Adeleke, O. V. (2023) · Elsevier eBooks · doi:10.1016/b978-0-443-15313-6.00006-5 · Cited by 2 · see citing works
A case report of autoinflammation and PLCy2-associated antibody deficiency and immune dysregulation
Leonteva, M. E., Bogdanova, D. V., Moiseeva, A. A., Бурлаков, В. И., Нестеренко, З. А., Merkushov, A. Y., Kan, N. Y., Khoreva, А. L., Rodina, Y. A., Shvets, O. A., et al. (2022) · Pediatric Hematology/Oncology and Immunopathology · doi:10.24287/1726-1708-2022-21-4-163-168 · Cited by 1 · see citing works
- Authors
- Koss, H., Bunney, T. D., Behjati, S., & Katan, M.
- Affiliations
- Institute of Structural and Molecular Biology (GB)
- Wellcome Sanger Institute (GB)
- Corresponding author
- Bunney, Tom D.
- Katan, Matilda
- Venue
- Trends in Biochemical Sciences
- Publisher
- Elsevier BV
- Published
- 2014-12
- Volume
- 39
- Issue
- 12
- Pages
- 603-611
- ISSN
- 0968-0004 (ISSN-L)
- OpenAlex
- W2090368019
- Cited by
- 115
- References
- 57
- Citations by year
- 2026: 1 · 2025: 7 · 2024: 6 · 2023: 17 · 2022: 14 · 2021: 13 · 2020: 20 · 2019: 12 · 2018: 5 · 2017: 6 · 2016: 6 · 2015: 8
- FWCI
- 0.63
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Trends in Biochemical Sciences (publishedVersion)
- PubMed (publishedVersion)
- UCL Discovery (University College London) (submittedVersion)
- Funders
- Wellcome Trust
- Cancer Research UK (16567)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Life Sciences › Immunology and Microbiology › Immunology › Immunodeficiency and Autoimmune Disorders
- Keywords
- phospholipase C-gamma, immune disorders, cancer, gain-of-function mutations, intracellular signaling, disease pathophysiology, genetic variants
- MeSH terms
- Animals, Diglycerides, Humans, Immune System Diseases, Models, Biological, Models, Molecular, Mutation, Neoplasms, Protein Conformation, Second Messenger Systems, Inositol 1,4,5-Trisphosphate, 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
