The DOI matches its Crossref record; 50 of the 50 references it cites were found in a registry or an index.
Regulation of Phosphoinositide-specific Phospholipase C Isozymes
Open accessAbstract
The hydrolysis of a minor membrane phospholipid, phosphatidylinositol 4,5-bisphosphate (PIP2), 1The abbreviations used are: PIP2, phosphatidylinositol 4,5-bisphosphate; PLC, phospholipase C; PKC, protein kinase C; PLD, phospholipase D; PI 3-kinase, phosphoinositide 3-kinase; PH, pleckstrin homology; SH, Src homology; GTPγS, guanosine 5′-3-O-(thio)triphosphate; IL, interleukin; PDGF, platelet-derived growth factor; PTK, protein tyrosine kinase; AA, arachidonic acid; PC, phosphatidylcholine; cPLA2, cytosolic phospholipase A2; PIP3, phosphatidylinositol 3,4,5-trisphosphate; α1-AR, α1-adrenergic receptor(s); PKA, cAMP-dependent protein kinase. by a specific phospholipase C (PLC) is one of the earliest key events in the regulation of various cell functions by more than 100 extracellular signaling molecules (1Rhee S.G. Choi K.D. J. Biol. Chem. 1992; 267: 12393-12396Abstract Full Text PDF PubMed Google Scholar, 2Cockcroft S. Thomas G.M.H. Biochem. J. 1992; 288: 1-14Crossref PubMed Scopus (371) Google Scholar, 3Berridge M.J. Nature. 1993; 361: 315-325Crossref PubMed Scopus (6196) Google Scholar, 4Noh D.-Y. Shin S.H. Rhee S.G. Biochim. Biophys. Acta. 1995; 1242: 99-114Crossref PubMed Scopus (256) Google Scholar). This reaction produces two intracellular messengers, diacylglycerol and inositol 1,4,5-trisphosphate, which mediate the activation of protein kinase C (PKC) and intracellular Ca2+ release, respectively. Furthermore, a decrease in the amount of PIP2 itself in the cell membrane is likely an important signal because the activities of several proteins are modulated by this phospholipid (5Lee S.B. Rhee S.G. Curr. Opin. Cell Biol. 1995; 7: 183-189Crossref PubMed Scopus (285) Google Scholar). PIP2 is a cofactor for phosphatidylcholine-specific phospholipase D (PLD) and a substrate for phosphoinositide 3-kinase (PI 3-kinase), both of which are also receptor-activated effector enzymes. In addition, PIP2modulates actin polymerization by interacting with various actin-binding proteins and serves as a membrane-attachment site for many signaling proteins that contain pleckstrin homology (PH) domains. Consequently, the activity of PLC is stringently regulated in cells through several distinct mechanisms that link multiple PLC isoforms to various receptors. The 10 mammalian PLC isozymes (excluding alternatively spliced forms) identified to date are all single polypeptides and can be divided into three types, β, γ, and δ, of which four PLC-β, two PLC-γ, and four PLC-δ proteins are known (1Rhee S.G. Choi K.D. J. Biol. Chem. 1992; 267: 12393-12396Abstract Full Text PDF PubMed Google Scholar, 2Cockcroft S. Thomas G.M.H. Biochem. J. 1992; 288: 1-14Crossref PubMed Scopus (371) Google Scholar, 3Berridge M.J. Nature. 1993; 361: 315-325Crossref PubMed Scopus (6196) Google Scholar, 4Noh D.-Y. Shin S.H. Rhee S.G. Biochim. Biophys. Acta. 1995; 1242: 99-114Crossref PubMed Scopus (256) Google Scholar, 5Lee S.B. Rhee S.G. Curr. Opin. Cell Biol. 1995; 7: 183-189Crossref PubMed Scopus (285) Google Scholar). The δ-type isozymes are smaller (M r 85,000) than the PLC-β and PLC-γ (M r 140,000–155,000) isoforms. Lower eukaryotes such as yeast and slime molds contain only δ-type isozymes, suggesting that β- and γ-type isoforms in higher eukaryotes evolved from the archetypal PLC-δ. Two regions of high sequence homology (40–60% identity), designated X and Y, constitute the PLC catalytic domain (1Rhee S.G. Choi K.D. J. Biol. Chem. 1992; 267: 12393-12396Abstract Full Text PDF PubMed Google Scholar, 2Cockcroft S. Thomas G.M.H. Biochem. J. 1992; 288: 1-14Crossref PubMed Scopus (371) Google Scholar, 3Berridge M.J. Nature. 1993; 361: 315-325Crossref PubMed Scopus (6196) Google Scholar, 4Noh D.-Y. Shin S.H. Rhee S.G. Biochim. Biophys. Acta. 1995; 1242: 99-114Crossref PubMed Scopus (256) Google Scholar, 5Lee S.B. Rhee S.G. Curr. Opin. Cell Biol. 1995; 7: 183-189Crossref PubMed Scopus (285) Google Scholar) (Fig.1). A PH domain is located in the NH2-terminal region, preceding the X domain, in all three types of PLC. Whereas PLC-β and PLC-δ isozymes contain a short sequence of 50–70 amino acids that separates the X and Y regions, PLC-γ isozymes have a long sequence of ∼400 amino acids that contains Src homology (SH) (two SH2 and one SH3) domains. PLC-γ isozymes contain an additional PH domain that is split by the SH domains. PH (∼100 residues), SH2 (∼100 residues), and SH3 (∼50 residues) domains are protein modules that are shared by many signaling proteins; whereas PH domains mediate interaction with the membrane surface by binding to PIP2, SH domains mediate interactions with other proteins by binding to phosphorylated tyrosine residues (SH2) or proline-rich sequences (SH3). The three-dimensional structure of a PLC-δ1 molecule lacking the PH domain has recently been determined (6Essen L.-O. Perisic O. Cheung R. Katan M. Williams R.L. Nature. 1996; 380: 595-602Crossref PubMed Scopus (519) Google Scholar). As expected, the X and Y regions are tightly assoc
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“PLCγ is known to be recruited to the vicinity of activated receptors through interaction of its dual SH2 domains with phosphotyrosine residues on receptor–adaptor complexes (Rhee and Bae 1997).”
From Localized Biphasic Changes in Phosphatidylinositol-4,5-Bisphosphate at Sites of Phagocytosis (2000) · cites this paper as Rhee and Bae 1997
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“PLCγ2 is a signalling enzyme activated through tyrosine phosphorylation by receptor and non-receptor kinases7.”
From PLCγ2 regulates TREM2 signalling and integrin-mediated adhesion and migration of human iPSC-derived macrophages (2021) · cites this paper as [7]
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
Inositol trisphosphate and calcium signalling
Berridge, M. J. (1993) · Nature · doi:10.1038/361315a0 · Cited by 6,545
Epidermal Growth Factor (EGF)-induced Generation of Hydrogen Peroxide
Bae, Y. S., Kang, S. W., Seo, M. S., Baines, I., Tekle, E., Chock, P. B., & Rhee, S. G. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.1.217 · Cited by 1,208
Self-citationA role for Pyk2 and Src in linking G-protein-coupled receptors with MAP kinase activation
Đikić, I., Tokiwa, G. Y., Lev, S., Courtneidge, S. A., & Schlessinger, J. (1996) · Nature · doi:10.1038/383547a0 · Cited by 955
Regulation of inositol phospholipid-specific phospholipase C isozymes.
Rhee, S. G., & Choi, K. D. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42284-3 · Cited by 741
Self-citationDivecha, N., & Irvine, R. F. (1995) · Cell · doi:10.1016/0092-8674(95)90409-3 · Cited by 570
G h : a GTP-Binding Protein with Transglutaminase Activity and Receptor Signaling Function
Nakaoka, H., Perez, D. M., Baek, K. J., Das, T., Husain, A., Misono, K. S., Im, M.-J., & Graham, R. M. (1994) · Science · doi:10.1126/science.7911253 · Cited by 547
Crystal structure of a mammalian phosphoinositide-specific phospholipase Cδ
Essen, L., Perišić, O., Cheung, R., Katan, M., & Williams, R. L. (1996) · Nature · doi:10.1038/380595a0 · Cited by 534
Inositol-lipid-specific phospholipase C isoenzymes and their differential regulation by receptors
Cockcroft, S., & Thomas, G. M. H. (1992) · Biochemical Journal · doi:10.1042/bj2880001 · Cited by 365
Nuclear localization and signalling activity of phosphoinositidase Cβ in Swiss 3T3 cells
Martelli, A. M., Gilmour, R., Bertagnolo, V., Neri, L. M., Manzoli, L., & Cocco, L. (1992) · Nature · doi:10.1038/358242a0 · Cited by 322
Significance of PIP2 hydrolysis and regulation of phospholipase C isozymes
Lee, S. B., & Rhee, S. G. (1995) · Current Opinion in Cell Biology · doi:10.1016/0955-0674(95)80026-3 · Cited by 284
Self-citation
Flagged first, then by citations
Research works printed but not linked: 3
- Noh, 1995, Biochim. Biophys. Acta, 1242, 99
- Manzoli, L., Billi, A. M., Rubbini, S., Bavelloni, A., Gilmour, R. S., Rhee, S. G., and Cocco, L. (1997) Cancer Res., in press.
- Flick, 1993, Mol. Cell. Biol., 13, 5861
Cited by
Sorted by citations
Items 601–700 of 877
Gentili, C., Boland, R., & de Boland, A. R. (2006) · Journal of Endocrinology · doi:10.1677/joe.1.06397 · Cited by 15
Bertagnolo, V., Marchisio, M., Pierpaoli, S., Colamussi, M. L., Brugnoli, F., Visani, G., Zauli, G., & Capitani, S. (2002) · Journal of Leukocyte Biology · doi:10.1189/jlb.71.6.957 · Cited by 19
Phospholipase Cγ activation and phosphoinositide hydrolysis are essential for embryonal development
Schlessinger, J. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.7.2798 · Cited by 15
Stimulation of phospholipase C-β2 by Rho GTPases
Illenberger, D., Stephan, I., Gierschik, P., & Schwald, F. (2000) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(00)25441-4 · Cited by 15
Phospholipase C activity from Catharanthus roseus transformed roots: aluminum effect
Piña-Chable, M. L., & Hernández‐Sotomayor, S. M. T. (2001) · Prostaglandins & Other Lipid Mediators · doi:10.1016/s0090-6980(01)00113-7 · Cited by 15
Z-scan fluorescence profile deconvolution of cytosolic and membrane-associated protein populations
Smith, E. M., Hennen, J., Chen, Y., & Mueller, J. D. (2015) · Analytical Biochemistry · doi:10.1016/j.ab.2015.03.030 · Cited by 14
Yamaga, M., Kawai, K., Kiyota, M., Homma, Y., & Yagisawa, H. (2007) · Advances in Enzyme Regulation · doi:10.1016/j.advenzreg.2007.11.006 · Cited by 14
Phospholipase C-β1 Hypofunction in the Pathogenesis of Schizophrenia
Kim, S.-W., Cho, T., & Lee, S. (2015) · Frontiers in Psychiatry · doi:10.3389/fpsyt.2015.00159 · Cited by 14
Waksmunski, A. R., Grunin, M., Kinzy, T. G., Igo, R. P., Haines, J. L., Cooke Bailey, J. N., & for the International Age-Related Macular Degeneration Genomics Consortium (2019) · Investigative Opthalmology & Visual Science · doi:10.1167/iovs.19-27827 · Cited by 14
Giguère, P. M., Laroche, G., Oestreich, E. A., & Siderovski, D. P. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.311712 · Cited by 14
Activators of G proteins inhibit GSK-3β and stabilize β-Catenin in Xenopus oocytes
Najafi, S. M. A. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.03.027 · Cited by 14
Highway to thermosensation: a traced review, from the proteins to the brain
Ezquerra-Romano, I., & Ezquerra, Á. (2016) · Reviews in the Neurosciences · doi:10.1515/revneuro-2016-0039 · Cited by 14
Acharya, S., Kundu, D., Choi, H. J., & Kim, K. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2020.118721 · Cited by 14
Inhibition of the EGF-induced activation of phospholipase C-γ1 by a single chain antibody fragment
Yi, K. S., Chung, J. H., Lee, Y. H., Chung, H. G., Kim, I. J., Suh, B., Kim, E., Cocco, L., Ryu, S. H., & Suh, P. (2001) · Oncogene · doi:10.1038/sj.onc.1204959 · Cited by 14
Phospholipid-mediated signaling in diseased myocardium
Tappia, P. S., Singal, T., Dent, M. R., Asemu, G., Rabban, M., & Dhalla, N. S. (2006) · Future Lipidology · doi:10.2217/17460875.1.6.701 · 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
Carraway, R. E., Gui, X., & Cochrane, D. E. (2003) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.102.052688 · Cited by 14
Differential effects of Cbl and 70Z/3 Cbl on T cell receptor‐induced phospholipase Cγ‐1 activity
Graham, L. J., DeBell, K. E., Verı́, M.-C., Stoica, B. A., Mostowski, H. S., Bonvini, E., & Rellahan, B. L. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01341-7 · Cited by 14
G Protein-Coupled Receptor-Mediated Calcium Signaling in Astrocytes
Pittà, M. D., Ben‐Jacob, E., & Berry, H. (2019) · Springer series in computational neuroscience · doi:10.1007/978-3-030-00817-8_5 · Cited by 15
Kinomic profiling of glioblastoma cells reveals PLCG1 as a target in restricted glucose
Walker, K. D., Boyd, N., Anderson, J. C., Willey, C. D., & Hjelmeland, A. B. (2018) · Biomarker Research · doi:10.1186/s40364-018-0136-9 · Cited by 13
Yun, S., Hong, W.-P., Choi, J. H., Yi, K. S., Chae, S., Ryu, S. H., & Suh, P. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704180200 · 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
Putative roles for phospholipase Cη enzymes in neuronal Ca2+ signal modulation
Popovics, P., & Stewart, A. J. (2012) · Biochemical Society Transactions · doi:10.1042/bst20110622 · Cited by 13
Hozumi, Y., Kakefuda, K., Yamasaki, M., Watanabe, M., Hara, H., & Goto, K. (2014) · Brain Research · doi:10.1016/j.brainres.2014.11.012 · Cited by 13
Guerra, F. M., Gommerman, J., Corfe, S. A., Paige, C., & Rottapel, R. (2012) · PLoS ONE · doi:10.1371/journal.pone.0035533 · Cited by 13
D’Andrea, M. R., Mei, J. M., Tuman, R. W., Galemmo, R. A., & Johnson, D. L. (2005) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-05-0004 · Cited by 13
The G‐protein‐coupled CCK2 receptor associates with phospholipase Cγ1
Arnould, M., Tassa, A., Ferrand, A., Archer-Lahlou, É., Estève, J., Pénalba, V., Portolan, G., Escherich, A., Moroder, L., Fourmy, D., et al. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.05.012 · Cited by 13
Nuclear factor-κB regulates expression of platelet phospholipase C-β2 (PLCB2)
Mao, G., Jin, J., Kunapuli, S. P., & Rao, A. K. (2016) · Thrombosis and Haemostasis · doi:10.1160/th15-09-0749 · Cited by 13
Kosugi, T., Osanai, T., Kamada, T., Nakano, T., & Okumura, K. (2003) · Journal of Hypertension · doi:10.1097/00004872-200303000-00025 · 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
Insulin secretion and IP levels in two distant lineages of the genusMus: comparisons with rat islets
Zawalich, W. S., Zawalich, K. C., Tesz, G. J., Sterpka, J., & Philbrick, W. M. (2001) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.2001.280.5.e720 · Cited by 14
Strassheim, D., Law, P., & Loh, H. H. (1998) · Molecular Pharmacology · doi:10.1016/s0026-895x(24)13275-0 · Cited by 13
Wu, Y.-N., Su, X., Wang, X., Liu, N., & Xu, Z.-W. (2023) · Frontiers in Oncology · doi:10.3389/fonc.2023.1231875 · Cited by 12
Chen, Y., Zhao, N., Xu, L., Jia, X., Liu, F., Huang, J., Li, X., Wang, Y., Lai, C., Shen, Y., et al. (2025) · Molecular Cancer · doi:10.1186/s12943-025-02359-x · Cited by 13
Tappia, P. S., Liu, S., Tong, Y., Ssenyange, S., & Panagia, V. (2001) · Advances in experimental medicine and biology · doi:10.1007/978-1-4615-1321-6_24 · Cited by 12
Phosphorylation of Phospholipase C‐δ1 Regulates its Enzymatic Activity
Fujii, M., Yi, K. S., Kim, M. J., Ha, S. H., Ryu, S. H., Suh, P., & Yagisawa, H. (2009) · Journal of Cellular Biochemistry · doi:10.1002/jcb.22297 · Cited by 12
Awasthi, M., Batra, J., & Kateriya, S. (2012) · PLoS ONE · doi:10.1371/journal.pone.0039258 · Cited by 12
Phospholipase Cγ1 is required for pre‐TCR signal transduction and pre‐T cell development
Fu, G., Yu, M., Chen, Y., Zheng, Y., Zhu, W., Newman, D. K., Wang, D., & Wen, R. (2016) · European Journal of Immunology · doi:10.1002/eji.201646522 · Cited by 12
Kimura, M., Kurihara, K., Moteki, H., & Ogihara, M. (2021) · Journal of Pharmacy & Pharmaceutical Sciences · doi:10.18433/jpps31586 · Cited by 12
Autocrine regulation of airway smooth muscle contraction by diacylglycerol kinase
Yadav, S. K., Sharma, P. K., Shah, S. D., Panettieri, R. A., Kambayashi, T., Penn, R. B., & Deshpande, D. A. (2021) · Journal of Cellular Physiology · doi:10.1002/jcp.30528 · Cited by 12
Santos-Briones, C. D. L., Cárdenas, L., Estrada‐Navarrete, G., Santana, O., Minero‐García, Y., Quinto, C., & Sánchez, F. (2008) · Physiologia Plantarum · doi:10.1111/j.1399-3054.2008.01184.x · Cited by 12
Song, M., Kim, M. J., Ha, S., Park, J. B., Ryu, S. H., & Suh, P. (2005) · Experimental & Molecular Medicine · doi:10.1038/emm.2005.22 · Cited by 12
Regulation of Surfactant-Associated Phospholipid Synthesis and Secretion
Rooney, S. A. (2004) · Elsevier eBooks · doi:10.1016/b978-0-7216-9654-6.50106-5 · Cited by 12
Mechanical strain modulates maximal phosphatidylinositol turnover in airway smooth muscle
An, S. S., & Hai, C.-M. (1999) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.1999.277.5.l968 · Cited by 12
Holbrook, P. G., Geetha, V., Beaven, M. A., & Munson, P. J. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00366-x · Cited by 12
Rellahan, B. L. (2003) · Experimental Cell Research · doi:10.1016/s0014-4827(03)00260-x · Cited by 12
Billi, A. M., Matteucci, A., Faenza, I., Manzoli, L., Rubbini, S., Gilmour, R. S., Rhee, S. G., & Cocco, L. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.7778 · Cited by 12
Self-citationYang, L., Guo, Y., Trygankova, O., Li, Q.-Y., Maloney, J. A., Steinhauer, M., & WILLIAMSON, J. R. (1999) · Biochemical Pharmacology · doi:10.1016/s0006-2952(98)00308-6 · Cited by 12
METTL3 regulates M6A methylation-modified EBV-pri-miR-BART3-3p to promote NK/T cell lymphoma growth
Wu, S., Wang, H., Yang, Q., Liu, Z., Du, J., Wang, L., Chen, S., Lu, Q., & Yang, D. (2024) · Cancer Letters · doi:10.1016/j.canlet.2024.217058 · Cited by 11
Yamamura, H., Ohya, S., Muraki, K., & Imaizumi, Y. (2012) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.112.194233 · Cited by 11
Exploring inflammatory disease drug effects on neutrophil function
Wu, X., Kim, D., Young, A. T., & Haynes, C. L. (2014) · The Analyst · doi:10.1039/c4an00541d · Cited by 11
Subcellular Distribution of Phospholipase C Isoforms in Rodent Pancreas and Gastric Mucosa
Wang, S., Lukinius, A., Zhou, Y., Stalberg, P. L. H., Gobl, A., Öberg, K., & Skogseid, B. M. (2000) · Endocrinology · doi:10.1210/endo.141.7.7533 · Cited by 10
Wood, T. R., Chow, R. Y., Hanes, C. M., Zhang, X., Kashiwagi, K., Shirai, Y., Trebak, M., Loegering, D. J., Saito, N., & Lennartz, M. R. (2013) · Journal of Leukocyte Biology · doi:10.1189/jlb.1212634 · Cited by 11
Calmodulin potentiates Gβγ activation of phospholipase C-β3
McCullar, J. S., Malencik, D. A., Vogel, W., Crofoot, K., Anderson, S. R., & Filtz, T. M. (2006) · Biochemical Pharmacology · doi:10.1016/j.bcp.2006.10.004 · Cited by 11
Zeng, C., Zhou, Y., Liu, G., & Sun, W. (2001) · Neuropeptides · doi:10.1054/npep.2001.0868 · Cited by 11
Characterization of maleimide-activated Ca2+ entry in neutrophils
Wang, J.-P. (2003) · Biochemical Pharmacology · doi:10.1016/s0006-2952(03)00194-1 · Cited by 11
Amyloid β peptide (Aβ42) activates PLC-δ1 promoter through the NF-κB binding site
Kim, J. Y., Kim, H., Lee, S., Choi, B. H., Kim, Y.-H., Huh, P., Lee, K.-H., Han, H. J., & Rha, H. K. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2003.09.100 · Cited by 11
Phospholipase Cδ regulates germination of Dictyostelium spores
van Dijken, P., & Haastert, P. J. M. V. (2001) · BMC Cell Biology · doi:10.1186/1471-2121-2-25 · Cited by 11
Analysis of G Protein-Mediated Activation of Phospholipase C in Cultured Cells
Liu, B., & Wu, D. (2003) · Humana Press eBooks · doi:10.1385/1-59259-430-1:99 · Cited by 11
Regulation of retinal angiogenesis by phospholipase C-β3 signaling pathway
Ha, J. M., Baek, S. H., Kim, Y. H., Jin, S. Y., Lee, H. S., Kim, S. J., Shin, H. K., Lee, D. H., Song, S. H., Kim, C. D., et al. (2016) · Experimental & Molecular Medicine · doi:10.1038/emm.2016.39 · Cited by 11
The SH2-SH2-SH3 Domain of Phospholipase C-γ1 Directly Binds to Translational Elongation factor-1α
Kim, M. J., Si, F., Kim, S., Hong, S.-B., Hwang, J., Lee, H.-J., Lee, S., Chang, J., Lee, Y. H., Ryu, S. H., et al. (1999) · Molecules and Cells · doi:10.1016/s1016-8478(23)13595-3 · Cited by 11
Olszewska-Pazdrak, B., Ives, K. L., Park, J., Townsend, C. M., & Hellmich, M. R. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m309481200 · Cited by 11
Rebecchi, M. J., Homme, M. B., & Scarlata, S. (1999) · PubMed Central · Cited by 11
Yamazaki, H., Zawalich, K. C., & Zawalich, W. S. (2006) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00137.2006 · Cited by 11
Nojiri, S., & Hoek, J. B. (2000) · Hepatology · doi:10.1053/jhep.2000.18662 · Cited by 11
Romoser, V. A., Graves, T. K., Wu, D., Jiang, H., & Hinkle, P. M. (2001) · Molecular Endocrinology · doi:10.1210/mend.15.1.0588 · Cited by 11
Interplay Between SNX27 and DAG Metabolism in the Control of Trafficking and Signaling at the IS
González-Mancha, N., & Mérida, I. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21124254 · Cited by 9
Cao, Y., Song, Y., Ding, Y., Ni, J., Zhu, B., Shen, J., & Miao, L. (2023) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2023.106356 · Cited by 10
Gomes, C. P., Leão-Ferreira, L. R., Caruso‐Neves, C., & Lopes, A. G. (2005) · Regulatory Peptides · doi:10.1016/j.regpep.2005.01.009 · Cited by 10
Mokrý, J., Jakubesová, M., Švihra, J., Urdzik, J., Hudec, M., Nosalova, G., & Kliment, J. (2005) · Physiological Research · doi:10.33549/physiolres.930641 · Cited by 10
Dearden-Badet, M.-T., & Mouchiroud, G. (2005) · Cellular Signalling · doi:10.1016/j.cellsig.2005.03.018 · Cited by 10
Effect of histone H1 on the cytosolic calcium levels in human breast cancer MCF 7 cells
Vani, G., & Devi, C. S. S. (2005) · Life Sciences · doi:10.1016/j.lfs.2005.01.002 · Cited by 10
Cuozzo, F. P., Mishra, S., Jiang, J. Y., & Aukema, H. M. (2002) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(02)00072-8 · Cited by 10
Negative signaling in health and disease
Coggeshall, K. M. (1999) · Immunologic Research · doi:10.1007/bf02786476 · Cited by 10
Components and organization of the nadph oxidase of phagocytic cells
Segal, A. W., Wientjes, F. B., Stockley, R. W., & Dekker, L. V. (1999) · Advances in cellular and molecular biology of membranes and organelles · doi:10.1016/s1874-5172(99)80043-1 · Cited by 9
Pei, Z., & WILLIAMSON, J. R. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)00063-5 · Cited by 10
Watanabe, A., Nakashima, S., Adachi, T., Saji, S., & Nozawa, Y. (2000) · Surgery Today · doi:10.1007/s005950070102 · Cited by 9
Phospholipase C-β2 interacts with mitogen-activated protein kinase kinase 3
Barr, A., Marjoram, R. J., Xu, J., & D, R. S. M. (2002) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)00259-0 · Cited by 9
New aspects of formation of 1,2-cyclic phosphates by phospholipase C-δ1
Liu, Y., Bruzik, K. S., Ananthanarayanan, B., & Cho, W. (2003) · Bioorganic & Medicinal Chemistry · doi:10.1016/s0968-0896(03)00150-0 · 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
Han, N.-L. R., Wen, J., Lin, Q., Tan, P. L., Liou, Y., & Sheu, F. (2007) · International Journal of Biological Sciences · doi:10.7150/ijbs.3.263 · Cited by 9
Shin, S. Y., Ko, J., Chang, J., Min, D. S., Choi, C., Bae, S. S., Kim, M. J., Hyun, D.-S., Kim, J.-H., Han, M. Y., et al. (2002) · The FASEB Journal · doi:10.1096/fj.02-0022com · Cited by 9
Fc receptor-mediated phagocytosis
Greenberg, S. (1999) · Advances in cellular and molecular biology of membranes and organelles · doi:10.1016/s1874-5172(99)80031-5 · Cited by 9
Leukotriene D4-Induced Calcium Signaling in Human Intestinal Epithelial Cells
Thodeti, C. K., & Sjölander, A. (2002) · Advances in experimental medicine and biology · doi:10.1007/978-1-4615-0193-0_29 · Cited by 9
Tyrosine Phosphatase CD45 Regulates Hydrogen Peroxide-Induced Calcium Mobilization in B Cells
Qin, S., & Chock, P. B. (2002) · Antioxidants and Redox Signaling · doi:10.1089/15230860260196281 · Cited by 9
Effects of hyperglycemia and hypercapnia on lipid metabolism during complete brain ischemia
Katsura, K., Turco, E., Siesjö, B. K., & Bazan, N. G. (2004) · Brain Research · doi:10.1016/j.brainres.2004.10.007 · Cited by 9
Blumberg, P. M., Acs, P. I., Bhattacharyya, D. K., & Lorenzo, P. S. (2000) · Humana Press eBooks · doi:10.1007/978-1-59259-218-0_18 · Cited by 9
Overexpression of PLCG2 and TMEM38A inhibit tumor progression in clear cell renal cell carcinoma
Zhao, Y., Yang, L., Bai, X., Du, L., Lai, H., Liu, Y., Chen, P., DiSanto, M. E., & Zhang, X. (2025) · Scientific Reports · doi:10.1038/s41598-025-86644-1 · Cited by 8
Phosphoinositide Signaling in Unicellular Eukaryotes
Shemarova, I. (2007) · Critical reviews in microbiology · doi:10.1080/10408410701415927 · Cited by 7
Taqi, M. M., Waseem, D., Ismatullah, H., Haider, S. A., & Faisal, M. (2016) · Functional & Integrative Genomics · doi:10.1007/s10142-016-0489-9 · Cited by 8
Distributional Patterns of Phospholipase C Isozymes in Rat Kidney
Ho, S., Cha, J., Cho, Y., Noh, D., Lee, K.-H., & Endou, H. (1998) · The Nephron journals/Nephron journals · doi:10.1159/000045192 · Cited by 8
The Structure and Molecular Biology of the Calcitonin Receptor
Goldring, S. R. (1998) · Advances in organ biology · doi:10.1016/s1569-2590(08)60113-5 · Cited by 8
Garro, M. A., de Jesús, M. L., de Azúa, I. R., Callado, L. F., Meana, J. J., & Sallés, J. (2004) · Neurochemical Research · doi:10.1023/b:nere.0000026412.66508.14 · Cited by 8
de Jesús, M. L., Zalduegui, A., de Azúa, I. R., Callado, L. F., Meana, J. J., & Sallés, J. (2006) · Neurochemistry International · doi:10.1016/j.neuint.2005.12.015 · Cited by 8
Privé, C., & Descoteaux, A. (2000) · European Journal of Immunology · doi:10.1002/1521-4141(2000)30:8 · Cited by 148
Differential coupling of Gαq family of G-protein to muscarinic M1 receptor and neurokinin-2 receptor
Lee, C. H., Shin, I. C., Kang, J., Koh, H. C., Ha, J. H., & Min, C. K. (1998) · Archives of Pharmacal Research · doi:10.1007/bf02974637 · Cited by 8
Marchisio, M., Baldassarre, A. D., Angelucci, D., Caramelli, E., Cataldi, A., Castorina, S., Antonucci, A. T., Giovannantonio, L. D., Schiavone, C., Biagio, R. D., et al. (2001) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)61754-3 · Cited by 8
van Dijk, M. C. M., & BLITTERSWIJK, W. J. V. (1998) · Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism · doi:10.1016/s0005-2760(98)00016-2 · Cited by 8
Sternfeld, L., Thévenod, F., & Schulz, I. (2000) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2000.1844 · Cited by 8
Nuclear domains involved in inositol lipid signal transduction✠
Maraldi, N. M., Zini, N., Santi, S., Riccio, M., Falconi, M., Capitani, S., & Manzoli, F. A. (2000) · Advances in Enzyme Regulation · doi:10.1016/s0065-2571(99)00032-1 · Cited by 8
Metadata
- Authors
- Rhee, S. G., & Bae, Y. S.
- Affiliations
- National Institutes of Health (US)
- Corresponding author
- Rhee, Sue Goo
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1997-06
- Volume
- 272
- Issue
- 24
- Pages
- 15045-15048
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1981182586
- Cited by
- 876
- References
- 50
- Citations by year
- 2026: 2 · 2025: 9 · 2024: 10 · 2023: 10 · 2022: 11 · 2021: 12 · 2020: 14 · 2019: 8 · 2018: 5 · 2017: 11 · 2016: 11 · 2015: 16 · 2014: 14 · 2013: 13 · 2012: 19
- FWCI
- 6.28
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- 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 › PI3K/AKT/mTOR signaling in cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Sphingolipid Metabolism and Signaling
- Keywords
- phosphatidylinositol-specific phospholipase C, PLC isoforms, phosphatidylinositol 4,5-bisphosphate, diacylglycerol, inositol 1,4,5-trisphosphate, protein kinase C, phospholipase D, phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 3-kinase, pleckstrin homology domain, Src homology domains, GTP gamma S, interleukins, platelet-derived growth factor
- MeSH terms
- Animals, Cell Nucleus, Enzyme Activation, Isoenzymes, Type C Phospholipases, Protein-Tyrosine Kinases, Phosphatidylinositol Diacylglycerol-Lyase
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
