The P2X7 Receptor in Infection and Inflammation
Open accessAbstract
Adenosine triphosphate (ATP) accumulates at sites of tissue injury and inflammation. Effects of extracellular ATP are mediated by plasma membrane receptors named P2 receptors (P2Rs). The P2R most involved in inflammation and immunity is the P2X7 receptor (P2X7R), expressed by virtually all cells of innate and adaptive immunity. P2X7R mediates NLRP3 inflammasome activation, cytokine and chemokine release, T lymphocyte survival and differentiation, transcription factor activation, and cell death. Ten human P2RX7 gene splice variants and several SNPs that produce complex haplotypes are known. The P2X7R is a potent stimulant of inflammation and immunity and a promoter of cancer cell growth. This makes P2X7R an appealing target for anti-inflammatory and anti-cancer therapy. However, an in-depth knowledge of its structure and of the associated signal transduction mechanisms is needed for an effective therapeutic development.
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P2X7 is widely expressed by immune cells and is the most studied purinergic receptor involved in neurodegeneration.
“P2X7, which is widely expressed by immune cells, is the most studied purinergic receptors involved in neurodegeneration.374,375”
From Role of neuroinflammation in neurodegeneration development (2023) · cites this paper as [374]
The Introduction describes P2X7 as having a firmly established role in multiple immune and inflammatory responses, and the inflammation section discusses its effects in lymphocytes and macrophages. This supports its broad relevance to immune cells, but the paper does not say it is the most studied purinergic receptor involved in neurodegeneration. (LLM, conf=0.85)
Experimental — accuracy not yet measuredHyperactivation of P2X7 receptors is closely related to inflammatory processes because they are stimulated by ATP released from distressed cells and induce inflammasome activation.
“Hyperactivation of P2X7 receptors is closely related to inflammatory processes since they are stimulated by ATP released from distressed cells and induce inflammasome activation [16–18].”
From Hyperactivation of P2X7 receptors as a culprit of COVID-19 neuropathology (2021) · cites this paper as [16]
ATP may act as a DAMP, which activates the nuclear transcription factor NF-κB, resulting in expression upregulation of pro-IL-1β and pro-IL-18 and the NLRP3 protein.
“In these circumstances, ATP may act as DAMP, which activates the nuclear transcription factor NF-κB resulting in expression upregulation of pro-IL-1β and pro-IL-18 and the NLRP3 protein [16, 71].”
From Hyperactivation of P2X7 receptors as a culprit of COVID-19 neuropathology (2021) · cites this paper as [16]
Consequently, there is an activation of caspase-1 and maturation of IL-1β and IL-18, resulting in pro-inflammatory cytokine release.
“Consequently, there is an activation of caspase-1 and maturation of IL-1β and IL-18, resulting in pro-inflammatory cytokine release [16, 20, 52, 71, 73].”
From Hyperactivation of P2X7 receptors as a culprit of COVID-19 neuropathology (2021) · cites this paper as [16]
The P2X7 receptor is a major activator of the NLRP3 inflammasome in several cell types, including macrophages and microglial cells.
“The P2X7 receptor is a major activator of the NLRP3 inflammasome in several cell types [16], including macrophages and microglial cells [72, 74–76].”
From Hyperactivation of P2X7 receptors as a culprit of COVID-19 neuropathology (2021) · cites this paper as [16]
The role of P2X7 receptor as a modulator of inflammatory response is well-established.
“In fact, the role of P2X7 receptor as a modulator of inflammatory response is well-established [16, 70].”
From Hyperactivation of P2X7 receptors as a culprit of COVID-19 neuropathology (2021) · cites this paper as [16]
Massive ATP release following lung mononuclear phagocytes invasion by SARS-CoV-2 can activate P2X7 receptors of antigen-presenting cells and macrophages, increasing cytokine, chemokine and ATP secretion.
“The massive ATP release following lung mononuclear phagocytes invasion by SARS-CoV-2 can activate P2X7 receptors of antigen-presenting cells and macrophages, increasing cytokine, chemokine and ATP secretion [16].”
From Hyperactivation of P2X7 receptors as a culprit of COVID-19 neuropathology (2021) · cites this paper as [16]
Many processes associated with lung impairment, as seen in COVID-19 patients, are mediated by P2X7 receptors.
“As discussed by Di Virgilio et al. [106], many processes associated with lung impairment, as seen in COVID-19 patients, are mediated by P2X7 receptors [16].”
From Hyperactivation of P2X7 receptors as a culprit of COVID-19 neuropathology (2021) · cites this paper as [16]
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Cites
Cleavage of GSDMD by inflammatory caspases determines pyroptotic cell death
Shi, J., Zhao, Y., Wang, K., Shi, X., Wang, Y., Huang, H., Zhuang, Y., Cai, T., Wang, F., & Shao, F. (2015) · Nature · doi:10.1038/nature15514 · Cited by 6,659 · see citing works
Martinon, F., Burns, K., & Tschopp, J. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00599-3 · Cited by 6,066 · see citing works
Caspase-11 cleaves gasdermin D for non-canonical inflammasome signalling
Kayagaki, N., Stowe, I. B., Lee, B. L., O’Rourke, K., Anderson, K., Warming, S., Cuellar, T., Haley, B., Roose-Girma, M., Phung, Q. T., et al. (2015) · Nature · doi:10.1038/nature15541 · Cited by 3,686 · see citing works
Immunogenic Cell Death in Cancer Therapy
Kroemer, G., Galluzzi, L., Kepp, O., & Zitvogel, L. (2013) · Annual Review of Immunology · doi:10.1146/annurev-immunol-032712-100008 · Cited by 3,303 · see citing works
Calreticulin exposure dictates the immunogenicity of cancer cell death
Obeid, M., Tesniere, A., Ghiringhelli, F., Fimia, G. M., Apetoh, L., Perfettini, J.-L., Castedo, M., Mignot, G., Panaretakis, T., Casares, N., et al. (2007) · Nature Medicine · doi:10.1038/nm1523 · Cited by 3,216 · see citing works
Immunogenic cell death in cancer and infectious disease
Galluzzi, L., Buqué, A., Kepp, O., Zitvogel, L., & Kroemer, G. (2017) · Nature Reviews Immunology · doi:10.1038/nri.2016.107 · Cited by 3,119 · see citing works
Functional Polarization of Tumour-Associated Macrophages by Tumour-Derived Lactic Acid
Colegio, O. R., Chu, N.-Q., Szabo, A. L., Chu, T., Rhebergen, A. M., Jairam, V., Cyrus, N., Brokowski, C. E., Eisenbarth, S. C., Phillips, G. M., et al. (2014) · Nature · doi:10.1038/nature13490 · Cited by 3,046 · see citing works
Molecular Physiology of P2X Receptors
North, R. A. (2002) · Physiological Reviews · doi:10.1152/physrev.00015.2002 · Cited by 2,919 · see citing works
Muñoz-Planillo, R., Kuffa, P., Martínez-Colón, G. J., Smith, B. L., Rajendiran, T. M., & Núñez, G. (2013) · Immunity · doi:10.1016/j.immuni.2013.05.016 · Cited by 2,167 · see citing works
BDNF from microglia causes the shift in neuronal anion gradient underlying neuropathic pain
Coull, J. A. M., Beggs, S., Boudreau, D., Boivin, D., Tsuda, M., Inoue, K., Gravel, C., Salter, M. W., & De Koninck, Y. (2005) · Nature · doi:10.1038/nature04223 · Cited by 1,965 · see citing works
Ghiringhelli, F., Apetoh, L., Tesniere, A., Aymeric, L., Ma, Y., Ortiz, C., Vermaelen, K., Panaretakis, T., Mignot, G., Ullrich, E., et al. (2009) · Nature Medicine · doi:10.1038/nm.2028 · Cited by 1,898 · see citing works
Surprenant, A., Rassendren, F., Kawashima, E., North, R. A., & Buell, G. (1996) · Science · doi:10.1126/science.272.5262.735 · Cited by 1,739 · see citing works
Control of TH17/Treg Balance by Hypoxia-Inducible Factor 1
Dang, E. V., Barbi, J., Yang, H.-Y., Jinasena, D., Yu, H., Zheng, Y., Bordman, Z., Fu, J., Kim, Y., Yen, H.-R., et al. (2011) · Cell · doi:10.1016/j.cell.2011.07.033 · Cited by 1,595 · see citing works
Physiology and Pathophysiology of Purinergic Neurotransmission
Burnstock, G. (2007) · Physiological Reviews · doi:10.1152/physrev.00043.2006 · Cited by 1,579 · see citing works
P2X4 receptors induced in spinal microglia gate tactile allodynia after nerve injury
Tsuda, M., Shigemoto‐Mogami, Y., Koizumi, S., Mizokoshi, A., Kohsaka, S., Salter, M. W., & Inoue, K. (2003) · Nature · doi:10.1038/nature01786 · Cited by 1,567 · see citing works
Understanding the mechanism of IL-1β secretion
Lopez-Castejon, G., & Brough, D. (2011) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2011.10.001 · Cited by 1,519 · see citing works
Caspase-dependent immunogenicity of doxorubicin-induced tumor cell death
Casares, N., Pequignot, M. O., Tesniere, A., Ghiringhelli, F., Roux, S., Chaput, N., Schmitt, E., Hamai, A., Hervas-Stubbs, S., Obeid, M., et al. (2005) · The Journal of Experimental Medicine · doi:10.1084/jem.20050915 · Cited by 1,512 · see citing works
NEK7 is an essential mediator of NLRP3 activation downstream of potassium efflux
He, Y., Zeng, M. Y., Yang, D., Motro, B., & Núñez, G. (2016) · Nature · doi:10.1038/nature16959 · Cited by 1,295 · see citing works
ATP drives lamina propria TH17 cell differentiation
Atarashi, K., Nishimura, J., Shima, T., Umesaki, Y., Yamamoto, M., Onoue, M., Yagita, H., Ishii, N., Evans, R., Honda, K., et al. (2008) · Nature · doi:10.1038/nature07240 · Cited by 1,089 · see citing works
The P2X7 Receptor: A Key Player in IL-1 Processing and Release
Ferrari, D., Pizzirani, C., Adinolfi, E., Lemoli, R. M., Curti, A., Idzko, M., Panther, E., & Di Virgilio, F. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.176.7.3877 · Cited by 1,025 · see citing works
Altered Cytokine Production in Mice Lacking P2X7Receptors
Solle, M., Labasi, J. M., Perregaux, D. G., Stam, E. J., Petrushova, N., Koller, B. H., Griffiths, R., & Gabel, C. A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m006781200 · Cited by 924 · see citing works
Nucleotide signalling during inflammation
Idzko, M., Ferrari, D., & Eltzschig, H. K. (2014) · Nature · doi:10.1038/nature13085 · Cited by 909 · see citing works
Rapid Secretion of Interleukin-1β by Microvesicle Shedding
Mackenzie, A. B., Wilson, H. L., Kiss‐Toth, E., Dower, S., North, R. A., & Surprenant, A. (2001) · Immunity · doi:10.1016/s1074-7613(01)00229-1 · Cited by 862 · see citing works
Immune cell regulation by autocrine purinergic signalling
JUNGER, W. G. (2011) · Nature reviews. Immunology · doi:10.1038/nri2938 · Cited by 813 · see citing works
Disruption of the P2X7 purinoceptor gene abolishes chronic inflammatory and neuropathic pain
Chessell, I. P., Hatcher, J. P., Bountra, C., Michel, A. D., Hughes, J. P., Green, P., Egerton, J., Murfin, M., Richardson, J. C., Peck, W. L., et al. (2005) · Pain · doi:10.1016/j.pain.2005.01.002 · Cited by 790 · see citing works
Purinergic regulation of the immune system
Cekic, C., & Linden, J. (2016) · Nature Reviews Immunology · doi:10.1038/nri.2016.4 · Cited by 787 · see citing works
Human Monocytes Engage an Alternative Inflammasome Pathway
Gaidt, M. M., Ebert, T. S., Chauhan, D., Schmidt, T., Schmid-Burgk, J. L., Rapino, F. A., Robertson, A. A. B., Cooper, M. A., Graf, T., & Hornung, V. (2016) · Immunity · doi:10.1016/j.immuni.2016.01.012 · Cited by 780 · see citing works
Perregaux, D. G., & Gabel, C. A. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36591-2 · Cited by 760 · see citing works
Crystal structure of the ATP-gated P2X4 ion channel in the closed state
Kawate, T., Michel, J. J. C., Birdsong, W. T., & Gouaux, E. (2009) · Nature · doi:10.1038/nature08198 · Cited by 739 · see citing works
Increased Level of Extracellular ATP at Tumor Sites: In Vivo Imaging with Plasma Membrane Luciferase
Pellegatti, P., Raffaghello, L., Bianchi, G., Piccardi, F., Pistoia, V., & Di Virgilio, F. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002599 · Cited by 668 · see citing works
Ferrari, D., Chiozzi, P., Falzoni, S., Susino, M. D., Melchiorri, L., Baricordi, O. R., & Virgilio, F. D. (1997) · The Journal of Immunology · doi:10.4049/jimmunol.159.3.1451 · Cited by 616 · see citing works
Self-citationYang, D., He, Y., Muñoz-Planillo, R., Liu, Q., & Núñez, G. (2015) · Immunity · doi:10.1016/j.immuni.2015.10.009 · Cited by 602 · see citing works
The IL-1 family and inflammatory diseases.
Dinarello, C. A. (2002) · PubMed · Cited by 600 · see citing works
Astrocyte-Derived ATP Induces Vesicle Shedding and IL-1β Release from Microglia
Bianco, F., Pravettoni, E., Colombo, A., Schenk, U., Möller, T., Matteoli, M., & Verderio, C. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.174.11.7268 · Cited by 596 · see citing works
Acid sphingomyelinase activity triggers microparticle release from glial cells
Bianco, F., Perrotta, C., Novellino, L., Francolini, M., Riganti, L., Menna, E., Saglietti, L., Schuchman, E. H., Furlan, R., Clementi, E., et al. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.45 · Cited by 594 · see citing works
Qu, Y., Franchi, L., Nunez, G., & Dubyak, G. R. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.179.3.1913 · Cited by 563 · see citing works
Extracellular purines, purinergic receptors and tumor growth
Virgilio, F. D., & Adinolfi, E. (2016) · Oncogene · doi:10.1038/onc.2016.206 · Cited by 555 · see citing works
Molecular mechanism of ATP binding and ion channel activation in P2X receptors
Hattori, M., & Gouaux, E. (2012) · Nature · doi:10.1038/nature11010 · Cited by 554 · see citing works
A Primary Role for K+ and Na+ Efflux in the Activation of Apoptosis
Bortner, C. D., Hughes, F. M., & Cidlowski, J. A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.51.32436 · Cited by 549 · see citing works
Programmed necrosis in inflammation: Toward identification of the effector molecules
Wallach, D., Kang, T., Dillon, C. P., & Green, D. R. (2016) · Science · doi:10.1126/science.aaf2154 · Cited by 547 · see citing works
Activation and Regulation of Purinergic P2X Receptor Channels
Coddou, C., Yan, Z., Obšil, T., Huidobro-Toro, J. P., & Stojilković, S. S. (2011) · Pharmacological Reviews · doi:10.1124/pr.110.003129 · Cited by 493 · see citing works
Neutrophil P2X7 receptors mediate NLRP3 inflammasome-dependent IL-1β secretion in response to ATP
Karmakar, M., Katsnelson, M. A., Dubyak, G. R., & Pearlman, E. (2016) · Nature Communications · doi:10.1038/ncomms10555 · Cited by 450 · see citing works
Metabolic control of type 1 regulatory T cell differentiation by AHR and HIF1-α
Mascanfroni, I. D., Takenaka, M. C., Yeste, A., Patel, B., Wu, Y., Kenison, J. E., Siddiqui, S., Basso, A. S., Otterbein, L. E., Pardoll, D. M., et al. (2015) · Nature Medicine · doi:10.1038/nm.3868 · Cited by 441 · see citing works
Graft-versus-host disease is enhanced by extracellular ATP activating P2X7R
Wilhelm, K., Ganesan, J., Müller, T., Dürr, C., Grimm, M., Beilhack, A., Krempl, C. D., Sorichter, S., Gerlach, U. V., Jüttner, E., et al. (2010) · Nature Medicine · doi:10.1038/nm.2242 · Cited by 435 · see citing works
Elssner, A., Duncan, M., Gavrilin, M. A., & Wewers, M. D. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.172.8.4987 · Cited by 425 · see citing works
The P2X7 Receptor Channel: Recent Developments and the Use of P2X7 Antagonists in Models of Disease
Bartlett, R., Stokes, L., & Sluyter, R. (2014) · Pharmacological Reviews · doi:10.1124/pr.113.008003 · Cited by 395 · see citing works
Lammas, D. A., Stober, C. B., Harvey, C. J., Kendrick, N., Panchalingam, S., & Kumararatne, D. S. (1997) · Immunity · doi:10.1016/s1074-7613(00)80364-7 · Cited by 393 · see citing works
Proteomic and functional evidence for a P2X7 receptor signalling complex
Kim, M., Jiang, L., Wilson, H. L., North, R. A., & Surprenant, A. (2001) · The EMBO Journal · doi:10.1093/emboj/20.22.6347 · Cited by 379 · see citing works
Oxidized ATP. An irreversible inhibitor of the macrophage purinergic P2Z receptor.
Murgia, M., Hanau, S., Pizzo, P., Rippa, M., & Virgilio, F. D. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53082-9 · Cited by 367 · see citing works
Mouse microglial cells express a plasma membrane pore gated by extracellular ATP
Ferrari, D., Villalba, M., Chiozzi, P., Falzoni, S., Ricciardi‐Castagnoli, P., & Virgilio, F. D. (1996) · The Journal of Immunology · doi:10.4049/jimmunol.156.4.1531 · Cited by 352 · see citing works
Self-citationSéman, M., Adriouch, S., Scheuplein, F., Krebs, C. F., Freese, D., Glowacki, G., Deterre, P., Haag, F., & Koch‐Nolte, F. (2003) · Immunity · doi:10.1016/s1074-7613(03)00266-8 · Cited by 336 · see citing works
Human astrocytes express a novel NLRP2 inflammasome
Minkiewicz, J., Vaccari, J. P. D. R., & Keane, R. W. (2013) · Glia · doi:10.1002/glia.22499 · Cited by 328 · see citing works
Mascanfroni, I. D., Yeste, A., Vieira, S. M., Burns, E. J., Patel, B., Sloma, I., Wu, Y., Mayo, L., Ben‐Hamo, R., Efroni, S., et al. (2013) · Nature Immunology · doi:10.1038/ni.2695 · Cited by 328 · see citing works
Keystone, E. C., Wang, M. M., Layton, M., Hollis, S., & McInnes, I. B. (2012) · Annals of the Rheumatic Diseases · doi:10.1136/annrheumdis-2011-143578 · Cited by 318 · see citing works
Woehrle, T., Yip, L., Elkhal, A., Sumi, Y., Chen, Y., Yao, Y., Insel, P. A., & JUNGER, W. G. (2010) · Blood · doi:10.1182/blood-2010-04-277707 · Cited by 315 · see citing works
A Glu-496 to Ala Polymorphism Leads to Loss of Function of the Human P2X7 Receptor
Gu, B. J., Zhang, W., Worthington, R. A., Sluyter, R., Dao‐Ung, P., Petrou, S., Barden, J. A., & Wiley, J. S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010353200 · Cited by 314 · see citing works
Structural basis for subtype-specific inhibition of the P2X7 receptor
Karasawa, A., & Kawate, T. (2016) · eLife · doi:10.7554/elife.22153 · Cited by 308 · see citing works
Niemi, K., Teirilä, L., Lappalainen, J., Rajamäki, K., Baumann, M. H., Öörni, K., Wolff, H., Kovanen, P. T., Matikainen, S., & Eklund, K. K. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1002843 · Cited by 298 · see citing works
A Novel Recombinant Plasma Membrane-targeted Luciferase Reveals a New Pathway for ATP Secretion
Pellegatti, P., Falzoni, S., Pinton, P., Rizzuto, R., & Virgilio, F. D. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-03-0222 · Cited by 296 · see citing works
Self-citationActivation of Microglia by Amyloid β Requires P2X7 Receptor Expression
Sanz, J. M., Chiozzi, P., Ferrari, D., Colaianna, M., Idzko, M., Falzoni, S., Fellin, R., Trabace, L., & Di Virgilio, F. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0803612 · Cited by 293 · see citing works
Self-citationExtracellular ATP mediates mast cell-dependent intestinal inflammation through P2X7 purinoceptors
Kurashima, Y., Amiya, T., Nochi, T., Fujisawa, K., Haraguchi, T., Iba, H., Tsutsui, H., Sato, S., Nakajima, S., Iijima, H., et al. (2012) · Nature Communications · doi:10.1038/ncomms2023 · Cited by 286 · see citing works
Schenk, U., Frascoli, M., Proietti, M., Geffers, R., Traggiai, E., Buer, J., Ricordi, C., Westendorf, A. M., & Grassi, F. (2011) · Science Signaling · doi:10.1126/scisignal.2001270 · Cited by 286 · see citing works
Stimulation of P2 receptors causes release of IL-1β–loaded microvesicles from human dendritic cells
Pizzirani, C., Ferrari, D., Chiozzi, P., Adinolfi, E., Sandonà, D., Savaglio, E., & Virgilio, F. D. (2006) · Blood · doi:10.1182/blood-2005-06-031377 · Cited by 280 · see citing works
Virgilio, F. D., Chiozzi, P., Falzoni, S., Ferrari, D., Sanz, J. M., Venketaraman, V., & Baricordi, O. R. (1998) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4400341 · Cited by 278 · see citing works
Self-citationPotassium‐inhibited processing of IL‐1 beta in human monocytes.
Walev, I., Reske, K., Palmer, M., Valeva, A., & Bhakdi, S. C. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07149.x · Cited by 278 · see citing works
Evolutionary origins of the purinergic signalling system
Burnstock, G., & Verkhratsky, A. (2009) · Acta Physiologica · doi:10.1111/j.1748-1716.2009.01957.x · Cited by 277 · see citing works
Ferrari, D., Łoś, M., Bauer, M. K. A., Vandenabeele, P., Wesselborg, S., & Schulze‐Osthoff, K. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00270-7 · Cited by 276 · see citing works
Beier, U. H., Angelin, A., Akimova, T., Wang, L., Liu, Y., Xiao, H., Koike, M. A., Hancock, S. A., Bhatti, T. R., Han, R., et al. (2015) · The FASEB Journal · doi:10.1096/fj.14-268409 · Cited by 275 · see citing works
Adinolfi, E., Callegari, M. G., Ferrari, D., Bolognesi, C., Minelli, M., Wieckowski, M. R., Pinton, P., Rizzuto, R., & Virgilio, F. D. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-11-1025 · Cited by 272 · see citing works
Reanalysis of P2X<sub>7</sub>Receptor Expression in Rodent Brain
Sim, J. A., Young, M. T., Sung, H.-Y., North, R. A., & Surprenant, A. (2004) · The Journal of Neuroscience · doi:10.1523/jneurosci.1469-04.2004 · Cited by 264 · see citing works
Medicinal chemistry of adenosine, P2Y and P2X receptors
Jacobson, K. A., & Müller, C. E. (2015) · Neuropharmacology · doi:10.1016/j.neuropharm.2015.12.001 · Cited by 262 · see citing works
X-ray structures define human P2X3 receptor gating cycle and antagonist action
Mansoor, S., Lü, W., Oosterheert, W., Shekhar, M., Tajkhorshid, E., & Gouaux, E. (2016) · Nature · doi:10.1038/nature19367 · Cited by 259 · see citing works
ATP Acts as an Agonist to Promote Stimulus-Induced Secretion of IL-1β and IL-18 in Human Blood
Perregaux, D. G., McNiff, P. A., Laliberte, R., Conklyn, M. J., & Gabel, C. A. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.165.8.4615 · Cited by 256 · see citing works
Trophic activity of a naturally occurring truncated isoform of the P2X7 receptor
Adinolfi, E., Cirillo, M., Woltersdorf, R., Falzoni, S., Chiozzi, P., Pellegatti, P., Callegari, M. G., Sandonà, D., Markwárdt, F., Schmalzing, G., et al. (2010) · The FASEB Journal · doi:10.1096/fj.09-153601 · Cited by 254 · see citing works
Self-citationATP induces nucleotide permeability in rat mast cells
Cockcroft, S., & Gomperts, B. D. (1979) · Nature · doi:10.1038/279541a0 · Cited by 253 · see citing works
Falzoni, S., Munerati, M., Ferrari, D., Spisani, S., Moretti, S., & Virgilio, F. D. (1995) · Journal of Clinical Investigation · doi:10.1172/jci117770 · Cited by 249 · see citing works
Self-citationStock, T. C., Bloom, B. J., Wei, N., Ishaq, S., Park, W., WANG, X., Gupta, P. K., & MEBUS, C. A. (2012) · The Journal of Rheumatology · doi:10.3899/jrheum.110874 · Cited by 246 · see citing works
Arulkumaran, N., Unwin, R. J., & Tam, F. W. K. (2011) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.2011.578068 · Cited by 241 · see citing works
Panenka, W. J., Jijon, H. B., Herx, L., Armstrong, J. N., Feighan, D., Wei, T., Yong, V. W., Ransohoff, R. M., & MacVicar, B. A. (2001) · Journal of Neuroscience · doi:10.1523/jneurosci.21-18-07135.2001 · Cited by 233 · see citing works
Nucleoside reverse transcriptase inhibitors possess intrinsic anti-inflammatory activity
Fowler, B. J., Gelfand, B. D., Kim, Y., Kerur, N., Tarallo, V., Hirano, Y., Amarnath, S., Fowler, D. H., Radwan, M., Young, M. T., et al. (2014) · Science · doi:10.1126/science.1261754 · Cited by 225 · see citing works
The P2X7 receptor directly interacts with the NLRP3 inflammasome scaffold protein
Franceschini, A., Capece, M., Chiozzi, P., Falzoni, S., Sanz, J. M., Sarti, A. C., Bonora, M., Pinton, P., & Di Virgilio, F. (2015) · The FASEB Journal · doi:10.1096/fj.14-268714 · Cited by 225 · see citing works
Self-citationBasso, A. M., Bratcher, N. A., Harris, R. R., Jarvis, M. F., Decker, M. W., & Rueter, L. E. (2009) · Behavioural Brain Research · doi:10.1016/j.bbr.2008.10.018 · Cited by 224 · see citing works
Molecular and functional properties of P2X receptors—recent progress and persisting challenges
Kaczmarek-Hájek, K., Lörinczi, É., Hausmann, R., & Nicke, A. (2012) · Purinergic Signalling · doi:10.1007/s11302-012-9314-7 · Cited by 223 · see citing works
Activation of NLRP3 and AIM2 Inflammasomes by Porphyromonas gingivalis Infection
Park, E.-J., Na, H. S., Song, Y., Shin, S. Y., Kim, Y., & Chung, J. (2013) · Infection and Immunity · doi:10.1128/iai.00862-13 · Cited by 219 · see citing works
Increased Proliferation Rate of Lymphoid Cells Transfected with the P2X7 ATP Receptor
Baricordi, O. R., Melchiorri, L., Adinolfi, E., Falzoni, S., Chiozzi, P., Buell, G. N., & Virgilio, F. D. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.47.33206 · Cited by 212 · see citing works
Self-citationExtracellular NAD+ shapes the Foxp3+ regulatory T cell compartment through the ART2–P2X7 pathway
Hubert, S., Rissiek, B., Klages, K., Huehn, J., Sparwasser, T. D., Haag, F., Koch‐Nolte, F., Boyer, O., Séman, M., & Adriouch, S. (2010) · The Journal of Experimental Medicine · doi:10.1084/jem.20091154 · Cited by 207 · see citing works
Identification and characterization of splice variants of the human P2X7 ATP channel
Cheewatrakoolpong, B., Gilchrest, H., Anthes, J. C., & Greenfeder, S. A. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.04.087 · Cited by 207 · see citing works
He, Y., Franchi, L., & Núñez, G. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1202737 · Cited by 206 · see citing works
The human P2X7 receptor and its role in innate immunity
Wiley, J. S., Sluyter, R., Gu, B. J., Stokes, L., & Fuller, S. J. (2011) · Tissue Antigens · doi:10.1111/j.1399-0039.2011.01780.x · Cited by 198 · see citing works
Extracellular ATP4- promotes cation fluxes in the J774 mouse macrophage cell line.
Steinberg, T. H., & Silverstein, S. C. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)61477-2 · Cited by 196 · see citing works
Fc receptor-mediated phagocytosis occurs in macrophages at exceedingly low cytosolic Ca2+ levels.
Virgilio, F. D., Meyer, B. C., Greenberg, S., & Silverstein, S. C. (1988) · The Journal of Cell Biology · doi:10.1083/jcb.106.3.657 · Cited by 190 · see citing works
Humphreys, B. D., & Dubyak, G. (1996) · The Journal of Immunology · doi:10.4049/jimmunol.157.12.5627 · Cited by 189 · see citing works
P2X7 receptor regulation of non-classical secretion from immune effector cells
Dubyak, G. (2012) · Cellular Microbiology · doi:10.1111/cmi.12001 · Cited by 189 · see citing works
Amoroso, F., Capece, M., Rotondò, A., Cangelosi, D., Ferracin, M., Franceschini, A., Raffaghello, L., Pistoia, V., Varesio, L., & Adinolfi, E. (2015) · Oncogene · doi:10.1038/onc.2014.444 · Cited by 187 · see citing works
Nicke, A., Kuan, Y., Masin, M., Rettinger, J., Marquez-Klaka, B., Bender, O., Górecki, D. C., Murrell‐Lagnado, R. D., & Soto, F. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.033134 · Cited by 187 · see citing works
An ATP-activated channel is involved in mitogenic stimulation of human T lymphocytes
Baricordi, O., Ferrari, D., Melchiorri, L., Chiozzi, P., Hanau, S., Chiari, E., Rubini, M., & Virgilio, F. D. (1996) · Blood · doi:10.1182/blood.v87.2.682.bloodjournal872682 · Cited by 185 · see citing works
Denlinger, L. C., Fisette, P. L., Sommer, J. A., Watters, J. J., Prabhu, U., Dubyak, G., Proctor, R. A., & Bertics, P. J. (2001) · The Journal of Immunology · doi:10.4049/jimmunol.167.4.1871 · Cited by 182 · see citing works
Verkhratsky, A., & Burnstock, G. (2014) · BioEssays · doi:10.1002/bies.201400024 · Cited by 182 · see citing works
Nanobodies that block gating of the P2X7 ion channel ameliorate inflammation
Danquah, W., Meyer‐Schwesinger, C., Rissiek, B., Pinto, C., Prat, A. S., Amadi, M., Iacenda, D., Knop, J., Hammel, A., Bergmann, P., et al. (2016) · Science Translational Medicine · doi:10.1126/scitranslmed.aaf8463 · Cited by 182 · see citing works
Proietti, M., Cornacchione, V., Rezzonico Jost, T., Romagnani, A., Faliti, C. E., Perruzza, L., Rigoni, R., Radaelli, E., Caprioli, F., Preziuso, S., et al. (2014) · Immunity · doi:10.1016/j.immuni.2014.10.010 · Cited by 181 · see citing works
Shieh, C., Heinrich, A., Serchov, T., van Calker, D., & Biber, K. (2014) · Glia · doi:10.1002/glia.22628 · Cited by 179 · see citing works
Accelerated Tumor Progression in Mice Lacking the ATP Receptor P2X7
Adinolfi, E., Capece, M., Franceschini, A., Falzoni, S., Giuliani, A. L., Rotondo, A., Sarti, A. C., Bonora, M., Syberg, S., Corigliano, D. M., et al. (2014) · Cancer Research · doi:10.1158/0008-5472.can-14-1259 · Cited by 177 · see citing works
Self-citationBoué‐Grabot, É., Archambault, V., & Séguéla, P. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.14.10190 · Cited by 175 · see citing works
Virgilio, F. D., Bronte, V., Collavo, D., & Zanovello, P. (1989) · The Journal of Immunology · doi:10.4049/jimmunol.143.6.1955 · Cited by 175 · see citing works
Panupinthu, N., Rogers, J. T., Zhao, L., Solano-Flores, L. P., Possmayer, F., Sims, S. M., & Dixon, S. J. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200708037 · Cited by 175 · see citing works
Pseudoapoptosis Induced by Brief Activation of ATP-gated P2X7 Receptors
Mackenzie, A. B., Young, M. T., Adinolfi, E., & Surprenant, A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m502705200 · Cited by 174 · see citing works
Stokes, L., Fuller, S. J., Sluyter, R., Skarratt, K. K., Gu, B. J., & Wiley, J. S. (2010) · The FASEB Journal · doi:10.1096/fj.09-150862 · Cited by 174 · see citing works
Ferrari, D., Sala, A. L., Chiozzi, P., Morelli, A., Falzoni, S., Girolomoni, G., Idzko, M., Dichmann, S., Norgauer, J., & Virgilio, F. D. (2000) · The FASEB Journal · doi:10.1096/fj.00-0031com · Cited by 173 · see citing works
Self-citationCabrini, G., Falzoni, S., Forchap, S., Pellegatti, P., Balboni, A., Agostini, P., Cuneo, A., Castoldi, G., Baricordi, O. R., & Virgilio, F. D. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.175.1.82 · Cited by 164 · see citing works
Self-citationRapid ATP-induced release of matrix metalloproteinase 9 is mediated by the P2X7 receptor
Gu, B. J., & Wiley, J. S. (2006) · Blood · doi:10.1182/blood-2005-07-2994 · Cited by 160 · see citing works
Solini, A., Chiozzi, P., Morelli, A., Fellin, R., & Virgilio, F. D. (1999) · Journal of Cell Science · doi:10.1242/jcs.112.3.297 · Cited by 159 · see citing works
Tomasinsig, L., Pizzirani, C., Skerlavaj, B., Pellegatti, P., Gulinelli, S., Tossi, A., Virgilio, F. D., & Zanetti, M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802185200 · Cited by 158 · see citing works
Zanovello, P., Bronte, V., Rosato, A., Pizzo, P., & Virgilio, F. D. (1990) · The Journal of Immunology · doi:10.4049/jimmunol.145.5.1545 · Cited by 158 · see citing works
The Therapeutic Potential of Modifying Inflammasomes and NOD-Like Receptors
Virgilio, F. D. (2013) · Pharmacological Reviews · doi:10.1124/pr.112.006171 · Cited by 158 · see citing works
Gu, B. J., Bendall, L. J., & Wiley, J. S. (1998) · Blood · doi:10.1182/blood.v92.3.946 · Cited by 157 · see citing works
Inhibition of Chlamydial Infectious Activity due to P2X7R-Dependent Phospholipase D Activation
Coutinho‐Silva, R., Welter-Stahl, L., Raymond, M., Jungas, T., Verbeke, P., Burnstock, G., Darville, T. L., & Ojcius, D. M. (2003) · Immunity · doi:10.1016/s1074-7613(03)00235-8 · Cited by 157 · see citing works
Kerur, N., Hirano, Y., Tarallo, V., Fowler, B. J., Bastos-Carvalho, A., Yasuma, T. R., Yasuma, R., Kim, Y., Hinton, D. R., Kirschning, C. J., et al. (2013) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.13-12500 · Cited by 156 · see citing works
P2X7 receptor activation induces CXCL2 production in microglia through NFAT and PKC/MAPK pathways
Shiratori, M., Tozaki‐Saitoh, H., Yoshitake, M., Tsuda, M., & Inoue, K. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.06809.x · Cited by 153 · cited 1× · see citing works
“…and mouse mast cells (Panenka et al., 2001; Kurashima et al., 2012), IL-8 in rat C6 glioma cells (Wei et al., 2008), CC-chemokine ligand 3 (CCL3) in mouse microglial MG-5 cells (Kataoka et al., 2009), and CXCL2 in mouse microglia and mast cells (Shiratori et al., 2010; Kurashima et al., 2012).”
El-Moatassim, C., & Dubyak, G. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)35890-3 · Cited by 153 · see citing works
Feng, Y., Li, X., Wang, L., Zhou, L., & Gorodeski, G. I. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602999200 · Cited by 152 · see citing works
P2X7 Receptor Channels Allow Direct Permeation of Nanometer-Sized Dyes
Browne, L. E., Compan, V., Bragg, L., & North, R. A. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.2235-12.2013 · Cited by 151 · see citing works
Gu, B. J., Bendall, L. J., & Wiley, J. S. (1998) · Blood · doi:10.1182/blood.v92.3.946.415a24_946_951 · Cited by 148 · see citing works
Significance of P2X7 Receptor Variants to Human Health and Disease
Sluyter, R., & Stokes, L. (2011) · Recent Patents on DNA & Gene Sequences · doi:10.2174/187221511794839219 · Cited by 147 · see citing works
Sung, S. S., Young, J. D., Origlio, A. M., Heiple, J. M., Kaback, H. R., & Silverstein, S. C. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38740-9 · Cited by 145 · see citing works
The P2X7 receptor is a key modulator of aerobic glycolysis
Amoroso, F., Falzoni, S., Adinolfi, E., Ferrari, D., & Virgilio, F. D. (2012) · Cell Death and Disease · doi:10.1038/cddis.2012.105 · Cited by 145 · see citing works
Self-citationGu, B. J., Sluyter, R., Skarratt, K. K., Shemon, A. N., Dao‐Ung, L., Fuller, S. J., Barden, J. A., Clarke, A. L., Petrou, S., & Wiley, J. S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313902200 · Cited by 145 · see citing works
The secretion of IL-1β and options for release
Piccioli, P., & Rubartelli, A. (2013) · Seminars in Immunology · doi:10.1016/j.smim.2013.10.007 · Cited by 142 · see citing works
The Role of the P2X7 Receptor in Infectious Diseases
Miller, C., Boulter, N. R., Fuller, S. J., Zakrzewski, A. M., Lees, M. P., Saunders, B. M., Wiley, J. S., & Smith, N. C. (2011) · PLoS Pathogens · doi:10.1371/journal.ppat.1002212 · Cited by 142 · see citing works
P2X7 receptor‐stimulation causes fever <i>via</i> PGE2 and IL‐1β release
Barberà‐Cremades, M., Baroja‐Mazo, A., Gomez, A. I., Machado, F., Di Virgilio, F., & Pelegrín, P. (2012) · The FASEB Journal · doi:10.1096/fj.12-205765 · Cited by 142 · see citing works
Csóka, B., Németh, Z. H., Törő, G., Idzko, M., Zech, A., Koscsó, B., Spolarics, Z., Antonioli, L., Cseri, K., Erdélyi, K., et al. (2015) · The FASEB Journal · doi:10.1096/fj.15-272450 · Cited by 139 · see citing works
Eser, A., Colombel, J., Rutgeerts, P. J., Vermeire, S., Vogelsang, H., Braddock, M., Persson, T., & Reinisch, W. (2015) · Inflammatory Bowel Diseases · doi:10.1097/mib.0000000000000514 · Cited by 138 · see citing works
Territo, P. R., Meyer, J. A., Peters, J. S., Riley, A. K., McCarthy, B. P., Gao, M., Wang, M., Green, M. A., Zheng, Q., & Hutchins, G. D. (2016) · Journal of Nuclear Medicine · doi:10.2967/jnumed.116.181354 · Cited by 138 · see citing works
Resta, V., Novelli, E., Vozzi, G., Scarpa, C., Caleo, M., Ahluwalia, A. D., Solini, A., Santini, E., Parisi, V., Virgilio, F. D., et al. (2007) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2007.05528.x · Cited by 137 · see citing works
ATP/P2X7 axis modulates myeloid-derived suppressor cell functions in neuroblastoma microenvironment
Bianchi, G., Vuerich, M., Pellegatti, P., Marimpietri, D., Emionite, L., Marigo, I., Bronte, V., Virgilio, F. D., Pistoia, V., & Raffaghello, L. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.109 · Cited by 128 · see citing works
Genetics of the P2X7 receptor and human disease
Fuller, S. J., Stokes, L., Skarratt, K. K., Gu, B. J., & Wiley, J. S. (2009) · Purinergic Signalling · doi:10.1007/s11302-009-9136-4 · Cited by 125 · see citing works
Kataoka, A., Tozaki‐Saitoh, H., Koga, Y., Tsuda, M., & Inoue, K. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05744.x · Cited by 121 · see citing works
Astrocyte-Mediated Ischemic Tolerance
Hirayama, Y., Ikeda‐Matsuo, Y., Notomi, S., Enaida, H., Kinouchi, H., & Koizumi, S. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.4218-14.2015 · Cited by 114 · see citing works
ATP-Induced Inflammation Drives Tissue-Resident Th17 Cells in Metabolically Unhealthy Obesity
Pandolfi, J., Ferraro, A., Sananez, I., Gancedo, M. C., Baz, P., Billordo, L. A., Fainboim, L., & Arruvito, L. (2016) · The Journal of Immunology · doi:10.4049/jimmunol.1502506 · Cited by 113 · see citing works
Masin, M., Young, C., Lim, K., Barnes, S. J., Xu, X., Marschall, V., Brutkowski, W., Mooney, E. R., Górecki, D. C., & Murrell‐Lagnado, R. D. (2011) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2011.01624.x · Cited by 112 · see citing works
P2X7 Receptor as a Therapeutic Target
Marchi, E. D., Orioli, E., Ben, D. D., & Adinolfi, E. (2016) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2015.11.004 · Cited by 111 · see citing works
Killeen, M. E., Ferris, L. K., Kupetsky, E. A., Falo, L. D., & Mathers, A. R. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1202045 · Cited by 109 · see citing works
Long-Term Heart Transplant Survival by Targeting the Ionotropic Purinergic Receptor P2X7
Vergani, A., Tezza, S., D’Addio, F., Fotino, C., Liu, K., Niewczas, M. A., Bassi, R., Molano, R. D., Kleffel, S., Petrelli, A., et al. (2012) · Circulation · doi:10.1161/circulationaha.112.123653 · Cited by 108 · see citing works
Jiang, L., Baldwin, J. M., Roger, S., & Baldwin, S. A. (2013) · Frontiers in Pharmacology · doi:10.3389/fphar.2013.00055 · Cited by 105 · see citing works
Gilbert, S. M., Baird, A. G., Glazer, S., Barden, J. A., Glazer, A., Teh, L. C., & King, J. (2017) · British Journal of Dermatology · doi:10.1111/bjd.15364 · Cited by 104 · see citing works
On the permeation of large organic cations through the pore of ATP-gated P2X receptors
Harkat, M., Peverini, L., Cerdan, A. H., Dunning, K., Beudez, J., Martz, A., Calimet, N., Specht, A., Cecchini, M., Chataigneau, T., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1701379114 · Cited by 104 · see citing works
Jimenez-Mateos, E. M., Arribas-Blázquez, M., Sanz‐Rodriguez, A., Concannon, C. G., Olivos-Oré, L. A., Reschke, C. R., Mooney, C. M., Mooney, C., Lugarà, E., Morgan, J., et al. (2015) · Scientific Reports · doi:10.1038/srep17486 · Cited by 103 · see citing works
Roger, S., Jelassi, B., Couillin, I., Pelegrı́n, P., Besson, P., & Jiang, L. (2014) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2014.10.029 · Cited by 101 · see citing works
Baroni, M., Pizzirani, C., Pinotti, M., Ferrari, D., Adinolfi, E., Calzavarini, S., Caruso, P., Bernardi, F., & Virgilio, F. D. (2007) · The FASEB Journal · doi:10.1096/fj.06-7238com · Cited by 101 · see citing works
P2X7 Receptors Regulate NKT Cells in Autoimmune Hepatitis
Kawamura, H., Aswad, F., Minagawa, M., Govindarajan, S., & Dennert, G. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.176.4.2152 · Cited by 98 · see citing works
Alzola, E., Pérez-Etxebarria, A., Kabré, E., Fogarty, D. J., Métioui, M., Chaı̈b, N., Macarulla, J. M., Matute, C., Dehaye, J., & Marino, A. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.46.30208 · Cited by 98 · see citing works
Amaral, E. P., Ribeiro, S. C. M., Lanes, V. R., Almeida, F. M., de Andrade, M. R. M., Bomfim, C. C. B., de Salles, É. M., Bortoluci, K. R., Coutinho‐Silva, R., Hirata, M. H., et al. (2014) · PLoS Pathogens · doi:10.1371/journal.ppat.1004188 · Cited by 97 · see citing works
BRADFORD, M. D., & Soltoff, S. P. (2002) · Biochemical Journal · doi:10.1042/bj20020358 · Cited by 97 · see citing works
Expression and function of the P2X7 receptor in rat C6 glioma cells
Wei, W., Ryu, J. K., Choi, H. B., & McLarnon, J. G. (2007) · Cancer Letters · doi:10.1016/j.canlet.2007.10.025 · Cited by 96 · see citing works
Ory, D., Celen, S., Gijsbers, R., den Haute, C. V., Postnov, A. A., Koole, M. J. B., Vandeputte, C., Andrés, J.-I., Alcázar, J., Angelis, M. D., et al. (2016) · Journal of Nuclear Medicine · doi:10.2967/jnumed.115.169995 · Cited by 93 · see citing works
P2X7 receptor antagonists: a patent review (2010–2015)
Park, J.-H., & Kim, Y. (2016) · Expert Opinion on Therapeutic Patents · doi:10.1080/13543776.2017.1246538 · Cited by 92 · see citing works
The Antibiotic Polymyxin B Modulates P2X7 Receptor Function
Ferrari, D., Pizzirani, C., Adinolfi, E., Forchap, S., Sitta, B., Turchet, L., Falzoni, S., Minelli, M., Baricordi, R., & Virgilio, F. D. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.173.7.4652 · Cited by 91 · see citing works
Self-citationCoutinho‐Silva, R., & Ojcius, D. M. (2012) · Microbes and Infection · doi:10.1016/j.micinf.2012.05.009 · Cited by 91 · see citing works
Ali, S. R., Timmer, A. M., Bilgrami, S., Park, E. J., Eckmann, L., Nizet, V., & Karin, M. (2011) · Immunity · doi:10.1016/j.immuni.2011.04.015 · Cited by 84 · see citing works
Jørgensen, N. R., Husted, L. B., Skarratt, K. K., Stokes, L., Tofteng, C. L., Kvist, T., Jensen, J. B., Eiken, P., Brixen, K., Fuller, S. J., et al. (2012) · European Journal of Human Genetics · doi:10.1038/ejhg.2011.253 · Cited by 82 · see citing works
Localization of the gate and selectivity filter of the full-length P2X7 receptor
Pippel, A., Stolz, M., Woltersdorf, R., Kless, A., Schmalzing, G., & Markwárdt, F. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1610414114 · Cited by 81 · see citing works
Mortimer, L. M., Moreau, F., Cornick, S., & Chadee, K. (2015) · PLoS Pathogens · doi:10.1371/journal.ppat.1004887 · Cited by 79 · see citing works
P2X purinergic receptor ligands: recently patented compounds
Gunosewoyo, H., & Kassiou, M. (2010) · Expert Opinion on Therapeutic Patents · doi:10.1517/13543771003702424 · Cited by 78 · see citing works
Is pannexin the pore associated with the P2X7 receptor?
Alberto, A. V. P., Faria, R. X., Couto, C. G. C., Ferreira, L. G. B., Souza, C. A. M., Teixeira, P. C. N., Fróes, M. M., & Alves, L. A. (2013) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-013-0868-x · Cited by 78 · see citing works
Structural Insights into Divalent Cation Modulations of ATP-Gated P2X Receptor Channels
Kasuya, G., Fujiwara, Y., Takemoto, M., Dohmae, N., Nakada-Nakura, Y., Ishitani, R., Hattori, M., & Nureki, O. (2016) · Cell Reports · doi:10.1016/j.celrep.2015.12.087 · Cited by 78 · see citing works
Graziano, F., Desdouits, M., Garzetti, L., Podini, P., Alfano, M., Rubartelli, A., Furlan, R., Benaroch, P., & Poli, G. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1500656112 · Cited by 77 · see citing works
Taylor, S. R. J., González–Begne, M., Dewhurst, S., Chimini, G., Higgins, C. F., Melvin, J. E., & Elliott, J. I. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.180.1.300 · Cited by 75 · see citing works
The trafficking and targeting of P2X receptors
Robinson, L. E., & Murrell‐Lagnado, R. D. (2013) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2013.00233 · Cited by 73 · see citing works
P2X7 Receptor Modulates Inflammatory and Functional Pulmonary Changes Induced by Silica
Monção-Ribeiro, L. C., Faffe, D. S., Santana, P. T., Vieira, F. S., da Graça, C. L. A. L., Marques-da-Silva, C., Machado, M. N., Caruso-Neves, C., Zin, W. A., Borojevic, R., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0110185 · Cited by 71 · see citing works
Sinadinos, A., Young, C., Al-khalidi, R. A. A., Teti, A. M., Kaliński, P., Mohamad, S., Floriot, L., Henry, T., Tozzi, G., Jiang, T., et al. (2015) · PLoS Medicine · doi:10.1371/journal.pmed.1001888 · Cited by 65 · see citing works
Karki, P., Seong, C. M., Kim, J.-E., Hur, K., Shin, S. Y., Lee, J. S., Cho, B. C., & Is, P. (2007) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402221 · Cited by 65 · see citing works
Shenker, B. J., Ojcius, D. M., Walker, L. M., Zekavat, A., Scuron, M. D., & Boesze‐Battaglia, K. (2015) · Infection and Immunity · doi:10.1128/iai.03132-14 · Cited by 65 · see citing works
Perregaux, D. G., & Gabel, C. A. (1998) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1998.275.6.c1538 · Cited by 63 · see citing works
Fantoni, E., Ben, D. D., Falzoni, S., Virgilio, F. D., Lovestone, S., & Gee, A. D. (2017) · EJNMMI Research · doi:10.1186/s13550-017-0275-2 · Cited by 62 · see citing works
Self-citationExploring the ATP-binding site of P2X receptors
Chataigneau, T., Lemoine, D. G., & Grütter, T. (2013) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2013.00273 · Cited by 61 · see citing works
Maître, B., Magnenat, S., Heim, V., Ravanat, C., Evans, R. J., de la Salle, H., Gachet, C., & Hechler, B. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1401786 · Cited by 57 · see citing works
Sun, C., Chu, J., Singh, S. G., & Salter, R. D. (2009) · Purinergic Signalling · doi:10.1007/s11302-009-9168-9 · Cited by 56 · see citing works
P2X7 and phospholipid signalling: The search of the “missing link” in epithelial cells
Garcia‐Marcos, M., Pochet, S., Marino, A., & Dehaye, J. (2006) · Cellular Signalling · doi:10.1016/j.cellsig.2006.05.008 · Cited by 56 · see citing works
Fan, Z., Zhang, Y., Yi-hong, G., Huang, N., Ma, H., Huang, H., & Yu, H. (2016) · Scientific Reports · doi:10.1038/srep35804 · Cited by 56 · see citing works
Rissiek, B., Danquah, W., Haag, F., & Koch‐Nolte, F. (2013) · Journal of Leukocyte Biology · doi:10.1189/jlb.0713407 · Cited by 55 · see citing works
Quantifying Ca2+ Current and Permeability in ATP-gated P2X7 Receptors
Liang, X., Samways, D. S. K., Wolf, K. J., Bowles, E. A., Richards, J. P., Bruno, J., Dutertre, S., DiPaolo, R. J., & Egan, T. M. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.627810 · Cited by 54 · see citing works
Contraction of intestinal effector T cells by retinoic acid-induced purinergic receptor P2X7
Hashimoto‐Hill, S., Friesen, L., Kim, M., & Kim, C. H. (2016) · Mucosal Immunology · doi:10.1038/mi.2016.109 · Cited by 52 · see citing works
Lymphocytes from P2X7-deficient mice exhibit enhanced P2X7 responses
Taylor, S. R. J., González–Begne, M., Sojka, D. K., Richardson, J. C., Sheardown, S. A., Harrison, S. M., Pusey, C. D., Tam, F. W. K., & Elliott, J. I. (2009) · Journal of Leukocyte Biology · doi:10.1189/jlb.0408251 · Cited by 49 · see citing works
P2 receptor blockade attenuates fever and cytokine responses induced by lipopolysaccharide in rats
Gourine, A. V., Poputnikov, D. M., Zhernosek, N., Melenchuk, E. V., Gerstberger, R., Spyer, K. M., & Gourine, V. N. (2005) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0706287 · Cited by 48 · see citing works
Lenertz, L. Y., Wang, Z., Guadarrama, A. G., Hill, L. M., Gavala, M. L., & Bertics, P. J. (2010) · Biochemistry · doi:10.1021/bi902083n · Cited by 47 · see citing works
Ledderose, C., Woehrle, T., Ledderose, S., Strasser, K., Seist, R., Bao, Y., Zhang, J., & JUNGER, W. G. (2016) · Purinergic Signalling · doi:10.1007/s11302-016-9510-y · Cited by 47 · see citing works
Ledderose, C., Bao, Y., Ledderose, S., Woehrle, T., Heinisch, M., Yip, L., Zhang, J., Robson, S. C., Shapiro, N. I., & JUNGER, W. G. (2015) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiv373 · Cited by 47 · see citing works
Exogenous ATP enhances calcium influx in intact thymocytes.
Lin, J. H.-C., Krishnaraj, R., & Kemp, R. G. (1985) · The Journal of Immunology · doi:10.4049/jimmunol.135.5.3403 · Cited by 45 · see citing works
Purinergic P2X receptors: Structural models and analysis of ligand-target interaction
Ben, D. D., Buccioni, M., Lambertucci, C., Marucci, G., Thomas, A., & Volpini, R. (2014) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2014.10.071 · Cited by 45 · see citing works
Barberà-Cremades, M., Baroja‐Mazo, A., & Pelegrı́n, P. (2015) · Journal of Leukocyte Biology · doi:10.1189/jlb.1a0514-267rr · Cited by 43 · see citing works
Norde, W. J., Overes, I. M., Maas, F., Fredrix, H., Vos, J. C. M., Kester, M. G. D., van der Voort, R., Jedema, I., Falkenburg, J. H. F., Schattenberg, A. V. M. B., et al. (2008) · Blood · doi:10.1182/blood-2008-04-153825 · Cited by 42 · see citing works
Omosun, Y., McKeithen, D. N., Ryans, K., Kibakaya, C., Blas‐Machado, U., Li, D., Singh, R., Inoue, K., Xiong, Z.-G., Eko, F. O., et al. (2015) · Infection and Immunity · doi:10.1128/iai.00993-15 · Cited by 41 · see citing works
Genetic Background Strongly Influences the Bone Phenotype of P2X7 Receptor Knockout Mice
Syberg, S., Petersen, S., Jensen, J. B., Gartland, A., Teilmann, J., Chessell, I. P., Steinberg, T. H., Schwarz, P., & Jørgensen, N. R. (2012) · Journal of Osteoporosis · doi:10.1155/2012/391097 · Cited by 41 · see citing works
Baconguis, I., Hattori, M., & Gouaux, E. (2013) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2013.04.005 · Cited by 36 · see citing works
Rizzo, R., Ferrari, D., Melchiorri, L., Stignani, M., Gulinelli, S., Baricordi, O. R., & Virgilio, F. D. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0804265 · Cited by 34 · see citing works
Murine macrophage P2X7 receptors support rapid prothrombotic responses
Moore, S., & Mackenzie, A. B. (2006) · Cellular Signalling · doi:10.1016/j.cellsig.2006.10.010 · Cited by 33 · see citing works
A Truncation Variant of the Cation Channel P2RX5 Is Upregulated during T Cell Activation
Abramowski, P., Ogrodowczyk, C., Martinꝉ, R., & Pongs, O. (2014) · PLoS ONE · doi:10.1371/journal.pone.0104692 · Cited by 30 · see citing works
Munerati, M., Cortesi, R., Ferrari, D., Virgilio, F. D., & Nastruzzi, C. (1994) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/0167-4889(94)90200-3 · Cited by 29 · see citing works
Laliberte, R. E., Perregaux, D. G., McNiff, P. A., & Gabel, C. A. (1997) · Journal of Leukocyte Biology · doi:10.1002/jlb.62.2.227 · Cited by 26 · see citing works
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DAMP-sensing receptors in sterile inflammation and inflammatory diseases
Gong, T., Liu, L., Jiang, W., & Zhou, R. (2020) · Nature Reviews Immunology · doi:10.1038/s41577-019-0215-7 · Cited by 1,672 · see citing works
Role of neuroinflammation in neurodegeneration development
Zhang, W., Xiao, D., Mao, Q., & Xia, H. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01486-5 · Cited by 1,668 · see citing works
Targeting the NLRP3 inflammasome in inflammatory diseases
Mangan, M. S. J., Olhava, E. J., Roush, W. R., Seidel, H. M., Glick, G. D., & Latz, E. (2018) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2018.97 · Cited by 1,885 · see citing works
Inflammation and atherosclerosis: signaling pathways and therapeutic intervention
Kong, P., Cui, Z.-Y., Huang, X.-F., Zhang, D.-D., Guo, R.-J., & Han, M. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-00955-7 · Cited by 1,183 · see citing works
Pyroptosis versus necroptosis: similarities, differences, and crosstalk
Frank, D., & Vince, J. E. (2019) · Cell Death & Differentiation · doi:10.1038/s41418-018-0212-6 · Cited by 1,062 · see citing works
Microglia in neuropathic pain: cellular and molecular mechanisms and therapeutic potential
Inoue, K., & Tsuda, M. (2018) · Nature Reviews Neuroscience · doi:10.1038/nrn.2018.2 · Cited by 908 · see citing works
Extracellular ATP and P2 purinergic signalling in the tumour microenvironment
Virgilio, F. D., Sarti, A. C., Falzoni, S., Marchi, E. D., & Adinolfi, E. (2018) · Nature reviews. Cancer · doi:10.1038/s41568-018-0037-0 · Cited by 730 · see citing works
Self-citationRole of pyroptosis in inflammation and cancer
Xiang, W. D., Xie, F., Zhou, X., Wu, Y., Yan, H., Liu, T., Huang, J. S., Wang, F., Zhou, F., & Zhang, L. (2022) · Cellular and Molecular Immunology · doi:10.1038/s41423-022-00905-x · Cited by 711 · see citing works
Mitochondria in health, disease, and aging
Harrington, J. S., Ryter, S. W., Plataki, M. E., Price, D. R., & Choi, A. M. K. (2023) · Physiological Reviews · doi:10.1152/physrev.00058.2021 · Cited by 622 · see citing works
Trebak, M., & Kinet, J.-P. (2019) · Nature reviews. Immunology · doi:10.1038/s41577-018-0110-7 · Cited by 506 · see citing works
From purines to purinergic signalling: molecular functions and human diseases
Huang, Z., Xie, N., Illés, P., Virgilio, F. D., Ulrich, H., Semyanov, A. V., Verkhratsky, A., Sperlágh, B., Yu, S., Huang, C., et al. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00553-z · Cited by 495 · see citing works
“Functional P2X7 receptor is a trimeric complex with a variable conformation switches between open (ATP-bound) and closed states, which is one of the most intensively studied purinergic receptors that shapes immune responses.(225,226) Mounting evidence suggests that P2X7 receptors control cytokine release and immune ce…”
BackgroundThe P2X7 Receptor in Inflammatory Diseases: Angel or Demon?
Savio, L. E. B., de Andrade Mello, P., da Silva, C. G., & Coutinho-Silva, R. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.00052 · Cited by 437 · see citing works
Han, X., Sun, S., Sun, Y., Song, Q., Zhu, J., Song, N., Chen, M., Sun, T., Xia, M., Ding, J., et al. (2019) · Autophagy · doi:10.1080/15548627.2019.1596481 · Cited by 408 · see citing works
Targeting the NLRP3 Inflammasome in Severe COVID-19
Freeman, T. L., & Swartz, T. H. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.01518 · Cited by 406 · see citing works
The gut–joint axis in rheumatoid arthritis
Zaiss, M. M., Wu, H.-J. J., Mauro, D., Schett, G. A., & Ciccia, F. (2021) · Nature Reviews Rheumatology · doi:10.1038/s41584-021-00585-3 · Cited by 394 · see citing works
The P2X7 receptor: A main player in inflammation
Adinolfi, E., Giuliani, A. L., De Marchi, E., Pegoraro, A., Orioli, E., & Di Virgilio, F. (2018) · Biochemical Pharmacology · doi:10.1016/j.bcp.2017.12.021 · Cited by 385 · see citing works
Self-citationMitochondria-associated membranes (MAMs) and inflammation
Missiroli, S., Patergnani, S., Caroccia, N., Pedriali, G., Perrone, M., Previati, M., Wieckowski, M. R., & Giorgi, C. (2018) · Cell Death and Disease · doi:10.1038/s41419-017-0027-2 · Cited by 389 · see citing works
Immune regulation by microbiome metabolites
Kim, C. H. (2018) · Immunology · doi:10.1111/imm.12930 · Cited by 375 · see citing works
Purine Release, Metabolism, and Signaling in the Inflammatory Response
Linden, J. M., Koch‐Nolte, F., & Dahl, G. (2019) · Annual Review of Immunology · doi:10.1146/annurev-immunol-051116-052406 · Cited by 378 · see citing works
Metal Drugs and the Anticancer Immune Response
Englinger, B., Pirker, C., Heffeter, P., Terenzi, A., Kowol, C. R., Keppler, B. K., & Berger, W. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00396 · Cited by 355 · see citing works
Moesta, A. K., Li, X.-Y., & Smyth, M. J. (2020) · Nature reviews. Immunology · doi:10.1038/s41577-020-0376-4 · Cited by 324 · see citing works
New keys for old locks: carborane-containing drugs as platforms for mechanism-based therapies
Stockmann, P., Gozzi, M., Kuhnert, R., Sárosi, M. B., & Hey‐Hawkins, E. (2019) · Chemical Society Reviews · doi:10.1039/c9cs00197b · Cited by 317 · see citing works
Update of P2X receptor properties and their pharmacology: IUPHAR Review 30
Illés, P., Müller, C. E., Jacobson, K. A., Grütter, T., Nicke, A., Fountain, S. J., Kennedy, C., Schmalzing, G., Jarvis, M. F., Stojilković, S. S., et al. (2020) · British Journal of Pharmacology · doi:10.1111/bph.15299 · Cited by 315 · see citing works
Microglia in Alzheimer’s disease: pathogenesis, mechanisms, and therapeutic potentials
Miao, J., Ma, H., Yang, Y., Liao, Y., Lin, C., Zheng, J., Yu, M., & Lan, J. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2023.1201982 · Cited by 293 · see citing works
Di Virgilio, F., Schmalzing, G., & Markwardt, F. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.01.005 · Cited by 279 · see citing works
Lüscher, B., Bütepage, M., Eckei, L., Krieg, S., Verheugd, P., & Shilton, B. H. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00122 · Cited by 258 · see citing works
The purinergic receptor P2RX7 directs metabolic fitness of long-lived memory CD8+ T cells
da Silva, H. B., Beura, L. K., Wang, H., Hanse, E. A., Gore, R., Scott, M. C., Walsh, D., Block, K. E., Fonseca, R., Yan, Y., et al. (2018) · Nature · doi:10.1038/s41586-018-0282-0 · Cited by 258 · see citing works
Regulation of phospholipid distribution in the lipid bilayer by flippases and scramblases
Sakuragi, T., & Nagata, S. (2023) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-023-00604-z · Cited by 258 · see citing works
Extracellular ATP: A Feasible Target for Cancer Therapy
Vultaggio-Poma, V., Sarti, A. C., & Virgilio, F. D. (2020) · Cells · doi:10.3390/cells9112496 · Cited by 251 · see citing works
“Over the years, a role for eATP has been identified in several, different physiological and pathological conditions such as [12]: glial-neuron interaction [13], sensory transmission [14], hormone secretion [15], disorders of central nervous system [16], cardiovascular diseases [17], infection [18], inflammation [19] a…”
BackgroundSelf-citationBurnstock, G., & Knight, G. E. (2018) · Purinergic Signalling · doi:10.1007/s11302-017-9593-0 · Cited by 248 · see citing works
P2X7 receptor and the NLRP3 inflammasome: Partners in crime
Pelegrı́n, P. (2020) · Biochemical Pharmacology · doi:10.1016/j.bcp.2020.114385 · Cited by 241 · see citing works
Regulation of Microglial Functions by Purinergic Mechanisms in the Healthy and Diseased CNS
Illés, P., Rubini, P., Ulrich, H., Zhao, Y., & Tang, Y. (2020) · Cells · doi:10.3390/cells9051108 · Cited by 235 · see citing works
Purinergic signaling, DAMPs, and inflammation
Virgilio, F. D., Sarti, A. C., & Coutinho‐Silva, R. (2020) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00053.2020 · Cited by 237 · see citing works
“In the IME and TME, ATP release and degradation (and therefore adenosine generation) are closely correlated; thus the final effect is often a result of the stimulation of both P2Rs and P1Rs, as it is clearly shown in the case of polymorphonuclear leukocyte chemotaxis, which is dependent on both P2Y2R and A3R stimulati…”
BackgroundSelf-citationMartínez-García, J. J., Martínez-Banaclocha, H., Angosto-Bazarra, D., de Torre-Minguela, C., Baroja-Mazo, A., Alarcón-Vila, C., Martínez-Alarcón, L., Amores-Iniesta, J., Martín-Sánchez, F., Ercole, G. A., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-10626-x · Cited by 233 · see citing works
P2X7 Interactions and Signaling – Making Head or Tail of It
Kopp, R., Krautloher, A., Ramírez-Fernández, A., & Nicke, A. (2019) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2019.00183 · Cited by 217 · see citing works
Extracellular nucleotides and nucleosides as signalling molecules
Giuliani, A. L., Sarti, A. C., & Virgilio, F. D. (2018) · Immunology Letters · doi:10.1016/j.imlet.2018.11.006 · Cited by 218 · see citing works
Self-citationRe-evaluation of neuronal P2X7 expression using novel mouse models and a P2X7-specific nanobody
Kaczmarek-Hájek, K., Zhang, J., Kopp, R., Grosche, A., Rissiek, B., Saul, A., Bruzzone, S., Engel, T., Jooss, T., Durner, A., et al. (2018) · eLife · doi:10.7554/elife.36217 · Cited by 210 · see citing works
Vujkovic, M., Ramdas, S., Lorenz, K. M., Guo, X., Darlay, R., Cordell, H. J., He, J., Gindin, Y., Chung, C., Myers, R. P., et al. (2022) · Nature Genetics · doi:10.1038/s41588-022-01078-z · Cited by 205 · see citing works
The Concise Guide to PHARMACOLOGY 2023/24: Ion channels
Alexander, S. P. H., Mathie, A. A., Peters, J. A., Veale, E. L., Striessnig, J., Kelly, E., Armstrong, J. F., Faccenda, E., Harding, S. D., Davies, J. A., et al. (2023) · British Journal of Pharmacology · doi:10.1111/bph.16178 · Cited by 199 · see citing works
Self-citationGilbert, S. M., Oliphant, C. J., Hassan, S., Peille, A., Bronsert, P., Falzoni, S., Virgilio, F. D., McNulty, S., & Lara, R. (2018) · Oncogene · doi:10.1038/s41388-018-0426-6 · Cited by 198 · see citing works
Self-citationMarchi, E. D., Orioli, E., Pegoraro, A., Sangaletti, S., Portararo, P., Curti, A., Colombo, M. P., Virgilio, F. D., & Adinolfi, E. (2019) · Oncogene · doi:10.1038/s41388-019-0684-y · Cited by 196 · see citing works
CD39 Regulation and Functions in T Cells
Timperi, E., & Barnaba, V. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22158068 · Cited by 188 · see citing works
Wei, Q., Zhu, R., Zhu, J., Zhao, R., & Li, M. (2019) · Oncology Research Featuring Preclinical and Clinical Cancer Therapeutics · doi:10.3727/096504018x15462920753012 · Cited by 185 · see citing works
Kong, H., Zhao, H., Chen, T., Song, Y., & Cui, Y. T. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-04786-w · Cited by 185 · see citing works
“Dysregulation of the overactive P2X7 calcium signal dysregulation is critical for the death of neurons and microvascular cells [55].”
Amores, J., Barberà-Cremades, M., Martínez, C. M., Pons, J. A., Revilla‐Nuin, B., Martínez-Alarcón, L., Virgilio, F. D., Parrilla, P., Baroja‐Mazo, A., & Pelegrı́n, P. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.11.079 · Cited by 181 · see citing works
Hepatic macrophages: Key players in the development and progression of liver fibrosis
Cheng, D., Chai, J., Wang, H., Fu, L., Peng, S., & Ni, X. (2021) · Liver International · doi:10.1111/liv.14940 · Cited by 188 · see citing works
Quan, J., Huang, R., Wang, Z., Huang, S., Choi, I.-W., Zhou, Y. J., Lee, Y., & Chu, J. (2018) · Parasites & Vectors · doi:10.1186/s13071-017-2573-y · Cited by 172 · see citing works
Chronic pain and neuroinflammation
Vergne‐Salle, P., & Bertin, P. (2021) · Joint Bone Spine · doi:10.1016/j.jbspin.2021.105222 · Cited by 172 · see citing works
Macrophage Recognition of Crystals and Nanoparticles
NAKAYAMA, M. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.00103 · Cited by 170 · see citing works
P2X7 in Cancer: From Molecular Mechanisms to Therapeutics
Lara, R., Adinolfi, E., Harwood, C. A., Philpott, M. P., Barden, J. A., Virgilio, F. D., & McNulty, S. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.00793 · Cited by 165 · see citing works
Radiation-Induced Salivary Gland Dysfunction: Mechanisms, Therapeutics and Future Directions
Jasmer, K. J., Gilman, K. E., Forti, K. M., Weisman, G. A., & Limesand, K. H. (2020) · Journal of Clinical Medicine · doi:10.3390/jcm9124095 · Cited by 166 · see citing works
Targeting CD73 to augment cancer immunotherapy
Roh, M., Wainwright, D. A., Wu, J. D., Wan, Y., & Zhang, B. (2020) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2020.07.001 · Cited by 166 · see citing works
Innate immune activation in neurodegenerative diseases
Castro‐Gomez, S., & Heneka, M. T. (2024) · Immunity · doi:10.1016/j.immuni.2024.03.010 · Cited by 165 · see citing works
P2RX7 inhibitor suppresses exosome secretion and disease phenotype in P301S tau transgenic mice
Ruan, Z., Delpech, J.-C., Venkatesan Kalavai, S., Van Enoo, A. A., Hu, J., Ikezu, S., & Ikezu, T. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00396-2 · Cited by 150 · see citing works
“Activation of P2RX7 has been shown to trigger Na/Ca influx, plasma membrane depolarization, secretion of EVs, chemotaxis and activation of inflammasomes [9].”
BackgroundHuman Microglia Show Unique Transcriptional Changes in Alzheimer's Disease
Prater, K. E., Green, K. J., Mamde, S., Sun, W., Cochoit, A., Smith, C. L., Chiou, K. L., Heath, L., Rose, S. E., Wiley, J., et al. (2023) · Nature Aging · doi:10.1038/s43587-023-00424-y · Cited by 164 · see citing works
Nová, Z., Škovierová, H., & Čalkovská, A. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20040831 · Cited by 164 · see citing works
PET Imaging of Neuroinflammation in Alzheimer’s Disease
Zhou, R., Ji, B., Kong, Y., Qin, L., Ren, W., Guan, Y., & Ni, R. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.739130 · Cited by 150 · see citing works
Calcium signalling and related ion channels in neutrophil recruitment and function
Immler, R., Simon, S. I., & Sperandio, M. (2018) · European Journal of Clinical Investigation · doi:10.1111/eci.12964 · Cited by 150 · see citing works
Jaeschke, H., Adelusi, O. B., Akakpo, J. Y., Nguyen, N. T., Sánchez-Guerrero, G., Umbaugh, D. S., Ding, W., & Ramachandran, A. (2021) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2021.09.023 · Cited by 152 · see citing works
<b>T</b> <sub> <b>RM</b> </sub> <b>maintenance is regulated by tissue damage via P2RX7</b>
Stark, R., Wesselink, T. H., Behr, F. M., Kragten, N. A. M., Arens, R., Koch-Nolte, F., van Gisbergen, K. P. J. M., & van Lier, R. A. W. (2018) · Science Immunology · doi:10.1126/sciimmunol.aau1022 · Cited by 141 · see citing works
Hyperactivation of P2X7 receptors as a culprit of COVID-19 neuropathology
Ribeiro, D. E., Oliveira-Giacomelli, Á., Glaser, T., Arnaud-Sampaio, V. F., Andrejew, R., Dieckmann, L., Baranova, J., Lameu, C., Ratajczak, M. Z., & Ulrich, H. (2021) · Molecular Psychiatry · doi:10.1038/s41380-020-00965-3 · Cited by 145 · see citing works
Microglial inflammation and phagocytosis in Alzheimer's disease: Potential therapeutic targets
Nizami, S., Hall‐Roberts, H., Warrier, S., Cowley, S. A., & Di Daniel, E. (2019) · British Journal of Pharmacology · doi:10.1111/bph.14618 · Cited by 147 · see citing works
Karasawa, A., Michalski, K., Mikhelzon, P., & Kawate, T. (2017) · eLife · doi:10.7554/elife.31186 · Cited by 127 · see citing works
Stress induced microglial activation contributes to depression
Li, B., Yang, W., Ge, T., Wang, Y., & Cui, R. (2022) · Pharmacological Research · doi:10.1016/j.phrs.2022.106145 · Cited by 147 · see citing works
Pyroptosis and Its Role in Autoimmune Disease: A Potential Therapeutic Target
You, R., He, X., Zeng, Z., Zhan, Y., Xiao, Y., & Xiao, R. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.841732 · Cited by 147 · see citing works
Control of adaptive immunity by pattern recognition receptors
Carroll, S. L., Pasare, C., & Barton, G. M. (2024) · Immunity · doi:10.1016/j.immuni.2024.03.014 · Cited by 146 · see citing works
Conversion of extracellular ATP into adenosine: a master switch in renal health and disease
Dwyer, K. M., Kishore, B. K., & Robson, S. C. (2020) · Nature Reviews Nephrology · doi:10.1038/s41581-020-0304-7 · Cited by 143 · see citing works
Microglial phenotypes in the human epileptic temporal lobe
Morin‐Brureau, M., Milior, G., Royer, J., Chali, F., Duigou, C. L., Savary, E., Blugeon, C., Jourdren, L., Akbar, D., Dupont, S., et al. (2018) · Brain · doi:10.1093/brain/awy276 · Cited by 140 · see citing works
P2X7 Receptors Amplify CNS Damage in Neurodegenerative Diseases
Illés, P. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21175996 · Cited by 141 · see citing works
Macrophage as a Peripheral Pain Regulator
Domoto, R., Sekiguchi, F., Tsubota, M., & Kawabata, A. (2021) · Cells · doi:10.3390/cells10081881 · Cited by 119 · see citing works
“Activation of P2X7 receptors in macrophages induces IL-1β release via activation of Nod-like receptor protein (NLRP) 3 inflammasome [80,81], which might lead to pyroptosis [81,82].”
BackgroundOkada, T., Suzuki, H., Travis, Z. D., & Zhang, J. H. (2020) · Current Neuropharmacology · doi:10.2174/1570159x18666200528143301 · Cited by 137 · see citing works
“ATP binds to P2X7 receptor (P2X7R) located on cell surface of neurons and glial cells, and leads to activation of the downstream signaling NLRP3 inflammasome and MAPKs followed by production of proinflammatory substances resulting in BBB injury [288-295].”
BackgroundOn the mechanism of anti-CD39 immune checkpoint therapy
Allard, D., Allard, B., & Stagg, J. (2020) · Journal for ImmunoTherapy of Cancer · doi:10.1136/jitc-2019-000186 · Cited by 132 · see citing works
“13 For instance, localized activation of P2X4 promotes Ca 2+ influx in T cells and selective activation of mitochondria at the immune synapse.”
Ion channelopathies of the immune system
Vaeth, M., & Feske, S. (2018) · Current Opinion in Immunology · doi:10.1016/j.coi.2018.03.021 · Cited by 129 · see citing works
Current understanding of meningeal and cerebral vascular function underlying migraine headache
Levy, D., Labastida‐Ramírez, A., & MaassenVanDenBrink, A. (2018) · Cephalalgia · doi:10.1177/0333102418771350 · Cited by 129 · see citing works
Li, Z., Huang, Z., Zhang, H., Lu, J., Tian, Y., Wei, Y., Yang, Y., & Bai, L. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/8868361 · Cited by 129 · see citing works
“Overall, P2X7 regulates a series of signaling pathways involved in inflammation, including ion flow, protease activation, membrane response, and secretion [10].”
BackgroundThe NLRP3 inflammasome renders cell death pro-inflammatory
Gaidt, M. M., & Hornung, V. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.11.013 · Cited by 124 · see citing works
da Silva, H. B., Peng, C., Wang, H.-G., Wanhainen, K. M., Ma, C.-Y., Lopez, S., Khoruts, A., Zhang, N., & Jameson, S. (2020) · Immunity · doi:10.1016/j.immuni.2020.06.010 · Cited by 115 · see citing works
The Antisocial Network: Cross Talk Between Cell Death Programs in Host Defense
Snyder, A. G., & Oberst, A. (2021) · Annual Review of Immunology · doi:10.1146/annurev-immunol-112019-072301 · Cited by 129 · see citing works
“The P2X7 receptor in infection and inflammation.”
BackgroundJaeschke, H., & Ramachandran, A. (2020) · Food and Chemical Toxicology · doi:10.1016/j.fct.2020.111240 · Cited by 128 · see citing works
Zhao, X., Wang, J., Deng, Y., Liao, L., Zhou, M., Peng, C. Y., & Li, Y. (2021) · Phytotherapy Research · doi:10.1002/ptr.7104 · Cited by 126 · see citing works
Distinct Molecular Mechanisms Underlying Potassium Efflux for NLRP3 Inflammasome Activation
Xu, Z., Chen, Z.-M., Wu, X., Zhang, L., Cao, Y., & Zhou, P. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.609441 · Cited by 122 · see citing works
Yu, L., Hong, W., Lu, S., Li, Y., Guan, Y., Weng, X., & Feng, Z. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.780496 · Cited by 122 · see citing works
Biochemistry, Cell Biology, and Pathophysiology of the Innate Immune cGAS–cGAMP–STING Pathway
Ritchie, C., Carozza, J. A., & Li, L. (2022) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-040320-101629 · Cited by 121 · see citing works
Xu, Q., Zhao, B., Ye, Y., Li, Y., Zhang, Y., Xiong, X., & Gu, L. (2021) · Journal of Neuroinflammation · doi:10.1186/s12974-021-02137-8 · Cited by 118 · see citing works
“crease in ATP concentration activates P2X7R, leading to intracellular K efflux that activates the NLRP3 inflammasome [88].”
BackgroundLiang, H., Chen, A., Lai, X., Liu, J., Wu, J., Kang, Y., Wang, X., & Shao, L. (2018) · Particle and Fibre Toxicology · doi:10.1186/s12989-018-0274-0 · Cited by 118 · see citing works
Extracellular ATP: A powerful inflammatory mediator in the central nervous system
Virgilio, F. D., Vultaggio-Poma, V., Falzoni, S., & Giuliani, A. L. (2022) · Neuropharmacology · doi:10.1016/j.neuropharm.2022.109333 · Cited by 121 · see citing works
Self-citationAlugoju, P., Swamy, V., Anthikapalli, N. V. A., & Tencomnao, T. (2022) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2022.2084600 · Cited by 122 · see citing works
Fumagalli, M., Lecca, D., Abbracchio, M. P., & Ceruti, S. (2017) · Frontiers in Pharmacology · doi:10.3389/fphar.2017.00941 · Cited by 116 · see citing works
Regulation of coenzyme A levels by degradation: the ‘Ins and Outs’
Naquet, P., Kerr, E. W., Vickers, S. D., & Leonardi, R. (2020) · Progress in Lipid Research · doi:10.1016/j.plipres.2020.101028 · Cited by 115 · see citing works
“These metabolites modulate purinergic signaling and are involved in multiple processes such as neurotransmission, bone mineralization, inflammation and platelet aggregation [183].”
BackgroundMarine Alkaloids with Anti-Inflammatory Activity: Current Knowledge and Future Perspectives
Souza, C. R. D. M., Bezerra, W. P., & de Souto, J. T. (2020) · Marine Drugs · doi:10.3390/md18030147 · Cited by 114 · see citing works
“P2X7 receptors are ATP receptors involved in the activation of inflammatory response mechanisms, such as the activation of NLRP3 inflammasomes, the synthesis of proinflammatory cytokines and chemokines, the activation of MAPK and phospholipase C, and the activation of transcription factors involved in the expression o…”
BackgroundNabekura, T., Riggan, L., Hildreth, A. D., O’Sullivan, T. E., & Shibuya, A. (2019) · Immunity · doi:10.1016/j.immuni.2019.11.004 · Cited by 106 · see citing works
Piezo1 expression in neutrophils regulates shear-induced NETosis
Baratchi, S., Danish, H., Chheang, C., Zhou, Y., Huang, A., Lai, A., Khanmohammadi, M., Quinn, K. M., Khoshmanesh, K., & Peter, K. (2024) · Nature Communications · doi:10.1038/s41467-024-51211-1 · Cited by 109 · see citing works
Targeting NLRP3 Inflammasome in the Treatment of CNS Diseases
Shao, B., Cao, Q., & Chong, L. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00320 · Cited by 102 · see citing works
Shokoples, B. G., Paradis, P., & Schiffrin, E. L. (2020) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.120.315116 · Cited by 102 · see citing works
Veeresh, P., Kaur, H., Sarmah, D., Mounica, L., Verma, G., Kotian, V., Kesharwani, R., Kalia, K., Borah, A., Wang, X., et al. (2019) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.14212 · Cited by 96 · see citing works
Quercetin Attenuates Atherosclerotic Inflammation by Inhibiting Galectin‐3‐NLRP3 Signaling Pathway
Li, H., Xiao, L., He, H., Zeng, H., Liu, J., Jiang, C., Mei, G., Yu, J., Chen, H., Yao, P., et al. (2021) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.202000746 · Cited by 98 · see citing works
Focusing on mitochondria in the brain: from biology to therapeutics
Song, N., Mei, S., Wang, X.-X., Hu, G., & Lu, M. (2024) · Translational Neurodegeneration · doi:10.1186/s40035-024-00409-w · Cited by 102 · see citing works
“Moreover, extra-cellular ATP even functions as a DAMP by binding to purinergic receptors (mainly P2X7R) expressed on myeloid cells to mediate inflammatory responses, especially inflammasome activation [170, 171].”
BackgroundCalzaferri, F., Ruiz‐Ruiz, C., de Diego, A. M. G., de Pascual, R., Méndez‐López, I., Cano‐Abad, M. F., Maneu, V., Rı́os, C. D. L., Gandı́a, L., & de Diego, A. M. G. (2020) · Medicinal Research Reviews · doi:10.1002/med.21710 · Cited by 98 · see citing works
“BBG has been utilized in both in vitro and in vivo experiments; however, this compound also targets P2X4, P2X5, rat P2Y1, and P2Y2 receptors, as well as voltage‐gated sodium channels.8,95,96 BBG was initially the main compound used for the proof‐ of‐concept of P2X7Rs role in NDDs, such as ALS and AD.97–99 Its permeabi…”
BackgroundInfluentialNeuroinflammation in Sepsis: Molecular Pathways of Microglia Activation
Moraes, C. A., Zaverucha-do-Valle, C., Fleurance, R., Sharshar, T., Bozza, F. A., & d’Avila, J. C. (2021) · Pharmaceuticals · doi:10.3390/ph14050416 · Cited by 97 · see citing works
Durán-Flores, D., & Heil, M. (2017) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2017.10.010 · Cited by 94 · see citing works
- Authors
- Di Virgilio, F., Dal Ben, D., Sarti, A. C., Giuliani, A. L., & Falzoni, S.
- Affiliations
- University of Ferrara (IT)
- Venue
- Immunity
- Publisher
- Elsevier BV
- Published
- 2017-07
- Volume
- 47
- Issue
- 1
- Pages
- 15-31
- ISSN
- 1074-7613 (ISSN-L)
- OpenAlex
- W2737555531
- Cited by
- 1,267
- References
- 199
- Citations by year
- 2026: 167 · 2025: 138 · 2024: 164 · 2023: 155 · 2022: 160 · 2021: 161 · 2020: 132 · 2019: 102 · 2018: 78 · 2017: 9 · 2012: 1
- FWCI
- 9.14
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Immunity (publishedVersion)
- PubMed (publishedVersion)
- Unicam Scientific Publications (University of Camerino) (submittedVersion, other-oa)
- Institutional Research Information System University of Ferrara (University of Ferrara) (submittedVersion, cc-by)
- Funders
- Italian Association for Cancer Research (IG 13025, IG 18581)
- Telethon of Italy (GGP06070)
- ERA-NET Neuron Joint Transnational Project “Nanostroke,” the Ministry of Health of Italy (RF-2011-02348435)
- Italian Ministry of Education, University and Research (RBAP11FXBC_001)
- University of Ferrara
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Adenosine and Purinergic Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
- Health Sciences › Medicine › Physiology › Pain Mechanisms and Treatments
- Keywords
- P2X7 receptor, extracellular ATP, purinergic receptors, NLRP3 inflammasome, inflammation, innate immunity, adaptive immunity, cytokine and chemokine secretion, single nucleotide polymorphisms, cancer, anti-inflammatory therapy, cancer therapy, signal transduction, receptor structure
- MeSH terms
- Animals, Cell Differentiation, Humans, Infections, Inflammation, Macrophages, T-Lymphocytes, Receptors, Purinergic P2X7, Inflammasomes, Purinergic P2X Receptor Agonists
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