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Erythroid mitochondrial retention triggers myeloid-dependent type I interferon in human SLE
Open accessAbstract
Emerging evidence supports that mitochondrial dysfunction contributes to systemic lupus erythematosus (SLE) pathogenesis. Here we show that programmed mitochondrial removal, a hallmark of mammalian erythropoiesis, is defective in SLE. Specifically, we demonstrate that during human erythroid cell maturation, a hypoxia-inducible factor (HIF)-mediated metabolic switch is responsible for the activation of the ubiquitin-proteasome system (UPS), which precedes and is necessary for the autophagic removal of mitochondria. A defect in this pathway leads to accumulation of red blood cells (RBCs) carrying mitochondria (Mito+ RBCs) in SLE patients and in correlation with disease activity. Antibody-mediated internalization of Mito+ RBCs induces type I interferon (IFN) production through activation of cGAS in macrophages. Accordingly, SLE patients carrying both Mito+ RBCs and opsonizing antibodies display the highest levels of blood IFN-stimulated gene (ISG) signatures, a distinctive feature of SLE.
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“Abnormal retention of mitochondria in mature erythrocytes in patients with SLE is caused by a defective hypoxia-inducible factor (HIF)-mediated metabolic switch that leads to impaired activation of the ubiquitin-proteasome system, necessary for the execution of mitophagy during human erythroid cell maturation”
From The role of mitochondria in rheumatic diseases (2022) · cites this paper as [119]
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“high interferon-stimulated gene signatures in patients with SLE are associated with the presence of mitochondria-containing erythrocytes and opsonizing antibodies119”
From The role of mitochondria in rheumatic diseases (2022) · cites this paper as [119]
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“phagocytosis of opsonized mitochondria-containing erythrocytes induces activation of the DNA-sensing cyclic GMP-AMP synthase–stimulator of interferon genes (cGAS–STING) pathway in macrophages and induces subsequent production of type I interferons119”
From The role of mitochondria in rheumatic diseases (2022) · cites this paper as [119]
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“a study published in 2021 revealed that a proportion of erythrocytes contain mitochondria in SLE119”
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1 retracted
Martinez, J., Almendinger, J., Oberst, A., Ness, R., Dillon, C. P., Fitzgerald, P., Hengartner, M. O., & Green, D. R. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1113421108 · Cited by 655
RetractedMetabolic regulation of gene expression by histone lactylation
Zhang, D., Tang, Z., Huang, H., Zhou, G., Cui, C., Weng, Y., Liu, W., Kim, S., Lee, S., Perez-Neut, M., et al. (2019) · Nature · doi:10.1038/s41586-019-1678-1 · Cited by 4,371
A Cold-Inducible Coactivator of Nuclear Receptors Linked to Adaptive Thermogenesis
Puigserver, P., Wu, Z., Park, C. W., Graves, R., Wright, M., & Spiegelman, B. M. (1998) · Cell · doi:10.1016/s0092-8674(00)81410-5 · Cited by 3,864
SYSTEMIC LUPUS ERYTHEMATOSUS DISEASE ACTIVITY INDEX
Gladman, D. D., Ibañez, D., & Urowitz, M. B. (2007) · Elsevier eBooks · doi:10.1016/b978-0-323-04434-9.50060-9 · Cited by 2,928
Mitophagy and Quality Control Mechanisms in Mitochondrial Maintenance
Pickles, S., Vigié, P., & Youle, R. J. (2018) · Current Biology · doi:10.1016/j.cub.2018.01.004 · Cited by 2,081
Mitochondrial DNA stress primes the antiviral innate immune response
West, A. P., Khoury-Hanold, W., Staron, M., Tal, M. C., Pineda, C. M., Lang, S. M., Bestwick, M., Duguay, B. A., Raimundo, N., MacDuff, D. A., et al. (2015) · Nature · doi:10.1038/nature14156 · Cited by 1,975
Lood, C., Blanco, L. P., Purmalek, M. M., Carmona-Rivera, C., De Ravin, S. S., Smith, C. K., Malech, H. L., Ledbetter, J. A., Elkon, K. B., & Kaplan, M. J. (2016) · Nature Medicine · doi:10.1038/nm.4027 · Cited by 1,570
DNA sensing by the cGAS–STING pathway in health and disease
Motwani, M., Pesiridis, S., & Fitzgerald, K. A. (2019) · Nature Reviews Genetics · doi:10.1038/s41576-019-0151-1 · Cited by 1,467
Trial of Anifrolumab in Active Systemic Lupus Erythematosus
Morand, E. F., Furie, R. A., Tanaka, Y., Bruce, I. N., Askanase, A., Richez, C., Bae, S., Brohawn, P. Z., Pineda, L., Berglind, A., et al. (2019) · New England Journal of Medicine · doi:10.1056/nejmoa1912196 · Cited by 1,390
Proteasome and p97 mediate mitophagy and degradation of mitofusins induced by Parkin
Tanaka, A., Cleland, M. M., Xu, S., Narendra, D. P., Suen, D.-F., Karbowski, M., & Youle, R. J. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201007013 · Cited by 1,369
Cellular Adaptation to Hypoxia through Hypoxia Inducible Factors and beyond
Lee, P., Chandel, N. S., & Simon, M. C. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0227-y · Cited by 1,272
Essential role for Nix in autophagic maturation of erythroid cells
Sandoval, H., Thiagarajan, P., Dasgupta, S. K., Schumacher, A., Prchal, J. T., Chen, M., & Wang, J. (2008) · Nature · doi:10.1038/nature07006 · Cited by 1,185
Systemic Lupus Erythematosus Disease Activity Index
National Cancer Institute (2020) · Definitions · doi:10.32388/n5g0vc · Cited by 1,022
Metabolic requirements for the maintenance of self-renewing stem cells
Ito, K., & Suda, T. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3772 · Cited by 1,014
Broad activation of the ubiquitin–proteasome system by Parkin is critical for mitophagy
Chan, N. C., Salazar, A. M., Pham, A. H., Sweredoski, M. J., Kolawa, N. J., Graham, R. L. J., Hess, S., & Chan, D. C. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr048 · Cited by 993
NIX is required for programmed mitochondrial clearance during reticulocyte maturation
Schweers, R. L., Zhang, J., Randall, M. S., Loyd, M. R., Li, W., Dorsey, F. C., Kundu, M., Opferman, J. T., Cleveland, J. L., Miller, J. L., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0708818104 · Cited by 979
The logic of the 26S proteasome.
Collins, G. A., & Goldberg, A. L. (2017) · Cell · doi:10.1016/j.cell.2017.04.023 · Cited by 933
Prohibitin 2 Is an Inner Mitochondrial Membrane Mitophagy Receptor
Wei, Y., Chiang, W., Sumpter, R., Mishra, P., & Levine, B. (2016) · Cell · doi:10.1016/j.cell.2016.11.042 · Cited by 878
Human lupus autoantibody–DNA complexes activate DCs through cooperation of CD32 and TLR9
Means, T. K., Latz, E., Hayashi, F., Murali, M. R., Golenbock, D. T., & Luster, A. D. (2005) · Journal of Clinical Investigation · doi:10.1172/jci23025 · Cited by 866
VDAC oligomers form mitochondrial pores to release mtDNA fragments and promote lupus-like disease
Kim, J., Gupta, R., Blanco, L. P., Yang, S., Shteinfer-Kuzmine, A., Wang, K., Zhu, J., Yoon, H. E., Wang, X., Kerkhofs, M., et al. (2019) · Science · doi:10.1126/science.aav4011 · Cited by 793
Personalized Immunomonitoring Uncovers Molecular Networks that Stratify Lupus Patients
Banchereau, R., Hong, S., Cantarel, B. L., Baldwin, N. E., Baisch, J. M., Edens, M., Cepika, A., Acs, P., Turner, J., Anguiano, E., et al. (2016) · Cell · doi:10.1016/j.cell.2016.03.008 · Cited by 751
Self-citationA Modular Analysis Framework for Blood Genomics Studies: Application to Systemic Lupus Erythematosus
Chaussabel, D., Quinn, C., Shen, J., Patel, P., Glaser, C., Baldwin, N., Stichweh, D., Blankenship, D., Li, L., Munagala, I., et al. (2008) · Immunity · doi:10.1016/j.immuni.2008.05.012 · Cited by 649
Self-citationThe Sedoheptulose Kinase CARKL Directs Macrophage Polarization through Control of Glucose Metabolism
Haschemi, A., Kosma, P., Gille, L., Evans, C. R., Burant, C. F., Starkl, P., Knapp, B., Haas, R., Schmid, J. A., Jandl, C., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.04.023 · Cited by 635
Digoxin and other cardiac glycosides inhibit HIF-1α synthesis and block tumor growth
Zhang, H., Qian, D. Z., Tan, Y. S., Lee, K., Gao, P., Ren, Y. R., Rey, S., Hammers, H., Chang, D., Pili, R., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0809763105 · Cited by 624
Yoshii, S. R., Kishi, C., Ishihara, N., & Mizushima, N. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.209338 · Cited by 612
Regulation of proteasome assembly and activity in health and disease
Rousseau, A., & Bertolotti, A. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0040-z · Cited by 510
Caielli, S., Athale, S., Domic, B., Murat, E., Chandra, M., Banchereau, R., Baisch, J., Phelps, K., Clayton, S., Gong, M., et al. (2016) · Journal of Experimental Medicine · doi:10.1084/jem.20151876 · Cited by 501
Self-citationAutoimmunity after Alpha-Interferon Therapy for Malignant Carcinoid Tumors
Rönnblom, L., Alm, G. V., & Öberg, K. E. (1991) · Annals of Internal Medicine · doi:10.7326/0003-4819-115-3-178 · Cited by 456
Digestion of Chromatin in Apoptotic Cell Microparticles Prevents Autoimmunity
Sisirak, V., Sally, B., D’Agati, V. D., Martinez‐Ortiz, W., Özçakar, Z. B., David, J., Rashidfarrokhi, A., Yeste, A., Panea, C., Chida, A. S., et al. (2016) · Cell · doi:10.1016/j.cell.2016.05.034 · Cited by 450
O-GlcNAc Modification Is an Endogenous Inhibitor of the Proteasome
Zhang, F., Su, K., Yang, X., Bowe, D. B., Paterson, A. J., & Kudlow, J. E. (2003) · Cell · doi:10.1016/s0092-8674(03)00974-7 · Cited by 432
Metabolic Regulation by Lysine Malonylation, Succinylation, and Glutarylation
Hirschey, M. D., & Zhao, Y. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.r114.046664 · Cited by 429
Mitochondrial Damage-Associated Molecular Patterns: From Inflammatory Signaling to Human Diseases
Grazioli, S., & Pugin, J. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.00832 · Cited by 429
Transancestral mapping and genetic load in systemic lupus erythematosus
Langefeld, C. D., Ainsworth, H. C., Graham, D. S. C., Kelly, J. A., Comeau, M. E., Marion, M. C., Howard, T. D., Ramos, P. S., Croker, J. A., Morris, D. L., et al. (2017) · Nature Communications · doi:10.1038/ncomms16021 · Cited by 425
Rod-Derived Cone Viability Factor Promotes Cone Survival by Stimulating Aerobic Glycolysis
Aït-Ali, N., Fridlich, R., Millet-Puel, G., Clérin, E., Delalande, F., Jaillard, C., Blond, F., Perrocheau, L., Reichman, S., Byrne, L. C., et al. (2015) · Cell · doi:10.1016/j.cell.2015.03.023 · Cited by 423
Increased proteasome activity in human embryonic stem cells is regulated by PSMD11
Vilchez, D., Boyer, L., Morantte, I., Lutz, M., Merkwirth, C., Joyce, D., Spencer, B., Page, L., Masliah, E., Berggren, W. T., et al. (2012) · Nature · doi:10.1038/nature11468 · Cited by 388
TLR recognition of self nucleic acids hampers glucocorticoid activity in lupus
Guiducci, C., Gong, M., Xu, Z., Gill, M. A., Chaussabel, D., Meeker, T., Chan, J. H., Wright, T. B., Punaro, M., Bolland, S. M., et al. (2010) · Nature · doi:10.1038/nature09102 · Cited by 382
Self-citationPatterns of gene expression in atrophying skeletal muscles: response to food deprivation
Jagoe, R. T., Lecker, S. H., Gomes, M., & Goldberg, A. L. (2002) · The FASEB Journal · doi:10.1096/fj.02-0312com · Cited by 344
Brehm, A., Liu, Y., Sheikh, A., Marrero, B., Omoyinmi, E., Zhou, Q., Montealegre, G., Biancotto, A., Reinhardt, A., de Jesus, A. A., et al. (2015) · Journal of Clinical Investigation · doi:10.1172/jci81260 · Cited by 343
Self-citationVallin, H., Perers, A., Alm, G. V., & Rönnblom, L. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.163.11.6306 · Cited by 300
A function for lipoxygenase in programmed organelle degradation
van Leyen, K., Duvoisin, R. M., Engelhardt, H., & Wiedmann, M. (1998) · Nature · doi:10.1038/26500 · Cited by 298
Quantitative Analysis of Human Red Blood Cell Proteome
Bryk, A. H., & Wiśniewski, J. R. (2017) · Journal of Proteome Research · doi:10.1021/acs.jproteome.7b00025 · Cited by 290
Vallin, H., Perers, A., ALM, G. V., & Rönnblom, L. (1999) · PubMed · Cited by 284
Cell-Free DNA as a Biomarker in Autoimmune Rheumatic Diseases
Duvvuri, B., & Lood, C. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.00502 · Cited by 282
From the Cradle to the Grave: The Role of Macrophages in Erythropoiesis and Erythrophagocytosis
Klei, T. R. L., Meinderts, S. M., van den Berg, T. K., & van Bruggen, R. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.00073 · Cited by 279
Caielli, S., Veiga, D. T., Balasubramanian, P., Athale, S., Domic, B., Murat, E., Banchereau, R., Xu, Z., Chandra, M., Chung, C.-H., et al. (2019) · Nature Medicine · doi:10.1038/s41591-018-0254-9 · Cited by 263
Self-citationLokireddy, S., Kukushkin, N. V., & Goldberg, A. L. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1522332112 · Cited by 228
Immunometabolism in systemic lupus erythematosus
Morel, L. M. (2017) · Nature Reviews Rheumatology · doi:10.1038/nrrheum.2017.43 · Cited by 219
Chapple, S. J., Siow, R. C. M., & Mann, G. E. (2012) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2012.04.021 · Cited by 218
Dalakas, M. C., Semino‐Mora, C., & Leon‐Monzon, M. (2001) · Laboratory Investigation · doi:10.1038/labinvest.3780367 · Cited by 211
Soni, C., Perez, O. A., Voss, W. N., Pucella, J. N., Serpas, L., Mehl, J., Ching, K. L., Goike, J., Georgiou, G., Ippolito, G. C., et al. (2020) · Immunity · doi:10.1016/j.immuni.2020.04.015 · Cited by 210
Intermediates of Metabolism: From Bystanders to Signalling Molecules
Haas, R., Cucchi, D., Smith, J., Pucino, V., Macdougall, C. E., & Mauro, C. (2016) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2016.02.003 · Cited by 199
Extrinsic Phagocyte-Dependent STING Signaling Dictates the Immunogenicity of Dying Cells
Ahn, J., Xia, T., Rabasa, A., Betancourt, D. M., & Barber, G. N. (2018) · Cancer Cell · doi:10.1016/j.ccell.2018.03.027 · Cited by 194
Mitochondrial DNA replication in mammalian cells: overview of the pathway
Falkenberg, M. (2018) · Essays in Biochemistry · doi:10.1042/ebc20170100 · Cited by 186
New insights into iron regulation and erythropoiesis
Kim, A., & Nemeth, E. (2015) · Current Opinion in Hematology · doi:10.1097/moh.0000000000000132 · Cited by 180
UBE2O remodels the proteome during terminal erythroid differentiation
Nguyen, A. T., Prado, M. A., Schmidt, P. J., Sendamarai, A. K., Wilson‐Grady, J., Min, M., Campagna, D. R., Tian, G., Shi, Y., Dederer, V., et al. (2017) · Science · doi:10.1126/science.aan0218 · Cited by 171
Means, R. T., & Krantz, S. B. (1993) · Journal of Clinical Investigation · doi:10.1172/jci116216 · Cited by 144
Malic Enzyme Couples Mitochondria with Aerobic Glycolysis in Osteoblasts
Lee, W., Ji, X., Nissim, I., & Long, F. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108108 · Cited by 143
Ldb1 complexes: the new master regulators of erythroid gene transcription
Love, P. E., Warzecha, C. C., & Li, L. (2013) · Trends in Genetics · doi:10.1016/j.tig.2013.10.001 · Cited by 140
Ubiquitin-Dependent Degradation of Mitochondrial Proteins Regulates Energy Metabolism
Lavie, J., Belvalet, H. D., Sonon, S., Ion, A. M., Dumon, E., Melser, S., Lacombe, D., Dupuy, J., Lalou, C., & Bénard, G. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.05.013 · Cited by 136
Monogenic lupus: Dissecting heterogeneity
Omarjee, O., Picard, C., Frachette, C., Moreews, M., Rieux‐Laucat, F., Soulas-Sprauel, P., Viel, S., Lega, J., Bader‐Meunier, B., Walzer, T., et al. (2019) · Autoimmunity Reviews · doi:10.1016/j.autrev.2019.102361 · Cited by 135
van den Akker, E., Satchwell, T. J., Pellegrin, S., Daniels, G. L., & Toye, A. M. (2010) · Haematologica · doi:10.3324/haematol.2009.019828 · Cited by 133
Regulation of Proteasome Activity by (Post-)transcriptional Mechanisms
Kors, S., Geijtenbeek, K. W., Reits, E. A., & Schipper-Krom, S. (2019) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2019.00048 · Cited by 111
Autophagy facilitates organelle clearance during differentiation of human erythroblasts
Betin, V. M. S., Singleton, B. K., Parsons, S. F., Anstee, D. J., & Lane, J. D. (2013) · Autophagy · doi:10.4161/auto.24172 · Cited by 109
Understanding Human Autoimmunity and Autoinflammation Through Transcriptomics
Banchereau, R., Cepika, A., Banchereau, J., & Pascual, V. (2017) · Annual Review of Immunology · doi:10.1146/annurev-immunol-051116-052225 · Cited by 98
Self-citationOaks, Z., Winans, T., Huang, N., Bánki, K., & Perl, A. (2016) · Current Rheumatology Reports · doi:10.1007/s11926-016-0622-8 · Cited by 93
High IL-13 production by human neonatal T cells: neonate immune system regulator?
Ribeiro-do-Couto, L. M., Boeije, L. C. M., Kroon, J., Hooibrink, B., Breur-Vriesendorp, B. S., Aarden, L. A., & Boog, C. J. P. (2001) · European Journal of Immunology · doi:10.1002/1521-4141(200111)31:11 · Cited by 91
Neutralizing interferon alpha as a therapeutic approach to autoimmune diseases
Stewart, T. A. (2003) · Cytokine & Growth Factor Reviews · doi:10.1016/s1359-6101(02)00088-6 · Cited by 85
Troegeler, A., Lastrucci, C., Duval, C., Tanne, A. J., Cougoule, C., Maridonneau‐Parini, I., Neyrolles, O., & Lugo‐Villarino, G. (2014) · Immunology and Cell Biology · doi:10.1038/icb.2014.39 · Cited by 85
Zhong, Y., Li, X., Yu, D., Li, X., Li, Y., Long, Y., Yuan, Y., Ji, Z., Zhang, M., Wen, J., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.5386 · Cited by 85
Inhibition of 15‐lipoxygenase leads to delayed organelle degradation in the reticulocyte
Grüllich, C., Duvoisin, R. M., Wiedmann, M., & van Leyen, K. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02080-4 · Cited by 77
Ahlqvist, K. J., Leoncini, S., Pecorelli, A., Wortmann, S. B., Ahola, S., Forsström, S., Guerranti, R., Felice, C. D., Smeitink, J. A. M., Ciccoli, L., et al. (2015) · Nature Communications · doi:10.1038/ncomms7494 · Cited by 72
Lee, H.-T., Lin, C.-S., Lee, C.-S., Tsai, C.-Y., & Wei, Y.-H. (2013) · Clinical & Experimental Immunology · doi:10.1111/cei.12256 · Cited by 71
Human and murine erythropoiesis
An, X., Schulz, V., Mohandas, N., & Gallagher, P. G. (2015) · Current Opinion in Hematology · doi:10.1097/moh.0000000000000134 · Cited by 66
Valvona, C. J., & Fillmore, H. L. (2018) · Brain Sciences · doi:10.3390/brainsci8040056 · Cited by 56
Sbardella, D., Tundo, G. R., Campagnolo, L., Valacchi, G., Orlandi, A., Curatolo, P., Borsellino, G., D’Esposito, M., Ciaccio, C., Cesare, S. D., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-12069-0 · Cited by 55
Regulation of Acetylation Restores Proteolytic Function of Diseased Myocardium in Mouse and Human
Wang, D., Fang, C., Zong, C., Liem, D. A., Cadeiras, M., Scruggs, S. B., Yu, H., Kim, A. K., Yang, P., Deng, M. C.-H. K., et al. (2013) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m113.028332 · Cited by 52
Mitochondrial Regulation of the 26S Proteasome
Meul, T., Berschneider, K., Schmitt, S., Mayr, C. H., Mattner, L. F., Schiller, H. B., Yazgili, A. S., Wang, X., Lukas, C., Schlesser, C., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108059 · Cited by 51
Reticulocyte mitophagy: Monitoring mitochondrial clearance in a mammalian model
Zhang, J., & Ney, P. A. (2010) · Autophagy · doi:10.4161/auto.6.3.11245 · Cited by 44
Are lupus animal models useful for understanding and developing new therapies for human SLE?
Moore, E., & Putterman, C. (2020) · Journal of Autoimmunity · doi:10.1016/j.jaut.2020.102490 · Cited by 40
PSMD5 Inactivation Promotes 26S Proteasome Assembly during Colorectal Tumor Progression
Levin, A., Minis, A., Lalazar, G., Rodriguez, J., & Steller, H. (2018) · Cancer Research · doi:10.1158/0008-5472.can-17-2296 · Cited by 39
Cell-free DNA profiling in patients with lupus nephritis
Truszewska, A., Wirkowska, A., Gala, K., Truszewski, P., Krzemień‐Ojak, Ł., Perkowska‐Ptasińska, A., Mucha, K., Pączek, L., & Foroncewicz, B. (2020) · Lupus · doi:10.1177/0961203320957717 · Cited by 39
KALUNIAN, K. C. (2016) · Lupus · doi:10.1177/0961203316652495 · Cited by 36
Son, M. J., Jeong, B. R., Kwon, Y., & Cho, Y. S. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.07.023 · Cited by 34
New method to quantify erythrophagocytosis by autologous monocytes
Fendel, R., Mordmüller, B. G., Kreidenweiss, A., Rudat, A., Steur, C., Ambrosch, C. J., Kirstein, M., Berdel, W. E., Kremsner, P. G., & Brandts, C. (2007) · Cytometry Part A · doi:10.1002/cyto.a.20360 · Cited by 18
Hanaoka, H., Iida, H., Kiyokawa, T., Takakuwa, Y., & Kawahata, K. (2018) · Lupus · doi:10.1177/0961203318809182 · Cited by 14
Anti-IFNαR Mabs for the treatment of systemic lupus erythematosus
Goulden, B., & Isenberg, D. A. (2020) · Expert Opinion on Biological Therapy · doi:10.1080/14712598.2021.1841164 · Cited by 14
Hair, P. S., GOLDMAN, D. W., Li, J., Petri, M., Krishna, N. K., & Cunnion, K. M. (2020) · Lupus · doi:10.1177/0961203320936347 · Cited by 9
Flagged first, then by citations
1 of the 88 references couldn’t be matched to a known paper.
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Sorted by citations
Lactate metabolism in human health and disease
Li, X., Yang, Y., Zhang, B., Lin, X., Fu, X., An, Y., Zou, Y., Wang, J.-X., Wang, Z., & Yu, T. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01151-3 · Cited by 1,454
Mitochondrial control of inflammation
Marchi, S., Guilbaud, E., Tait, S. W. G., Yamazaki, T., & Galluzzi, L. (2023) · Nature Reviews Immunology · doi:10.1038/s41577-022-00760-x · Cited by 1,027
Mitochondrial DNA Release in Innate Immune Signaling
Newman, L. E., & Shadel, G. S. (2023) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-032620-104401 · Cited by 349
Role of the cGAS–STING pathway in systemic and organ-specific diseases
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Caielli, S., Wan, Z., & Pascual, V. (2023) · Annual Review of Immunology · doi:10.1146/annurev-immunol-101921-042422 · Cited by 229
Self-citation
Metadata
- Authors
- Caielli, S., Cardenas, J., de Jesus, A. A., Baisch, J., Walters, L., Blanck, J. P., Balasubramanian, P., Stagnar, C., Ohouo, M., Hong, S., Nassi, L., Stewart, K., Fuller, J., Gu, J., Banchereau, J. F., Wright, T., Goldbach-Mansky, R., & Pascual, V.
- Affiliations
- Weill Cornell Medicine (US)
- Texas Scottish Rite Hospital for Children (US)
- The Jackson Laboratory for Genomic Medicine (US)
- Corresponding author
- Caielli, Simone
- Pascual, Virginia
- ORCID
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2021-08
- Volume
- 184
- Issue
- 17
- Pages
- 4464-4479.e19
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC8380737
- OpenAlex
- W3189265697
- Cited by
- 228
- References
- 88
- Citations by year
- 2026: 36 · 2025: 53 · 2024: 60 · 2023: 40 · 2022: 33 · 2021: 6
- FWCI
- 26.18
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 384 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- The Mouseion at the JAXlibrary (Jackson Laboratory) (submittedVersion)
- Funders
- NIH (U19 AI082715)
- Sanofi
- AstraZeneca
- Weill Cornell Medical College
- National Institute of Allergy and Infectious Diseases
- Lupus Research Alliance
- National Institute of Arthritis and Musculoskeletal and Skin Diseases
- Topics
- Health Sciences › Medicine › Rheumatology › Systemic Lupus Erythematosus Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Immunology and Microbiology › Immunology › interferon and immune responses
- Keywords
- systemic lupus erythematosus, erythropoiesis, autophagy, hypoxia-inducible factor, ubiquitin-proteasome system, mitochondrial dysfunction, type I interferon, cGAS, macrophages, opsonic antibodies, interferon-stimulated genes, disease activity
- MeSH terms
- Endothelial PAS Domain-Containing Protein 1, Adolescent, Child, Child, Preschool, Erythroblasts, Erythrocytes, Erythropoiesis, Humans, Interferon Type I, Lupus Erythematosus, Systemic, Mitochondria, Myeloid Cells, Ubiquitin, Proteasome Endopeptidase Complex, Basic Helix-Loop-Helix Transcription Factors, Basic Helix-Loop-Helix Proteins, Mitophagy
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