Inhibition of serum- and glucocorticoid-inducible kinase 1 enhances TLR-mediated inflammation and promotes endotoxin-driven organ failure
Open accessAbstract
Serum- and glucocorticoid-regulated kinase (SGK)1 is associated with several important pathologic conditions and plays a modulatory role in adaptive immune responses. However, the involvement and functional role of SGK1 in innate immune responses remain entirely unknown. In this study, we establish that SGK1 is a novel and potent negative regulator of TLR-induced inflammation. Pharmacologic inhibition of SGK1 or suppression by small interfering RNA enhances proinflammatory cytokine (TNF, IL-12, and IL-6) production in TLR-engaged monocytes, a result confirmed in Cre-loxP-mediated SGK1-deficient cells. SGK1 inhibition or gene deficiency results in increased phosphorylation of IKK, IκBα, and NF-κB p65 in LPS-stimulated cells. Enhanced NF-κB p65 DNA binding also occurs upon SGK1 inhibition. The subsequent enhancement of proinflammatory cytokines is dependent on the phosphorylation of TGF-β-activated kinase 1 (TAK1), as confirmed by TAK1 gene silencing. In vivo relevance was established in a murine endotoxin model, in which we found that SGK1 inhibition aggravates the severity of multiple organ damage and enhances the inflammatory response by heightening both proinflammatory cytokine levels and neutrophil infiltration. These findings have identified an anti-inflammatory function of SGK1, elucidated the underlying intracellular mechanisms, and establish, for the first time, that SGK1 holds potential as a novel target for intervention in the control of inflammatory diseases.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
SGK1 acts as an effective negative regulator in TLR-induced inflammation; pharmacological inhibition or siRNA of SGK1 enhances production of pro-inflammatory cytokines TNF, IL-12, and IL-6 in monocytes bound to TLR.
“In contrast, SGK1 acts as an effective negative regulator in TLR-induced inflammation. Pharmacological inhibition or suppression using small interfering RNA (siRNA) of SGK1 enhances the production of pro-inflammatory cytokines (such as TNF, IL-12, and IL-6) in monocytes bound to TLR”
From Serum/glucocorticoid regulated kinase 1 (SGK1) in neurological disorders: pain or gain (2024) · cites this paper as Zhou et al., 2015
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Vagus nerve stimulation attenuates the systemic inflammatory response to endotoxin
Borovikova, L. V., Ivanova, S., Zhang, M., Yang, H., Botchkina, G. I., Watkins, L. R., Wang, H., Abumrad, N., Eaton, J. W., & Tracey, K. J. (2000) · Nature · doi:10.1038/35013070 · Cited by 4,211 · see citing works
Self-citationLutz, M. B., Kukutsch, N. A., Ogilvie, A. L. J., Rößner, S., Koch, F., Romani, N., & Schuler, G. (1999) · Journal of Immunological Methods · doi:10.1016/s0022-1759(98)00204-x · Cited by 2,972 · see citing works
Kawai, T., & Akira, S. (2007) · Seminars in Immunology · doi:10.1016/j.smim.2006.12.004 · Cited by 1,404 · see citing works
Sodium chloride drives autoimmune disease by the induction of pathogenic TH17 cells
Kleinewietfeld, M., Manzel, A., Titze, J., Kvakan, H., Yosef, N., Linker, R. A., Muller, D. N., & Hafler, D. A. (2013) · Nature · doi:10.1038/nature11868 · Cited by 1,394 · see citing works
Martin, M., Rehani, K., Jope, R. S., & Michalek, S. M. (2005) · Nature Immunology · doi:10.1038/ni1221 · Cited by 1,080 · see citing works
Induction of pathogenic TH17 cells by inducible salt-sensing kinase SGK1
Wu, C., Yosef, N., Thalhamer, T., Zhu, C., Xiao, S., Kishi, Y., Regev, A., & Kuchroo, V. K. (2013) · Nature · doi:10.1038/nature11984 · Cited by 1,022 · see citing works
Essential function for the kinase TAK1 in innate and adaptive immune responses
Sato, S., Sanjo, H., Takeda, K., Ninomiya‐Tsuji, J., Yamamoto, M., Kawai, T., Matsumoto, K., Takeuchi, O., & Akira, S. (2005) · Nature Immunology · doi:10.1038/ni1255 · Cited by 974 · see citing works
Sgk1-Dependent Stimulation of Cardiac Na+/H+Exchanger Nhe1 by Dexamethasone
Voelkl, J. G. J., Pasham, V., Ahmed, M. S. E., Walker, B., Szteyn, K., Kuhl, D., Metzler, B., Alesutan, I., & Lang, F. J. W. (2013) · Cellular Physiology and Biochemistry · doi:10.1159/000350120 · Cited by 859 · see citing works
Understanding the Inflammatory Cytokine Response in Pneumonia and Sepsis
Kellum, J. A. (2007) · Archives of Internal Medicine · doi:10.1001/archinte.167.15.1655 · Cited by 818 · see citing works
Guha, M., & Mackman, N. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203298200 · Cited by 799 · see citing works
Regulation of mTORC1 by amino acids
Bar-Peled, L., & Sabatini, D. M. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.03.003 · Cited by 773 · see citing works
Signaling Pathways Downstream of Pattern-Recognition Receptors and Their Cross Talk
Lee, M. S., & Kim, Y. (2007) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.76.060605.122847 · Cited by 756 · see citing works
Cytokines in Sepsis: Potent Immunoregulators and Potential Therapeutic Targets—An Updated View
Schulte, W., Bernhagen, J., & Bucala, R. (2013) · Mediators of Inflammation · doi:10.1155/2013/165974 · Cited by 745 · see citing works
TAK1, but not TAB1 or TAB2, plays an essential role in multiple signaling pathways in vivoPreprint
Shim, J., Xiao, C., Paschal, A. E., Bailey, S. T., Rao, P., Hayden, M. S., Lee, K., Bussey, C., Steckel, M., Tanaka, N., et al. (2005) · Genes & Development · doi:10.1101/gad.1360605 · Cited by 735 · see citing works
Kobayashi, T., & Cohen, P. (1999) · Biochemical Journal · doi:10.1042/bj3390319 · Cited by 614 · see citing works
Brown, J. R., Wang, H., Hajishengallis, G., & Martin, M. (2010) · Journal of Dental Research · doi:10.1177/0022034510381264 · Cited by 534 · see citing works
Self-citationPI3K-mediated negative feedback regulation of IL-12 production in DCs
Fukao, T., Tanabe, M., Terauchi, Y., Ota, T., Matsuda, S., Asano, T., Kadowaki, T., Takeuchi, T., & Koyasu, S. (2002) · Nature Immunology · doi:10.1038/ni825 · Cited by 529 · see citing works
Ninomiya‐Tsuji, J., Kajino, T., Ono, K., Ohtomo, T., Matsumoto, M., Shiina, M., Mihara, M., Tsuchiya, M., & Matsumoto, K. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m207453200 · Cited by 407 · see citing works
Bethin, K. E., Vogt, S. K., & Muglia, L. J. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.16.9317 · Cited by 382 · see citing works
Targeting of TAK1 in inflammatory disorders and cancer
Sakurai, H. (2012) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2012.06.007 · Cited by 377 · see citing works
Cell type-specific function of TAK1 in innate immune signaling
Alagbala, A. A., Wang, H. Y., & Wang, R. (2013) · Trends in Immunology · doi:10.1016/j.it.2013.03.007 · Cited by 372 · see citing works
Self-citationRegulation and Physiological Roles of Serum- and Glucocorticoid-Induced Protein Kinase Isoforms
Lang, F. J. W., & Cohen, P. (2001) · Science s STKE · doi:10.1126/stke.2001.108.re17 · Cited by 274 · see citing works
Luyendyk, J. P., Schabbauer, G., Tencati, M., Holscher, T. D., Pawliński, R., & Mackman, N. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.180.6.4218 · Cited by 272 · see citing works
Martin, M., Schifferle, R. E., Cuesta, N., Vogel, S. N., Katz, J., & Michalek, S. M. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.171.2.717 · Cited by 259 · see citing works
Zhang, W., Hao, W., Hagen, T. M., & Frei, B. B. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0700305104 · Cited by 258 · see citing works
Perlstein, R. S., Whitnall, M. H., Abrams, J. S., Mougey, E. H., & Neta, R. (1993) · Endocrinology · doi:10.1210/endo.132.3.8382602 · Cited by 257 · see citing works
PI3K-Akt Pathway Suppresses Coagulation and Inflammation in Endotoxemic Mice
Schabbauer, G., Tencati, M., Pedersen, B., Pawliński, R., & Mackman, N. (2004) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000143096.15099.ce · Cited by 244 · see citing works
Novel pathway for LPS-induced afferent vagus nerve activation: Possible role of nodose ganglion
Hosoi, T., Okuma, Y., Matsuda, T., & Nomura, Y. (2005) · Autonomic Neuroscience · doi:10.1016/j.autneu.2004.11.012 · Cited by 223 · see citing works
Toll-like receptors, signaling adapters and regulation of the pro-inflammatory response by PI3K
Troutman, T. D., Bazán, J. F., & Pasare, C. (2012) · Cell Cycle · doi:10.4161/cc.21572 · Cited by 222 · see citing works
Neutrophil migration during endotoxemia
Wagner, J. G., & Roth, R. A. (1999) · Journal of Leukocyte Biology · doi:10.1002/jlb.66.1.10 · Cited by 198 · see citing works
The AGC kinase SGK1 regulates TH1 and TH2 differentiation downstream of the mTORC2 complex
Heikamp, E., Patel, C. H., Collins, S., Waickman, A. T., Oh, M. H., Sun, I., Illei, P. B., Sharma, A., Náray‐Fejes‐Tóth, A., Fejes‐Tóth, G., et al. (2014) · Nature Immunology · doi:10.1038/ni.2867 · Cited by 194 · see citing works
Selective loss of gastrointestinal mast cells and impaired immunity in PI3K-deficient mice
Fukao, T., Yamada, T., Tanabe, M., Terauchi, Y., Ota, T., Takayama, T., Asano, T., Takeuchi, T., Kadowaki, T., Hata, J.-I., et al. (2002) · Nature Immunology · doi:10.1038/ni768 · Cited by 193 · see citing works
Serum and glucocorticoid‐regulated protein kinases: Variations on a theme
Tessier, M., & Woodgett, J. R. (2006) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20894 · Cited by 175 · see citing works
TAK1 regulates multiple protein kinase cascades activated by bacterial lipopolysaccharide
Lee, J., Arbibe, L., & Ulevitch, R. J. (2000) · Journal of Leukocyte Biology · doi:10.1189/jlb.68.6.909 · Cited by 173 · see citing works
Restraint of inflammatory signaling by interdependent strata of negative regulatory pathways
Murray, P. J., & Smale, S. T. (2012) · Nature Immunology · doi:10.1038/ni.2391 · Cited by 170 · see citing works
Fan, Y., Yu, Y., Shi, Y., Sun, W., Xie, M., Ge, N., Mao, R., Chang, A., Xu, G., Schneider, M. D., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.076976 · Cited by 168 · see citing works
TAK1 Negatively Regulates NF-κB and p38 MAP Kinase Activation in Gr-1+CD11b+ Neutrophils
Alagbala, A. A., Wang, Q., Cui, J., Zou, J., Xia, X., Wang, M., Tong, Y., Hui, W., Liu, D., Su, B., et al. (2012) · Immunity · doi:10.1016/j.immuni.2011.12.010 · Cited by 159 · see citing works
Self-citationWaldegger, S., Klingel, K., Barth, P., Sauter, M., Lanzendörfer, M., Kandolf, R., & Lang, F. J. W. (1999) · Gastroenterology · doi:10.1016/s0016-5085(99)70011-9 · Cited by 144 · see citing works
New Insights into the Regulation of Signalling by Toll-Like Receptors and Nod-Like Receptors
Coll, R. C., & O'Neill, L. A. J. (2010) · Journal of Innate Immunity · doi:10.1159/000315469 · Cited by 134 · see citing works
EMD638683, a Novel SGK Inhibitor with Antihypertensive Potency
Ackermann, T. F., Boini, K. M., Beier, N., Scholz, W., Fuchß, T., & Lang, F. (2011) · Cellular Physiology and Biochemistry · doi:10.1159/000331722 · Cited by 121 · see citing works
Wang, H., Brown, J. R., Gu, Z., Garcia, C. A., Liang, R., Alard, P., Beurel, E., Jope, R. S., Greenway, T., & Martin, M. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1002513 · Cited by 103 · see citing works
Self-citationYu, Y., Nagai, S., Wu, H., Neish, A. S., Koyasu, S., & Gewirtz, A. T. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.176.10.6194 · Cited by 87 · see citing works
Rehani, K., Scott, D. A., Renaud, D. E., Hamza, H., Williams, L., Wang, H., & Martin, M. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2007.12.003 · Cited by 83 · see citing works
Self-citationThe Role of JAK-3 in Regulating TLR-Mediated Inflammatory Cytokine Production in Innate Immune Cells
Wang, H., Brown, J. R., Gao, S., Liang, S., Jotwani, R., Zhou, H., Suttles, J., Scott, D. A., & Lamont, R. J. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1203084 · Cited by 76 · see citing works
Self-citationWrann, C. D., Tabriz, N., Barkhausen, T., Klos, A., van Griensven, M., Pape, H., Kendoff, D., Guo, R., Ward, P. A., Krettek, C., et al. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.178.9.5940 · Cited by 70 · see citing works
Courties, G., Seiffart, V., Présumey, J., Escriou, V., Scherman, D., Zwerina, J., Ruiz, G., Ziętara, N., Jabłońska, J., Weiß, S., et al. (2010) · Blood · doi:10.1182/blood-2010-02-269605 · Cited by 62 · see citing works
Zheng, H., Li, Q., Chen, R., Zhang, J., Ran, Y., He, X., Li, S., & Shu, H. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.412643 · Cited by 49 · see citing works
Regulation of Innate Immunity Signaling and its Connection with Human Diseases
Li, L. (2004) · Current Drug Targets - Inflammation & Allergy · doi:10.2174/1568010043483863 · Cited by 49 · see citing works
Gu, M., Ouyang, C., Lin, W., Zhang, T., Cao, X., Xia, Z., & Wang, X. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1302537 · Cited by 45 · see citing works
NF-κB Inhibits Sodium Transport via Down-regulation of SGK1 in Renal Collecting Duct Principal Cells
de Seigneux, S., Leroy, V., Ghzili, H., Rousselot, M., Nielsen, S., Rossier, B. C., Martin, P., & Féraille, E. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803812200 · Cited by 44 · see citing works
S6K1 Negatively Regulates TAK1 Activity in the Toll-Like Receptor Signaling Pathway
Kim, S. Y., Baik, K.-H., Baek, K., Chah, K.-H., Kim, K. A., Moon, G., Jung, E., Kim, S., Shim, J., Greenblatt, M. B., et al. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.01225-13 · Cited by 42 · see citing works
Burgon, J., Robertson, A. L., Sadiku, P., Wang, X., Hooper-Greenhill, E., Prince, L. R., Walker, P., Hoggett, E. E., Ward, J. R., Farrow, S. N., et al. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1300087 · Cited by 40 · see citing works
O'Neill, L. A. J. (2008) · Nature Immunology · doi:10.1038/ni0508-459 · Cited by 35 · see citing works
Blunt, M. D., & Ward, S. G. (2012) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2012.02.015 · Cited by 26 · see citing works
Lu, X., Li, M., Zhou, L.-J., Jiang, H., Wang, H., & Chen, J. (2014) · Nephrology · doi:10.1111/nep.12225 · Cited by 13 · see citing works
Self-citation
Flagged first, then by citations
Research works printed but not linked: 1
- [17]Lu X., Li M., Zhou L., Jiang H., Wang H., Chen J. (2014) Serum- and glucocorticoid-inducible kinase SGK1 as a deleterious mediator of IgA nephropathy. [E-pub ahead of print] Nephrology (Carlton) 19, 307–317 [DOI] [PubMed] [Google Scholar]
Cited by
Sorted by citations
Glucocorticoid-Induced Leucine Zipper: A Novel Anti-inflammatory Molecule
Bereshchenko, O., Migliorati, G., Bruscoli, S., & Riccardi, C. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.00308 · Cited by 86 · see citing works
Gu, Z., Lamont, G. J., Lamont, R. J., Uriarte, S. M., Wang, H., & Scott, D. A. (2016) · Innate Immunity · doi:10.1177/1753425916628618 · Cited by 85 · see citing works
Self-citationRen, J., Han, X., Lohner, H., Liang, R., Liang, S., & Wang, H. (2021) · The Journal of Immunology · doi:10.4049/jimmunol.2001455 · Cited by 50 · see citing works
Self-citationLou, Y., Hu, M., Wang, Q., Yuan, M., Wang, N., Fang, L., Li, L., Huang, S., Wang, L., Xu, X., et al. (2017) · International Journal of Biological Sciences · doi:10.7150/ijbs.18278 · Cited by 44 · see citing works
Zhang, D., Yu, W., Liu, J., Kong, L., Zhang, N., Song, Y., Li, X., Fan, Z., Lyu, Y., Li, N., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-36949-4 · Cited by 47 · see citing works
Self-citationRollins, D. A., Kharlyngdoh, J. B., Coppo, M., Tharmalingam, B., Mimouna, S., Guo, Z., Sacta, M. A., Pufall, M. A., Fisher, R. P., Hu, X., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-01569-2 · Cited by 44 · see citing works
He, J., Qi, D., Tang, X., Deng, W., Deng, X., Zhao, Y., & Wang, D. (2019) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-019-0154-0 · Cited by 37 · see citing works
Yang, D., Li, S., Duan, X., Ren, J., Liang, S., Yakoumatos, L., Kang, Y., Uriarte, S. M., Shang, J., Li, W., et al. (2019) · Molecular Immunology · doi:10.1016/j.molimm.2019.12.013 · Cited by 32 · see citing works
Self-citationLou, Y., Fu, Z., Tian, Y., Hu, M., Wang, Q., Zhou, Y., Wang, N., Zhang, Q., & Jin, F. (2023) · Reproductive Biology and Endocrinology · doi:10.1186/s12958-023-01102-9 · Cited by 29 · see citing works
Han, X., Ren, J., Lohner, H., Yakoumatos, L., Liang, R., & Wang, H. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102036 · Cited by 28 · see citing works
Self-citationShen, C., Chen, J. H., Lee, Y., Hassan, M. M., Kim, S. J., Choi, E. Y., Hong, S., Park, B., & Park, J. H. (2018) · The Journal of Immunology · doi:10.4049/jimmunol.1700954 · Cited by 24 · see citing works
Serum- and glucocorticoid-inducible kinases in microglia
Inoue, K., Sakuma, E., Morimoto, H., Asai, H., Koide, Y., Leng, T., Wada, I., Xiong, Z., & Ueki, T. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.07.094 · Cited by 23 · see citing works
Clauzure, M., Valdivieso, Á. G., Dugour, A. V., Mori, C., Massip-Copiz, M. M., Aguilar, M. Á., Sotomayor, V., Asensio, C. J. A., Figueroa, J. M., & Santa-Coloma, T. A. (2021) · Immunology · doi:10.1111/imm.13336 · Cited by 22 · see citing works
Meng, Q., Bai, M., Guo, M., Li, Z., Liu, W., Fan, X., Sun, R., Yang, X.-R., Ding-fen, Y., Shi, Y., et al. (2023) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2022.12.013 · Cited by 21 · see citing works
Sisti, F., Wang, S., Brandt, S. L., Glosson, N. L., Mayo, L. D., Son, Y. M., Sturgeon, S. M., Filgueiras, L. R., Jancar, S., Wong, H. R., et al. (2018) · Science Signaling · doi:10.1126/scisignal.aai9085 · Cited by 19 · see citing works
Oral mucosa: anti-inflammatory function, mechanisms, and applications
Chen, Y., Gao, B., Cai, W., Lai, J., Lai, K., & Wang, Y. (2025) · Journal of Materials Chemistry B · doi:10.1039/d4tb02845g · Cited by 17 · see citing works
Noor, S., Mohammad, T., Ashraf, G. M., Farhat, J., Bilgrami, A. L., Eapen, M. S., Sohal, S. S., Yadav, D. K., & Hassan, M. I. (2021) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2021.10.165 · Cited by 16 · see citing works
Zaal, A., Nota, B., Moore, K., Dieker, M. C., van Ham, S. M., & ten Brinke, A. (2017) · Journal of Leukocyte Biology · doi:10.1189/jlb.2ma0217-058r · Cited by 16 · see citing works
Chang, S., Chen, J., Chuang, Y., & Chen, B. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms22010166 · Cited by 14 · see citing works
Serum/glucocorticoid regulated kinase 1 (SGK1) in neurological disorders: pain or gain
Howard, P. G., Zou, P., Zhang, Y., Huang, F., Tesic, V., Wu, C. Y.-C., & Lee, R. H.-C. (2024) · Experimental Neurology · doi:10.1016/j.expneurol.2024.114973 · Cited by 13 · see citing works
Suthprasertporn, N., Mingchinda, N., Fukunaga, K., & Thangnipon, W. (2020) · Cytotechnology · doi:10.1007/s10616-019-00366-7 · Cited by 13 · see citing works
Gao, Y., Cao, F., Tian, X.-Y., Zhang, Q., Xu, C., Ji, B., Zhang, Y.-A., Du, L., Han, J., Li, L., et al. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.116447 · Cited by 12 · see citing works
RetractedLai, Y., Hu, L., Lu, Y., Hu, X., Song, X., Yang, J., Li, H., Chen, K., Li, H., & Wang, D. (2021) · Allergy Asthma and Immunology Research · doi:10.4168/aair.2021.13.5.776 · Cited by 10 · see citing works
Shu, H.-P., Wang, Y., Zhang, H., Dong, Q., Sun, L., Tu, Y.-C., Liao, Q., Li, F., & Yao, L. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1169054 · Cited by 9 · see citing works
Modulation of microglial activity by salt load and SGK1
Inoue, K., Morimoto, H., & Ueki, T. (2020) · NeuroReport · doi:10.1097/wnr.0000000000001449 · Cited by 8 · see citing works
Wang, H., GRAVES, M. W., Zhou, H., Gu, Z., Lamont, R. J., & Scott, D. A. (2015) · Inflammation Research · doi:10.1007/s00011-015-0891-0 · Cited by 7 · see citing works
Self-citationZhao, H., Yang, J., Wang, M., Zhang, H., Zhan, Y., Cao, Z., Gu, Z., & Wang, Y. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.117019 · Cited by 6 · see citing works
AGC kinase inhibitors regulate STING signaling through SGK-dependent and SGK-independent mechanisms
Cabrera, J. C., Dang, H., Graves, A. C., Zhang, Z., Torres-Castillo, J. L., Li, K., King, Z. T., Liu, P., Aubé, J., Bear, J. E., et al. (2023) · Cell chemical biology · doi:10.1016/j.chembiol.2023.10.008 · Cited by 5 · see citing works
Al-Hajj, S., Lemoine, R., Chadet, S., Goumard, A., Legay, L., Roxburgh, E., Héraud, A., Deluce, N. K.-N., Lamendour, L., Burlaud‐Gaillard, J., et al. (2022) · Cellular Immunology · doi:10.1016/j.cellimm.2022.104658 · Cited by 4 · see citing works
Sun, C., Zhang, L., Gao, C., Zhang, H., Yu, R., & Kang, C. (2020) · New Journal of Chemistry · doi:10.1039/d0nj02249g · Cited by 4 · see citing works
Sangphech, N., & Palaga, T. (2021) · International Immunopharmacology · doi:10.1016/j.intimp.2021.108312 · Cited by 3 · see citing works
Gao, S., Wang, D., Kong, G., Li, S., Wang, W., Wang, H., & Zhou, F. (2017) · Oncology Letters · doi:10.3892/ol.2017.5927 · Cited by 3 · see citing works
Self-citationŠíma, M., Líbalová, H., Závodná, T., Vrbová, K., Kléma, J., & Rössner, P. (2024) · Environmental Toxicology and Pharmacology · doi:10.1016/j.etap.2024.104469 · Cited by 2 · see citing works
Голюченко, О. А., & Стефанович, О. С. (2022) · Рецепт · doi:10.34883/pi.2022.25.3.006 · Cited by 1 · see citing works
AGC Kinase Inhibitors Regulate STING Signaling Through SGK-Dependent and SGK-Independent MechanismsPreprint
Cabrera, J. C., Dang, H., Zhang, Z., Torres-Castillo, J. L., Li, K., Liu, P., Aubé, J., Damania, B., Hagan, R. S., & Baldwin, A. S. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.07.21.500994
AGC Kinase Inhibitors Regulate STING Signaling Through SGK-Dependent and SGK-Independent MechanismsPreprint
Cabrera, J. C., Dang, H., Zhang, Z., Torres-Castillo, J. L., Li, K., Liu, P., Aubé, J., Damania, B., Hagan, R. S., & Baldwin, A. S. (2022) · SSRN Electronic Journal · doi:10.2139/ssrn.4190671
Lou, Y., Fu, Z., Tian, Y., Hu, M., Wang, Q., Zhou, Y., Wang, N., Zhang, Q., & Jin, F. (2024) · Figshare · doi:10.6084/m9.figshare.26591516
Lou, Y., Fu, Z., Tian, Y., Hu, M., Wang, Q., Zhou, Y., Wang, N., Zhang, Q., & Jin, F. (2024) · Figshare · doi:10.6084/m9.figshare.26591513
Grad, M., Volkov, H., & Shomron, N. (2026) · Journal of Molecular Neuroscience · doi:10.1007/s12031-026-02597-8
- Authors
- Zhou, H., Gao, S., Duan, X., Liang, S., Scott, D. A., Lamont, R. J., & Wang, H.
- Affiliations
- University of Louisville (US)
- Venue
- The FASEB Journal
- Publisher
- Wiley
- Published
- 2015-09
- Volume
- 29
- Issue
- 9
- Pages
- 3737-3749
- ISSN
- 0892-6638 (ISSN-L)
- 1530-6860
- PMC
- PMC4550376
- OpenAlex
- W1894200683
- Cited by
- 40
- References
- 55
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 6 · 2023: 5 · 2022: 5 · 2021: 5 · 2020: 4 · 2019: 4 · 2018: 2 · 2017: 4 · 2016: 2 · 2015: 1
- FWCI
- 1.48
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- The FASEB Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of Dental and Craniofacial Research (R01DE017680, DE017680, R01DE017921, R21DE023633, DE 011111, R37DE011111, DE 017921, DE023633, R01DE011111)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Life Sciences › Immunology and Microbiology › Immunology › Inflammation biomarkers and pathways
- Keywords
- SGK1, Toll-like receptor signaling, innate immunity, inflammation, NF-κB signaling, TAK1, inflammatory cytokines, endotoxin, multiple organ failure, monocytes, neutrophil infiltration, anti-inflammatory targets
- MeSH terms
- MAP Kinase Kinase Kinase 7, Serum-Glucocorticoid Regulated Kinases, Animals, Female, Humans, Inflammation, Lipopolysaccharides, Male, Mice, Transgenic, Multiple Organ Failure, Cytokines, Protein Serine-Threonine Kinases, Immediate-Early Proteins, MAP Kinase Kinase Kinases, RNA, Small Interfering, Toll-Like Receptors, Mice, I-kappa B Kinase, Transcription Factor RelA
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
