The RSK family of kinases: emerging roles in cellular signalling

AKT/PKB signaling: navigating downstream

Manning, B. D., & Cantley, L. C. (2007) · Cell · doi:10.1016/j.cell.2007.06.009 · Cited by 6,115

Targeting the Raf-MEK-ERK mitogen-activated protein kinase cascade for the treatment of cancer

Roberts, P. J., & Der, C. J. (2007) · Oncogene · doi:10.1038/sj.onc.1210422 · Cited by 2,788

ERK and p38 MAPK-Activated Protein Kinases: a Family of Protein Kinases with Diverse Biological Functions

Roux, P. P., & Blenis, J. (2004) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.68.2.320-344.2004 · Cited by 2,540

The selectivity of protein kinase inhibitors: a further update

Bain, J., Plater, L., Elliott, M., Shpiro, N., Hastie, C. J., McLauchlan, H., Klevernic, I. V., Arthur, J. S. C., Alessi, D. R., & Cohen, P. (2007) · Biochemical Journal · doi:10.1042/bj20070797 · Cited by 2,522

Glycogen synthase kinase-3β regulates cyclin D1 proteolysis and subcellular localization

Diehl, J. A., Cheng, M., Roussel, M. F., & Sherr, C. J. (1998) · Genes & Development · doi:10.1101/gad.12.22.3499 · Cited by 2,130

Cell Survival Promoted by the Ras-MAPK Signaling Pathway by Transcription-Dependent and -Independent Mechanisms

Bonni, A., Brunet, A., West, A. E., Datta, S. R., Takasu, M. A., & Greenberg, M. E. (1999) · Science · doi:10.1126/science.286.5443.1358 · Cited by 1,908

The renaissance of GSK3

Cohen, P., & Frame, S. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35096075 · Cited by 1,493

Multiple Ras-dependent phosphorylation pathways regulate Myc protein stabilityPreprint

Sears, R. C., Nuckolls, F., Haura, E. B., Taya, Y., Tamai, K., & Nevins, J. R. (2000) · Genes & Development · doi:10.1101/gad.836800 · Cited by 1,411

Gene silencing in mammals by small interfering RNAs

McManus, M. T., & Sharp, P. A. (2002) · Nature Reviews Genetics · doi:10.1038/nrg908 · Cited by 1,400

Target of rapamycin (TOR): an integrator of nutrient and growth factor signals and coordinator of cell growth and cell cycle progression

Fingar, D. C., & Blenis, J. (2004) · Oncogene · doi:10.1038/sj.onc.1207542 · Cited by 1,264

Regulation of the insulin–Akt signaling pathway and glycolysis during dehydration stress in the African clawed frog Xenopus laevis

Wu, C., Tessier, S. N., & Storey, K. B. (2017) · Biochemistry and Cell Biology · doi:10.1139/bcb-2017-0117 · Cited by 18

Genome-wide classification, evolutionary analysis and gene expression patterns of the kinome in Gossypium

Yan, J., Li, G., Guo, X., Li, Y., & Cao, X. (2018) · PLoS ONE · doi:10.1371/journal.pone.0197392 · Cited by 18

Substituted pteridinones as p90 ribosomal S6 protein kinase (RSK) inhibitors: A structure-activity study

Casalvieri, K. A., Matheson, C. J., Backos, D. S., & Reigan, P. (2020) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2019.115303 · Cited by 18

ERK1/2 pathway is involved in renal gluconeogenesis inhibition under conditions of lowered NADPH oxidase activity

Winiarska, K., Jarzyna, R., Dzik, J. M., Jagielski, A. K., Grabowski, M., Nowosielska, A., Focht, D., & Sierakowski, B. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.12.024 · Cited by 18

RSK2 protects mice against TNF-induced bone loss

Böhm, C., Derer, A., Axmann, R., Hillienhoff, U., Zaiss, M. M., Luther, J., Zech, C., Stock, M., Scholtysek, C., Engelke, K., et al. (2012) · Journal of Cell Science · doi:10.1242/jcs.096008 · Cited by 18

Computational and Biochemical Discovery of RSK2 as a Novel Target for Epigallocatechin Gallate (EGCG)

Chen, H., Yao, K., Chang, X., Shim, J., Kim, H.-G., Malakhova, M. L., Kim, D. J., Bode, A. M., & Dong, Z. (2015) · PLoS ONE · doi:10.1371/journal.pone.0130049 · Cited by 18

The historical Coffin–Lowry syndrome family revisited: Identification of two novel mutations of RPS6KA3 in three male patients

Nishimoto, H. K., Ha, K., Jones, J. R., Dwivedi, A., Cho, H., Layman, L. C., & Kim, H. (2014) · American Journal of Medical Genetics Part A · doi:10.1002/ajmg.a.36488 · Cited by 17

Interfering with S100B–effector protein interactions for cancer therapy

Wu, K., Wang, W., Wang, H., Leung, C., & Ma, D. (2020) · Drug Discovery Today · doi:10.1016/j.drudis.2020.07.010 · Cited by 17

Targeting phosphodiesterase 4 as a therapeutic strategy for cognitive improvement

Wei, X., Yu, G., Shen, H., Luo, Y., Shang, T., Shen, R., Xi, M., & Sun, H. (2022) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2022.106278 · Cited by 17

Quantitative proteomics and phosphoproteomics of PP2A-PPP2R5D variants reveal deregulation of RPS6 phosphorylation via converging signaling cascades

Smolen, K. A., Papke, C. M., Swingle, M. R., Musiyenko, A., Li, C., Salter, E. A., Camp, A. D., Honkanen, R. E., & Kettenbach, A. N. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105154 · Cited by 17

Serine residue 115 of MAPK-activated protein kinase MK5 is crucial for its PKA-regulated nuclear export and biological function

Kostenko, S., Shiryaev, A., Gerits, N., Dumitriu, G., Klenow, H. B., Johannessen, M., & Moens, U. L. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0496-2 · Cited by 17

Genome-wide pathway analysis of breast cancer

Lee, Y. H., Kim, J., & Song, G. G. (2014) · Tumor Biology · doi:10.1007/s13277-014-2027-5 · Cited by 17

Dysfunctional ryanodine receptor and cardiac hypertrophy: role of signaling molecules

Yamaguchi, N., Chakraborty, A., Pasek, D. A., Molkentin, J. D., & Meissner, G. (2011) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00719.2010 · Cited by 17

The Ser/Thr kinase p90RSK promotes kidney fibrosis by modulating fibroblast–epithelial crosstalk

Lin, L., Shi, C., Sun, Z., Le, N., Abe, J., & Hu, K. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.007904 · Cited by 19

ErbB3 is a critical regulator of cytoskeletal dynamics in brain microvascular endothelial cells: Implications for vascular remodeling and blood brain barrier modulation

Wu, L., Islam, M. R., Lee, J. C. L., Takase, H., Guo, S., Andrews, A. M., Buzhdygan, T. P., Mathew, J., Li, W., Arai, K., et al. (2021) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1177/0271678x20984976 · Cited by 18

RSK Isoforms in Acute Myeloid Leukemia

Youn, M., Gomez, J. O., Mark, K., & Sakamoto, K. M. (2021) · Biomedicines · doi:10.3390/biomedicines9070726 · Cited by 17

A multiscale cell‐based model of tumor growth for chemotherapy assessment and tumor‐targeted therapy through a 3D computational approach

Nivlouei, S. J., Soltani, M., Shirani, E., Salimpour, M. R., Travasso, R. D. M., & Carvalho, J. (2022) · Cell Proliferation · doi:10.1111/cpr.13187 · Cited by 17

A combination of SILAC and nucleotide acyl phosphate labelling reveals unexpected targets of the Rsk inhibitor BI-D1870

Edgar, A. J., Trost, M., Watts, C. K. W., & Zaru, R. (2013) · Bioscience Reports · doi:10.1042/bsr20130094 · Cited by 18

Differential mTOR and ERK pathway utilization by effector CD4 T cells suggests combinatorial drug therapy of arthritis

Lin, J. T., Stein, E. A., Wong, M. T., Kalpathy, K. J., Su, L., Utz, P. J., Robinson, W. H., & Fathman, C. G. (2011) · Clinical Immunology · doi:10.1016/j.clim.2011.09.008 · Cited by 17

In Vitro and Ex vivo Analysis of Hyaluronan Supplementation of Integra ® Dermal Template on Human Dermal Fibroblasts and Keratinocytes

Hodgkinson, T., & Bayat, A. (2015) · Journal of Applied Biomaterials & Functional Materials · doi:10.5301/jabfm.5000259 · Cited by 17

The p90 ribosomal S6 kinase 2 specifically affects mitotic progression by regulating the basal level, distribution and stability of mitotic spindles

Park, Y. Y., Nam, H.-J., Do, M., & Lee, J. (2016) · Experimental & Molecular Medicine · doi:10.1038/emm.2016.61 · Cited by 17

The p90rsk-mediated signaling of ethanol-induced cell proliferation in HepG2 cell line

Kim, H. S., Kim, S.-J., Bae, J., Wang, Y., Park, S. Y., Chi, Y. M., Je, H. D., & Sohn, U. D. (2016) · Korean Journal of Physiology and Pharmacology · doi:10.4196/kjpp.2016.20.6.595 · Cited by 17

MYSM1 induces apoptosis and sensitizes TNBC cells to cisplatin via RSK3–phospho-BAD pathway

Guan, X., Meng, X., Zhu, K., Kai, J., Liu, Y., Ma, Q., Tong, Y., Zheng, H., Xie, S., Ma, X., et al. (2022) · Cell Death Discovery · doi:10.1038/s41420-022-00881-1 · Cited by 17

Anti-Cancer Effects of an Optimised Combination of Ginsenoside Rg3 Epimers on Triple Negative Breast Cancer Models

Nakhjavani, M., Smith, E., Palethorpe, H. M., Tomita, Y., Yeo, K. K. L., Price, T. J., Townsend, A. R., & Hardingham, J. E. (2021) · Pharmaceuticals · doi:10.3390/ph14070633 · Cited by 16

Peritoneal and hematogenous metastases of ovarian cancer cells are both controlled by the p90RSK through a self-reinforcing cell autonomous mechanism

Torchiaro, E., Lorenzato, A., Olivero, M., Valdembri, D., Gagliardi, P. A., Gai, M., Erriquez, J., Serini, G., & Renzo, M. F. D. (2015) · Oncotarget · doi:10.18632/oncotarget.6412 · Cited by 16

Computer simulations of the signalling network in FLT3 +-acute myeloid leukaemia – indications for an optimal dosage of inhibitors against FLT3 and CDK6

Buetti‐Dinh, A., & Friedman, R. (2018) · BMC Bioinformatics · doi:10.1186/s12859-018-2145-y · Cited by 16

Inhibition of p90 ribosomal S6 kinase potentiates cisplatin activity in A549 human lung adenocarcinoma cells

Abdulrahman, N., Siveen, K. S., Joseph, J. M., Osman, A., Yalcin, H. C., Hasan, A., Shahab Uddin, M. S., & Mraiche, F. (2020) · Journal of Pharmacy and Pharmacology · doi:10.1111/jphp.13335 · Cited by 16

Krüppel‐Like Factor 15/Interleukin 11 Axis‐Mediated Adventitial Remodeling Depends on Extracellular Signal‐Regulated Kinases 1 and 2 Activation in Angiotensin II–Induced Hypertension

Guo, Y., Lu, Y., Lu, X., He, S., Li, S., Shao, S., Zhou, H., Wang, R. L., Li, X., & Gao, P. (2021) · Journal of the American Heart Association · doi:10.1161/jaha.120.020554 · Cited by 16

The promise and challenges of targeting RSK for the treatment of cancer

Stratford, A. L., & Dunn, S. E. (2010) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2011.537656 · Cited by 16

Integrins Promote Cytokinesis through the RSK Signaling Axis

Mathew‐Steiner, S. S., Nieves, B., Sequeira, S. J., Sambandamoorthy, S., Pumiglia, K. M., Larsen, M., & LaFlamme, S. E. (2013) · Journal of Cell Science · doi:10.1242/jcs.133280 · Cited by 17

RSK2 is a kinetochore-associated protein that participates in the spindle assembly checkpoint

Vigneron, S., Brioudes, E., Burgess, A., Labbé, J., Lorca, T., & Castro, A. (2010) · Oncogene · doi:10.1038/onc.2010.105 · Cited by 16

Fluoxetine induces alkalinization of astroglial cytosol through stimulation of sodium-hydrogen exchanger 1: dissection of intracellular signaling pathways

Ren, J., Song, D., Bai, Q., Verkhratsky, A., & Peng, L. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00061 · Cited by 16

Identification of quercitrin as an inhibitor of the p90 S6 ribosomal kinase (RSK): structure of its complex with the N-terminal domain of RSK2 at 1.8 Å resolution

Derewenda, U., Artamonov, M. V., Szukalska, G., Utepbergenov, D., Olekhnovich, N., Parikh, H. I., Kellogg, G. E., Somlyo, A. V., & Derewenda, Z. S. (2013) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444912045520 · Cited by 16

Changes in growth-related kinases in head, neck and limb muscles with age

Rahnert, J. A., Luo, Q., Balog, E. M., Sokoloff, A. J., & Burkholder, T. J. (2010) · Experimental Gerontology · doi:10.1016/j.exger.2010.11.004 · Cited by 19

p90 ribosomal S6 kinase 3 contributes to cardiac insufficiency in α-tropomyosin Glu180Gly transgenic mice

Passariello, C. L., Gayanilo, M., Kritzer, M. D., Thakur, H. S., Cozacov, Z., Rusconi, F., Wieczorek, D. F., Sanders, M., Li, J., & Kapiloff, M. S. (2013) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00237.2013 · Cited by 16

Predisposition to apoptosis in keratin 8-null liver is related to inactivation of NF-κB and SAPKs but not decreased c-Flip

Lee, J., Jang, K., Kim, H., Lim, Y., Kim, S.-J., Yoon, H., Chung, I. K., Roth, J., & Ku, N. (2013) · Biology Open · doi:10.1242/bio.20134606 · Cited by 16

The RSK Inhibitor BIX02565 Limits Cardiac Ischemia/Reperfusion Injury

Shi, X., O’Neill, M. M., MacDonnell, S. M., Brookes, P. S., Chen, Y., & Berk, B. C. (2015) · Journal of Cardiovascular Pharmacology and Therapeutics · doi:10.1177/1074248415591700 · Cited by 16

Oncogenic Ras Pushes (and Pulls) Cell Cycle Progression Through ERK Activation

Campbell, P. M. (2014) · Methods in molecular biology · doi:10.1007/978-1-4939-0888-2_9 · Cited by 16

Phosphorylated S6 as an immunohistochemical biomarker of vulvar intraepithelial neoplasia

Pinto, Á. P., Degen, M., Barron, P., Crum, C. P., & Rheinwald, J. G. (2013) · Modern Pathology · doi:10.1038/modpathol.2013.85 · Cited by 16

Plakophilin 3 facilitates G1/S phase transition and enhances proliferation by capturing RB protein in the cytoplasm and promoting EGFR signaling

Müller, L., Keil, R., & Hatzfeld, M. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112031 · Cited by 15

pTDP-43 levels correlate with cell type–specific molecular alterations in the prefrontal cortex of C9orf72 ALS/FTD patients

Wang, H. V., Xiang, J., Yuan, C., Veire, A. M., Gendron, T. F., Murray, M. E., Tansey, M. G., Hu, J., Gearing, M., Glass, J. D., et al. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2419818122 · Cited by 15

YB-1 drives preneoplastic progression: Insight into opportunities for cancer prevention

Davies, A., & Dunn, S. E. (2011) · Oncotarget · doi:10.18632/oncotarget.276 · Cited by 15

Inhibition of p90RSK is critical to abolish Angiotensin II-induced rat aortic smooth muscle cell proliferation and migration

Huynh, D. T. N., Jin, Y., Myung, C., & Heo, K. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2019.12.053 · Cited by 15

The overview of Mitogen-activated extracellular signal-regulated kinase (MEK)-based dual inhibitor in the treatment of cancers

Wang, H., Chi, L., Yu, F., Dai, H., Si, X., Gao, C., Wang, Z., Liu, L., Zheng, J., Ke, Y., et al. (2022) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2022.116922 · Cited by 15

Role of the phosphatidylinositol-3-kinase/Akt/target of rapamycin pathway during ambidensovirus infection of insect cells

Salasc, F., Mutuel, D., Debaisieux, S., Perrin, A., Dupressoir, T., Grenet, A.-S. G., & Ogliastro, M. (2015) · Journal of General Virology · doi:10.1099/jgv.0.000327 · Cited by 15

Specific RSK kinase inhibition by dibenzyl trisulfide and implication for therapeutic treatment of cancer.

Lowe, H. I. C., Facey, C. O. B., Toyang, N. J., & Bryant, J. (2014) · PubMed · Cited by 15

Phospholipase C∈ Activates Nuclear Factor-κB Signaling by Causing Cytoplasmic Localization of Ribosomal S6 Kinase and Facilitating Its Phosphorylation of Inhibitor κB in Colon Epithelial Cells

Wakita, M., Edamatsu, H., Li, M., Emi, A., Kitazawa, S., & Kataoka, T. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.717561 · Cited by 15

Age-dependent regulation of antioxidant genes by p38α MAPK in the liver

Pérez, S., Rius‐Pérez, S., Tormos, A. M., Finamor, I., Nebreda, Á. R., Taléns‐Visconti, R., & Sastre, J. (2018) · Redox Biology · doi:10.1016/j.redox.2018.02.017 · Cited by 15

RSK1 SUMOylation is required for KSHV lytic replication

Liu, Z., Liu, C., Wang, X., Li, W., Zhou, J., Dong, P., Xiao, M. Z. X., Wang, C., Zhang, Y., Fu, J., et al. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1010123 · Cited by 14

PD-L1 expression is regulated by ATP-binding of the ERBB3 pseudokinase domain

Li, Y., Liu, Z., Zhao, Y., Yang, J., Xiao, T. S., Conlon, R. A., & Wang, Z. (2022) · Genes & Diseases · doi:10.1016/j.gendis.2022.11.003 · Cited by 14

Activation of the MEK–S6 Pathway in High-grade Ovarian Cancers

Ventura, A. P., Radhakrishnan, S. V., Green, A. F., Rajaram, S. K., Allen, A. N., O'Briant, K. C., Schummer, M., Karlan, B. Y., Urban, N. D., Tewari, M., et al. (2010) · Applied immunohistochemistry & molecular morphology · doi:10.1097/pai.0b013e3181e53e1c · Cited by 14

Assaying multiple biochemical variables from the same tissue sample

Leak, R. K., Castro, S. L., Jaumotte, J. D., Smith, A. D., & Zigmond, M. J. (2010) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2010.06.023 · Cited by 14

Ras-activated RSK1 phosphorylates EBP50 to regulate its nuclear localization and promote cell proliferation

Lim, H., & Jou, T. (2016) · Oncotarget · doi:10.18632/oncotarget.7184 · Cited by 14

PDK1 promotes the inflammatory progress of fibroblast-like synoviocytes by phosphorylating RSK2

Sun, C. C., Sun, Y., Jiang, D., Bao, G., Zhu, X., Xu, D., Wang, Y., & Cui, Z. (2016) · Cellular Immunology · doi:10.1016/j.cellimm.2016.10.007 · Cited by 14

Disturbed flow-induced FAK K152 SUMOylation initiates the formation of pro-inflammation positive feedback loop by inducing reactive oxygen species production in endothelial cells

Velatooru, L. R., Abe, R. J., Imanishi, M., Gi, Y. J., Ko, K. A., Heo, K., Fujiwara, K., Le, N.-T., & Kotla, S. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.09.023 · Cited by 14

A Co-Module Regulated by Therapeutic Drugs in a Molecular Subnetwork of Alzheimer’s Disease Identified on the Basis of Traditional Chinese Medicine and SAMP8 Mice

Cheng, X., Cui, X., Zheng, Y., Zhang, G., Li, P., Huang, H., Zhao, Y., Bo, X., Wang, S., Zhou, W., et al. (2015) · Current Alzheimer Research · doi:10.2174/1567205012666150710111858 · Cited by 14

ERK1/2 regulates hepatocyte Trib1 in response to mitochondrial dysfunction

Soubeyrand, S., Naing, T., Martinuk, A., & McPherson, R. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.10.001 · Cited by 16

C/EBPβ-LAP*/LAP Expression Is Mediated by RSK/eIF4B-Dependent Signalling and Boosted by Increased Protein Stability in Models of Monocytic Differentiation

Huber, R., Panterodt, T., Welz, B., Christmann, M., Friesenhagen, J., Westphal, A., Pietsch, D., & Brand, K. (2015) · PLoS ONE · doi:10.1371/journal.pone.0144338 · Cited by 14

The p90 ribosomal S6 kinase–UBR5 pathway controls Toll-like receptor signaling via miRNA-induced translational inhibition of tumor necrosis factor receptor–associated factor 3

Cho, J. H., Kim, S. A., Seo, Y., Park, S. G., Park, B. C., Kim, J., & Kim, S. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.785170 · Cited by 15

Na+/H+ Exchanger Isoform 1 Induced Cardiomyocyte Hypertrophy Involves Activation of p90 Ribosomal S6 Kinase

Jaballah, M. Y., Mohamed, I. A., Alemrayat, B., Al‐Sulaiti, F. K., Mlih, M., & Mraiche, F. (2015) · PLoS ONE · doi:10.1371/journal.pone.0122230 · Cited by 14

The Effects of Adiponectin and Leptin on Human Endothelial Cell Proliferation: A Live-Cell Study

Álvarez, G., Bartolomé, M. V., Miana, M., Jurado-López, R., Martín, R., Zuluaga, P., Martínez‐Martínez, E., Nieto, M. L., Alvarez-Sala, L. A., Millán, J., et al. (2012) · Journal of Vascular Research · doi:10.1159/000332332 · Cited by 14

P90 ribosomal S6 kinases: A bona fide target for novel targeted anticancer therapies?

Koutsougianni, F., Alexopoulou, D., Üvez, A., Lamprianidou, A., Sereti, E., Tsimplouli, C., Armutak, E. İ., & DIMAS, K. S. (2023) · Biochemical Pharmacology · doi:10.1016/j.bcp.2023.115488 · Cited by 13

Global profiling of protein kinase activities in cancer cells by mass spectrometry

Beltran, L., Casado, P., Rodríguez‐Prados, J., & Cutillas, P. R. (2012) · Journal of Proteomics · doi:10.1016/j.jprot.2012.09.029 · Cited by 13

mTORC2 Is Involved in the Induction of RSK Phosphorylation by Serum or Nutrient Starvation

Chou, P.-C., Rajput, S., Zhao, X., Patel, C., Albaciete, D., Oh, W. J., Queen, H., Patel, N., Su, B., Werlen, G., et al. (2020) · Cells · doi:10.3390/cells9071567 · Cited by 15

A Novel Protein–Protein Interaction between RSK3 and IκBα and a New Binding Inhibitor That Suppresses Breast Cancer Tumorigenesis

Yoon, H.-S., Choi, S. H., Park, J., Min, J.-Y., Hyon, J., Yang, Y., Jung, S., Kim, J., Kim, N. D., Lee, J. H., et al. (2021) · Cancers · doi:10.3390/cancers13122973 · Cited by 13

The SUMO E3 ligase activity of ORF45 determines KSHV lytic replication

Liu, Z., Wang, X., Liu, C., Deng, H., Li, W., Wang, X., Xu, X., Xiao, M. Z. X., Wang, C., Zhang, Y., et al. (2022) · PLoS Pathogens · doi:10.1371/journal.ppat.1010504 · Cited by 13

RSK4 promotes the macrophage recruitment and M2 polarization in esophageal squamous cell carcinoma

He, S., Lu, M., Zhang, L., & Wang, Z. (2023) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2023.166996 · Cited by 13

Initiation of DNA replication after fertilization is regulated by p90Rsk at pre-RC/pre-IC transition in starfish eggs

Tachibana, K., Mori, M., Matsuhira, T., Karino, T., Inagaki, T., Nagayama, A., Nishiyama, A., Hara, M., & Kishimoto, T. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1000587107 · Cited by 13

RSK-3 promotes cartilage regeneration via interacting with rpS6 in cartilage stem/progenitor cells

Zhang, S., Hamid, M. R., Wang, T., Liao, J., Wen, L., Zhou, Y., Wei, P., Zou, X., Chen, G., Chen, J., et al. (2020) · Theranostics · doi:10.7150/thno.44875 · Cited by 13

Cross-talk between protein kinase A and the MAPK-activated protein kinases RSK1 and MK5

Kostenko, S., Shiryaev, A., Dumitriu, G., Gerits, N., & Moens, U. L. (2010) · Journal of Receptors and Signal Transduction · doi:10.3109/10799893.2010.515593 · Cited by 13

The p90 Ribosomal S6 Kinase (RSK) Is a Mediator of Smooth Muscle Contractility

Artamonov, M. V., Momotani, K., Utepbergenov, D., Franke, A. S., Khromov, A. S., Derewenda, Z. S., & Somlyo, A. V. (2013) · PLoS ONE · doi:10.1371/journal.pone.0058703 · Cited by 13

Development of an ORF45-Derived Peptide To Inhibit the Sustained RSK Activation and Lytic Replication of Kaposi's Sarcoma-Associated Herpesvirus

Li, X., Huang, L., Xiao, Y., Yao, X., Long, X., Zhu, F., & Kuang, E. (2019) · Journal of Virology · doi:10.1128/jvi.02154-18 · Cited by 13

17 β -Estradiol inhibits vascular smooth muscle cell migration via up-regulation of striatin protein

Zheng, S., Chen, X., Hong, S., Long, L., Xu, Y., Simoncini, T., & Fu, X. (2015) · Gynecological Endocrinology · doi:10.3109/09513590.2015.1021325 · Cited by 12

Discovery, Optimization, and Structure–Activity Relationship Study of Novel and Potent RSK4 Inhibitors as Promising Agents for the Treatment of Esophageal Squamous Cell Carcinoma

Yuan, Y., Xu, J., Jiang, L., Yu, K., Ge, Y., Li, M., He, H., Niu, Q., Shi, X., Fan, L., et al. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c00969 · Cited by 12

The ORF45 Protein of Kaposi’s Sarcoma-Associated Herpesvirus and Its Critical Role in the Viral Life Cycle

Atyeo, N., & Papp, B. (2022) · Viruses · doi:10.3390/v14092010 · Cited by 12

CdGAP/ARHGAP31 is regulated by RSK phosphorylation and binding to 14-3-3β adaptor protein

Ouadda, A. B. D., He, Y., Calabrese, V., Ishii, H., Chidiac, R., Gratton, J., Roux, P. P., & Lamarche‐Vane, N. (2018) · Oncotarget · doi:10.18632/oncotarget.24126 · Cited by 12

Identifying requirements for RSK2 specific inhibitors

Wright, E. B., Fukuda, S., Li, M., Li, Y., O'Doherty, G. A., & Lannigan, D. A. (2021) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2021.1957862 · Cited by 12

Effect of siRNA pre-Exposure on Subsequent Response to siRNA Therapy

Aliabadi, H. M., Mahdipoor, P., Kucharski, C., Chan, N., & Uludağ, H. (2015) · Pharmaceutical Research · doi:10.1007/s11095-015-1741-z · Cited by 12

90‐kDa ribosomal S6 kinase 1 is inhibited by S‐glutathionylation of its active‐site cysteine residue during oxidative stress

Takata, T., Tsuchiya, Y., & Watanabe, Y. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.04.017 · Cited by 12

P2Y2 receptor inhibits EGF-induced MAPK pathway to stabilise keratinocyte hemidesmosomes.

Faure, E., Garrouste, F. L., Parat, F., Monferran, S., Leloup, L., Pommier, G. J., Kovacic, H., & Lehmann, M. (2012) · Journal of Cell Science · doi:10.1242/jcs.097600 · Cited by 12

Inflammation and Sleep

Zielinski, M. R., & Krueger, J. M. (2011) · Elsevier eBooks · doi:10.1016/b978-1-4377-1703-7.10048-9 · Cited by 12

Mechanism and cellular actions of the potent AMPK inhibitor BAY-3827

Bringas, C. F., Ahangar, M. S., Cuenco, J., Liu, H., Addinsall, A. B., Lindahl, M., Ovens, A. J., Febbraio, M. A., Foretz, M., Göransson, O., et al. (2025) · Science Advances · doi:10.1126/sciadv.adx2434 · Cited by 11

Cytoplasmic Protein Serine/Threonine Kinases

Thiriet, M. (2012) · Biomathematical and biomechanical modeling of the circulatory and ventilatory systems · doi:10.1007/978-1-4614-4370-4_5 · Cited by 11

The ribosomal S6 kinase 2 (RSK2)–SPRED2 complex regulates the phosphorylation of RSK substrates and MAPK signaling

Lopez, J., Bonsor, D. A., Sale, M. J., Urisman, A., Mehalko, J. L., Cabanski-Dunning, M., Castel, P., Simanshu, D. K., & McCormick, F. P. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.104789 · Cited by 11

Sustained ERK1/2 signaling is necessary for follicular rupture during ovulation in mice

Madogwe, E., Schuermann, Y., Siddappa, D., Bordignon, V., Roux, P. P., & Duggavathi, R. (2020) · Reproduction · doi:10.1530/rep-20-0087 · Cited by 11

Kaposi’s Sarcoma-Associated Herpesvirus Immediate Early Proteins Trigger FOXQ1 Expression in Oral Epithelial Cells, Engaging in a Novel Lytic Cycle-Sustaining Positive Feedback Loop

Atyeo, N., Chae, M. Y., Tóth, Z., Sharma, A., & Papp, B. (2023) · Journal of Virology · doi:10.1128/jvi.01696-22 · Cited by 11

Oncogenes and Signal Transduction

Grumolato, L., & Aaronson, S. A. (2015) · Elsevier eBooks · doi:10.1016/b978-1-4557-4066-6.00002-0 · Cited by 11

Protein Translation and Signaling in Human Eosinophils

Esnault, S. J., Shen, Z.-J., & Malter, J. S. (2017) · Frontiers in Medicine · doi:10.3389/fmed.2017.00150 · Cited by 12

Strategies to Enhance Logic Modeling-Based Cell Line-Specific Drug Synergy Prediction

Niederdorfer, B., Touré, V., Vázquez, M., Thommesen, L., Kuiper, M. T. R., Lægreid, A., & Flobak, Å. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.00862 · Cited by 11

N-Substituted pyrrolopyrimidines and purines as p90 ribosomal S6 protein kinase-2 (RSK2) inhibitors

Casalvieri, K. A., Matheson, C. J., Warfield, B. M., Backos, D. S., & Reigan, P. (2021) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2021.116220 · Cited by 11

Investigation on the active ingredient and mechanism of Cannabis sativa L. for treating epilepsy based on network pharmacology

Li, Y., Ding, Y., Xiao, W., & Zhu, J. (2021) · Biotechnology & Biotechnological Equipment · doi:10.1080/13102818.2021.1942208 · Cited by 11

Structural basis for the autoinhibition of the C-terminal kinase domain of human RSK1

Li, D., Fu, T., Nan, J., Liu, C., Li, L.-F., & Su, X. (2012) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444912007457 · Cited by 11

Regulation of the kinase RSK1 by arsenic trioxide and generation of antileukemic responses

Galvin, J. P., Altman, J. K., Szilard, A., Goussetis, D. J., Vakana, E., Sassano, A., & Platanias, L. C. (2013) · Cancer Biology & Therapy · doi:10.4161/cbt.23760 · Cited by 11

The conserved ancestral signaling pathway from cilium to nucleus

Satir, P., & Satir, B. H. (2019) · Journal of Cell Science · doi:10.1242/jcs.230441 · Cited by 11

Roles of mammalian Scribble in polarity signaling, virus offense and cell-fate determination

Wigerius, M. (2010) · KTH Publication Database DiVA (KTH Royal Institute of Technology) · Cited by 11

Kinetoplastid AGC Kinases

Bachmaier, S., & Boshart, M. (2013) · Wiley eBooks · doi:10.1002/9783527675401.ch05 · Cited by 11

The thyroid hormone receptors as tumor suppressors

Ruiz-Llorente, L., Martínez-Iglesias, O. A., Garcı́a-Silva, S., Tenbaum, S. P., Regadera, J., & Aranda, A. (2011) · Hormone Molecular Biology and Clinical Investigation · doi:10.1515/hmbci.2010.045 · Cited by 10

A Human Ribonuclease Variant and ERK-Pathway Inhibitors Exhibit Highly Synergistic Toxicity for Cancer Cells

Hoang, T. T., Tanrikulu, I. C., Vatland, Q. A., Hoang, T. M., & Raines, R. T. (2018) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-18-0724 · Cited by 10

Divergent off-target effects of RSK N-terminal and C-terminal kinase inhibitors in cardiac myocytes

Σταθοπούλου, Κ., Schobesberger, S., Bork, N. I., Sprenger, J., Perera, R. K., Sotoud, H., Geertz, B., David, J.-P., Christ, T., Nikolaev, V. O., et al. (2019) · Cellular Signalling · doi:10.1016/j.cellsig.2019.109362 · Cited by 10

Thrombin-induced tolerance against oxygen-glucose deprivation in astrocytes: role of protease-activated receptor-1.

Bao, X., Hua, Y., Keep, R. F., & Xi, G. (2018) · PubMed · Cited by 10

Role of ribosomal S6 kinase family in message patheway

Song, X. (2009) · Zhonghua zhongliu fangzhi zazhi

Role and regulation of 90 kDa ribosomal S6 kinase (RSK) in signal transduction

Frödin, M., & Gammeltoft, S. (1999) · Molecular and Cellular Endocrinology · doi:10.1016/s0303-7207(99)00061-1 · Cited by 719

Regulation and function of the RSK family of protein kinases

Roméo, Y., Zhang, X., & Roux, P. P. (2011) · Biochemical Journal · doi:10.1042/bj20110289 · Cited by 392

The RSK factors of activating the Ras/MAPK signaling cascade

Carriere, A. (2008) · Frontiers in bioscience · doi:10.2741/3003 · Cited by 218

Editorial: Functions and regulation of p90RSK and its family: mechanisms, roles in diseases, and implications in therapeutics

Lin, L., Le, N., & Hu, K. (2025) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2025.1648101