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 · see citing works

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 · see citing works

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 · see citing works

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 2,494 · see citing works

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 · see citing works

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 1,887 · see citing works

The renaissance of GSK3

Cohen, P., & Frame, S. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35096075 · Cited by 1,478 · see citing works

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 · see citing works

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 1,379 · see citing works

mTOR and S6K1 Mediate Assembly of the Translation Preinitiation Complex through Dynamic Protein Interchange and Ordered Phosphorylation Events

Holz, M. K., Ballif, B. A., Gygi, S. P., & Blenis, J. (2005) · Cell · doi:10.1016/j.cell.2005.10.024 · Cited by 1,262 · see citing works

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 1,250 · see citing works

Coupling of the RAS-MAPK Pathway to Gene Activation by RSK2, a Growth Factor-Regulated CREB Kinase

Xing, J. W., Ginty, D. D., & Greenberg, M. E. (1996) · Science · doi:10.1126/science.273.5277.959 · Cited by 1,246 · see citing works

Rapamycin-FKBP specifically blocks growth-dependent activation of and signaling by the 70 kd S6 protein kinases

Chung, J., Kuo, C. J., Crabtree, G. R., & Blenis, J. (1992) · Cell · doi:10.1016/0092-8674(92)90643-q · Cited by 1,151 · see citing works

Nuclear Localization and Regulation of erk- and rsk-Encoded Protein Kinases

Chen, R., Sarnecki, C., & Blenis, J. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.3.915 · Cited by 1,081 · see citing works

A large-scale RNAi screen in human cells identifies new components of the p53 pathway

Berns, K., Hijmans, E. M., Mullenders, J., Brummelkamp, T. R., Velds, A., Heimerikx, M., Kerkhoven, R. M., Madiredjo, M., Nijkamp, W., Weigelt, B., et al. (2004) · Nature Cell Biology · doi:10.1038/nature02371 · Cited by 1,059 · see citing works

Insulin-stimulated MAP-2 kinase phosphorylates and activates ribosomal protein S6 kinase II

Sturgill, T. W., Ray, L. B., ERIKSON, E., & Maller, J. L. (1988) · Nature · doi:10.1038/334715a0 · Cited by 1,017 · see citing works

Mitogen‐ and stress‐activated protein kinase‐1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB

Deák, M., Clifton, A. D., Lucocq, J. M., & Alessi, D. R. (1998) · The EMBO Journal · doi:10.1093/emboj/17.15.4426 · Cited by 992 · see citing works

Molecular interpretation of ERK signal duration by immediate early gene products

Murphy, L. O., Smith, S. W., Chen, R., Fingar, D. C., & Blenis, J. (2002) · Nature Cell Biology · doi:10.1038/ncb822 · Cited by 928 · see citing works

Inactivation of glycogen synthase kinase-3 <i>β</i> by phosphorylation: new kinase connections in insulin and growth-factor signalling

Sutherland, C., Leighton, I. A., & Cohen, P. (1993) · Biochemical Journal · doi:10.1042/bj2960015 · Cited by 903 · see citing works

ras mediates nerve growth factor receptor modulation of three signal-transducing protein kinases: MAP kinase, Raf-1, and RSK

Wood, K. W., Sarnecki, C., Roberts, T. M., & Blenis, J. (1992) · Cell · doi:10.1016/0092-8674(92)90076-o · Cited by 903 · see citing works

Regulation of elongation factor 2 kinase by p90RSK1 and p70 S6 kinase

Wang, X.-M., Li, W., Williams, M. R., Terada, N., Alessi, D., & Proud, C. G. (2001) · EMBO Journal · doi:10.1093/emboj/20.16.4370 · Cited by 862 · see citing works

PDK1, the master regulator of AGC kinase signal transduction

Mora, A., Komander, D., van Aalten, D. M. F., & Alessi, D. R. (2004) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2003.12.022 · Cited by 802 · see citing works

Regulation of the ABC kinases by phosphorylation: protein kinase C as a paradigm

Newton, A. C. (2003) · Biochemical Journal · doi:10.1042/bj20021626 · Cited by 799 · see citing works

Tumor-promoting phorbol esters and activated Ras inactivate the tuberous sclerosis tumor suppressor complex via p90 ribosomal S6 kinase

Roux, P. P., Ballif, B. A., Anjum, R., Gygi, S. P., & Blenis, J. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0405659101 · Cited by 750 · see citing works

RAS/ERK Signaling Promotes Site-specific Ribosomal Protein S6 Phosphorylation via RSK and Stimulates Cap-dependent Translation

Roux, P. P., Shahbazian, D., Vu, H., Holz, M. K., Cohen, M. S., Taunton, J., Sonenberg, N., & Blenis, J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700906200 · Cited by 749 · see citing works

S6K1 −/− / S6K2 −/− Mice Exhibit Perinatal Lethality and Rapamycin-Sensitive 5′-Terminal Oligopyrimidine mRNA Translation and Reveal a Mitogen-Activated Protein Kinase-Dependent S6 Kinase Pathway

Pende, M., Um, S. H., Mieulet, V., Sticker, M., Goss, V. L., Mestan, J., Mueller, M., Fumagalli, S., Kozma, S. C., & Thomas, G. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.8.3112-3124.2004 · Cited by 743 · see citing works

Nerve growth factor activates a Ras-dependent protein kinase that stimulates c-fos transcription via phosphorylation of CREB

Ginty, D. D., Bonni, A., & Greenberg, M. E. (1994) · Cell · doi:10.1016/0092-8674(94)90055-8 · Cited by 732 · see citing works

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 716 · see citing works

Bidirectional RNA Helicase Activity of Eucaryotic Translation Initiation Factors 4A and 4F

Rozen, F., Edery, I., Meerovitch, K., Dever, T. E., Merrick, W. C., & Sonenberg, N. (1990) · Molecular and Cellular Biology · doi:10.1128/mcb.10.3.1134 · Cited by 632 · see citing works

Inhibition of HeLa cell protein synthesis following poliovirus infection correlates with the proteolysis of a 220,000-dalton polypeptide associated with eucaryotic initiation factor 3 and a cap binding protein complex.

Etchison, D., Milburn, S. C., Edery, I., Sonenberg, N., & Hershey, J. W. B. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)33352-0 · Cited by 583 · see citing works

The mTOR/PI3K and MAPK pathways converge on eIF4B to control its phosphorylation and activity

Shahbazian, D., Roux, P. P., Mieulet, V., Cohen, M. S., Raught, B., Taunton, J., Hershey, J. W. B., Blenis, J., Pende, M., & Sonenberg, N. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601166 · Cited by 532 · see citing works

c-Kit triggers dual phosphorylations, which couple activation and degradation of the essential melanocyte factor MiPreprint

Wu, M., Hemesath, T. J., Takemoto, C. M., Horstmann, M. A., Wells, A. G., Price, E. R., Fisher, D. Z., & Fisher, D. E. (2000) · Genes & Development · doi:10.1101/gad.14.3.301 · Cited by 530 · see citing works

Structural Bioinformatics-Based Design of Selective, Irreversible Kinase Inhibitors

Cohen, M. S., Zhang, C., Shokat, K. M., & Taunton, J. (2005) · Science · doi:10.1126/science1108367 · Cited by 509 · see citing works

MSK2 and MSK1 mediate the mitogen‐ and stress‐induced phosphorylation of histone H3 and HMG‐14

Soloaga, A., Thomson, S., Wiggin, G. R., Rampersaud, N., Dyson, M. H., Hazzalin, C. A., Mahadevan, L. C., & Arthur, J. S. C. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg273 · Cited by 508 · see citing works

Phosphorylation of eucaryotic translation initiation factor 4B Ser422 is modulated by S6 kinases

Raught, B., Peiretti, F., Gingras, A., Livingstone, M., Shahbazian, D., Mayeur, G. L., Polakiewicz, R. D., Sonenberg, N., & Hershey, J. W. B. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600193 · Cited by 473 · see citing works

The role of 3-phosphoinositide-dependent protein kinase 1 in activating AGC kinases defined in embryonic stem cells

Williams, M. R., Arthur, J. S. C., Balendran, A., KAAY, J. V. D., Poli, V., Cohen, P., & Alessi, D. R. (2000) · Current Biology · doi:10.1016/s0960-9822(00)00441-3 · Cited by 471 · see citing works

Silencing of Epidermal Growth Factor Receptor Suppresses Hypoxia-Inducible Factor-2–Driven VHL −/− Renal Cancer

Smith, K., Gunaratnam, L., Morley, M., Franovic, A., Mekhail, K., & Lee, S. (2005) · Cancer Research · doi:10.1158/0008-5472.can-05-0169 · Cited by 456 · see citing works

MSK1 and MSK2 Are Required for the Mitogen- and Stress-Induced Phosphorylation of CREB and ATF1 in Fibroblasts

Wiggin, G. R., Soloaga, A., Foster, J. M., Murray-Tait, V., Cohen, P., & Arthur, J. S. C. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.8.2871-2881.2002 · Cited by 445 · see citing works

Molecular mechanisms mediating mammalian mitogen-activated protein kinase (MAPK) kinase (MEK)-MAPK cell survival signals.

Ballif, B. A., & Blenis, J. (2001) · PubMed · Cited by 419 · see citing works

Mutations in the kinase Rsk-2 associated with Coffin-Lowry syndrome

Trivier, E., Cesare, D. D., Jacquot, S., Pannetier, S., Zackai, E. H., Young, I., Mandel, J., Sassone‐Corsi, P., & Hanauer, A. (1996) · Nature · doi:10.1038/384567a0 · Cited by 405 · see citing works

Identification of Regulatory Phosphorylation Sites in Mitogen-activated Protein Kinase (MAPK)-activated Protein Kinase-1a/p90 That Are Inducible by MAPK

Dalby, K. N., MORRICE, N. A., Caudwell, F. B., Avruch, J., & Cohen, P. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.3.1496 · Cited by 373 · see citing works

pp90rsk1 Regulates Estrogen Receptor-Mediated Transcription through Phosphorylation of Ser-167

Joel, P. B., Smith, J. A., Sturgill, T. W., Fisher, T. L., Blenis, J., & Lannigan, D. A. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.4.1978 · Cited by 345 · see citing works

Oncogenic MAPK Signaling Stimulates mTORC1 Activity by Promoting RSK-Mediated Raptor Phosphorylation

Carrière, A., Cargnello, M., Julien, L.-A., Gao, H., Bonneil, É., Thibault, P., & Roux, P. P. (2008) · Current Biology · doi:10.1016/j.cub.2008.07.078 · Cited by 332 · see citing works

A link between MAP kinase and p34cdc2/cyclin B during oocyte maturation: p90rsk phosphorylates and inactivates the p34cdc2 inhibitory kinase Myt1

Palmer, A., Gavin, A., & Nebreda, A. R. (1998) · The EMBO Journal · doi:10.1093/emboj/17.17.5037 · Cited by 330 · see citing works

A phosphoserine‐regulated docking site in the protein kinase RSK2 that recruits and activates PDK1

Frödin, M., Jensen, C. J., Mérienne, K., & Gammeltoft, S. (2000) · The EMBO Journal · doi:10.1093/emboj/19.12.2924 · Cited by 317 · see citing works

BI-D1870 is a specific inhibitor of the p90 RSK (ribosomal S6 kinase) isoforms in vitro and in vivo

Sapkota, G. P., Cummings, L., Newell, F., Armstrong, C. G., Bain, J., Frödin, M., Grauert, M., Hoffmann, M., Schnapp, G., Steegmaier, M., et al. (2006) · Biochemical Journal · doi:10.1042/bj20061088 · Cited by 313 · see citing works

Rsk-2 activity is necessary for epidermal growth factor-induced phosphorylation of CREB protein and transcription of c- fos gene

Cesare, D. D., Jacquot, S., Hanauer, A., & Sassone‐Corsi, P. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.21.12202 · Cited by 309 · see citing works

Rsk1 mediates a MEK–MAP kinase cell survival signal

Shimamura, A., Ballif, B. A., Richards, S. A., & Blenis, J. (2000) · Current Biology · doi:10.1016/s0960-9822(00)00310-9 · Cited by 296 · see citing works

Phosphorylation of the c-Fos transrepression domain by mitogen-activated protein kinase and 90-kDa ribosomal S6 kinase.

Chen, R., Abate, C., & Blenis, J. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.23.10952 · Cited by 294 · see citing works

Identification of the First Specific Inhibitor of p90 Ribosomal S6 Kinase (RSK) Reveals an Unexpected Role for RSK in Cancer Cell Proliferation

Smith, J. A., Poteet-Smith, C. E., Xu, Y.-M., Errington, T. M., Hecht, S. M., & Lannigan, D. A. (2005) · Cancer Research · doi:10.1158/0008-5472.1027.65.3 · Cited by 287 · see citing works

Identification of an Extracellular Signal-regulated Kinase (ERK) Docking Site in Ribosomal S6 Kinase, a Sequence Critical for Activation by ERK in Vivo

Smith, J. A., Poteet-Smith, C. E., Malarkey, K., & Sturgill, T. W. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.5.2893 · Cited by 283 · see citing works

A Xenopus ribosomal protein S6 kinase has two apparent kinase domains that are each similar to distinct protein kinases.

Jones, S. W., ERIKSON, E., Blenis, J., Maller, J. L., & Erikson, R. L. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.10.3377 · Cited by 280 · see citing works

A phosphoserine/threonine-binding pocket in AGC kinases and PDK1 mediates activation by hydrophobic motif phosphorylation

Frödin, M., Antal, T. L., Dümmler, B. A., Jensen, C. J., Deak, M., Gammeltoft, S., & Biondi, R. M. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf551 · Cited by 275 · see citing works

90-kDa Ribosomal S6 Kinase Is Phosphorylated and Activated by 3-Phosphoinositide-dependent Protein Kinase-1

Jensen, C. J., Buch, M.-B., Krag, T. O. B., Hemmings, B. A., Gammeltoft, S., & Frödin, M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.38.27168 · Cited by 263 · see citing works

ERK-Dependent Phosphorylation of the Transcription Initiation Factor TIF-IA Is Required for RNA Polymerase I Transcription and Cell Growth

Zhao, J., Yuan, X., Frödin, M., & Grummt, I. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00036-4 · Cited by 259 · see citing works

Regulation of the meiotic cell cycle in oocytes

Nebreda, Á. R., & Ferby, I. (2000) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(00)00150-2 · Cited by 258 · see citing works

The Signal-Dependent Coactivator CBP Is a Nuclear Target for pp90RSK

Nakajima, T., Fukamizu, A., Takahashi, J. B., Gage, F. H., Fisher, T., Blenis, J., & Montminy, M. (1996) · Cell · doi:10.1016/s0092-8674(00)80119-1 · Cited by 254 · see citing works

Activation of PI3K/Akt and MAPK pathways regulates Myc-mediated transcription by phosphorylating and promoting the degradation of Mad1

Zhu, J., Blenis, J., & Yuan, J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0802785105 · Cited by 246 · see citing works

p90RSK Blocks Bad-mediated Cell Death via a Protein Kinase C-dependent Pathway

Tan, Y., Ruan, H., Demeter, M. R., & Comb, M. J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.49.34859 · Cited by 241 · see citing works

p90RSK Is a Serum-stimulated Na+/H+ Exchanger Isoform-1 Kinase

Takahashi, E., Abe, J., Gallis, B. M., Aebersold, R. H., Spring, D. J., Krebs, E. G., & Berk, B. C. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.29.20206 · Cited by 231 · see citing works

IκBα is a target for the mitogen‐activated 90 kDa ribosomal S6 kinase

Schouten, G. J., Vertegaal, A. C. O., Whiteside, S. T., Israël, A., Toebes, M., Dorsman, J. C., van der Eb, A. J., & Zantema, A. (1997) · The EMBO Journal · doi:10.1093/emboj/16.11.3133 · Cited by 225 · see citing works

Mitogen- and Stress-Activated Protein Kinase 1 Mediates cAMP Response Element-Binding Protein Phosphorylation and Activation by Neurotrophins

Simon, J., Arthur, J. S. C., Fong, A. L., Dwyer, J. M., Davare, M. A., Reese, E. A., Obrietan, K. H., & Impey, S. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.5227-03.2004 · Cited by 225 · see citing works

The RSK factors of activating the Ras/MAPK signaling cascade

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

Phosphorylation of p27Kip1 at Threonine 198 by p90 Ribosomal Protein S6 Kinases Promotes Its Binding to 14-3-3 and Cytoplasmic Localization

Fujita, N., Sato, S., & Tsuruo, T. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306614200 · Cited by 210 · see citing works

The 90-kDa Ribosomal S6 Kinase (pp90rsk) Phosphorylates the N-terminal Regulatory Domain of IκBα and Stimulates Its Degradation in Vitro

Ghoda, L. Y., Lin, X., & Greene, W. C. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.34.21281 · Cited by 204 · see citing works

The Serine/Threonine Protein Kinase, p90 Ribosomal S6 Kinase, Is an Important Regulator of Prostate Cancer Cell Proliferation

Clark, D. E., Errington, T. M., Smith, J. A., Frierson, H. F., Weber, M. J., & Lannigan, D. A. (2005) · Cancer Research · doi:10.1158/0008-5472.can-04-3151 · Cited by 200 · see citing works

Evidence for Two Catalytically Active Kinase Domains in pp90 rsk

Fisher, T. L., & Blenis, J. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.3.1212 · Cited by 196 · see citing works

Phosphorylation of p90 Ribosomal S6 Kinase (RSK) Regulates Extracellular Signal-Regulated Kinase Docking and RSK Activity

Roux, P. P., Richards, S. A., & Blenis, J. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.14.4796-4804.2003 · Cited by 196 · see citing works

MSK1 is required for CREB phosphorylation in response to mitogens in mouse embryonic stem cells

Arthur, J. S. C., & Cohen, P. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)02031-7 · Cited by 192 · see citing works

A protein kinase from Xenopus eggs specific for ribosomal protein S6.

ERIKSON, E., & Maller, J. L. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.3.742 · Cited by 191 · see citing works

Glycogen synthase kinase 3 phosphorylates Jun family members in vitro and negatively regulates their transactivating potential in intact cells.

Nikolakaki, E., Coffer, P. J., Hemelsoet, R., Woodgett, J. R., & Defize, L. H. K. (1993) · PubMed · Cited by 188 · see citing works

Regulation of multisite phosphorylation and 14-3-3 binding of AS160 in response to IGF-1, EGF, PMA and AICAR

Geraghty, K. M., Chen, S., Harthill, J. E., Ibrahim, A. F., Toth, R., Morrice, N. A., Vandermoere, F., Moorhead, G. B., Hardie, D. G., & MacKintosh, C. (2007) · Biochemical Journal · doi:10.1042/bj20070649 · Cited by 181 · see citing works

Ribosomal S6 Kinase (RSK) Regulates Phosphorylation of Filamin A on an Important Regulatory Site

Woo, M. S., Ohta, Y., Rabinovitz, I., Stossel, T. P., & Blenis, J. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.7.3025-3035.2004 · Cited by 179 · see citing works

Signaling control of mRNA translation in cancer pathogenesis

Holland, E. C., Sonenberg, N., Pandolfi, P. P., & Thomas, G. (2004) · Oncogene · doi:10.1038/sj.onc.1207590 · Cited by 168 · see citing works

The Protein Kinase p90 Rsk as an Essential Mediator of Cytostatic Factor Activity

Bhatt, R. R., & Ferrell, J. E. (1999) · Science · doi:10.1126/science.286.5443.1362 · Cited by 165 · see citing works

RSK-B, a Novel Ribosomal S6 Kinase Family Member, Is a CREB Kinase under Dominant Control of p38α Mitogen-activated Protein Kinase (p38αMAPK)

Pierrat, B., Correia, J. D. S., Mary, J., Tomás-Zuber, M., & Lesslauer, W. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.45.29661 · Cited by 163 · see citing works

C/EBPβ Phosphorylation by RSK Creates a Functional XEXD Caspase Inhibitory Box Critical for Cell Survival

Buck, M., Poli, V., Hunter, T. R., & Chojkier, M. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00374-4 · Cited by 162 · see citing works

MSK1 activity is controlled by multiple phosphorylation sites

McCoy, C. E., CAMPBELL, D. G., Deák, M., Bloomberg, G. B., & Arthur, J. S. C. (2005) · Biochemical Journal · doi:10.1042/bj20041501 · Cited by 160 · see citing works

Increased phosphorylation of ribosomal protein S6 during meiotic maturation of Xenopus oocytes.

Nielsen, P. J., Thomas, G., & Maller, J. L. (1982) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.79.9.2937 · Cited by 159 · see citing works

The Tumor Suppressor DAP Kinase Is a Target of RSK-Mediated Survival Signaling

Anjum, R. S., Roux, P. P., Ballif, B. A., Gygi, S. P., & Blenis, J. (2005) · Current Biology · doi:10.1016/j.cub.2005.08.050 · Cited by 157 · see citing works

FGFR3 Activates RSK2 to Mediate Hematopoietic Transformation through Tyrosine Phosphorylation of RSK2 and Activation of the MEK/ERK Pathway

Kang, S., Dong, S., Gu, T.-L., Guo, A., Cohen, M. S., Lonial, S., Khoury, H. J., Fabbro, D., Gilliland, D. G., Bergsagel, P. L., et al. (2007) · Cancer Cell · doi:10.1016/j.ccr.2007.08.003 · Cited by 154 · see citing works

Induction of Metaphase Arrest in Cleaving Xenopus Embryos by the Protein Kinase p90 Rsk

Gross, S. D., Schwab, M. S., Lewellyn, A. L., & Maller, J. L. (1999) · Science · doi:10.1126/science.286.5443.1365 · Cited by 146 · see citing works

The MAPK-activated kinase Rsk controls an acute Toll-like receptor signaling response in dendritic cells and is activated through two distinct pathways

Zaru, R., Ronkina, N., Gaestel, M., Arthur, J. S. C., & Watts, C. K. W. (2007) · Nature Immunology · doi:10.1038/ni1517 · Cited by 143 · see citing works

Ribosomal S6 kinase 1 (RSK1) activation requires signals dependent on and independent of the MAP kinase ERK

Richards, S. A., Fu, J., Romanelli, A., Shimamura, A., & Blenis, J. (1999) · Current Biology · doi:10.1016/s0960-9822(99)80364-9 · Cited by 142 · see citing works

Identification of insulin‐stimulated protein kinase‐1 as the rabbit equivalent of rskmo‐2

Sutherland, C. D., Campbell, D. G., & Cohen, P. (1993) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1993.tb17696.x · Cited by 141 · see citing works

RSK3 Encodes a Novel pp90 rsk Isoform with a Unique N-Terminal Sequence: Growth Factor-Stimulated Kinase Function and Nuclear Translocation

Zhao, Y., Bjørbæk, C., Weremowicz, S., Morton, C. C., & Moller, D. E. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.8.4353 · Cited by 141 · see citing works

Altered Extracellular Signal-Regulated Kinase Signaling and Glycogen Metabolism in Skeletal Muscle from p90 Ribosomal S6 Kinase 2 Knockout Mice

Dufresne, S. D., Bjørbæk, C., El-Haschimi, K., Zhao, Y., Aschenbach, W. G., Moller, D. E., & Goodyear, L. J. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.1.81-87.2001 · Cited by 139 · see citing works

A direct link of the Mos–MAPK pathway to Erp1/Emi2 in meiotic arrest of Xenopus laevis eggs

Inoue, D., Ohe, M., Kanemori, Y., Nobui, T., & Sagata, N. (2007) · Nature · doi:10.1038/nature05688 · Cited by 135 · see citing works

The in vivo role of PtdIns(3,4,5)P3 binding to PDK1 PH domain defined by knockin mutation

McManus, E. J., Collins, B., Ashby, P. R., Prescott, A. R., Murray-Tait, V., Armit, L. J., Arthur, J. S. C., & Alessi, D. R. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600218 · Cited by 132 · see citing works

Comparison of the specificities of p70 S6 kinase and MAPKAP kinase‐1 identifies a relatively specific substrate for p70 S6 kinase: the N‐terminal kinase domain of MAPKAP kinase‐1 is essential for peptide phosphorylation

Leighton, I. A., Dalby, K. N., Caudwell, F. B., Cohen, P. T. W., & Cohen, P. (1995) · FEBS Letters · doi:10.1016/0014-5793(95)01170-j · Cited by 126 · see citing works

Functional Characterization of Human RSK4, a New 90-kDa Ribosomal S6 Kinase, Reveals Constitutive Activation in Most Cell Types

Dummler, B. A., Hauge, C., Silber, J., Yntema, H. G., Kruse, L. S., Kofoed, B., Hemmings, B. A., Alessi, D. R., & Frödin, M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m408194200 · Cited by 124 · see citing works

A Novel Ribosomal S6-Kinase (RSK4; RPS6KA6) Is Commonly Deleted in Patients with Complex X-Linked Mental Retardation

Yntema, H. G., van den Helm, B., Kissing, J., van Duijnhoven, G., Poppelaars, F. A. M., Chelly, J., Moraine, C., Fryns, J., Hamel, B. C. J., Heilbronner, H., et al. (1999) · Genomics · doi:10.1006/geno.1999.6004 · Cited by 121 · see citing works

Phosphorylation of Erp1 by p90rsk is required for cytostatic factor arrest in Xenopus laevis eggs

Nishiyama, T., Ohsumi, K., & Kishimoto, T. (2007) · Nature · doi:10.1038/nature05696 · Cited by 118 · see citing works

RPS6KA2, a putative tumour suppressor gene at 6q27 in sporadic epithelial ovarian cancer

Bignone, P. A., Lee, K. Y., Liu, Y., Emilion, G., Finch, J., Soosay, A. E. R., Charnock, F. M. L., Beck, S., Dunham, I., Mungall, A. J. J., et al. (2006) · Oncogene · doi:10.1038/sj.onc.1209827 · Cited by 115 · see citing works

Spatially Separate Docking Sites on ERK2 Regulate Distinct Signaling Events In Vivo

Dimitri, C. A., Dowdle, W., MacKeigan, J. P., Blenis, J., & Murphy, L. O. (2005) · Current Biology · doi:10.1016/j.cub.2005.06.037 · Cited by 114 · see citing works

Expression analysis of RSK gene family members: the RSK2 gene, mutated in Coffin-Lowry syndrome, is prominently expressed in brain structures essential for cognitive function and learning

Zeniou, M. (2002) · Human Molecular Genetics · doi:10.1093/hmg/11.23.2929 · Cited by 110 · see citing works

Bub1 is activated by the protein kinase p90 Rsk during Xenopus oocyte maturation

Schwab, M. S., Roberts, B. T., Gross, S. D., Tunquist, B. J., Taieb, F. E., Lewellyn, A. L., & Maller, J. L. (2001) · Current Biology · doi:10.1016/s0960-9822(01)00045-8 · Cited by 109 · see citing works

Divergent Functional Roles for p90 Kinase Domains

Bj⊘rbæk, C., Zhao, Y., & Moller, D. E. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.32.18848 · Cited by 105 · see citing works

Involvement of p90 in Neurite Outgrowth Mediated by the Cell Adhesion Molecule L1

Wong, E. V., Schaefer, A. W., Landreth, G. E., & Lemmon, V. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.30.18217 · Cited by 104 · see citing works

Distinct mechanisms for the activation of the RSK kinases/MAP2 kinase/pp90rsk and pp70-S6 kinase signaling systems are indicated by inhibition of protein synthesis.

Blenis, J., Chung, J., ERIKSON, E., Alcorta, D. A., & Erikson, R. L. (1991) · PubMed · Cited by 104 · see citing works

Characterization of Regulatory Events Associated with Membrane Targeting of p90 Ribosomal S6 Kinase 1

Richards, S. A., Dreisbach, V. C., Murphy, L. O., & Blenis, J. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.21.7470-7480.2001 · Cited by 104 · see citing works

Regulation of the ETS Transcription Factor ER81 by the 90-kDa Ribosomal S6 Kinase 1 and Protein Kinase A

Wu, J., & Janknecht, R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205501200 · Cited by 95 · see citing works

Nur77 is phosphorylated in cells by RSK in response to mitogenic stimulation

Wingate, A. D., Campbell, D. G., Peggie, M. W., & Arthur, J. S. C. (2006) · Biochemical Journal · doi:10.1042/bj20050967 · Cited by 91 · see citing works

Deletion of the Coffin–Lowry Syndrome Gene Rsk2 in Mice is Associated With Impaired Spatial Learning and Reduced Control of Exploratory Behavior

Poirier, R., Jacquot, S., Vaillend, C., Soutthiphong, A. A., Libbey, M., Davis, S., Laroche, S., Hanauer, A., Welzl, H., Lipp, H., et al. (2006) · Behavior Genetics · doi:10.1007/s10519-006-9116-1 · Cited by 87 · see citing works

p90Rsk is not involved in cytostatic factor arrest in mouse oocytes

Dumont, J., Umbhauer, M., Rassinier, P., Hanauer, A., & Verlhac, M. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200501027 · Cited by 86 · see citing works

Metabotropic glutamate receptor-initiated translocation of protein kinase p90rsk to polyribosomes: a possible factor regulating synaptic protein synthesis.

Angenstein, F., Greenough, W., & Weiler, I. (1998) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.95.25.15078 · Cited by 83 · see citing works

Aberrant Expression of X-Linked Genes RbAp46, Rsk4, and Cldn2 in Breast Cancer

Thakur, A. B., Rahman, K. W., Wu, J., Bollig-Fischer, A. B., Biliran, H., Lin, X., Nassar, H., Grignon, D. J., Sarkar, F. H., & Liao, J. D. (2007) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-06-0071 · Cited by 83 · see citing works

Ran-Binding Protein 3 Phosphorylation Links the Ras and PI3-Kinase Pathways to Nucleocytoplasmic Transport

Yoon, S.-O., Shin, S., Liu, Y., Ballif, B. A., Woo, M. S., Gygi, S. P., & Blenis, J. (2008) · Molecular Cell · doi:10.1016/j.molcel.2007.12.024 · Cited by 80 · see citing works

The S6KII ( rsk ) Gene of Drosophila melanogaster Differentially Affects an Operant and a Classical Learning Task

Putz, G., Bertolucci, F., Raabe, T., Zars, T. D., & Heisenberg, M. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.3211-04.2004 · Cited by 79 · see citing works

Ribosomal subunit kinase-2 is required for growth factor-stimulated transcription of the c- Fos gene

Brüning, J. C., Gillette, J. A., Zhao, Y., Bjørbæk, C., Kotzka, J., Knebel, B., Avci, H., Hanstein, B., Lingohr, P., Moller, D. E., et al. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.6.2462 · Cited by 75 · see citing works

Inhibition of ERK‐MAP kinase signaling by RSK during Drosophila development

Kim, M.-J., Lee, J. H., Koh, H., Lee, S. Y., Jang, C., Chung, C. J., Sung, J. H., Blenis, J., & Chung, J. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601180 · Cited by 72 · see citing works

Phosphorylation of the ribosomal protein S6 is elevated in cells transformed by a variety of tumor viruses

Blenis, J., & Erikson, R. L. (1984) · Journal of Virology · doi:10.1128/jvi.50.3.966-969.1984 · Cited by 61 · see citing works

The MAP kinase ERK5 binds to and phosphorylates p90 RSK

Ranganathan, A., Pearson, G. W., Chrestensen, C. A., Sturgill, T. W., & Cobb, M. H. (2006) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2006.02.023 · Cited by 60 · see citing works

Characterization of Mouse Rsk4 as an Inhibitor of Fibroblast Growth Factor-RAS-Extracellular Signal-Regulated Kinase Signaling

Myers, A. P., Corson, L., Rossant, J., & Baker, J. C. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.10.4255-4266.2004 · Cited by 60 · see citing works

The kinase MSK1 is required for induction of c-fos by lysophosphatidic acid in mouse embryonic stem cells

Schuck, S., Soloaga, A., Schratt, G. M., Arthur, J. S. C., & Nordheim, A. (2003) · BMC Molecular Biology · doi:10.1186/1471-2199-4-6 · Cited by 57 · see citing works

Insulin Resistance and Lipodystrophy in Mice Lacking Ribosomal S6 Kinase 2

El-Haschimi, K., Dufresne, S. D., Hirshman, M. F., Flier, J. S., Goodyear, L. J., & Bjørbæk, C. (2003) · Diabetes · doi:10.2337/diabetes.52.6.1340 · Cited by 53 · see citing works

Subcellular Localization and Biological Actions of Activated RSK1 Are Determined by Its Interactions with Subunits of Cyclic AMP-Dependent Protein Kinase

Chaturvedi, D., Poppleton, H., Stringfield, T. M., Barbier, A., & Patel, T. B. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01422-05 · Cited by 50 · see citing works

A p90rskMutant Constitutively Interacting with MAP Kinase Uncouples MAP Kinase from p34cdc2/Cyclin B Activation inXenopusOocytes

Gavin, A., Ainle, A. N., Chierici, E., Jones, M., & Nebreda, Á. R. (1999) · Molecular Biology of the Cell · doi:10.1091/mbc.10.9.2971 · Cited by 48 · see citing works

p70S6K Controls Selective mRNA Translation during Oocyte Maturation and Early Embryogenesis inXenopus laevis

Schwab, M., Kim, S. H., Terada, N., Edfjall, C., Kozma, S., Thomas, G., & Maller, J. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.4.2485 · Cited by 48 · see citing works

IOP1, a novel hydrogenase-like protein that modulates hypoxia-inducible factor-1α activity

Huang, J., Song, D., Flores, A. G., Zhao, Q., Mooney, S. M., Shaw, L. M., & Lee, F. S. (2006) · Biochemical Journal · doi:10.1042/bj20060635 · Cited by 44 · see citing works

C-terminal Elements Control Location, Activation Threshold, and p38 Docking of Ribosomal S6 Kinase B (RSKB)

Tomás-Zuber, M., Mary, J., Lamour, F., Bur, D., & Lesslauer, W. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m005822200 · Cited by 35 · see citing works

Activation of p90Rsk1 Is Sufficient for Differentiation of PC12 Cells

Silverman, E., Frödin, M., Gammeltoft, S., & Maller, J. L. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.24.10573-10583.2004 · Cited by 34 · see citing works

p90 ribosomal S6 kinase 2 is associated with and dephosphorylated by protein phosphatase 2Cδ

Doehn, U., Gammeltoft, S., Shen, S., & Jensen, C. J. (2004) · Biochemical Journal · doi:10.1042/bj20040948 · Cited by 31 · see citing works

p90 RSK-1 associates with and inhibits neuronal nitric oxide synthase

Song, T., Sugimoto, K., Ihara, H., Mizutani, A., Hatano, N., Kume, K., Kambe, T., Yamaguchi, F., Tokuda, M., & Watanabe, Y. (2006) · Biochemical Journal · doi:10.1042/bj20060580 · Cited by 19 · see citing works

Epidermal Growth Factor Receptor Cell Proliferation Signaling Pathways

Wee, P., & Wang, Z. (2017) · Cancers · doi:10.3390/cancers9050052 · Cited by 2,027 · see citing works

The Ras-ERK and PI3K-mTOR pathways: cross-talk and compensation

Mendoza, M. C., Er, E. E., & Blenis, J. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2011.03.006 · Cited by 1,817 · see citing works

Bidirectional Transport of Amino Acids Regulates mTOR and Autophagy

Nicklin, P., Bergman, P., Zhang, B., Triantafellow, E., Wang, H., Nyfeler, B., Yang, H., Hild, M., Kung, C., Wilson, C., et al. (2009) · Cell · doi:10.1016/j.cell.2008.11.044 · Cited by 1,798 · see citing works

ERK1/2 MAP kinases: Structure, function, and regulation

Roskoski, R. J. (2012) · Pharmacological Research · doi:10.1016/j.phrs.2012.04.005 · Cited by 1,642 · see citing works

ERK/MAPK signalling pathway and tumorigenesis (Review)

Guo, Y., Pan, W., Liu, S., Shen, Z., Xu, Y., & Hu, L. (2020) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2020.8454 · Cited by 1,475 · see citing works

The nuts and bolts of AGC protein kinases

Pearce, L. R., Komander, D., & Alessi, D. R. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2822 · Cited by 1,294 · see citing works

How ERK1/2 activation controls cell proliferation and cell death: Is subcellular localization the answer?

Mebratu, Y. A., & Tesfaigzi, Y. (2009) · Cell Cycle · doi:10.4161/cc.8.8.8147 · Cited by 959 · see citing works

Protein kinases: evolution of dynamic regulatory proteins

Taylor, S. S., & Kornev, A. P. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.09.006 · Cited by 940 · see citing works

FGFR1 Amplification Drives Endocrine Therapy Resistance and Is a Therapeutic Target in Breast Cancer

Turner, N. C., Pearson, A., Sharpe, R., Lambros, M. B. K., Geyer, F. C., López‐García, M. Á., Natrajan, R., Marchiò, C., Iorns, E. J., Mackay, A. G., et al. (2010) · Cancer Research · doi:10.1158/0008-5472.can-09-3746 · Cited by 732 · see citing works

The ERK Cascade: Distinct Functions within Various Subcellular Organelles

Wortzel, I., & Seger, R. (2011) · Genes &amp; Cancer · doi:10.1177/1947601911407328 · Cited by 563 · see citing works

Mitochondrial Regulation of Cell Cycle and Proliferation

Arciuch, V. G. A., Elguero, M. E., Poderoso, J. J., & Carreras, M. C. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4085 · Cited by 428 · see citing works

Diversity, classification and function of the plant protein kinase superfamily

Lehti‐Shiu, M. D., & Shiu, S. (2012) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2012.0003 · Cited by 382 · see citing works

Phosphorylation of the Human MicroRNA-Generating Complex Mediates MAPK/Erk Signaling

Paroo, Z., Ye, X., Chen, S., & Liu, Q. (2009) · Cell · doi:10.1016/j.cell.2009.06.044 · Cited by 366 · see citing works

Enzyme Inhibitor Discovery by Activity-Based Protein Profiling

Niphakis, M. J., & Cravatt, B. F. (2014) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060713-035708 · Cited by 366 · see citing works

Deregulation of the PI3K and KRAS signaling pathways in human cancer cells determines their response to everolimus

Nicolantonio, F. D., Arena, S., Tabernero, J. M., Grosso, S., Molinari, F., Macarulla, T. M., Russo, M., Cancelliere, C., Zecchin, D., Mazzucchelli, L., et al. (2010) · Journal of Clinical Investigation · doi:10.1172/jci37539 · Cited by 343 · see citing works

Functions and regulation of the 70 kDa ribosomal S6 kinases

Fenton, T. R., & Gout, I. T. (2010) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2010.09.018 · Cited by 338 · see citing works

MAPK signalling in cellular metabolism: stress or wellness?

Gehart, H., Kumpf, S., Ittner, A., & Ricci, R. (2010) · EMBO Reports · doi:10.1038/embor.2010.160 · Cited by 327 · see citing works

The Role of Mitogen-Activated Protein Kinase-Activated Protein Kinases (MAPKAPKs) in Inflammation

Moens, U. L., Kostenko, S., & Sveinbjørnsson, B. (2013) · Genes · doi:10.3390/genes4020101 · Cited by 323 · see citing works

The KSEA App: a web-based tool for kinase activity inference from quantitative phosphoproteomics

Wiredja, D. D., Koyutürk, M., & Chance, M. R. (2017) · Bioinformatics · doi:10.1093/bioinformatics/btx415 · Cited by 319 · see citing works

Akt–RSK–S6 Kinase Signaling Networks Activated by Oncogenic Receptor Tyrosine Kinases

Moritz, A., Yu, L., Guo, A., Villén, J., Wang, Y., MacNeill, J., Kornhauser, J. M., Sprott, K. M., Zhou, J., Possemato, A. P., et al. (2010) · Science Signaling · doi:10.1126/scisignal.2000998 · Cited by 293 · see citing works

ERK2 but Not ERK1 Induces Epithelial-to-Mesenchymal Transformation via DEF Motif-Dependent Signaling Events

Shin, S., Dimitri, C. A., Yoon, S.-O., Dowdle, W. E., & Blenis, J. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.02.020 · Cited by 291 · see citing works

ERK1/2 Phosphorylate Raptor to Promote Ras-dependent Activation of mTOR Complex 1 (mTORC1)

Carriere, A., Romeo, Y., Acosta-Jaquez, H. A., Moreau, J., Bonneil, E., Thibault, P., Fingar, D. C., & Roux, P. P. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.159046 · Cited by 268 · see citing works

The extracellular signal-regulated kinase 1/2 pathway in neurological diseases: A potential therapeutic target (Review)

Sun, J., & Nan, G. (2017) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2017.2962 · Cited by 241 · see citing works

Integrin inactivators: balancing cellular functions in vitro and in vivo

Bouvard, D., Pouwels, J., Franceschi, N. D., & Ivaska, J. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3599 · Cited by 233 · see citing works

ERK/MAPK signalling in the developing brain: Perturbations and consequences

Iroegbu, J. D., Ijomone, O. K., Femi-Akinlosotu, O. M., & Ijomone, O. M. (2021) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2021.10.009 · Cited by 206 · see citing works

Cisplatin based therapy: the role of the mitogen activated protein kinase signaling pathway

Achkar, I. W., Abdulrahman, N., Al-Sulaiti, H., Joseph, J. M., Shahab Uddin, M. S., & Mraiche, F. (2018) · Journal of Translational Medicine · doi:10.1186/s12967-018-1471-1 · Cited by 201 · see citing works

Early activation of mTORC1 signalling in response to mechanical overload is independent of phosphoinositide 3‐kinase/Akt signalling

Miyazaki, M., McCarthy, J. J., Fedele, M. J., & Esser, K. A. (2011) · The Journal of Physiology · doi:10.1113/jphysiol.2011.205658 · Cited by 194 · see citing works

A Validated Tumorgraft Model Reveals Activity of Dovitinib Against Renal Cell Carcinoma

Sivanand, S., Peña‐Llopis, S., Zhao, H., Kucejová, B., Spence, P., Pavía-Jiménez, A., Yamasaki, T., McBride, D. J., Gillen, J. M., Wolff, N. C., et al. (2012) · Science Translational Medicine · doi:10.1126/scitranslmed.3003643 · Cited by 193 · see citing works

βTrCP- and Rsk1/2-Mediated Degradation of BimEL Inhibits Apoptosis

Dehan, E., Bassermann, F. C., Guardavaccaro, D., Vasiliver-Shamis, G., Cohen, M. S., Lowes, K. N., Dustin, M. L., Huang, D. C. S., Taunton, J., & Pagano, M. (2009) · Molecular Cell · doi:10.1016/j.molcel.2008.12.020 · Cited by 186 · see citing works

Collective and individual migration following the epithelial–mesenchymal transition

Wong, I. Y., Javaid, S., Wong, E. A., Perk, S., Haber, D. A., Toner, M., & Irimia, D. (2014) · Nature Materials · doi:10.1038/nmat4062 · Cited by 183 · see citing works

AGC protein kinases: From structural mechanism of regulation to allosteric drug development for the treatment of human diseases

Arencibia, J. M., Pastor‐Flores, D., Bauer, A. F., Schulze, J. O., & Biondi, R. M. (2013) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2013.03.010 · Cited by 181 · see citing works

Specificity of Linear Motifs That Bind to a Common Mitogen-Activated Protein Kinase Docking Groove

Garai, Á., Zeke, A., Gógl, G., Törő, I., Fördős, F., Blankenburg, H., Bárkai, T., Varga, J., Alexa, A., Emig, D., et al. (2012) · Science Signaling · doi:10.1126/scisignal.2003004 · Cited by 177 · see citing works

Myelination and mTOR

Figlia, G., Gerber, D., & Suter, U. (2018) · Glia · doi:10.1002/glia.23273 · Cited by 165 · see citing works

ERK signalling as a regulator of cell motility

Tanimura, S., & Takeda, K. (2017) · The Journal of Biochemistry · doi:10.1093/jb/mvx048 · Cited by 163 · see citing works

MAPK-Activated Protein Kinases: Servant or Partner?

Ronkina, N., & Gaestel, M. (2022) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-081720-114505 · Cited by 162 · see citing works

BRAF V600E Mutation Is Associated with mTOR Signaling Activation in Glioneuronal Tumors

Prabowo, A. S., Iyer, A. M., Veersema, T. J., Anink, J. J., Meeteren, A. Y. N. S., Spliet, W. G. M., van Rijen, P. C., Ferrier, C. H., Capper, D., Thom, M., et al. (2013) · Brain Pathology · doi:10.1111/bpa.12081 · Cited by 159 · see citing works

Chapter 10 The Primary Cilium Coordinates Signaling Pathways in Cell Cycle Control and Migration During Development and Tissue Repair

Christensen, S. T., Pedersen, S. F., Satir, P., Veland, I. R., & Schneider, L. H. (2008) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/s0070-2153(08)00810-7 · Cited by 156 · see citing works

ERK is a Pivotal Player of Chemo-Immune-Resistance in Cancer

Salaroglio, I. C., Mungo, E., Gazzano, E., Kopecka, J., & Riganti, C. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20102505 · Cited by 156 · see citing works

Bone and skeletal muscle: Key players in mechanotransduction and potential overlapping mechanisms

Goodman, C. A., Hornberger, T. A., & Robling, A. G. (2015) · Bone · doi:10.1016/j.bone.2015.04.014 · Cited by 155 · see citing works

Integrin Signaling, Cell Survival, and Anoikis: Distinctions, Differences, and Differentiation

Vachon, P. H. (2011) · Journal of Signal Transduction · doi:10.1155/2011/738137 · Cited by 154 · see citing works

Extracellular-Signal Regulated Kinase: A Central Molecule Driving Epithelial–Mesenchymal Transition in Cancer

Olea‐Flores, M., Zuñiga‐Eulogio, M. D., Catalán, M. A. M., Rodríguez-Ruiz, H. A., Castañeda-Saucedo, E., Ortuño‐Pineda, C., Padilla‐Benavides, T., & Navarro‐Tito, N. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20122885 · Cited by 149 · see citing works

The Role of mTORC1 in Regulating Protein Synthesis and Skeletal Muscle Mass in Response to Various Mechanical Stimuli

Goodman, C. A. (2013) · Reviews of physiology, biochemistry and pharmacology · doi:10.1007/112_2013_17 · Cited by 139 · see citing works

RSK3/4 mediate resistance to PI3K pathway inhibitors in breast cancer

Serra, V., Eichhorn, P. J. A., García-García, C., Ibrahim, Y. H., Prudkin, L., Sánchez, G., Rodríguez, O., Antón, P., Parra, J.-L., Marlow, S., et al. (2013) · Journal of Clinical Investigation · doi:10.1172/jci66343 · Cited by 135 · see citing works

Characterization of GSK2334470, a novel and highly specific inhibitor of PDK1

Najafov, A., Sommer, E. M., Axten, J. M., DeYoung, M. P., & Alessi, D. R. (2010) · Biochemical Journal · doi:10.1042/bj20101732 · Cited by 134 · see citing works

Secreted human glycyl-tRNA synthetase implicated in defense against ERK-activated tumorigenesis

Park, M., Kang, T., Jin, D., Han, J. M., Kim, S. B., Park, Y. J., Cho, K., Park, Y. W., Guo, M., He, W., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1200194109 · Cited by 134 · see citing works

RSK Isoforms in Cancer Cell Invasion and Metastasis

Sulzmaier, F. J., & Ramos, J. W. (2013) · Cancer Research · doi:10.1158/0008-5472.can-13-1087 · Cited by 126 · see citing works

The Role of Specific Mitogen-Activated Protein Kinase Signaling Cascades in the Regulation of Steroidogenesis

Manna, P. R., & Stocco, D. M. (2011) · Journal of Signal Transduction · doi:10.1155/2011/821615 · Cited by 126 · see citing works

The ERK signaling cascade—Views from different subcellular compartments

Yao, Z., & Seger, R. (2009) · BioFactors · doi:10.1002/biof.52 · Cited by 123 · see citing works

Reactive oxygen species (ROS) in cancer: from mechanism to therapeutic implications

Akter, S., Madhuvilakku, R., Kar, A. K., Nila, I. S., Liu, P., Inuzuka, H., Wei, W., & Hong, Y. (2026) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-026-02583-x · Cited by 119 · see citing works

Recent insights into PERK-dependent signaling from the stressed endoplasmic reticulum

McQuiston, A. S., & Diehl, J. A. (2017) · F1000Research · doi:10.12688/f1000research.12138.1 · Cited by 116 · see citing works

Evidence for mTOR pathway activation in a spectrum of epilepsy-associated pathologies

Liu, J. Y. W., Reeves, C., Michalak, Z., Coppola, A., Diehl, B., Sisodiya, S. M., & Thom, M. (2014) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-2-71 · Cited by 114 · see citing works

Defining the role of the RSK isoforms in cancer

Houlès, T., & Roux, P. P. (2017) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2017.04.016 · Cited by 113 · see citing works

Prion protein interaction with stress-inducible protein 1 enhances neuronal protein synthesis via mTOR

Roffé, M., Beraldo, F. H., Bester, R., Nunziante, M., Bach, C., Mancini, G. L., Gilch, S., Vorberg, I. M., Castilho, B. A., Martins, V. R., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1000784107 · Cited by 111 · see citing works

Global ischemia induces lysosomal-mediated degradation of mTOR and activation of autophagy in hippocampal neurons destined to die

Hwang, J.-Y., Gertner, M. J., Pontarelli, F., Court-Vazquez, B. L., Bennett, M. V. L., Ofengeim, D., & Zukin, R. S. (2016) · Cell Death and Differentiation · doi:10.1038/cdd.2016.140 · Cited by 111 · see citing works

Oxidative Stress Orchestrates MAPK and Nitric-Oxide Synthase Signal

Takata, T., Araki, S., Tsuchiya, Y., & Watanabe, Y. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21228750 · Cited by 111 · see citing works

Interplay Between pVHL and mTORC1 Pathways in Clear-Cell Renal Cell Carcinoma

Kucejová, B., Peña‐Llopis, S., Yamasaki, T., Sivanand, S., Tran, T. A. T., Alexander, S., Wolff, N. C., Lotan, Y., Xie, X.-J., Kabbani, W., et al. (2011) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-11-0302 · Cited by 110 · see citing works

Dimethyl fumarate blocks pro-inflammatory cytokine production via inhibition of TLR induced M1 and K63 ubiquitin chain formation

McGuire, V. A., Diez, T. R.-Z., Emmerich, C. H., Strickson, S., Ritorto, M. S., Sutavani, R. V., Weiβ, A., Houslay, K. F., Knebel, A., Meakin, P. J., et al. (2016) · Scientific Reports · doi:10.1038/srep31159 · Cited by 110 · see citing works

Interleukin-6-driven progranulin expression increases cholangiocarcinoma growth by an Akt-dependent mechanism

Frampton, G. A., Invernizzi, P., Bernuzzi, F., Pae, H. Y., Quinn, M. A., Horvat, D., Galindo, C., Huang, L., McMillin, M., Cooper, B., et al. (2011) · Gut · doi:10.1136/gutjnl-2011-300643 · Cited by 110 · see citing works

miR-26a and miR-384-5p are required for LTP maintenance and spine enlargement

Gu, Q.-H., Yu, D., Hu, Z., Liu, X., Yang, Y., Luo, Y., Zhu, J., & Li, Z. (2015) · Nature Communications · doi:10.1038/ncomms7789 · Cited by 109 · see citing works

Extracellular progranulin protects cortical neurons from toxic insults by activating survival signaling

Xu, J., Xilouri, M., Bruban, J., Shioi, J., Shao, Z., Papazoglou, I., Vekrellis, K., & Robakis, N. K. R. K. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.06.017 · Cited by 107 · see citing works

Phosphodiesterase-4 enzyme as a therapeutic target in neurological disorders

Bhat, A., Ray, B., Mahalakshmi, A. M., Tuladhar, S., Nandakumar, D., Srinivasan, M., Essa, M. M., Chidambaram, S. B., Guillemin, G. J., & Sakharkar, M. K. (2020) · Pharmacological Research · doi:10.1016/j.phrs.2020.105078 · Cited by 107 · see citing works

PDK1: The Major Transducer of PI 3-Kinase Actions

Bayascas, J. R. (2010) · Current topics in microbiology and immunology · doi:10.1007/82_2010_43 · Cited by 107 · see citing works

Phosphodiesterases in the Central Nervous System: Implications in Mood and Cognitive Disorders

Xu, Y., Zhang, H., & O’Donnell, J. M. (2011) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-17969-3_19 · Cited by 104 · see citing works

Prolactin-stimulated activation of ERK1/2 mitogen-activated protein kinases is controlled by PI3-kinase/Rac/PAK signaling pathway in breast cancer cells

Aksamitiene, E., Achanta, S., Kölch, W., Kholodenko, B. Ν., Hoek, J. B., & Kiyatkin, A. B. (2011) · Cellular Signalling · doi:10.1016/j.cellsig.2011.06.014 · Cited by 103 · see citing works

ESRP2 controls an adult splicing programme in hepatocytes to support postnatal liver maturation

Bhate, A., Parker, D. J., Bebee, T. W., Ahn, J., Arif, W., Rashan, E. H., Chorghade, S., Chau, A., Lee, J.-H., Anakk, S., et al. (2015) · Nature Communications · doi:10.1038/ncomms9768 · Cited by 103 · see citing works

A novel NOD1- and CagA-independent pathway of interleukin-8 induction mediated by the Helicobacter pylori type IV secretion system

Gorrell, R. J., Guan, J., Xin, Y., Tafreshi, M., Hutton, M. L., McGuckin, M. A., Ferrero, R. L., & Kwok, T. (2012) · Cellular Microbiology · doi:10.1111/cmi.12055 · Cited by 102 · see citing works

Sensitive multiplexed analysis of kinase activities and activity-based kinase identification

Kubota, K., Anjum, R., Yu, Y., Kunz, R. C., Andersen, J. N., Kraus, M., Keilhack, H., Nagashima, K., Krauss, S., Paweletz, C. P., et al. (2009) · Nature Biotechnology · doi:10.1038/nbt.1566 · Cited by 102 · see citing works

PI3K/AKT pathway activation in bladder carcinogenesis

Caldéraro, J., Rebouissou, S., de Koning, L., Masmoudi, A., Hérault, A., Dubois, T., Maillé, P., Soyeux, P., Sibony, M., TAILLE, A. D. L., et al. (2013) · International Journal of Cancer · doi:10.1002/ijc.28518 · Cited by 102 · see citing works

Diverse Roles for MAPK Signaling in Circadian Clocks

Goldsmith, C. S., & Bell‐Pedersen, D. (2013) · Advances in genetics · doi:10.1016/b978-0-12-407703-4.00001-3 · Cited by 100 · see citing works

Signaling pathways governing osteoblast proliferation, differentiation and function.

Chau, J. F. L., Leong, W. F., & Li, B. (2009) · PubMed · doi:10.14670/hh-24.1593 · Cited by 100 · see citing works

A novel sphingolipid-TORC1 pathway critically promotes postembryonic development in Caenorhabditis elegans

Zhu, H., Shen, H., Sewell, A. K., Kniazeva, M., & Han, M. (2013) · eLife · doi:10.7554/elife.00429 · Cited by 100 · see citing works

Neurotrophin-mediated dendrite-to-nucleus signaling revealed by microfluidic compartmentalization of dendrites

Cohen, M. S., Orth, C. B., Kim, H. J., Jeon, N. L., & Jaffrey, S. R. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1012401108 · Cited by 99 · see citing works

The mitogen‐activated protein kinase signaling pathways: role in megakaryocyte differentiation

Séverin, S., Ghevaert, C., & Mazharian, A. (2009) · Journal of Thrombosis and Haemostasis · doi:10.1111/j.1538-7836.2009.03658.x · Cited by 96 · see citing works

Distinct Roles of mTOR Targets S6K1 and S6K2 in Breast Cancer

Sridharan, S., & Basu, A. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21041199 · Cited by 95 · see citing works

Patient-specific Immune States before Surgery Are Strong Correlates of Surgical Recovery

Fragiadakis, G. K., Gaudilliere, B. L., Ganio, E. A., Aghaeepour, N., Tingle, M. S., Nolan, G. P., & Angst, M. S. (2015) · Anesthesiology · doi:10.1097/aln.0000000000000887 · Cited by 95 · see citing works

The role of the PI3K/Akt/mTOR pathway in glial scar formation following spinal cord injury

Chen, C., Sung, C., Huang, S., Feng, C., Hung, H.-C., Yang, S., Chen, N., Tai, M., Wen, Z., & Chen, W.-F. (2016) · Experimental Neurology · doi:10.1016/j.expneurol.2016.01.023 · Cited by 95 · see citing works

PDGFRα signaling in the primary cilium regulates NHE1-dependent fibroblast migration via coordinated differential activity of MEK1/2-ERK1/2-p90RSK and AKT signaling pathways

Clement, D. L., Mally, S., Stock, C., Lethan, M., Satir, P., Schwab, A., Pedersen, S. F., & Christensen, S. T. (2012) · Journal of Cell Science · doi:10.1242/jcs.116426 · Cited by 94 · see citing works

An siRNA screen identifies RSK1 as a key modulator of lung cancer metastasis

Lara, R., Mauri, F. A., Taylor, H., Derua, R., Shia, A., Gray, C., Nicols, A., Shiner, R. J., Schofield, E., Bates, P. A., et al. (2011) · Oncogene · doi:10.1038/onc.2011.61 · Cited by 94 · see citing works

Alteration in basal and depolarization induced transcriptional network in iPSC derived neurons from Timothy syndrome

Tian, Y., Voineagu, I., Paşca, S. P., Won, H., Chandran, V., Horvath, S., Dolmetsch, R. E., & Geschwind, D. H. (2014) · Genome Medicine · doi:10.1186/s13073-014-0075-5 · Cited by 93 · see citing works

Phosphorylation of Nur77 by the MEK-ERK-RSK Cascade Induces Mitochondrial Translocation and Apoptosis in T Cells

Wang, A., Rud, J., Olson, C. M., Anguíta, J., & Osborne, B. A. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0900894 · Cited by 93 · see citing works

Genetic Demonstration of a Redundant Role of Extracellular Signal-Regulated Kinase 1 (ERK1) and ERK2 Mitogen-Activated Protein Kinases in Promoting Fibroblast Proliferation

Voisin, L., Saba-El-Leil, M. K., Julien, C., Frémin, C., & Meloche, S. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00131-10 · Cited by 93 · see citing works

ERK reinforces actin polymerization to power persistent edge protrusion during motility

Mendoza, M. C., Vilela, M., Juarez, J. E., Blenis, J., & Danuser, G. M. (2015) · Science Signaling · doi:10.1126/scisignal.aaa8859 · Cited by 92 · see citing works

Frontier of Epilepsy Research - mTOR signaling pathway

Cho, C. (2011) · Experimental & Molecular Medicine · doi:10.3858/emm.2011.43.5.032 · Cited by 92 · see citing works

Multiple low dose therapy as an effective strategy to treat EGFR inhibitor-resistant NSCLC tumours

Neto, J. M. F., Nadal, E., Bosdriesz, E., Ooft, S., Farré, L., McLean, C. M., Klarenbeek, S., Jurgens, A. P., Hagen, H., Wang, L., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-16952-9 · Cited by 91 · see citing works

Myricetin inhibits proliferation and induces apoptosis and cell cycle arrest in gastric cancer cells

Feng, J., Chen, X., Wang, Y., Du, Y., Sun, Q., Zang, W., & Zhao, G. (2015) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-015-2492-1 · Cited by 91 · see citing works

p90 Ribosomal S6 Kinase and p70 Ribosomal S6 Kinase Link Phosphorylation of the Eukaryotic Chaperonin Containing TCP-1 to Growth Factor, Insulin, and Nutrient Signaling

Abe, Y., Yoon, S.-O., Kubota, K., Mendoza, M. C., Gygi, S. P., & Blenis, J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m900097200 · Cited by 90 · see citing works

Paclitaxel suppresses proliferation and induces apoptosis through regulation of ROS and the AKT/MAPK signaling pathway in canine mammary gland tumor cells

Ren, X., Zhao, B., Chang, H., Xiao, M., Wu, Y., & Liu, Y. (2018) · Molecular Medicine Reports · doi:10.3892/mmr.2018.8868 · Cited by 88 · see citing works

Mechanical Stimulation Induces mTOR Signaling via an ERK-Independent Mechanism: Implications for a Direct Activation of mTOR by Phosphatidic Acid

You, J. S., Frey, J. W., & Hornberger, T. A. (2012) · PLoS ONE · doi:10.1371/journal.pone.0047258 · Cited by 88 · see citing works

Chrysophanol Induces Apoptosis of Choriocarcinoma Through Regulation of ROS and the AKT and ERK1/2 Pathways

Lim, W., Yang, C., Bazer, F. W., & Song, G. (2016) · Journal of Cellular Physiology · doi:10.1002/jcp.25423 · Cited by 86 · see citing works

Elevated ERK/p90 ribosomal S6 kinase activity underlies audiogenic seizure susceptibility in fragile X mice

Sawicka, K., Pyronneau, A., Chao, M., Bennett, M. V. L., & Zukin, R. S. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1610812113 · Cited by 84 · see citing works

Seasonal Differences of Gene Expression Profiles in Song Sparrow (Melospiza melodia) Hypothalamus in Relation to Territorial Aggression

Mukai, M., Replogle, K. L., Drnevich, J. M., Wang, G., Wacker, D. W., Band, M., Clayton, D. F., & Wingfield, J. C. (2009) · PLoS ONE · doi:10.1371/journal.pone.0008182 · Cited by 84 · see citing works

Ligation of cell surface GRP78 with antibody directed against the COOH-terminal domain of GRP78 suppresses Ras/MAPK and PI 3-kinase/AKT signaling while promoting caspase activation in human prostate cancer cells

Misra, U. K., & Pizzo, S. V. (2010) · Cancer Biology & Therapy · doi:10.4161/cbt.9.2.10422 · Cited by 84 · see citing works

Role of IGF signaling in catch-up growth and accelerated temporal development in zebrafish embryos in response to oxygen availability

Kamei, H., Ding, Y., Kajimura, S., Wells, M. B., Chiang, P., & Duan, C. (2011) · Development · doi:10.1242/dev.056853 · Cited by 84 · see citing works

Activating Transcription Factor 3 Deficiency Promotes Cardiac Hypertrophy, Dysfunction, and Fibrosis Induced by Pressure Overload

Zhou, H., She, Z., Bian, Z., Zong, J., Deng, W., Zhang, Y., Guo, Y., Li, H., & Tang, Q. (2011) · PLoS ONE · doi:10.1371/journal.pone.0026744 · Cited by 84 · see citing works

Andrographolide activates the canonical Wnt signalling pathway by a mechanism that implicates the non-ATP competitive inhibition of GSK-3β: autoregulation of GSK-3βin vivo

Tapia‐Rojas, C., Schüller, A., Lindsay, C. B., Ureta, R. C., Mejías-Reyes, C., Hancke, J. L., Melo, F., & Inestrosa, N. C. (2014) · Biochemical Journal · doi:10.1042/bj20140207 · Cited by 84 · see citing works

Determining the ERK-regulated phosphoproteome driving KRAS-mutant cancer

Klomp, J. E., Diehl, J. N., Klomp, J. A., Edwards, A. C., Yang, R., Morales, A. J., Taylor, K. E., Drizyte-Miller, K., Bryant, K. L., Schaefer, A., et al. (2024) · Science · doi:10.1126/science.adk0850 · Cited by 83 · see citing works

Autophagy in Hydra: A response to starvation and stress in early animal evolution

Chera, S., Buzgariu, W., Ghila, L., & Galliot, B. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2009.03.010 · Cited by 83 · see citing works

Prothoracicotropic Hormone

Smith, W. A., & Rybczynski, R. (2011) · Elsevier eBooks · doi:10.1016/b978-0-12-384749-2.10001-9 · Cited by 83 · see citing works

Mechanism of metastasis suppression by luteolin in breast cancer

Cook, M. T. (2018) · Breast Cancer Targets and Therapy · doi:10.2147/bctt.s144202 · Cited by 82 · see citing works

Noncatalytic Function of ERK1/2 Can Promote Raf/MEK/ERK-mediated Growth Arrest Signaling

Hong, S., Yoon, S., Moelling, C., Arthan, D., & Park, J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.012591 · Cited by 82 · see citing works

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 716 · see citing works

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 379 · see citing works

The RSK factors of activating the Ras/MAPK signaling cascade

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

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