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European Journal of Immunology|December 1, 1993
Activation of MAP kinases, pp90rsk and pp70-S6 kinases in mouse mast cells by signaling through the c-kit receptor tyrosine kinase or Fc epsilon RI: rapamycin inhibits activation of pp70-S6 kinase and proliferation in mouse mast cellsM Tsai, R H Chen, S Y Tam, et al.
Oncogene|September 22, 1999
Characterization of S6K2, a novel kinase homologous to S6K1K K Lee-Fruman, C J Kuo, J Lippincott, et al.
The Journal of Biological Chemistry|June 5, 1993
Failure of rapamycin to block proliferation once resting cells have entered the cell cycle despite inactivation of p70 S6 kinaseN Terada, R A Franklin, J J Lucas, et al.
Proceedings of the National Academy of Sciences of the United States of America|May 1, 1988
A Xenopus ribosomal protein S6 kinase has two apparent kinase domains that are each similar to distinct protein kinasesS W Jones, E Erikson, J Blenis, et al.
The Journal of Biological Chemistry|December 8, 2000
Ribosomal S6 kinase 2 inhibition by a potent C-terminal repressor domain is relieved by mitogen-activated protein-extracellular signal-regulated kinase kinase-regulated phosphorylationK A Martin, S S Schalm, A Romanelli, et al.
Neuron|April 10, 1999
Caspase-8 is required for cell death induced by expanded polyglutamine repeatsI Sánchez, C J Xu, P Juo, et al.
Molecular and Cellular Biology|June 1, 1995
Interleukin-2 triggers a novel phosphatidylinositol 3-kinase-dependent MEK activation pathwayL M Karnitz, L A Burns, S L Sutor, et al.
Molecular Endocrinology (Baltimore, Md.)|August 1, 1993
Functional domains and phosphorylation of the orphan receptor Nur77I J Davis, T G Hazel, R H Chen, et al.
Molecular and Cellular Biology|July 1, 1994
Phosphatidylinositol 3-kinase activation is required for insulin stimulation of pp70 S6 kinase, DNA synthesis, and glucose transporter translocationB Cheatham, C J Vlahos, L Cheatham, et al.
Oncogene|May 23, 2006
Rapamycin inhibits cell motility by suppression of mTOR-mediated S6K1 and 4E-BP1 pathwaysL Liu, F Li, J A Cardelli, et al.
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