George Thomas

The principal target of rapamycin‐induced p70s6k inactivation is a novel phosphorylation site within a conserved hydrophobic domain.

R. Pearson, G. Thomas, S. Kozma, 1995, The EMBO journal.

p70s6k/p85s6k: mechanism of activation and role in mitogenesis.

G. Thomas, S. Kozma, George Thomas, 1994, Seminars in cancer biology.

S6 phosphorylation and the p70s6k/p85s6k.

S. Ferrari, G. Thomas, George Thomas, 1994, Critical reviews in biochemistry and molecular biology.

Dual requirement for a newly identified phosphorylation site in p70s6k

R. Pearson, G. Thomas, S. Kozma, 1997, Molecular and Cellular Biology.

The immunosuppressant rapamycin induces inactivation of p70s6k through dephosphorylation of a novel set of sites.

M. Siegmann, R. Pearson, S. Ferrari, 1993, The Journal of biological chemistry.

Serine/threonine kinases in the propagation of the early mitogenic response.

S. Kozma, G. Thomas, George Thomas, 1992, Reviews of physiology, biochemistry and pharmacology.

The Drosophila p70s6k homolog exhibits conserved regulatory elements and rapamycin sensitivity.

G. Thomas, S. Kozma, C. O. Berry, 1996, Proceedings of the National Academy of Sciences of the United States of America.

Activation of p70s6k is associated with phosphorylation of four clustered sites displaying Ser/Thr-Pro motifs.

S. Ferrari, G. Thomas, S. Morley, 1992, Proceedings of the National Academy of Sciences of the United States of America.