Mark A. Lemmon

EGF Activates Its Receptor by Removing Interactions that Autoinhibit Ectodomain Dimerization

Kathryn M. Ferguson, Mitchell B. Berger, Jeannine M. Mendrola et al. · Molecular Cell · 2003 · 801 citations · Full text

Signal Transduction, Developmental Biology, Signaling Pathway +6

Signal-dependent membrane targeting by pleckstrin homology (PH) domains

Mark A. Lemmon, Kathryn M. Ferguson · Biochemical Journal · 2000 · 707 citations · Full text

Pleckstrin Homology, Proteinlipid Interaction, Signal Transduction +15

Heparin-induced oligomerization of FGF molecules is responsible for FGF receptor dimerization, activation, and cell proliferation

Taly R. Spivak-Kroizman, Mark A. Lemmon, John E. Ladbury et al. · Cell · 1994 · 662 citations

Developmental Biology, Signal Transduction, Signaling Pathway +11

Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain

Kathryn M. Ferguson, Mark A. Lemmon, Joseph Schlessinger et al. · Cell · 1995 · 598 citations · Full text

Specific and high-affinity binding of inositol phosphates to an isolated pleckstrin homology domain.

Mark A. Lemmon, K M Ferguson, Ronan O’Brien et al. · Proceedings of the National Academy of Sciences · 1995 · 574 citations · Full text