2016 - Fellow of the Royal Society, United Kingdom
Mark A. Lemmon mainly focuses on Biochemistry, Pleckstrin homology domain, Cell biology, Protein structure and Signal transduction. His Pleckstrin homology domain research integrates issues from Amino acid, Phosphotyrosine-binding domain, Phosphatidylinositol and Binding site. His Cell biology research incorporates themes from Receptor and Cytoskeleton.
His Protein structure research is multidisciplinary, incorporating perspectives in EVH1 domain, Peptide sequence, Dynamin, Biophysics and Protein folding. Mark A. Lemmon interconnects ROR1, Platelet-derived growth factor receptor, Cell surface receptor and Enzyme-linked receptor in the investigation of issues within Receptor tyrosine kinase. As part of the same scientific family, he usually focuses on Platelet-derived growth factor receptor, concentrating on JAK-STAT signaling pathway and intersecting with Receptor Protein-Tyrosine Kinases.
Mark A. Lemmon spends much of his time researching Cell biology, Biochemistry, Pleckstrin homology domain, Receptor and Receptor tyrosine kinase. His Cell biology research is multidisciplinary, incorporating elements of Allosteric regulation and Epidermal growth factor receptor. His research investigates the connection between Biochemistry and topics such as Biophysics that intersect with issues in Transmembrane protein, Integral membrane protein and Transmembrane domain.
His Pleckstrin homology domain research incorporates elements of Amino acid, Guanine nucleotide exchange factor, GTPase, Dynamin and Phosphatidylinositol. His research integrates issues of Extracellular and Cell growth in his study of Receptor. The concepts of his Receptor tyrosine kinase study are interwoven with issues in Tropomyosin receptor kinase C, Proto-oncogene tyrosine-protein kinase Src, ROR1, Autophosphorylation and ErbB.
Cell biology, Receptor, Cancer research, Receptor tyrosine kinase and Kinase are his primary areas of study. His research in Cell biology intersects with topics in Cell surface receptor and Allosteric regulation. His Receptor study which covers T cell that intersects with Phosphatidylserine.
His Cancer research research is multidisciplinary, relying on both Mutation, Tyrosine kinase, ROS1, Osimertinib and Drug. Biochemistry covers Mark A. Lemmon research in Receptor tyrosine kinase. His study in Cell signaling is interdisciplinary in nature, drawing from both ROR1, Protein structure and PTK7.
The scientist’s investigation covers issues in Cell biology, Receptor, Receptor tyrosine kinase, Kinase and Biochemistry. His work on Frizzled is typically connected to Acylation as part of general Cell biology study, connecting several disciplines of science. His Receptor study combines topics from a wide range of disciplines, such as Extracellular and Cell signaling.
His Cell signaling study incorporates themes from Epidermal growth factor receptor and Functional selectivity. His biological study spans a wide range of topics, including Phospholipid Binding, Mutagenesis, Vesicle, Yeast and Protein kinase domain. His work on Binding site, Inositol phosphate and Phospholipid as part of general Biochemistry study is frequently linked to BAR domain, bridging the gap between disciplines.
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Cell signaling by receptor-tyrosine kinases
Mark A. Lemmon;Joseph Schlessinger.
Cell (2000)
Membrane recognition by phospholipid-binding domains.
Mark A. Lemmon.
Nature Reviews Molecular Cell Biology (2008)
An Open-and-Shut Case? Recent Insights into the Activation of EGF/ErbB Receptors
Antony W. Burgess;Hyun Soo Cho;Hyun Soo Cho;Charles Eigenbrot;Kathryn M. Ferguson.
Molecular Cell (2003)
EGF Activates Its Receptor by Removing Interactions that Autoinhibit Ectodomain Dimerization
Kathryn M. Ferguson;Mitchell B. Berger;Jeannine M. Mendrola;Hyun Soo Cho.
Molecular Cell (2003)
Signal-dependent membrane targeting by pleckstrin homology (PH) domains
Mark A. Lemmon;Kathryn M. Ferguson.
Biochemical Journal (2000)
Heparin-induced oligomerization of FGF molecules is responsible for FGF receptor dimerization, activation, and cell proliferation.
T. Spivak-Kroizman;M.A. Lemmon;I. Dikic;J.E. Ladbury.
Cell (1994)
Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain
Kathryn M. Ferguson;Mark A. Lemmon;Joseph Schlessinger;Paul B. Sigler.
Cell (1995)
Phosphoinositide Recognition Domains
Mark A. Lemmon.
Traffic (2003)
Activation of phospholipase Cγ by PI 3‐kinase‐induced PH domain‐mediated membrane targeting
M. Falasca;S.K. Logan;V.P. Lehto;G. Baccante.
The EMBO Journal (1998)
Regulation of signal transduction and signal diversity by receptor oligomerization.
Mark A. Lemmon;Joseph Schlessinger.
Trends in Biochemical Sciences (1994)
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