D-Index & Metrics Best Publications

D-Index & Metrics D-index (Discipline H-index) only includes papers and citation values for an examined discipline in contrast to General H-index which accounts for publications across all disciplines.

Discipline name D-index D-index (Discipline H-index) only includes papers and citation values for an examined discipline in contrast to General H-index which accounts for publications across all disciplines. Citations Publications World Ranking National Ranking
Biology and Biochemistry D-index 92 Citations 37,593 219 World Ranking 1406 National Ranking 826

Research.com Recognitions

Awards & Achievements

2016 - Fellow of the Royal Society, United Kingdom

Overview

What is he best known for?

The fields of study he is best known for:

  • Gene
  • Amino acid
  • Cell membrane

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.

His most cited work include:

  • Cell signaling by receptor-tyrosine kinases (5690 citations)
  • Membrane recognition by phospholipid-binding domains. (1109 citations)
  • An Open-and-Shut Case? Recent Insights into the Activation of EGF/ErbB Receptors (748 citations)

What are the main themes of his work throughout his whole career to date?

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.

He most often published in these fields:

  • Cell biology (53.40%)
  • Biochemistry (32.04%)
  • Pleckstrin homology domain (24.76%)

What were the highlights of his more recent work (between 2014-2021)?

  • Cell biology (53.40%)
  • Receptor (24.76%)
  • Cancer research (13.11%)

In recent papers he was focusing on the following fields of study:

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.

Between 2014 and 2021, his most popular works were:

  • EGFR Ligands Differentially Stabilize Receptor Dimers to Specify Signaling Kinetics. (114 citations)
  • EGFR Ligands Differentially Stabilize Receptor Dimers to Specify Signaling Kinetics. (114 citations)
  • The ALK/ROS1 inhibitor PF-06463922 overcomes primary resistance to crizotinib in ALK-driven neuroblastoma (90 citations)

In his most recent research, the most cited papers focused on:

  • Gene
  • Amino acid
  • Cell membrane

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.

This overview was generated by a machine learning system which analysed the scientist’s body of work. If you have any feedback, you can contact us here.

Best Publications

Cell signaling by receptor-tyrosine kinases

Mark A. Lemmon;Joseph Schlessinger.
Cell (2000)

6405 Citations

Membrane recognition by phospholipid-binding domains.

Mark A. Lemmon.
Nature Reviews Molecular Cell Biology (2008)

1631 Citations

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)

1204 Citations

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)

1022 Citations

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

Mark A. Lemmon;Kathryn M. Ferguson.
Biochemical Journal (2000)

986 Citations

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)

860 Citations

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)

760 Citations

Phosphoinositide Recognition Domains

Mark A. Lemmon.
Traffic (2003)

752 Citations

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)

723 Citations

Regulation of signal transduction and signal diversity by receptor oligomerization.

Mark A. Lemmon;Joseph Schlessinger.
Trends in Biochemical Sciences (1994)

707 Citations

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