Gordon Todderud
Bristol-Myers Squibb
13 Papers
240 Citations
Gordon Todderud is an academic researcher from Bristol-Myers Squibb. The author has contributed to research in topics: Ligand (biochemistry) & Selectin. The author has an hindex of 11, co-authored 13 publications.
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Papers
Synthesis and SAR of p38α MAP kinase inhibitors based on heterobicyclic scaffolds
T. G. Murali Dhar,Stephen T. Wrobleski,Shuqun Lin,Joseph A. Furch,David S. Nirschl,Yi Fan,Gordon Todderud,Sidney Pitt,Arthur M. Doweyko,John S. Sack,Arvind Mathur,Murray McKinnon,Joel C. Barrish,John H. Dodd,Gary L. Schieven,Katerina Leftheris +15 more
TL;DR: The synthesis and structure-activity relationships (SAR) of p38alpha MAP kinase inhibitors based on heterobicyclic scaffolds and x-ray co-crystallography of an oxalamide analog bound to unphosphorylated p37alpha led to the identification of compound (21) as a potent inhibitor of p 38alphaMAP kinase with good cellular potency toward the inhibition of TNF-alpha production.
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Phosphorylation and calcium influx are not sufficient for the activation of cytosolic phospholipase A2 in U937 cells: Requirement for a Giα-type G-protein
James R. Burke,Lynda B. Davern,Kurt R. Gregor,Gordon Todderud,Julie Alford,Kenneth M. Tramposch +5 more
TL;DR: It is demonstrated that activation of a pertussis toxin-sensitive Gi alpha-type G-protein is required as evidenced by the production of arachidonate in undifferentiated cells stimulated with mastoparan, an activator of Gi alpha subunits, in combination with ionomycin.
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Temporal infiltration of leukocyte subsets into mouse skin inflamed with phorbol ester
TL;DR: The identification of specific cell types and their time course of infiltration is consistent with the development of a chronic inflammatory lesion.
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PMN binding to P‐selectin is inhibited by sulfatide
TL;DR: It is demonstrated that the presence of sulfatide in the P‐selectin–PMN adhesion assay inhibits binding in a dose‐dependent manner.
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De novo design, synthesis, and in vitro activity of LFA-1 antagonists based on a bicyclic[5.5]hydantoin scaffold.
Dominique Potin,Michele Launay,Eric Nicolai,Maud Fabreguette,Patrice Malabre,Francois Caussade,Dominique Besse,Stacey Skala,Dawn K. Stetsko,Gordon Todderud,Brett R. Beno,Daniel L. Cheney,ChiehYing J. Chang,Steven Sheriff,Diane Hollenbaugh,Joel C. Barrish,Edwin J. Iwanowicz,Suzanne J. Suchard,T. G. Murali Dhar +18 more
TL;DR: The de novo design, synthesis and in vitro activity of LFA-1 antagonists based on a bicyclic[5.5]hydantoin scaffold are described, providing support for L FA-1 as a target in several different inflammatory diseases.
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