Mark W. Majewski
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View article: Synthesis and initial pharmacology of dual-targeting ligands for putative complexes of integrin αVβ3 and PAR2
Synthesis and initial pharmacology of dual-targeting ligands for putative complexes of integrin αVβ3 and PAR2 Open
The first examples of dual-targeting ligands for protease-activated receptors (PARs) and integrins are described, with potential anti-inflammatory applications.
View article: Synthesis and Initial Pharmacology of Heterobivalent Ligands Targeting Putative Complexes of Integrin αVβ3 and PAR2
Synthesis and Initial Pharmacology of Heterobivalent Ligands Targeting Putative Complexes of Integrin αVβ3 and PAR2 Open
Unpublished data from our labs led us to hypothesize that activated Protein C (aPC) may initiate an anti-inflammatory signal in endothelial cells by modulating both the integrin αVβ3 and Protease-Activated Receptor 2 (PAR2), which may exis…
View article: Synthesis and Initial Pharmacology of Heterobivalent Ligands Targeting Putative Complexes of Integrin αVβ3 and PAR2
Synthesis and Initial Pharmacology of Heterobivalent Ligands Targeting Putative Complexes of Integrin αVβ3 and PAR2 Open
Unpublished data from our labs led us to hypothesize that activated Protein C (aPC) may initiate an anti-inflammatory signal in endothelial cells by modulating both the integrin αVβ3 and Protease-Activated Receptor 2 (PAR2), which may exis…
View article: Synthesis and Initial Pharmacology of Heterobivalent Ligands Targeting Putative Complexes of Integrin αVβ3 and PAR2
Synthesis and Initial Pharmacology of Heterobivalent Ligands Targeting Putative Complexes of Integrin αVβ3 and PAR2 Open
Unpublished data from our labs led us to hypothesize that activated Protein C (aPC) may initiate an anti-inflammatory signal in endothelial cells by modulating both the integrin αVβ3 and Protease-Activated Receptor 2 (PAR2), which may exis…
View article: Design and Evaluation of Heterobivalent PAR1–PAR2 Ligands as Antagonists of Calcium Mobilization
Design and Evaluation of Heterobivalent PAR1–PAR2 Ligands as Antagonists of Calcium Mobilization Open
A novel class of bivalent ligands targeting putative protease-activated receptor (PAR) heteromers has been prepared based upon reported antagonists for the subtypes PAR1 and PAR2. Modified versions of the PAR1 antagonist RWJ-58259 containi…
View article: Design and Evaluation of Heterobivalent PAR1–PAR2 Ligands as Antagonists of Calcium Mobilization
Design and Evaluation of Heterobivalent PAR1–PAR2 Ligands as Antagonists of Calcium Mobilization Open
A novel class of bivalent ligands targeting putative Protease-Activated Receptor (PAR) heteromers has been prepared based upon reported antagonists for the subtypes PAR1 and PAR2. Modified versions of the PAR1 antagonist RWJ-58259 containi…
View article: NMR spectra and LC-MS traces for: Characterization of Protease-Activated Receptor (PAR) ligands: Parmodulins are reversible allosteric inhibitors of PAR1-driven calcium mobilization in endothelial cells
NMR spectra and LC-MS traces for: Characterization of Protease-Activated Receptor (PAR) ligands: Parmodulins are reversible allosteric inhibitors of PAR1-driven calcium mobilization in endothelial cells Open
NMR spectra and LC-MS traces
View article: Characterization of Protease-Activated Receptor (PAR) Ligands: Parmodulins Are Reversible Allosteric Inhibitors of PAR1-Driven Calcium Mobilization in Endothelial Cells
Characterization of Protease-Activated Receptor (PAR) Ligands: Parmodulins Are Reversible Allosteric Inhibitors of PAR1-Driven Calcium Mobilization in Endothelial Cells Open
We report a detailed protocol for an intracellular calcium mobilization assay with adherent endothelial cells in multiwell plates that was used to study a number of different PAR1 and PAR2 ligands, including an alkynylated version of the P…
View article: Characterization of Protease-Activated Receptor (PAR) Ligands: Parmodulins Are Reversible Allosteric Inhibitors of PAR1-Driven Calcium Mobilization in Endothelial Cells
Characterization of Protease-Activated Receptor (PAR) Ligands: Parmodulins Are Reversible Allosteric Inhibitors of PAR1-Driven Calcium Mobilization in Endothelial Cells Open
We report a detailed protocol for an intracellular calcium mobilization assay with adherent endothelial cells in multiwell plates that was used to study a number of different PAR1 and PAR2 ligands, including an alkynylated version of the P…
View article: Design and Evaluation of Heterobivalent PAR1–PAR2 Ligands as Antagonists of Calcium Mobilization
Design and Evaluation of Heterobivalent PAR1–PAR2 Ligands as Antagonists of Calcium Mobilization Open
A novel class of bivalent ligands targeting putative Protease-Activated Receptor (PAR) heteromers has been prepared based upon reported antagonists for the subtypes PAR1 and PAR2. Modified versions of the PAR1 antagonist RWJ-58259 containi…
View article: CCDC 1838066: Experimental Crystal Structure Determination
CCDC 1838066: Experimental Crystal Structure Determination Open
An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available …
View article: CCDC 1528792: Experimental Crystal Structure Determination
CCDC 1528792: Experimental Crystal Structure Determination Open
An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available …