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

Name: 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
Creator: Chris Dockendorff
Published: 2018-04-20T12:10:46.039Z
Keywords: Organic Chemistry, Pharmaceutical Chemistry

Dockendorff, Chris; Greve, Eric; Gandhi, Disha; Foster, Trevor; Kentala, Kaitlin; Majewski, Mark; Rosas, Jr., Ricardo

doi:10.17632/xsmxzgbh4t.1

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

Published: 20 April 2018| Version 1 | DOI: 10.17632/xsmxzgbh4t.1

Contributors:

Chris Dockendorff, Eric Greve, Disha Gandhi, Trevor Foster, Kaitlin Kentala, Mark Majewski, Ricardo Rosas, Jr.

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NMR spectra and LC-MS traces

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

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