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Scientific Reports|June 4, 2020
A Simple and Scalable Strategy for Analysis of Endogenous Protein DynamicsMarie K Schwinn, Leta S Steffen, Kris Zimmerman, et al.
Cell Chemical Biology|July 31, 2018
Real-Time Ligand Binding of Fluorescent VEGF-A Isoforms that Discriminate between VEGFR2 and NRP1 in Living CellsChloe J Peach, Laura E Kilpatrick, Rachel Friedman-Ohana, et al.
The Journal of Biological Chemistry|February 29, 2020
The luminescent HiBiT peptide enables selective quantitation of G protein-coupled receptor ligand engagement and internalization in living cellsMichelle E Boursier, Sergiy Levin, Kris Zimmerman, et al.
ACS Chemical Biology|May 27, 2015
NanoBRET--A Novel BRET Platform for the Analysis of Protein-Protein InteractionsThomas Machleidt, Carolyn C Woodroofe, Marie K Schwinn, et al.
ACS Chemical Biology|September 12, 2017
CRISPR-Mediated Tagging of Endogenous Proteins with a Luminescent PeptideMarie K Schwinn, Thomas Machleidt, Kris Zimmerman, et al.
ACS Chemical Biology|September 22, 2011
A luminescent biosensor with increased dynamic range for intracellular cAMPBrock F Binkowski, Braeden L Butler, Peter F Stecha, et al.
ACS Chemical Biology|July 12, 2015
Deciphering the Cellular Targets of Bioactive Compounds Using a Chloroalkane Capture TagRachel Friedman Ohana, Thomas A Kirkland, Carolyn C Woodroofe, et al.
ACS Chemical Biology|July 15, 2016
Improved Deconvolution of Protein Targets for Bioactive Compounds Using a Palladium Cleavable Chloroalkane Capture TagRachel Friedman Ohana, Sergiy Levin, Monika G Wood, et al.
Biochemical Pharmacology|April 11, 2017
Real-time analysis of the binding of fluorescent VEGF<sub>165</sub>a to VEGFR2 in living cells: Effect of receptor tyrosine kinase inhibitors and fate of internalized agonist-receptor complexesLaura E Kilpatrick, Rachel Friedman-Ohana, Diana C Alcobia, et al.
ACS Chemical Biology|November 17, 2015
NanoLuc Complementation Reporter Optimized for Accurate Measurement of Protein Interactions in CellsAndrew S Dixon, Marie K Schwinn, Mary P Hall, et al.
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