Laurie Louise Parker
Ph.D. Synthetic Organic Chemistry, 2003, University of Glasgow, Scotland (Prof. David Robins)
B.A. Chemistry, 2000, University of St. Thomas, St. Paul, MN
My research interests center on using chemical biology and proteomics to develop biosensors for intracellular phosphorylation signaling. We will use synthetic peptide and protein chemistry to design and synthesize probes for multiplexed analysis of cancer-related signaling proteins e.g. Abl, other Src-family kinases, receptor tyrosine kinases, etc. We will explore a wide variety of multidisciplinary analytical methods including mass spectrometry, fluorescence microscopy and flow cytometry to develop novel techniques for monitoring these signaling proteins and their activities. Our technology development goals will lead us to new methods for asking increasingly complex questions about multiple signaling activities, their disruption in cancer, and response of signaling profiles to cancer treatment.
Co-instructor for MCMP 204 Organic Chemistry I (with Prof. Marc Loudon).
2013 ABSCIEX Young Investigator Award (with Mark Hall)
2011-2013: R21CA160129 NIH/NCI Application of Emerging Technologies to Cancer Research
2011-2014: R21CA157395 NIH/NCI Innovative Technology Development for Cancer Research (Parker, PI/Irudayaraj, Co-PI)
2011-2012: ICTSI Core Pilot Grant
2010-2013: R00CA127161 NIH/NCI Pathway to Independence Award (R00 Phase)
2009-2011: ICTSI Project Development Team funding support
2009-2010: DOD/CDMRP Breast Cancer Concept Award (Parker, PI/Irudayaraj, Co-PI)
2009-2010: Showalter Trust Grant (Parker, PI/Rochet, Co-PI)
Martin VA, Wang WH, Lipchik AM, Parker LL, He Y, Zhang S, Zhang ZY, Geahlen RL, “Akt2 inhibits the activation of NFAT in lymphocytes by modulating calcium release from intracellular stores” Cell Cycle, 24(5):1064-73 (2012)
Bremmer SC, Hall H, Martinez JS, Eissler CL, Hinrichsen TH, Rossie S, Parker LL, Hall MC, Charbonneau H, “Cdc14 phosphatases preferentially dephosphorylate a subset of cyclin-dependent kinase (Cdk) sites containing phosphoserine” J. Biol. Chem., 287(3):1662-9 (2012)
Eissler, CL, Bremmer, SC, Martinez, JS, Parker, LL, Charbonneau, H and Hall, MC, “A general strategy for studying multisite protein phosphorylation using label-free selected reaction monitoring mass spectrometry” Analytical Biochemistry, 418(2):267-75
Placzek EA, Plebanek MP, Lipchik AM, Kidd SR, Parker LL, “A peptide biosensor for detecting intracellular Abl kinase activity using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry” Analytical Biochemistry, 397:73-8 (2010)
Parker, L. L. and Kron, S. J. Kinase activation in circulating cells: Opportunities for diagnosis and therapeutic monitoring, Expert Opinion on Medical Diagnostics, 2, 33 (2008).
Parker, L. L., Engel-Hall, A., Drew, K., Steinhardt, G., Helseth, D. L., Jabon, D., McMurry, T., Angulo, D. S., and Kron, S. J. Investigating quantitation of phosphorylation using MALDI-TOF mass spectrometry, Journal of Mass Spectrometry, 43, 518 (2008).
Parker, L. L., Kurutz, J., Kent, S. B. H., Kron, S. J. Control of the yeast cell cycle with a photocleavable alpha-factor analog, Angewandte Chemie International Edition, 45, 6322-25 (2006). Featured in Nature, Research Highlights, 443, 374 (2006) and ACS Chemical Biology, Spotlight, 9, 545 (2006)
Parker, L. L., Brueggemeier, S. B., Rhee, W. J., Wu, D., Kent, S. B. H., Kron, S. J. and Palecek S. P. Photocleavable peptide hydrogel arrays for MALDI-TOF analysis of kinase activity, The Analyst, 151, 1097-1104 (2006)
Parker, L. L., Kron, S. J., Kent, S. B. Optimizing thiophosphorylation in the presence of competing phosphorylation with MALDI-TOF-MS detection, Journal of Proteome Research, 4, 1863-66 (2005).
Parker, L. L., Lacy, S. M., Farrugia, L. J., Evans, C., Robins, D. J., O'Hare, C. C., Hartley, J. A., Jaffar, M., Stratford, I. J. A novel design strategy for stable metal complexes of nitrogen mustards as bioreductive prodrugs. Journal of Medicinal Chemistry, 47, 5683-89 (2004).