J. V. Veetil
Affiliations: | NIAAA | National Institutes of Health, Bethesda, MD |
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Publications
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| Sarkar P, Davis KA, Puhl HL, et al. (2017) Deciphering CaMKII Multimerization Using Fluorescence Correlation Spectroscopy and Homo-FRET Analysis. Biophysical Journal. 112: 1270-1281 |
| Sarkar P, Veetil JV, Davis K, et al. (2016) Deciphering CaMKII Multimerization using Holoenzyme Assembly Mutants, FCS, and Concurrent Homo- and Hetero-FRET Analysis Biophysical Journal. 110: 217a |
| Nguyen TA, Sarkar P, Veetil JV, et al. (2015) Covert Changes in CaMKII Holoenzyme Structure Identified for Activation and Subsequent Interactions. Biophysical Journal. 108: 2158-70 |
| Veetil JV, Davis K, Puhl HL, et al. (2014) Characterization of Calcium-Calmodulin Kinase II Inhibitor Protein (CaMKIIN) by Fluorescence Polarization and Fluctuation Analysis Biophysical Journal. 106: 679a-680a |
| Sarkar P, Davis K, Puhl HL, et al. (2014) Positive Cooperativity and T286 Autophosphorylation is Observed in a Dimeric Mutant of Calcium-Calmodulin Dependent Protein Kinase II (CaMKII) Biophysical Journal. 106: 679a |
| Nguyen TA, Veetil JV, Sarkar P, et al. (2014) Fluorescence Polarization and Fluctuation Analysis Reveals Covert Changes in CaMKII Holoenzyme Organization Triggered by Calmodulin and Camkiintide Biophysical Journal. 106: 679a |
| Nguyen TA, Sarkar P, Veetil JV, et al. (2013) Fluorescence Polarization and Fluctuation Analysis Reveals CAMKIIα Catalytic Domain Pair Extension Triggered by Ca2+/Calmodulin Biophysical Journal. 104: 99a-100a |
| Veetil JV, Sarkar P, Nguyen TA, et al. (2013) CAMKIIα Catalytic Domain Dimerization is Regulated through T-Site Interactions Biophysical Journal. 104: 99a |
| Sarkar P, Davis K, Nguyen TA, et al. (2013) Reducing the Number of Subunits in the CAMKIIα Holoenzyme Alters Catalytic Domain Pairing, Diffusion Time, and T286 Autophosphorylation Biophysical Journal. 104: 99a |
| Nguyen TA, Sarkar P, Veetil JV, et al. (2012) Fluorescence polarization and fluctuation analysis monitors subunit proximity, stoichiometry, and protein complex hydrodynamics. Plos One. 7: e38209 |