University of Iowa
Department of Biochemistry
4-403 BSB
Iowa City, IA 52242-1109 USA phone: 877-846-8569
or 319-335-7932
fax: (319) 335-9570
biochem@uiowa.edu
Department of Biochemistry
4-403 BSB
Iowa City, IA 52242-1109 USA phone: 877-846-8569
or 319-335-7932
fax: (319) 335-9570
biochem@uiowa.edu
Department of Biochemistry
Recent Publications :: Madeline Shea
- Erickson, J.R., Joiner, M.L., Guan X., Kutschke, W., Wang, J., Oddis, C.V., Bartlett, R.K., Lowe, J.S., O'Donnell, S., Aykin-Burns, N., Zimmerman, M.C., Zimmerman, K., Ham, A.L., Weiss, R.M., Spitz, D.R., Shea, M.A., Colbran, R.J., Mohler, P.J., Anderson, M. (2008) Direct Oxidation Results in Ca2+ Independent Activation of CaMKII Cell (accepted, January 28).
- Theoharis, N.T., Sorensen, B.R., Shea, M.A. (2008) Neuronal Voltage–Dependent Sodium Channel Type II (NaV1.2) IQ Motif Lowers Calcium Affinity of the C–domain of Calmodulin Biochemistry 47: 112-123 (http://dx.doi.org/10.1021/bi7013129) (12 pp)
- Newman, R.A., VanScyoc, W.S., Jaren, O.R., and Shea, M.A. (2007) Domain-Specific Interactions of Calmodulin with Melittin: Peptide Docks with the C-domain of Apo CaM but Preferentially Increases Calcium Binding Affinity of the N-domain. (in press, Proteins: Structure, Function, Bioinformatics). (http://dx.doi.org/10.1002/prot.21861) (21 pp)
- Akyol, Z., Gakhar, L., Sorensen, B.R., Hell, J.W., and Shea, M.A. (2007) The NMDA Receptor NR1 C1 Region Bound to Calmodulin: Structural Insights into Functional Differences between Homologous Domains. (PDB entry: 2HQW) Structure 15: 1603-1617 (http://dx.doi.org/10.1016/j.str.2007.10.012) (15 pp)
- Li, Q., Cooper, J.J., Altwerger, G.H., Feldkamp, M.D., Shea, M.A., and Price, D.P. (2007) HEXIM1 is a promiscuous double-stranded RNA-binding protein and interacts with RNAs in addition to 7SK in cultured cells. Nucleic Acids Research 35: 2503–2512. (http://dx.doi.org/10.1093/nar/gkm150) (10 pp)
- Merrill, M.A., Malik, Z., Akyol, Z., Bartos, J.A., Leonard, A.S., Hudmon, A., Shea, M.A. and Hell, J.W. (2007) Displacement of a-Actinin from the NMDA Receptor NR1 C0 Domain by Ca2+/Calmodulin Promotes CaMKII Binding. Biochemistry 46:8485-97 (http://dx.doi.org/10.1021/bi0623025) (13 pp)
- VanScyoc, W.S., Newman, R.A., Sorensen, B.R., Shea, M.A. (2006) Calcium Binding to Paramecium Calmodulin Mutants Having Domain–Specific Effects on Regulation of Ion Channels. Biochemistry 45: 14311-14324 (http://dx.doi.org/10.1021/bi061134d) (14 pp)
- Ross JBA, Laws W, Shea M. (2006) Intrinsic Fluorescence in Protein Structure Analysis. in Protein Structures: Methods in Protein Structure and Structure Analysis: Luinescence Spectroscopy and Circular Dichroism, Eds. VN Uversky, EA Permyakov, Nova Science Publishers, Inc., New York. 55-72 ISBN 1600214045 (http://www.vanstockum.nl/product/7188809/Methods-In-Protein-Structure-And-Stability-Analysis.html) (18 pp)
- Wang, B., Martin, S.R, Newman, R.A., Hamilton, S.L., Shea, M.A., Bayley, P.M., and Beckingham, K. (2004) Biochemical properties of V91G calmodulin: A calmodulin point mutation that deregulates muscle contraction in Drosophila. Protein Science 13 3285-3297 (http://dx.doi.org/10.1110/ps.04928204) (13 pp)
- Hines, R., Sorensen, B.R., Shea, M.A., Maury, W. (2004) PU.1 Binding to ets Motifs within the Equine Infectious Anemia Virus Long Terminal Repeat (LTR) Enhancer: Regulation of LTR Activity and Virus Replication in Macrophages J. Virology 78: 3407–3418. (http://dx.doi.org/10.1128/JVI.78.7.3407-3418.2004) (12 pp)
- Akyol, Z., Bartos, J., Jaren, O.R., Faga, L., Shea, M.A. and Hell, J. (2004) Apo-Calmodulin Binds with its COOH-terminal Domain to the N-methyl-D-aspartate Receptor NR1 C0 Region J. Biol. Chem. 279(3): 2166-2175. (http://dx.doi.org/10.1074/jbc.M302542200 (10 pp)
- Faga, L.A., Sorensen, B.R., VanScyoc, W.S., and Shea, M.A. (2003) Basic Interdomain Boundary Residues in Calmodulin Decrease Calcium Affinity of Sites I and II by Stabilizing Helix-Helix Interactions Proteins: Structure, Function & Genetics 50: 381-391. (http://dx.doi.org/10.1002/prot.10281) (11 pp)
- Leonard, A.S., Bayer, K-U, Merrill, M., Shea, M.A., Schulman, H., and Hell, J.W. (2002) Regulation of CaMKII Docking to NMDA Receptors by Calcium/Calmodulin and a-Actinin J. Biol. Chem. 277: 48441-48448 (http://dx.doi.org/10.1074/jbc.M205164200) (8 pp)
- Jaren, O.R., Kranz, J.K., Sorensen, B.R., Wand, A.J., Shea, M.A. (2002) Calcium-Induced Conformational Switching of Paramecium Calmodulin: Changes in the Protein Backbone Observed by Heteronuclear NMR Studies. Biochemistry 41: 14158-14166. (http://dx.doi.org/10.1021/bi026340+) (9 pp)
- VanScyoc, W.S., Sorensen, B.R., Rusinova, E., Laws, W., Ross, J.B.A., and Shea, M.A. (2002) Domain-Specific Fluorescence of Calmodulin: Phenylalanine Reports Exclusively on Calcium Binding to the N-Domain Biophysical Journal 83: 2767-2790. (http://dx.doi.org/10.1529/biophysj.102 (24 pp)
- Xiong, L-W, Newman, R.A., Rodney, G.C., Thomas, O., Zhang, J-Z, Persechini, A., Shea, M.A., and Hamilton, S.L. (2002) Lobe Dependent Regulation of Ryanodine Receptor Type One by Calmodulin J. Biol. Chem. 277:40862–40870. (http://dx.doi.org/10.1074/jbc.M206763200) (9 pp)
- Sorensen, B.R., Faga, L.A., Hultman, R., Shea, M.A. (2002) Interdomain Linker Increases Thermostability and Decreases Calcium Affinity of Calmodulin N-Domain. Biochemistry 41: 15-20. (http://dx.doi.org/10.1021/bi011718+) (6 pp)
- Sun, H., Yin, D., Coffeen, L.A., Shea, M.A., and Squier, T.C. (2001) Mutation of Tyr138 Disrupts the Structural Coupling Between the Opposing Domains in Vertebrate Calmodulin. Biochemistry 40:9605-9617. (http://dx.doi.org/10.1021/bi0104266) (13 pp)
- VanScyoc, W. and Shea, M.A. (2001) Phenylalanine fluorescence studies of calcium binding to N-domain fragments of Paramecium calmodulin mutants show increased calcium affinity correlates with increased disorder. Protein Science 10:1758-1768. (http://dx.doi.org/10.1110/ps.11601) (11 pp)
- Sorensen, B.R., Eppel, J.T., Shea, and M.A. (2001) Paramecium Calmodulin Mutants Defective in Ion Channel Regulation Associate with Melittin in the Absence of Calcium but Require it for Tertiary Collapse. Biochemistry 40:896-903. (http://dx.doi.org/10.1021/bi0023091) (8 pp)
Also see PubMed for recent publications.
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