Year |
Citation |
Score |
2017 |
Hovey L, Fowler CA, Mahling R, Lin Z, Miller MS, Marx DC, Yoder JB, Kim EH, Tefft KM, Waite BC, Feldkamp MD, Yu L, Shea MA. Calcium triggers reversal of calmodulin on nested anti-parallel sites in the IQ motif of the neuronal voltage-dependent sodium channel NaV1.2. Biophysical Chemistry. 224: 1-19. PMID 28343066 DOI: 10.1016/J.Bpc.2017.02.006 |
0.8 |
|
2015 |
Feldkamp MD, Gakhar L, Pandey N, Shea MA. Opposing orientations of the anti-psychotic drug trifluoperazine selected by alternate conformations of M144 in calmodulin. Proteins. 83: 989-96. PMID 25694384 DOI: 10.1002/Prot.24781 |
0.727 |
|
2014 |
Frank AO, Vangamudi B, Feldkamp MD, Souza-Fagundes EM, Luzwick JW, Cortez D, Olejniczak ET, Waterson AG, Rossanese OW, Chazin WJ, Fesik SW. Discovery of a potent stapled helix peptide that binds to the 70N domain of replication protein A. Journal of Medicinal Chemistry. 57: 2455-61. PMID 24491171 DOI: 10.1021/Jm401730Y |
0.321 |
|
2014 |
Miller MS, Fowler A, Feldkamp MD, Yu L, Shea MA. Calcium-Mediated Reversal of CaM on the Nav 1.2 IQ Motif: Nested Anti-Parallel Sites Biophysical Journal. 106: 48a. DOI: 10.1016/J.Bpj.2013.11.346 |
0.793 |
|
2014 |
Marx DC, Miller MS, Hovey L, Tefft KM, Yoder JB, Kim E, Martin SC, Feldkamp MD, Shea MA. Specificity of Calmodulin Recognition of Human Voltage-Gated Sodium Channels Biophysical Journal. 106: 326a. DOI: 10.1016/J.Bpj.2013.11.1876 |
0.783 |
|
2013 |
Damo SM, Feldkamp MD, Chagot B, Chazin WJ. NMR studies of the interaction of calmodulin with IQ motif peptides. Methods in Molecular Biology (Clifton, N.J.). 963: 173-86. PMID 23296611 DOI: 10.1007/978-1-62703-230-8_11 |
0.466 |
|
2013 |
Marx DC, Kim EH, Miller MS, Yoder JB, Martin SC, Tarleton D, Waite BC, Feldkamp MD, Shea MA. Two Classes of Calmodulin Binding to IQ Motifs of Voltage-Gated Sodium Channels Biophysical Journal. 104: 100a. DOI: 10.1016/J.Bpj.2012.11.589 |
0.785 |
|
2013 |
Shea MA, Miller MS, Yoder JB, Fowler CA, Feldkamp MD, Yu L. Calcium-Mediated Tailspin of Calmodulin on the IQ Motif of the Neuronal Voltage-Dependent Sodium Channel Nav1.2 Biophysical Journal. 104: 14a. DOI: 10.1016/J.Bpj.2012.11.109 |
0.805 |
|
2012 |
Shea MA, Miller MS, Yoder JB, Martin SC, Marx DC, Kim E, Tarleton A, Miller ES, Waite BC, Wold AO, Feldkamp MD. Calmodulin Discrimination Between Voltage-Dependent Sodium Channel IQ Motifs Biophysical Journal. 102: 325a. DOI: 10.1016/J.Bpj.2011.11.1784 |
0.794 |
|
2011 |
Feldkamp MD, Yu L, Shea MA. Structural and energetic determinants of apo calmodulin binding to the IQ motif of the Na(V)1.2 voltage-dependent sodium channel. Structure (London, England : 1993). 19: 733-47. PMID 21439835 DOI: 10.1016/J.Str.2011.02.009 |
0.728 |
|
2011 |
Shea MA, Feldkamp M, Yu L. Recognition of Voltage-Dependent Sodium Channels by Calmodulin Biophysical Journal. 100: 7a. DOI: 10.1016/J.Bpj.2010.12.248 |
0.704 |
|
2010 |
Feldkamp MD, O'Donnell SE, Yu L, Shea MA. Allosteric effects of the antipsychotic drug trifluoperazine on the energetics of calcium binding by calmodulin. Proteins. 78: 2265-82. PMID 20544963 DOI: 10.1002/Prot.22739 |
0.767 |
|
2010 |
Feldkamp MD, Yu L, Shea MA. Calmodulin Regulation of the Neuronal Voltage-Dependent Sodium Channel Biophysical Journal. 98: 310a. DOI: 10.1016/J.Bpj.2009.12.1685 |
0.794 |
|
2009 |
Feldkamp MD, Shea MA. Interactions of the Anti-Psychotic Drug Trifluoperazine with Calmodulin Biophysical Journal. 96: 117a. DOI: 10.1016/J.Bpj.2008.12.514 |
0.754 |
|
2007 |
Li Q, Cooper JJ, Altwerger GH, Feldkamp MD, Shea MA, Price DH. HEXIM1 is a promiscuous double-stranded RNA-binding protein and interacts with RNAs in addition to 7SK in cultured cells. Nucleic Acids Research. 35: 2503-12. PMID 17395637 DOI: 10.1093/Nar/Gkm150 |
0.583 |
|
2004 |
Bernat B, Sun M, Dwyer M, Feldkamp M, Kossiakoff AA. Dissecting the binding energy epitope of a high-affinity variant of human growth hormone: cooperative and additive effects from combining mutations from independently selected phage display mutagenesis libraries. Biochemistry. 43: 6076-84. PMID 15147191 DOI: 10.1021/Bi036069B |
0.341 |
|
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