| Year |
Citation |
Score |
| 2024 |
Gordon SE, Evans EGB, Otto SC, Tessmer MH, Shaffer KD, Gordon MT, Petersson EJ, Stoll S, Zagotta WN. Long-distance tmFRET using bipyridyl- and phenanthroline-based ligands. Biophysical Journal. PMID 38350449 DOI: 10.1016/j.bpj.2024.01.034 |
0.655 |
|
| 2024 |
Zagotta WN, Evans EGB, Eggan P, Tessmer MH, Shaffer KD, Petersson EJ, Stoll S, Gordon SE. Measuring conformational equilibria in allosteric proteins with time-resolved tmFRET. Biophysical Journal. PMID 38303511 DOI: 10.1016/j.bpj.2024.01.033 |
0.656 |
|
| 2023 |
Gordon SE, Evans EGB, Otto SC, Tessmer MH, Shaffer KD, Gordon MT, Petersson EJ, Stoll S, Zagotta WN. Long-distance tmFRET using bipyridyl- and phenanthroline-based ligands. Biorxiv : the Preprint Server For Biology. PMID 37873407 DOI: 10.1101/2023.10.09.561591 |
0.654 |
|
| 2023 |
Zagotta WN, Evans EGB, Eggan P, Tessmer MH, Shaffer KD, Petersson EJ, Stoll S, Gordon SE. Measuring conformational equilibria in allosteric proteins with time-resolved tmFRET. Biorxiv : the Preprint Server For Biology. PMID 37873384 DOI: 10.1101/2023.10.09.561594 |
0.656 |
|
| 2023 |
Jana S, Evans EGB, Jang HS, Zhang S, Zhang H, Rajca A, Gordon SE, Zagotta WN, Stoll S, Mehl RA. Ultrafast Bioorthogonal Spin-Labeling and Distance Measurements in Mammalian Cells Using Small, Genetically Encoded Tetrazine Amino Acids. Journal of the American Chemical Society. PMID 37364003 DOI: 10.1021/jacs.3c00967 |
0.633 |
|
| 2023 |
Jana S, Evans EGB, Jang HS, Zhang S, Zhang H, Rajca A, Gordon SE, Zagotta WN, Stoll S, Mehl RA. Ultra-Fast Bioorthogonal Spin-Labeling and Distance Measurements in Mammalian Cells Using Small, Genetically Encoded Tetrazine Amino Acids. Biorxiv : the Preprint Server For Biology. PMID 36747808 DOI: 10.1101/2023.01.26.525763 |
0.632 |
|
| 2021 |
Jones CM, Robkis DM, Blizzard RJ, Munari M, Venkatesh Y, Mihaila TS, Eddins AJ, Mehl RA, Zagotta WN, Gordon SE, Petersson EJ. Genetic encoding of a highly photostable, long lifetime fluorescent amino acid for imaging in mammalian cells. Chemical Science. 12: 11955-11964. PMID 34976337 DOI: 10.1039/d1sc01914g |
0.636 |
|
| 2021 |
Zagotta WN, Sim BS, Nhim AK, Raza MM, Evans EG, Venkatesh Y, Jones CM, Mehl RA, Petersson EJ, Gordon SE. An improved fluorescent noncanonical amino acid for measuring conformational distributions using time-resolved transition metal ion FRET. Elife. 10. PMID 34623258 DOI: 10.7554/eLife.70236 |
0.676 |
|
| 2021 |
Dai G, Aman TK, DiMaio F, Zagotta WN. Electromechanical coupling mechanism for activation and inactivation of an HCN channel. Nature Communications. 12: 2802. PMID 33990563 DOI: 10.1038/s41467-021-23062-7 |
0.889 |
|
| 2021 |
Evans EGB, Zagotta WN. Illuminating new structures of a rod CNG channel: The eye's chemoelectrical converter. Neuron. 109: 1245-1247. PMID 33887188 DOI: 10.1016/j.neuron.2021.03.034 |
0.399 |
|
| 2020 |
Evans EGB, Morgan JLW, DiMaio F, Zagotta WN, Stoll S. Allosteric conformational change of a cyclic nucleotide-gated ion channel revealed by DEER spectroscopy. Proceedings of the National Academy of Sciences of the United States of America. PMID 32358188 DOI: 10.1073/Pnas.1916375117 |
0.699 |
|
| 2020 |
Dai G, Zagotta WN. Structural Determinants of the Hyperpolarization-Dependent Gating of HCN Channels Biophysical Journal. 118: 331a-332a. DOI: 10.1016/J.Bpj.2019.11.1853 |
0.81 |
|
| 2019 |
Dai G, Aman TK, Dimaio F, Zagotta WN. The HCN channel voltage sensor undergoes a large downward motion during hyperpolarization. Nat Struct Mol Biol.. PMID 31285608 DOI: 10.1038/S41594-019-0259-1 |
0.876 |
|
| 2019 |
Morgan JLW, Evans EGB, Zagotta WN. Functional characterization and optimization of a bacterial cyclic nucleotide-gated channel. The Journal of Biological Chemistry. PMID 30885945 DOI: 10.1074/jbc.RA119.007699 |
0.659 |
|
| 2019 |
Morgan J, Evans E, Zagotta W. Functional Characterization of Gating in a Bacterial Cyclic Nucleotide-Gated Channel Biophysical Journal. 116: 108a. DOI: 10.1016/j.bpj.2018.11.616 |
0.627 |
|
| 2019 |
Evans EG, Morgan JL, Stoll S, Zagotta WN. Allosteric Gating Rearrangements of a Prokaryotic Cyclic Nucleotide-Gated Ion Channel Revealed with Pulsed Dipolar Spectroscopy Biophysical Journal. 116: 108a. DOI: 10.1016/J.Bpj.2018.11.615 |
0.578 |
|
| 2018 |
Gordon SE, Munari M, Zagotta WN. Correction: Visualizing conformational dynamics of proteins in solution and at the cell membrane. Elife. 7. PMID 30499444 DOI: 10.7554/eLife.44029 |
0.65 |
|
| 2018 |
Flynn GE, Zagotta WN. Insights into the molecular mechanism for hyperpolarization-dependent activation of HCN channels. Proceedings of the National Academy of Sciences of the United States of America. PMID 30076228 DOI: 10.1073/pnas.1805596115 |
0.64 |
|
| 2018 |
Gordon SE, Munari M, Zagotta WN. Visualizing conformational dynamics of proteins in solution and at the cell membrane. Elife. 7. PMID 29923827 DOI: 10.7554/eLife.37248 |
0.678 |
|
| 2018 |
Dai G, James ZM, Zagotta WN. Dynamic rearrangement of the intrinsic ligand regulates KCNH potassium channels. The Journal of General Physiology. PMID 29567795 DOI: 10.1085/Jgp.201711989 |
0.808 |
|
| 2018 |
Evans EG, Morgan JL, James ZM, Stoll S, Zagotta WN. Functional and Spectroscopic Studies of Prokaryotic Cyclic Nucleotide-Gated Ion Channels Biophysical Journal. 114: 128a. DOI: 10.1016/J.Bpj.2017.11.729 |
0.594 |
|
| 2018 |
Dai G, James ZM, Zagotta WN. Dynamic Rearrangement of the Intrinsic Ligand Regulates Gating of KCNH Potassium Channels Biophysical Journal. 114: 292a. DOI: 10.1016/J.Bpj.2017.11.1669 |
0.783 |
|
| 2017 |
James ZM, Zagotta WN. Structural insights into the mechanisms of CNBD channel function. The Journal of General Physiology. PMID 29233886 DOI: 10.1085/Jgp.201711898 |
0.671 |
|
| 2017 |
Borst AJ, James ZM, Zagotta WN, Ginsberg M, Rey FA, DiMaio F, Backovic M, Veesler D. The Therapeutic Antibody LM609 Selectively Inhibits Ligand Binding to Human αVβ3 Integrin via Steric Hindrance. Structure (London, England : 1993). PMID 29033288 DOI: 10.1016/J.Str.2017.09.007 |
0.325 |
|
| 2017 |
Bankston JR, DeBerg HA, Stoll S, Zagotta WN. Mechanism for the inhibition of the cAMP dependence of HCN ion channels by the auxiliary subunit TRIP8b. The Journal of Biological Chemistry. PMID 28864772 DOI: 10.1074/Jbc.M117.800722 |
0.823 |
|
| 2017 |
Collauto A, DeBerg HA, Kaufmann R, Zagotta WN, Stoll S, Goldfarb D. Rates and equilibrium constants of the ligand-induced conformational transition of an HCN ion channel protein domain determined by DEER spectroscopy. Physical Chemistry Chemical Physics : Pccp. PMID 28569901 DOI: 10.1039/C7Cp01925D |
0.438 |
|
| 2017 |
Zagotta WN, Dai G. Molecular mechanism of voltage-dependent potentiation of KCNH potassium channels. Elife. 6. PMID 28443815 DOI: 10.7554/Elife.26355 |
0.822 |
|
| 2017 |
James ZM, Borst AJ, Haitin Y, Frenz B, DiMaio F, Zagotta WN, Veesler D. CryoEM structure of a prokaryotic cyclic nucleotide-gated ion channel. Proceedings of the National Academy of Sciences of the United States of America. PMID 28396445 DOI: 10.1073/Pnas.1700248114 |
0.693 |
|
| 2017 |
Dai G, Zagotta WN. Author response: Molecular mechanism of voltage-dependent potentiation of KCNH potassium channels Elife. DOI: 10.7554/Elife.26355.015 |
0.77 |
|
| 2017 |
James ZM, Evans EG, Zagotta WN. Spectroscopic Studies of a Bacterial Cyclic Nucleotide-Gated Ion Channel Biophysical Journal. 112: 40a. DOI: 10.1016/J.Bpj.2016.11.254 |
0.692 |
|
| 2017 |
Dai G, Zagotta W. Molecular Mechanisms of the Voltage-Dependent Potentiation of KCNH Potassium Channels Biophysical Journal. 112. DOI: 10.1016/J.Bpj.2016.11.248 |
0.828 |
|
| 2017 |
Aman TK, Zagotta WN. HCN Channel Gating Studied with tmFRET and a Fluorescent Noncanonical Amino Acid Biophysical Journal. 112: 249a. DOI: 10.1016/J.Bpj.2016.11.1362 |
0.846 |
|
| 2017 |
Flynn GE, Zagotta WN. Insights into the Molecular Mechanism Coupling the S4 Voltage-Sensor to the Pore Domain in HCN Channels Biophysical Journal. 112: 248a. DOI: 10.1016/j.bpj.2016.11.1356 |
0.504 |
|
| 2016 |
Aman TK, Gordon SE, Zagotta WN. Regulation of CNGA1 channel gating by interactions with the membrane. The Journal of Biological Chemistry. PMID 26969165 DOI: 10.1016/J.Bpj.2015.11.1577 |
0.856 |
|
| 2016 |
Gordon SE, Senning EN, Aman TK, Zagotta WN. Transition metal ion FRET to measure short-range distances at the intracellular surface of the plasma membrane. The Journal of General Physiology. PMID 26755772 DOI: 10.1083/Jcb.2124Oia26 |
0.774 |
|
| 2016 |
Zagotta WN, Gordon MT, Senning EN, Munari MA, Gordon SE. Measuring distances between TRPV1 and the plasma membrane using a noncanonical amino acid and transition metal ion FRET. The Journal of General Physiology. PMID 26755770 DOI: 10.1083/Jcb.2124Oia27 |
0.806 |
|
| 2015 |
DeBerg HA, Brzovic PS, Flynn GE, Zagotta WN, Stoll S. Structure and Energetics of Allosteric Regulation of HCN2 Ion Channels by Cyclic Nucleotides. The Journal of Biological Chemistry. PMID 26559974 DOI: 10.1074/Jbc.M115.696450 |
0.677 |
|
| 2015 |
DeBerg HA, Bankston JR, Rosenbaum JC, Brzovic PS, Zagotta WN, Stoll S. Structural mechanism for the regulation of HCN ion channels by the accessory protein TRIP8b. Structure (London, England : 1993). 23: 734-44. PMID 25800552 DOI: 10.1016/J.Str.2015.02.007 |
0.864 |
|
| 2015 |
Aman TK, Gordon SE, Zagotta WN. Transition Metal FRET of Cyclic Nucleotide-Gated Channels Labeled with the Fluorescent Unnatural Amino Acid Anap Biophysical Journal. 108: 155a. DOI: 10.1016/J.Bpj.2014.11.854 |
0.862 |
|
| 2015 |
Senning E, Zagotta WN, Gordon SE. Transition Metal Ion FRET Measurements in Plasma Membrane Sheets Prepared by Deroofing Cultured Mammalian Cells Biophysical Journal. 108: 152a. DOI: 10.1016/J.Bpj.2014.11.836 |
0.779 |
|
| 2015 |
Bankston JR, DeBerg HA, Rosenbaum JC, Brzovic PS, Stoll S, Zagotta WN. Spectroscopic and Biochemical Studies of TRIP8b Regulation of HCN Channels Biophysical Journal. 108: 348a. DOI: 10.1016/J.Bpj.2014.11.1907 |
0.843 |
|
| 2015 |
DeBerg HA, Islam SM, Puljung MC, Roux B, Zagotta WN, Stoll S. Allosteric Regulation of the Cyclic Nucleotide-Binding Domain in HCN Channels Biophysical Journal. 108: 192a-193a. DOI: 10.1016/J.Bpj.2014.11.1064 |
0.621 |
|
| 2014 |
Puljung MC, DeBerg HA, Zagotta WN, Stoll S. Double electron-electron resonance reveals cAMP-induced conformational change in HCN channels. Proceedings of the National Academy of Sciences of the United States of America. 111: 9816-21. PMID 24958877 DOI: 10.1073/Pnas.1405371111 |
0.588 |
|
| 2014 |
Sun J, Bankston JR, Payandeh J, Hinds TR, Zagotta WN, Zheng N. Crystal structure of the plant dual-affinity nitrate transporter NRT1.1. Nature. 507: 73-7. PMID 24572362 DOI: 10.1038/Nature13074 |
0.691 |
|
| 2014 |
Haitin Y, Carlson AE, Zagotta WN. The Molecular Basis of KCNH Channel Regulation by the EAG Domain Biophysical Journal. 106: 737a. DOI: 10.1016/J.Bpj.2013.11.4063 |
0.743 |
|
| 2014 |
DeBerg HA, Puljung MC, Zagotta WN, Stoll S. Double Electron-Electron Resonance Studies of Ligand Induced Rearrangements of HCN Channels Biophysical Journal. 106: 737a. DOI: 10.1016/J.Bpj.2013.11.4062 |
0.613 |
|
| 2014 |
Manrao EA, Merz AJ, Zagotta WN, Gordon SE. Tmfret to Study Short-Range Interactions at the Membrane Biophysical Journal. 106: 502a. DOI: 10.1016/J.Bpj.2013.11.2807 |
0.678 |
|
| 2013 |
Carlson AE, Rosenbaum JC, Brelidze TI, Klevit RE, Zagotta WN. Flavonoid regulation of HCN2 channels. The Journal of Biological Chemistry. 288: 33136-45. PMID 24085296 DOI: 10.1074/Jbc.M113.501759 |
0.878 |
|
| 2013 |
Haitin Y, Carlson AE, Zagotta WN. The structural mechanism of KCNH-channel regulation by the eag domain. Nature. 501: 444-8. PMID 23975098 DOI: 10.1038/Nature12487 |
0.755 |
|
| 2013 |
Brelidze TI, Gianulis EC, DiMaio F, Trudeau MC, Zagotta WN. Structure of the C-terminal region of an ERG channel and functional implications. Proceedings of the National Academy of Sciences of the United States of America. 110: 11648-53. PMID 23801759 DOI: 10.1073/Pnas.1306887110 |
0.867 |
|
| 2013 |
Puljung MC, Zagotta WN. A secondary structural transition in the C-helix promotes gating of cyclic nucleotide-regulated ion channels. The Journal of Biological Chemistry. 288: 12944-56. PMID 23525108 DOI: 10.1074/Jbc.M113.464123 |
0.567 |
|
| 2013 |
Carlson AE, Brelidze TI, Zagotta WN. Flavonoid regulation of EAG1 channels. The Journal of General Physiology. 141: 347-58. PMID 23440277 DOI: 10.1085/Jgp.201210900 |
0.886 |
|
| 2013 |
Bankston JR, Camp SS, Zagotta WN. Dimeric TRIP8b Binds to the Cyclic Nucleotide Binding Domain of HCN Channels Biophysical Journal. 104: 542a-543a. DOI: 10.1016/J.Bpj.2012.11.3006 |
0.796 |
|
| 2013 |
Brelidze TI, DiMaio F, Trudeau MC, Zagotta WN. Structure of the C-Terminal Region of an ERG Channel and Functional Implications for Long-QT Syndrome Biophysical Journal. 104: 356a. DOI: 10.1016/J.Bpj.2012.11.1978 |
0.865 |
|
| 2013 |
Puljung MC, Zagotta WN, Stoll S. Spectroscopic Investigation of Agonist-Induced Rearrangements of Cyclic Nucleotide-Modulated Ion Channels Biophysical Journal. 104: 271a. DOI: 10.1016/J.Bpj.2012.11.1519 |
0.586 |
|
| 2012 |
Puljung MC, Zagotta WN. Fluorescent labeling of specific cysteine residues using CyMPL. Current Protocols in Protein Science / Editorial Board, John E. Coligan ... [Et Al.]. Unit14.14. PMID 23151742 DOI: 10.1002/0471140864.Ps1414S70 |
0.342 |
|
| 2012 |
Bankston JR, Camp SS, DiMaio F, Lewis AS, Chetkovich DM, Zagotta WN. Structure and stoichiometry of an accessory subunit TRIP8b interaction with hyperpolarization-activated cyclic nucleotide-gated channels. Proceedings of the National Academy of Sciences of the United States of America. 109: 7899-904. PMID 22550182 DOI: 10.1073/Pnas.1201997109 |
0.851 |
|
| 2012 |
Brelidze TI, Carlson AE, Sankaran B, Zagotta WN. Structure of the carboxy-terminal region of a KCNH channel. Nature. 481: 530-3. PMID 22230959 DOI: 10.1038/Nature10735 |
0.881 |
|
| 2012 |
Bankston JR, Camp SS, Lewis AS, Chetkovich DM, Zagotta WN. Molecular Determinants of the Interaction Between HCN2 and its Accessory Subunit TRIP8b Biophysical Journal. 102: 129a. DOI: 10.1016/J.Bpj.2011.11.719 |
0.838 |
|
| 2012 |
Puljung MC, Zagotta WN. Agonist-Induced Conformational Changes in the Ligand Binding Domain of Cyclic Nucleotide-Regulated Channels Biophysical Journal. 102: 612a. DOI: 10.1016/J.Bpj.2011.11.3337 |
0.519 |
|
| 2012 |
Brelidze TI, Carlson AE, Sankaran B, Zagotta WN. Structure of the C-Terminal Region of a KCNH Channel Biophysical Journal. 102: 37a. DOI: 10.1016/J.Bpj.2011.11.230 |
0.886 |
|
| 2012 |
Carlson AE, Brelidze TI, Zagotta WN. Fisetin Regulation of HCN2 and Eag1 Channels Reveals Conserved Gating Mechanisms Biophysical Journal. 102: 330a. DOI: 10.1016/J.Bpj.2011.11.1810 |
0.88 |
|
| 2011 |
Shuart NG, Haitin Y, Camp SS, Black KD, Zagotta WN. Molecular mechanism for 3:1 subunit stoichiometry of rod cyclic nucleotide-gated ion channels. Nature Communications. 2: 457. PMID 21878911 DOI: 10.1038/Ncomms1466 |
0.884 |
|
| 2011 |
Puljung MC, Zagotta WN. Labeling of specific cysteines in proteins using reversible metal protection. Biophysical Journal. 100: 2513-21. PMID 21575586 DOI: 10.1016/J.Bpj.2011.03.063 |
0.337 |
|
| 2011 |
Flynn GE, Zagotta WN. Molecular mechanism underlying phosphatidylinositol 4,5-bisphosphate-induced inhibition of SpIH channels. The Journal of Biological Chemistry. 286: 15535-42. PMID 21383006 DOI: 10.1074/jbc.M110.214650 |
0.597 |
|
| 2011 |
Brelidze TI, Zagotta WN. Exploring Ligand Regulation of Ion Channels in the EAG Family Biophysical Journal. 100: 103a. DOI: 10.1016/J.Bpj.2010.12.771 |
0.813 |
|
| 2011 |
Carlson AE, Drum BM, Zagotta WN. Deletion of the Amino-Terminus Uncovers an Inactivated State in Eag1 Channels Biophysical Journal. 100: 30a. DOI: 10.1016/J.Bpj.2010.12.367 |
0.808 |
|
| 2010 |
Mercado J, Gordon-Shaag A, Zagotta WN, Gordon SE. Ca2+-dependent desensitization of TRPV2 channels is mediated by hydrolysis of phosphatidylinositol 4,5-bisphosphate. The Journal of Neuroscience : the Official Journal of the Society For Neuroscience. 30: 13338-47. PMID 20926660 DOI: 10.1523/Jneurosci.2108-10.2010 |
0.88 |
|
| 2010 |
Brelidze TI, Carlson AE, Davies DR, Stewart LJ, Zagotta WN. Identifying regulators for EAG1 channels with a novel electrophysiology and tryptophan fluorescence based screen. Plos One. 5. PMID 20824064 DOI: 10.1371/Journal.Pone.0012523 |
0.862 |
|
| 2010 |
Linton JD, Holzhausen LC, Babai N, Song H, Miyagishima KJ, Stearns GW, Lindsay K, Wei J, Chertov AO, Peters TA, Caffe R, Pluk H, Seeliger MW, Tanimoto N, Fong K, ... ... Zagotta WN, et al. Flow of energy in the outer retina in darkness and in light. Proceedings of the National Academy of Sciences of the United States of America. 107: 8599-604. PMID 20445106 DOI: 10.1073/Pnas.1002471107 |
0.577 |
|
| 2010 |
Taraska JW, Zagotta WN. Fluorescence applications in molecular neurobiology. Neuron. 66: 170-89. PMID 20434995 DOI: 10.1016/J.Neuron.2010.02.002 |
0.661 |
|
| 2010 |
Puljung MC, Zagotta WN. Site-Specific Protein Labeling using Reversible Transition Metal Ion Binding Biophysical Journal. 98: 706a. DOI: 10.1016/J.Bpj.2009.12.3873 |
0.414 |
|
| 2010 |
Mercado J, Zagotta WN, Gordon SE. Role Of Pip2 On Ca2+-Dependent Desensitization of Trpv2 Biophysical Journal. 98: 227a. DOI: 10.1016/J.Bpj.2009.12.1229 |
0.813 |
|
| 2010 |
Carlson AE, Brelidze TI, Davies DR, Zagotta W. Flavonoids Regulate Eag1 Channels Biophysical Journal. 98: 1a. DOI: 10.1016/J.Bpj.2009.11.037 |
0.874 |
|
| 2009 |
Taraska JW, Puljung MC, Zagotta WN. Short-distance probes for protein backbone structure based on energy transfer between bimane and transition metal ions. Proceedings of the National Academy of Sciences of the United States of America. 106: 16227-32. PMID 19805285 DOI: 10.1073/Pnas.0905207106 |
0.65 |
|
| 2009 |
Brelidze TI, Carlson AE, Zagotta WN. Absence of direct cyclic nucleotide modulation of mEAG1 and hERG1 channels revealed with fluorescence and electrophysiological methods. The Journal of Biological Chemistry. 284: 27989-97. PMID 19671703 DOI: 10.1074/Jbc.M109.016337 |
0.878 |
|
| 2009 |
Taraska JW, Puljung MC, Olivier NB, Flynn GE, Zagotta WN. Mapping the structure and conformational movements of proteins with transition metal ion FRET. Nature Methods. 6: 532-7. PMID 19525958 DOI: 10.1038/Nmeth.1341 |
0.728 |
|
| 2009 |
Carlson AE, Davies D, Zagotta WN. A Regulator for Eag Family Channels Biophysical Journal. 96: 562a. DOI: 10.1016/J.Bpj.2008.12.3684 |
0.784 |
|
| 2008 |
Gordon-Shaag A, Zagotta WN, Gordon SE. Mechanism of Ca(2+)-dependent desensitization in TRP channels. Channels (Austin, Tex.). 2: 125-9. PMID 18849652 DOI: 10.4161/Chan.2.2.6026 |
0.839 |
|
| 2008 |
Craven KB, Olivier NB, Zagotta WN. C-terminal movement during gating in cyclic nucleotide-modulated channels. The Journal of Biological Chemistry. 283: 14728-38. PMID 18367452 DOI: 10.1074/Jbc.M710463200 |
0.879 |
|
| 2007 |
Taraska JW, Zagotta WN. Cyclic nucleotide-regulated ion channels: spotlight on symmetry. Structure (London, England : 1993). 15: 1023-4. PMID 17850739 DOI: 10.1016/J.Str.2007.08.004 |
0.779 |
|
| 2007 |
Taraska JW, Zagotta WN. Structural dynamics in the gating ring of cyclic nucleotide-gated ion channels. Nature Structural & Molecular Biology. 14: 854-60. PMID 17694071 DOI: 10.1038/Nsmb1281 |
0.829 |
|
| 2007 |
Flynn GE, Black KD, Islas LD, Sankaran B, Zagotta WN. Structure and rearrangements in the carboxy-terminal region of SpIH channels. Structure (London, England : 1993). 15: 671-82. PMID 17562314 DOI: 10.1016/j.str.2007.04.008 |
0.799 |
|
| 2006 |
Islas LD, Zagotta WN. Short-range molecular rearrangements in ion channels detected by tryptophan quenching of bimane fluorescence. The Journal of General Physiology. 128: 337-46. PMID 16940556 DOI: 10.1085/jgp.200609556 |
0.821 |
|
| 2006 |
Zagotta WN. Membrane biology: permutations of permeability. Nature. 440: 427-9. PMID 16554793 DOI: 10.1038/440427a |
0.592 |
|
| 2006 |
Craven KB, Zagotta WN. CNG and HCN channels: two peas, one pod. Annual Review of Physiology. 68: 375-401. PMID 16460277 DOI: 10.1146/Annurev.Physiol.68.040104.134728 |
0.891 |
|
| 2005 |
Johnson JP, Zagotta WN. The carboxyl-terminal region of cyclic nucleotide-modulated channels is a gating ring, not a permeation path. Proceedings of the National Academy of Sciences of the United States of America. 102: 2742-7. PMID 15710893 DOI: 10.1073/pnas.0408323102 |
0.68 |
|
| 2004 |
Craven KB, Zagotta WN. Salt bridges and gating in the COOH-terminal region of HCN2 and CNGA1 channels. The Journal of General Physiology. 124: 663-77. PMID 15572346 DOI: 10.1085/Jgp.200409178 |
0.887 |
|
| 2004 |
Trudeau MC, Zagotta WN. Dynamics of Ca2+-calmodulin-dependent inhibition of rod cyclic nucleotide-gated channels measured by patch-clamp fluorometry. The Journal of General Physiology. 124: 211-23. PMID 15314069 DOI: 10.1085/Jgp.200409101 |
0.715 |
|
| 2004 |
Zheng J, Zagotta WN. Stoichiometry and assembly of olfactory cyclic nucleotide-gated channels. Neuron. 42: 411-21. PMID 15134638 DOI: 10.1016/S0896-6273(04)00253-3 |
0.659 |
|
| 2003 |
Matulef K, Zagotta WN. Cyclic nucleotide-gated ion channels. Annual Review of Cell and Developmental Biology. 19: 23-44. PMID 14570562 DOI: 10.1146/annurev.cellbio.19.110701.154854 |
0.854 |
|
| 2003 |
Zagotta WN, Olivier NB, Black KD, Young EC, Olson R, Gouaux E. Structural basis for modulation and agonist specificity of HCN pacemaker channels. Nature. 425: 200-5. PMID 12968185 DOI: 10.1038/Nature01922 |
0.661 |
|
| 2003 |
Zheng J, Varnum MD, Zagotta WN. Disruption of an intersubunit interaction underlies Ca2+-calmodulin modulation of cyclic nucleotide-gated channels. The Journal of Neuroscience : the Official Journal of the Society For Neuroscience. 23: 8167-75. PMID 12954880 DOI: 10.1523/Jneurosci.23-22-08167.2003 |
0.863 |
|
| 2003 |
Flynn GE, Zagotta WN. A cysteine scan of the inner vestibule of cyclic nucleotide-gated channels reveals architecture and rearrangement of the pore. The Journal of General Physiology. 121: 563-82. PMID 12771192 DOI: 10.1085/jgp.200308819 |
0.678 |
|
| 2003 |
Zheng J, Zagotta WN. Patch-clamp fluorometry recording of conformational rearrangements of ion channels. Science's Stke : Signal Transduction Knowledge Environment. 2003: PL7. PMID 12671191 DOI: 10.1126/stke.2003.176.pl7 |
0.595 |
|
| 2003 |
Trudeau MC, Zagotta WN. Calcium/calmodulin modulation of olfactory and rod cyclic nucleotide-gated ion channels. The Journal of Biological Chemistry. 278: 18705-8. PMID 12626507 DOI: 10.1074/Jbc.R300001200 |
0.722 |
|
| 2002 |
Zheng J, Trudeau MC, Zagotta WN. Rod cyclic nucleotide-gated channels have a stoichiometry of three CNGA1 subunits and one CNGB1 subunit. Neuron. 36: 891-6. PMID 12467592 DOI: 10.1016/S0896-6273(02)01099-1 |
0.774 |
|
| 2002 |
Matulef K, Zagotta WN. Multimerization of the ligand binding domains of cyclic nucleotide-gated channels. Neuron. 36: 93-103. PMID 12367509 DOI: 10.1016/S0896-6273(02)00878-4 |
0.874 |
|
| 2002 |
Trudeau MC, Zagotta WN. Mechanism of calcium/calmodulin inhibition of rod cyclic nucleotide-gated channels. Proceedings of the National Academy of Sciences of the United States of America. 99: 8424-9. PMID 12048242 DOI: 10.1073/Pnas.122015999 |
0.69 |
|
| 2002 |
Trudeau MC, Zagotta WN. An intersubunit interaction regulates trafficking of rod cyclic nucleotide-gated channels and is disrupted in an inherited form of blindness. Neuron. 34: 197-207. PMID 11970862 DOI: 10.1016/S0896-6273(02)00647-5 |
0.727 |
|
| 2001 |
Flynn GE, Johnson JP, Zagotta WN. Cyclic nucleotide-gated channels: shedding light on the opening of a channel pore. Nature Reviews. Neuroscience. 2: 643-51. PMID 11533732 DOI: 10.1038/35090015 |
0.678 |
|
| 2001 |
Johnson JP, Zagotta WN. Rotational movement during cyclic nucleotide-gated channel opening. Nature. 412: 917-21. PMID 11528481 DOI: 10.1038/35091089 |
0.656 |
|
| 2001 |
Flynn GE, Zagotta WN. Conformational changes in S6 coupled to the opening of cyclic nucleotide-gated channels. Neuron. 30: 689-98. PMID 11430803 DOI: 10.1016/S0896-6273(01)00324-5 |
0.657 |
|
| 2001 |
Zagotta WN. Structure that opens the gate and opens the door. Neuron. 29: 547-8. PMID 11301011 DOI: 10.1016/S0896-6273(01)00227-6 |
0.638 |
|
| 2000 |
Zheng J, Zagotta WN. Gating rearrangements in cyclic nucleotide-gated channels revealed by patch-clamp fluorometry. Neuron. 28: 369-74. PMID 11144348 DOI: 10.1016/S0896-6273(00)00117-3 |
0.687 |
|
| 2000 |
Shapiro MS, Zagotta WN. Structural basis for ligand selectivity of heteromeric olfactory cyclic nucleotide-gated channels. Biophysical Journal. 78: 2307-20. PMID 10777729 DOI: 10.1016/S0006-3495(00)76777-4 |
0.483 |
|
| 1999 |
Matulef K, Flynn GE, Zagotta WN. Molecular rearrangements in the ligand-binding domain of cyclic nucleotide-gated channels. Neuron. 24: 443-52. PMID 10571237 DOI: 10.1016/S0896-6273(00)80857-0 |
0.857 |
|
| 1999 |
Sunderman ER, Zagotta WN. Sequence of events underlying the allosteric transition of rod cyclic nucleotide-gated channels. The Journal of General Physiology. 113: 621-40. PMID 10228179 DOI: 10.1085/jgp.113.5.621 |
0.584 |
|
| 1999 |
Sunderman ER, Zagotta WN. Mechanism of allosteric modulation of rod cyclic nucleotide-gated channels. The Journal of General Physiology. 113: 601-20. PMID 10228178 DOI: 10.1085/jgp.113.5.601 |
0.579 |
|
| 1998 |
Shapiro MS, Zagotta WN. Stoichiometry and arrangement of heteromeric olfactory cyclic nucleotide-gated ion channels. Proceedings of the National Academy of Sciences of the United States of America. 95: 14546-51. PMID 9826737 DOI: 10.1073/pnas.95.24.14546 |
0.447 |
|
| 1998 |
Eaholtz G, Zagotta WN, Catterall WA. Kinetic analysis of block of open sodium channels by a peptide containing the isoleucine, phenylalanine, and methionine (IFM) motif from the inactivation gate. The Journal of General Physiology. 111: 75-82. PMID 9417136 DOI: 10.1085/jgp.111.1.75 |
0.571 |
|
| 1997 |
Fodor AA, Black KD, Zagotta WN. Tetracaine reports a conformational change in the pore of cyclic nucleotide-gated channels. The Journal of General Physiology. 110: 591-600. PMID 9348330 DOI: 10.1085/jgp.110.5.591 |
0.805 |
|
| 1997 |
Varnum MD, Zagotta WN. Interdomain interactions underlying activation of cyclic nucleotide-gated channels. Science (New York, N.Y.). 278: 110-3. PMID 9311913 DOI: 10.1126/science.278.5335.110 |
0.883 |
|
| 1997 |
Li J, Zagotta WN, Lester HA. Cyclic nucleotide-gated channels: structural basis of ligand efficacy and allosteric modulation. Quarterly Reviews of Biophysics. 30: 177-93. PMID 9293605 DOI: 10.1017/S0033583597003326 |
0.503 |
|
| 1997 |
Gordon SE, Varnum MD, Zagotta WN. Direct interaction between amino- and carboxyl-terminal domains of cyclic nucleotide-gated channels. Neuron. 19: 431-41. PMID 9292731 DOI: 10.1016/S0896-6273(00)80951-4 |
0.868 |
|
| 1997 |
Fodor AA, Gordon SE, Zagotta WN. Mechanism of tetracaine block of cyclic nucleotide-gated channels. The Journal of General Physiology. 109: 3-14. PMID 8997661 DOI: 10.1085/jgp.109.1.3 |
0.881 |
|
| 1996 |
Zagotta WN, Siegelbaum SA. Structure and function of cyclic nucleotide-gated channels. Annual Review of Neuroscience. 19: 235-63. PMID 8833443 DOI: 10.1146/annurev.ne.19.030196.001315 |
0.525 |
|
| 1996 |
Zagotta WN. Molecular mechanisms of cyclic nucleotide-gated channels. Journal of Bioenergetics and Biomembranes. 28: 269-78. PMID 8807401 DOI: 10.1007/BF02110700 |
0.624 |
|
| 1996 |
Varnum MD, Zagotta WN. Subunit interactions in the activation of cyclic nucleotide-gated ion channels. Biophysical Journal. 70: 2667-79. PMID 8744304 DOI: 10.1016/S0006-3495(96)79836-3 |
0.893 |
|
| 1996 |
Gordon SE, Oakley JC, Varnum MD, Zagotta WN. Altered ligand specificity by protonation in the ligand binding domain of cyclic nucleotide-gated channels. Biochemistry. 35: 3994-4001. PMID 8672432 DOI: 10.1021/bi952607b |
0.886 |
|
| 1995 |
Ogielska EM, Zagotta WN, Hoshi T, Heinemann SH, Haab J, Aldrich RW. Cooperative subunit interactions in C-type inactivation of K channels. Biophysical Journal. 69: 2449-57. PMID 8599651 DOI: 10.1016/S0006-3495(95)80114-1 |
0.852 |
|
| 1995 |
Varnum MD, Black KD, Zagotta WN. Molecular mechanism for ligand discrimination of cyclic nucleotide-gated channels. Neuron. 15: 619-25. PMID 7546741 DOI: 10.1016/0896-6273(95)90150-7 |
0.869 |
|
| 1995 |
Gordon SE, Zagotta WN. Localization of regions affecting an allosteric transition in cyclic nucleotide-activated channels. Neuron. 14: 857-64. PMID 7536427 DOI: 10.1016/0896-6273(95)90229-5 |
0.842 |
|
| 1995 |
Gordon SE, Zagotta WN. A histidine residue associated with the gate of the cyclic nucleotide-activated channels in rod photoreceptors. Neuron. 14: 177-83. PMID 7530019 |
0.82 |
|
| 1995 |
Gordon SE, Zagotta WN. Subunit interactions in coordination of Ni2+ in cyclic nucleotide-gated channels. Proceedings of the National Academy of Sciences of the United States of America. 92: 10222-6. PMID 7479756 DOI: 10.1073/Pnas.92.22.10222 |
0.829 |
|
| 1994 |
Zagotta WN, Hoshi T, Aldrich RW. Shaker potassium channel gating. III: Evaluation of kinetic models for activation. The Journal of General Physiology. 103: 321-62. PMID 8189208 DOI: 10.1085/Jgp.103.2.321 |
0.848 |
|
| 1994 |
Zagotta WN, Hoshi T, Dittman J, Aldrich RW. Shaker potassium channel gating. II: Transitions in the activation pathway. The Journal of General Physiology. 103: 279-319. PMID 8189207 DOI: 10.1085/Jgp.103.2.279 |
0.792 |
|
| 1994 |
Hoshi T, Zagotta WN, Aldrich RW. Shaker potassium channel gating. I: Transitions near the open state. The Journal of General Physiology. 103: 249-78. PMID 8189206 DOI: 10.1085/Jgp.103.2.249 |
0.829 |
|
| 1993 |
Hoshi T, Zagotta WN. Recent advances in the understanding of potassium channel function. Current Opinion in Neurobiology. 3: 283-90. PMID 8369623 DOI: 10.1016/0959-4388(93)90119-J |
0.698 |
|
| 1992 |
Foster CD, Chung S, Zagotta WN, Aldrich RW, Levitan IB. A peptide derived from the Shaker B K+ channel produces short and long blocks of reconstituted Ca(2+)-dependent K+ channels. Neuron. 9: 229-36. PMID 1497892 DOI: 10.1016/0896-6273(92)90162-7 |
0.778 |
|
| 1991 |
Hoshi T, Zagotta WN, Aldrich RW. Two types of inactivation in Shaker K+ channels: effects of alterations in the carboxy-terminal region. Neuron. 7: 547-56. PMID 1931050 DOI: 10.1016/0896-6273(91)90367-9 |
0.823 |
|
| 1991 |
Zagotta WN, Hoshi T, Aldrich RW. Erratum: Restoration of Inactivation in Mutants Of Shaker Potassium Channels by a Peptide Derived from ShB Science. 252: 1049-1049. DOI: 10.1126/science.252.5009.1049-b |
0.805 |
|
| 1990 |
Zagotta WN, Aldrich RW. Alterations in activation gating of single Shaker A-type potassium channels by the Sh5 mutation. The Journal of Neuroscience : the Official Journal of the Society For Neuroscience. 10: 1799-810. PMID 2355250 DOI: 10.1523/Jneurosci.10-06-01799.1990 |
0.821 |
|
| 1990 |
Zagotta WN, Aldrich RW. Voltage-dependent gating of Shaker A-type potassium channels in Drosophila muscle. The Journal of General Physiology. 95: 29-60. PMID 2299331 DOI: 10.1085/Jgp.95.1.29 |
0.828 |
|
| 1990 |
Aldrich RW, Hoshi T, Zagotta WN. Differences in gating among amino-terminal variants of Shaker potassium channels. Cold Spring Harbor Symposia On Quantitative Biology. 55: 19-27. PMID 2132814 DOI: 10.1101/Sqb.1990.055.01.005 |
0.859 |
|
| 1990 |
Zagotta WN, Hoshi T, Aldrich RW. Restoration of inactivation in mutants of Shaker potassium channels by a peptide derived from ShB. Science (New York, N.Y.). 250: 568-71. PMID 2122520 DOI: 10.1126/Science.2122520 |
0.82 |
|
| 1990 |
Hoshi T, Zagotta WN, Aldrich RW. Biophysical and molecular mechanisms of Shaker potassium channel inactivation. Science (New York, N.Y.). 250: 533-8. PMID 2122519 DOI: 10.1126/Science.2122519 |
0.871 |
|
| 1989 |
Zagotta WN, Hoshi T, Aldrich RW. Gating of single Shaker potassium channels in Drosophila muscle and in Xenopus oocytes injected with Shaker mRNA. Proceedings of the National Academy of Sciences of the United States of America. 86: 7243-7. PMID 2506548 DOI: 10.1073/Pnas.86.18.7243 |
0.852 |
|
| 1989 |
Zagotta WN, Germeraad S, Garber SS, Hoshi T, Aldrich RW. Properties of ShB A-type potassium channels expressed in Shaker mutant Drosophila by germline transformation. Neuron. 3: 773-82. PMID 2484347 DOI: 10.1016/0896-6273(89)90246-8 |
0.786 |
|
| 1988 |
Zagotta WN, Brainard MS, Aldrich RW. Single-channel analysis of four distinct classes of potassium channels in Drosophila muscle. The Journal of Neuroscience : the Official Journal of the Society For Neuroscience. 8: 4765-79. PMID 3199204 DOI: 10.1523/Jneurosci.08-12-04765.1988 |
0.834 |
|
| 1987 |
Solc CK, Zagotta WN, Aldrich RW. Single-channel and genetic analyses reveal two distinct A-type potassium channels in Drosophila. Science (New York, N.Y.). 236: 1094-8. PMID 2437657 DOI: 10.1126/Science.2437657 |
0.827 |
|
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