Year |
Citation |
Score |
2022 |
Casto J, Mandato A, Hofmann L, Yakobov I, Ghosh S, Ruthstein S, Saxena S. Cu(ii)-based DNA labeling identifies the structural link between transcriptional activation and termination in a metalloregulator. Chemical Science. 13: 1693-1697. PMID 35282619 DOI: 10.1039/d1sc06563g |
0.722 |
|
2021 |
Gamble Jarvi A, Bogetti X, Singewald K, Ghosh S, Saxena S. Going the dHis-tance: Site-Directed Cu Labeling of Proteins and Nucleic Acids. Accounts of Chemical Research. PMID 33476119 DOI: 10.1021/acs.accounts.0c00761 |
0.757 |
|
2020 |
Ghosh S, Casto J, Bogetti X, Arora C, Wang J, Saxena S. Orientation and dynamics of Cu based DNA labels from force field parameterized MD elucidates the relationship between EPR distance constraints and DNA backbone distances. Physical Chemistry Chemical Physics : Pccp. PMID 33159779 DOI: 10.1039/d0cp05016d |
0.735 |
|
2020 |
Bogetti X, Ghosh S, Gamble Jarvi A, Wang J, Saxena S. Molecular Dynamics Simulations Based on Newly Developed Force Field Parameters for Cu Spin Labels Provide Insights Into Double Histidine-Based Double Electron-Electron Resonance. The Journal of Physical Chemistry. B. PMID 32181671 DOI: 10.1021/Acs.Jpcb.0C00739 |
0.715 |
|
2020 |
Ghosh S, Lawless MJ, Brubaker HJ, Singewald K, Kurpiewski MR, Jen-Jacobson L, Saxena S. Cu2+-based distance measurements by pulsed EPR provide distance constraints for DNA backbone conformations in solution. Nucleic Acids Research. PMID 32095832 DOI: 10.1093/Nar/Gkaa133 |
0.757 |
|
2019 |
Wagner EP, Gronborg KC, Ghosh S, Saxena S. An Undergraduate Experiment To Explore Cu(II) Coordination Environment in Multihistidine Compounds through Electron Spin Resonance Spectroscopy Journal of Chemical Education. 96: 1752-1759. DOI: 10.1021/Acs.Jchemed.9B00190 |
0.584 |
|
2019 |
Sameach H, Ghosh S, Gevorkyan‐Airapetov L, Saxena S, Ruthstein S. Inside Cover: EPR Spectroscopy Detects Various Active State Conformations of the Transcriptional Regulator CueR (Angew. Chem. Int. Ed. 10/2019) Angewandte Chemie. 58: 2908-2908. DOI: 10.1002/Anie.201900968 |
0.486 |
|
2019 |
Sameach H, Ghosh S, Gevorkyan‐Airapetov L, Saxena S, Ruthstein S. Innentitelbild: EPR Spectroscopy Detects Various Active State Conformations of the Transcriptional Regulator CueR (Angew. Chem. 10/2019) Angewandte Chemie. 131: 2934-2934. DOI: 10.1002/Ange.201900968 |
0.484 |
|
2018 |
Sameach H, Ghosh S, Gevorkyan-Airapetov L, Saxena S, Ruthstein S. EPR spectroscopy detects various active state conformations of the transcriptional regulator CueR. Angewandte Chemie (International Ed. in English). PMID 30566257 DOI: 10.1002/Anie.201810656 |
0.641 |
|
2018 |
Gamble Jarvi A, Ranguelova K, Ghosh S, Weber RT, Saxena S. On the Use of Q-Band DEER to Resolve the Relative Orientations of Two Double Histidine Bound Cu-Ions in a Protein. The Journal of Physical Chemistry. B. PMID 30372072 DOI: 10.1021/Acs.Jpcb.8B07727 |
0.699 |
|
2018 |
Ghosh S, Garcia V, Singewald K, Damo SM, Saxena S. Cu(II) EPR Reveals Two Distinct Binding Sites and Oligomerization of Innate Immune Protein Calgranulin C Applied Magnetic Resonance. 49: 1299-1311. DOI: 10.1007/S00723-018-1053-7 |
0.753 |
|
2018 |
Ghosh S, Saxena S, Jeschke G. Rotamer Modelling of Cu(II) Spin Labels Based on the Double-Histidine Motif Applied Magnetic Resonance. 49: 1281-1298. DOI: 10.1007/S00723-018-1052-8 |
0.744 |
|
2017 |
Ghosh S, Lawless MJ, Rule GS, Saxena S. The Cu2+-nitrilotriacetic acid complex improves loading of α-helical double histidine site for precise distance measurements by pulsed ESR. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 286: 163-171. PMID 29272745 DOI: 10.1016/J.Jmr.2017.12.005 |
0.761 |
|
2017 |
Lawless MJ, Ghosh S, Cunningham TF, Shimshi A, Saxena S. On the use of the Cu(2+)-iminodiacetic acid complex for double histidine based distance measurements by pulsed ESR. Physical Chemistry Chemical Physics : Pccp. PMID 28745737 DOI: 10.1039/C7Cp02564E |
0.75 |
|
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