| Year |
Citation |
Score |
| 2024 |
Hasanbasri Z, Tessmer MH, Stoll S, Saxena S. Modeling of Cu(II)-based protein spin labels using rotamer libraries. Physical Chemistry Chemical Physics : Pccp. 26: 6806-6816. PMID 38324256 DOI: 10.1039/d3cp05951k |
0.367 |
|
| 2023 |
Heubach CA, Hasanbasri Z, Abdullin D, Reuter A, Korzekwa B, Saxena S, Schiemann O. Differentiating between Label and Protein Conformers in Pulsed Dipolar EPR Spectroscopy with the dHis-Cu (NTA) Motif. Chemistry (Weinheim An Der Bergstrasse, Germany). e202302541. PMID 37755452 DOI: 10.1002/chem.202302541 |
0.401 |
|
| 2023 |
Hasanbasri Z, Moriglioni NA, Saxena S. Efficient sampling of molecular orientations for Cu(II)-based DEER on protein labels. Physical Chemistry Chemical Physics : Pccp. PMID 36939213 DOI: 10.1039/d3cp00404j |
0.323 |
|
| 2023 |
Casto J, Bogetti X, Hunter HR, Hasanbasri Z, Saxena S. "Store-bought is fine": Sensitivity considerations using shaped pulses for DEER measurements on Cu(II) labels. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 349: 107413. PMID 36867974 DOI: 10.1016/j.jmr.2023.107413 |
0.301 |
|
| 2022 |
Hasanbasri Z, Poncelet M, Hunter H, Driesschaert B, Saxena S. A new C trityl-based spin label enables the use of DEER for distance measurements. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 347: 107363. PMID 36620971 DOI: 10.1016/j.jmr.2022.107363 |
0.313 |
|
| 2022 |
Osei MK, Mirzaei S, Bogetti X, Castro E, Rahman MA, Saxena S, Hernandez Sanchez R. Synthesis of Square Planar Cu4 Clusters. Angewandte Chemie (International Ed. in English). PMID 35998086 DOI: 10.1002/anie.202209529 |
0.3 |
|
| 2022 |
Singewald K, Wilkinson JA, Hasanbasri Z, Saxena S. Beyond structure: Deciphering site-specific dynamics in proteins from double histidine-based EPR measurements. Protein Science : a Publication of the Protein Society. 31: e4359. PMID 35762707 DOI: 10.1002/pro.4359 |
0.802 |
|
| 2022 |
Bogetti X, Hasanbasri Z, Hunter HR, Saxena S. An optimal acquisition scheme for Q-band EPR distance measurements using Cu-based protein labels. Physical Chemistry Chemical Physics : Pccp. PMID 35574729 DOI: 10.1039/d2cp01032a |
0.358 |
|
| 2022 |
Yakobov I, Mandato A, Hofmann L, Singewald K, Shenberger Y, Gevorkyan-Airapetov L, Saxena S, Ruthstein S. Allostery-driven changes in dynamics regulate the activation of bacterial copper transcription factor. Protein Science : a Publication of the Protein Society. 31: e4309. PMID 35481642 DOI: 10.1002/pro.4309 |
0.803 |
|
| 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 |
0.702 |
|
| 2022 |
Bondarenko V, Wells MM, Chen Q, Tillman TS, Singewald K, Lawless MJ, Caporoso J, Brandon N, Coleman JA, Saxena S, Lindahl E, Xu Y, Tang P. Structures of highly flexible intracellular domain of human α7 nicotinic acetylcholine receptor. Nature Communications. 13: 793. PMID 35145092 DOI: 10.1038/s41467-022-28400-x |
0.77 |
|
| 2021 |
Schiemann O, Heubach CA, Abdullin D, Ackermann K, Azarkh M, Bagryanskaya EG, Drescher M, Endeward B, Freed JH, Galazzo L, Goldfarb D, Hett T, Esteban Hofer L, Fábregas Ibáñez L, Hustedt EJ, ... ... Saxena S, et al. Benchmark Test and Guidelines for DEER/PELDOR Experiments on Nitroxide-Labeled Biomolecules. Journal of the American Chemical Society. PMID 34664948 DOI: 10.1021/jacs.1c07371 |
0.481 |
|
| 2021 |
Hasanbasri Z, Singewald K, Gluth TD, Driesschaert B, Saxena S. Cleavage-Resistant Protein Labeling With Hydrophilic Trityl Enables Distance Measurements . The Journal of Physical Chemistry. B. PMID 33983738 DOI: 10.1021/acs.jpcb.1c02371 |
0.772 |
|
| 2021 |
Casto J, Mandato A, Saxena S. dHis-troying Barriers: Deuteration Provides a Pathway to Increase Sensitivity and Accessible Distances for Cu Labels. The Journal of Physical Chemistry Letters. 12: 4681-4685. PMID 33979151 DOI: 10.1021/acs.jpclett.1c01002 |
0.396 |
|
| 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 |
0.834 |
|
| 2020 |
Schulte ZM, Kwon YH, Han Y, Liu C, Li L, Yang Y, Jarvi AG, Saxena S, Veser G, Johnson JK, Rosi NL. H/CO separations in multicomponent metal-adeninate MOFs with multiple chemically distinct pore environments. Chemical Science. 11: 12807-12815. PMID 34094475 DOI: 10.1039/d0sc04979d |
0.764 |
|
| 2020 |
Gamble Jarvi A, Casto J, Saxena S. Buffer effects on site directed Cu-labeling using the double histidine motif. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 320: 106848. PMID 33164758 DOI: 10.1016/j.jmr.2020.106848 |
0.361 |
|
| 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 |
0.708 |
|
| 2020 |
Singewald K, Bogetti X, Sinha K, Rule G, Saxena SK. Double Histidine based EPR measurements at physiological temperatures permit site-specific elucidation of hidden dynamics in enzymes. Angewandte Chemie (International Ed. in English). PMID 32910837 DOI: 10.1002/Anie.202009982 |
0.794 |
|
| 2020 |
Gamble Jarvi A, Sargun A, Bogetti X, Wang J, Achim C, Saxena S. Development of Cu Based EPR Distance Methods and Force Field Parameters for the Determination of PNA Conformations and Dynamics by EPR and MD Simulations. The Journal of Physical Chemistry. B. PMID 32790374 DOI: 10.1021/Acs.Jpcb.0C05509 |
0.499 |
|
| 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 |
0.751 |
|
| 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 |
0.83 |
|
| 2020 |
Izmailov SA, Rabdano SO, Hasanbasri Z, Podkorytov IS, Saxena S, Skrynnikov NR. Structural and dynamic origins of ESR lineshapes in spin-labeled GB1 domain: the insights from spin dynamics simulations based on long MD trajectories. Scientific Reports. 10: 957. PMID 31969574 DOI: 10.1038/S41598-019-56750-Y |
0.41 |
|
| 2019 |
Bondarenko V, Wells MM, Chen Q, Singewald KC, Saxena S, Xu Y, Tang P. F Paramagnetic Relaxation-Based NMR for Quaternary Structural Restraints of Ion Channels. Acs Chemical Biology. PMID 31525026 DOI: 10.1021/Acschembio.9B00692 |
0.794 |
|
| 2019 |
Mohamed MH, Yang Y, Li L, Zhang S, Ruffley JP, Jarvi AG, Saxena S, Veser G, Johnson JK, Rosi NL. Designing Open Metal Sites in Metal-Organic Frameworks for Paraffin/Olefin Separations. Journal of the American Chemical Society. PMID 31381855 DOI: 10.1021/Jacs.9B06582 |
0.79 |
|
| 2019 |
Gamble Jarvi A, Cunningham TF, Saxena S. Efficient localization of a native metal ion within a protein by Cu-based EPR distance measurements. Physical Chemistry Chemical Physics : Pccp. PMID 30734790 DOI: 10.1039/C8Cp07143H |
0.837 |
|
| 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 |
0.702 |
|
| 2019 |
Huang J, Dai Y, Singewald K, Liu C, Saxena S, Zhang H. Effects of MnO2 of different structures on activation of peroxymonosulfate for bisphenol A degradation under acidic conditions Chemical Engineering Journal. 370: 906-915. DOI: 10.1016/J.Cej.2019.03.238 |
0.767 |
|
| 2019 |
Wells MM, Bondarenko V, Tillman TS, Singewald K, Lawless MJ, Caporoso J, Brandon N, Chen C, Kinde MN, Saxena S, Xu Y, Lindahl E, Tang P. Integrative Structure Determination of α7nAChR Intracellular Domain Biophysical Journal. 116: 394a. DOI: 10.1016/J.Bpj.2018.11.2133 |
0.747 |
|
| 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 |
0.627 |
|
| 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 |
0.626 |
|
| 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 |
0.7 |
|
| 2018 |
Singewald K, Lawless MJ, Saxena S. Increasing nitroxide lifetime in cells to enable in-cell protein structure and dynamics measurements by electron spin resonance spectroscopy. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 299: 21-27. PMID 30550988 DOI: 10.1016/J.Jmr.2018.12.005 |
0.804 |
|
| 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 |
0.739 |
|
| 2018 |
Lawless MJ, Pettersson JR, Rule GS, Lanni F, Saxena S. ESR Resolves the C Terminus Structure of the Ligand-free Human Glutathione S-Transferase A1-1. Biophysical Journal. 114: 592-601. PMID 29414705 DOI: 10.1016/J.Bpj.2017.12.016 |
0.426 |
|
| 2018 |
Kaseman DC, Jarvi AG, Gan XY, Saxena S, Millstone JE. Evolution of Surface Copper(II) Environments in Cu2–xSe Nanoparticles Chemistry of Materials. 30: 7313-7321. DOI: 10.1021/Acs.Chemmater.8B03967 |
0.793 |
|
| 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 |
0.831 |
|
| 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 |
0.746 |
|
| 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 |
0.744 |
|
| 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 |
0.827 |
|
| 2017 |
Saxena SK, Lawless MJ, Shimshi A, Cunningham TF, Kinde MN, Tang P. An analysis of nitroxide based distance measurements in cell extract and in-cell by pulsed ESR spectroscopy. Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry. PMID 28295910 DOI: 10.1002/Cphc.201700115 |
0.79 |
|
| 2017 |
Lawless MJ, Sarver JL, Saxena S. Nucleotide-Independent Copper(II)-Based Distance Measurements in DNA by Pulsed ESR Spectroscopy. Angewandte Chemie (International Ed. in English). PMID 28090713 DOI: 10.1002/Anie.201611197 |
0.808 |
|
| 2016 |
Cunningham TF, Pornsuwan S, Horne WS, Saxena S. Rotameric preferences of a protein spin label at edge-strand β-sheet sites. Protein Science : a Publication of the Protein Society. PMID 26948069 DOI: 10.1002/Pro.2918 |
0.799 |
|
| 2015 |
De Santis E, Minicozzi V, Proux O, Rossi GC, Silva KI, Lawless MJ, Stellato F, Saxena S, Morante S. Cu(II)-Zn(II) Cross-Modulation in Amyloid-Beta Peptide Binding: An X-Ray Absorption Spectroscopy Study. The Journal of Physical Chemistry. B. PMID 26646533 DOI: 10.1021/Acs.Jpcb.5B10264 |
0.807 |
|
| 2015 |
Yang Z, Ji M, Cunningham TF, Saxena S. Cu(2+) as an ESR Probe of Protein Structure and Function. Methods in Enzymology. 563: 459-81. PMID 26478495 DOI: 10.1016/Bs.Mie.2015.05.026 |
0.829 |
|
| 2015 |
Ruthstein S, Ji M, Shin BK, Saxena S. A simple double quantum coherence ESR sequence that minimizes nuclear modulations in Cu(2+)-ion based distance measurements. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 257: 45-50. PMID 26057636 DOI: 10.1016/J.Jmr.2015.05.005 |
0.68 |
|
| 2015 |
Kinde MN, Chen Q, Lawless MJ, Mowrey DD, Xu J, Saxena S, Xu Y, Tang P. Conformational Changes Underlying Desensitization of the Pentameric Ligand-Gated Ion Channel ELIC. Structure (London, England : 1993). 23: 995-1004. PMID 25960405 DOI: 10.1016/J.Str.2015.03.017 |
0.324 |
|
| 2015 |
Cunningham TF, Putterman MR, Desai A, Horne WS, Saxena S. The double-histidine Cu²⁺-binding motif: a highly rigid, site-specific spin probe for electron spin resonance distance measurements. Angewandte Chemie (International Ed. in English). 54: 6330-4. PMID 25821033 DOI: 10.1002/Anie.201501968 |
0.834 |
|
| 2015 |
Cunningham TF, Shannon MD, Putterman MR, Arachchige RJ, Sengupta I, Gao M, Jaroniec CP, Saxena S. Cysteine-specific Cu2+ chelating tags used as paramagnetic probes in double electron electron resonance. The Journal of Physical Chemistry. B. 119: 2839-43. PMID 25608028 DOI: 10.1021/Jp5103143 |
0.826 |
|
| 2015 |
Sengupta I, Gao M, Arachchige RJ, Nadaud PS, Cunningham TF, Saxena S, Schwieters CD, Jaroniec CP. Protein structural studies by paramagnetic solid-state NMR spectroscopy aided by a compact cyclen-type Cu(II) binding tag. Journal of Biomolecular Nmr. 61: 1-6. PMID 25432438 DOI: 10.1007/S10858-014-9880-9 |
0.835 |
|
| 2014 |
Ji M, Tan L, Jen-Jacobson L, Saxena S. Insights into copper coordination in the EcoRI-DNA complex by ESR spectroscopy. Molecular Physics. 112: 3173-3182. PMID 25750461 DOI: 10.1080/00268976.2014.934313 |
0.495 |
|
| 2014 |
Tavenor NA, Silva KI, Saxena S, Horne WS. Origins of structural flexibility in protein-based supramolecular polymers revealed by DEER spectroscopy. The Journal of Physical Chemistry. B. 118: 9881-9. PMID 25060334 DOI: 10.1021/Jp505643W |
0.79 |
|
| 2014 |
Silva KI, Michael BC, Geib SJ, Saxena S. ESEEM analysis of multi-histidine Cu(II)-coordination in model complexes, peptides, and amyloid-β. The Journal of Physical Chemistry. B. 118: 8935-44. PMID 25014537 DOI: 10.1021/Jp500767N |
0.801 |
|
| 2014 |
Jiang J, Bakan A, Kapralov AA, Silva KI, Huang Z, Amoscato AA, Peterson J, Garapati VK, Saxena S, Bayir H, Atkinson J, Bahar I, Kagan VE. Designing inhibitors of cytochrome c/cardiolipin peroxidase complexes: mitochondria-targeted imidazole-substituted fatty acids. Free Radical Biology & Medicine. 71: 221-30. PMID 24631490 DOI: 10.1016/J.Freeradbiomed.2014.02.029 |
0.774 |
|
| 2014 |
Ji M, Ruthstein S, Saxena S. Paramagnetic metal ions in pulsed ESR distance distribution measurements. Accounts of Chemical Research. 47: 688-95. PMID 24289139 DOI: 10.1021/Ar400245Z |
0.5 |
|
| 2013 |
Silva KI, Saxena S. Zn(II) ions substantially perturb Cu(II) ion coordination in amyloid-β at physiological pH. The Journal of Physical Chemistry. B. 117: 9386-94. PMID 23841511 DOI: 10.1021/Jp406067N |
0.807 |
|
| 2013 |
Ruthstein S, Ji M, Mehta P, Jen-Jacobson L, Saxena S. Sensitive Cu2+-Cu2+ distance measurements in a protein-DNA complex by double-quantum coherence ESR. The Journal of Physical Chemistry. B. 117: 6227-30. PMID 23631829 DOI: 10.1021/Jp4037149 |
0.489 |
|
| 2013 |
Sarver J, Silva KI, Saxena S. Measuring Cu2+-Nitroxide Distances Using Double Electron–Electron Resonance and Saturation Recovery Applied Magnetic Resonance. 44: 583-594. DOI: 10.1007/S00723-012-0422-X |
0.789 |
|
| 2012 |
Mamonov AB, Lettieri S, Ding Y, Sarver JL, Palli R, Cunningham TF, Saxena S, Zuckerman DM. Tunable, mixed-resolution modeling using library-based Monte Carlo and graphics processing units. Journal of Chemical Theory and Computation. 8: 2921-2929. PMID 23162384 DOI: 10.1021/Ct300263Z |
0.78 |
|
| 2012 |
Cunningham TF, McGoff MS, Sengupta I, Jaroniec CP, Horne WS, Saxena S. High-resolution structure of a protein spin-label in a solvent-exposed β-sheet and comparison with DEER spectroscopy. Biochemistry. 51: 6350-9. PMID 22809334 DOI: 10.1021/Bi300328W |
0.812 |
|
| 2012 |
Yang Z, Kurpiewski MR, Ji M, Townsend JE, Mehta P, Jen-Jacobson L, Saxena S. ESR spectroscopy identifies inhibitory Cu2+ sites in a DNA-modifying enzyme to reveal determinants of catalytic specificity. Proceedings of the National Academy of Sciences of the United States of America. 109: E993-1000. PMID 22493217 DOI: 10.1073/Pnas.1200733109 |
0.649 |
|
| 2012 |
Sarver JL, Townsend JE, Rajapakse G, Jen-Jacobson L, Saxena S. Simulating the dynamics and orientations of spin-labeled side chains in a protein-DNA complex. The Journal of Physical Chemistry. B. 116: 4024-33. PMID 22404310 DOI: 10.1021/Jp211094N |
0.808 |
|
| 2011 |
Shin BK, Saxena S. Insight into potential Cu(II)-binding motifs in the four pseudorepeats of tau protein. The Journal of Physical Chemistry. B. 115: 15067-78. PMID 22085212 DOI: 10.1021/Jp204410H |
0.682 |
|
| 2011 |
Shin BK, Saxena S. Substantial contribution of the two imidazole rings of the His13-His14 dyad to Cu(II) binding in amyloid-β(1-16) at physiological pH and its significance. The Journal of Physical Chemistry. A. 115: 9590-602. PMID 21491887 DOI: 10.1021/Jp200379M |
0.626 |
|
| 2011 |
Sarver J, Stone K, Townsend J, Sapienza P, Jen-Jacobson L, Saxena S. In the Arms of EcoRI - probing the Binding Specificity of the Restriction Endonuclease Using Electron Spin Resonance Biophysical Journal. 100. DOI: 10.1016/J.Bpj.2010.12.995 |
0.815 |
|
| 2011 |
Ji M, Yang Z, Mehta P, Jen-Jacobson L, Saxena S. Insights on Copper Coordination and Reactivity of Endonuclease EcoRI by ESR Spectroscopy and Modeling Biophysical Journal. 100. DOI: 10.1016/J.Bpj.2010.12.594 |
0.658 |
|
| 2011 |
Shin B, Saxena SK. ESR Spectroscopy Suggests Unequal Contributions of the Three Histidine Residues to Cu(II) Binding in Amyloid-β at Physiological PH Biophysical Journal. 100: 1-5. DOI: 10.1016/J.Bpj.2010.12.1000 |
0.677 |
|
| 2010 |
Ruthstein S, Stone KM, Cunningham TF, Ji M, Cascio M, Saxena S. Pulsed electron spin resonance resolves the coordination site of Cu²(+) ions in α1-glycine receptor. Biophysical Journal. 99: 2497-506. PMID 20959090 DOI: 10.1016/J.Bpj.2010.08.050 |
0.803 |
|
| 2010 |
Yang Z, Kise D, Saxena S. An approach towards the measurement of nanometer range distances based on Cu2+ ions and ESR. The Journal of Physical Chemistry. B. 114: 6165-74. PMID 20397677 DOI: 10.1021/Jp911637S |
0.616 |
|
| 2010 |
Yang Z, Ji M, Saxena S. Practical Aspects of Copper Ion-Based Double Electron Electron Resonance Distance Measurements Applied Magnetic Resonance. 39: 487-500. DOI: 10.1007/S00723-010-0181-5 |
0.595 |
|
| 2009 |
Jun S, Gillespie JR, Shin BK, Saxena S. The second Cu(II)-binding site in a proton-rich environment interferes with the aggregation of amyloid-beta(1-40) into amyloid fibrils. Biochemistry. 48: 10724-32. PMID 19824649 DOI: 10.1021/Bi9012935 |
0.743 |
|
| 2009 |
Walczak MA, Shin BK, Wipf P, Saxena S. An ESR analysis of the mechanism of pericyclic reactions of bicyclobutane. Organic & Biomolecular Chemistry. 7: 2363-6. PMID 19462047 DOI: 10.1039/B815469B |
0.513 |
|
| 2009 |
Townsend JE, Stone K, Yang Z, Sarver J, Saxena S, Jen-Jacobson L. The Enfolding Arms of EcoRI Endonuclease as Probed by ESR Experiments Biophysical Journal. 96. DOI: 10.1016/J.Bpj.2008.12.222 |
0.817 |
|
| 2008 |
Bird GH, Pornsuwan S, Saxena S, Schafmeister CE. Distance distributions of end-labeled curved bispeptide oligomers by electron spin resonance. Acs Nano. 2: 1857-64. PMID 19206425 DOI: 10.1021/Nn800327G |
0.403 |
|
| 2008 |
Stone KM, Townsend JE, Sarver J, Sapienza PJ, Saxena S, Jen-Jacobson L. Electron spin resonance shows common structural features for different classes of EcoRI-DNA complexes. Angewandte Chemie (International Ed. in English). 47: 10192-4. PMID 19021169 DOI: 10.1002/Anie.200803588 |
0.795 |
|
| 2008 |
Shin BK, Saxena S. Direct evidence that all three histidine residues coordinate to Cu(II) in amyloid-beta1-16. Biochemistry. 47: 9117-23. PMID 18690709 DOI: 10.1021/Bi801014X |
0.685 |
|
| 2008 |
Pornsuwan S, Schafmeister CE, Saxena S. Analysis of the dynamical flexibility of bis-peptide nanostructures Journal of Physical Chemistry C. 112: 1377-1384. DOI: 10.1021/Jp077523E |
0.346 |
|
| 2007 |
Yang Z, Becker J, Saxena S. On Cu(II)-Cu(II) distance measurements using pulsed electron electron double resonance. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 188: 337-43. PMID 17825593 DOI: 10.1016/J.Jmr.2007.08.006 |
0.634 |
|
| 2007 |
Jun S, Saxena S. The aggregated state of amyloid-beta peptide in vitro depends on Cu2+ ion concentration. Angewandte Chemie (International Ed. in English). 46: 3959-61. PMID 17427167 DOI: 10.1002/Anie.200700318 |
0.566 |
|
| 2006 |
Jun S, Becker JS, Yonkunas M, Coalson R, Saxena S. Unfolding of alanine-based peptides using electron spin resonance distance measurements. Biochemistry. 45: 11666-73. PMID 16981726 DOI: 10.1021/Bi061195B |
0.63 |
|
| 2006 |
Pornsuwan S, Bird G, Schafmeister CE, Saxena S. Flexibility and lengths of bis-peptide nanostructures by electron spin resonance. Journal of the American Chemical Society. 128: 3876-7. PMID 16551072 DOI: 10.1021/Ja058143E |
0.358 |
|
| 2005 |
Meng R, Becker J, Lin FT, Saxena S, Weber SG. Binding of copper(II) to thyrotropin-releasing hormone (TRH) and its analogs. Inorganica Chimica Acta. 358: 2933-2942. PMID 17160139 DOI: 10.1016/J.Ica.2004.11.045 |
0.426 |
|
| 2005 |
Becker JS, Saxena S. Double quantum coherence electron spin resonance on coupled Cu(II)-Cu(II) electron spins Chemical Physics Letters. 414: 248-252. DOI: 10.1016/J.Cplett.2005.08.072 |
0.467 |
|
| 2004 |
Bonora M, Becker J, Saxena S. Suppression of electron spin-echo envelope modulation peaks in double quantum coherence electron spin resonance Journal of Magnetic Resonance. 170: 278-283. PMID 15388091 DOI: 10.1016/J.Jmr.2004.07.006 |
0.353 |
|
| 2004 |
Bonora M, Pornsuwan S, Saxena S. Nitroxide Spin−Relaxation over the Entire Motional Range Journal of Physical Chemistry B. 108: 4196-4198. DOI: 10.1021/Jp0365864 |
0.302 |
|
| 2003 |
Moulé AJ, Spence MM, Han SI, Seeley JA, Pierce KL, Saxena S, Pines A. Amplification of xenon NMR and MRI by remote detection. Proceedings of the National Academy of Sciences of the United States of America. 100: 9122-7. PMID 12876195 DOI: 10.1073/Pnas.1133497100 |
0.761 |
|
| 2002 |
Wong-Foy A, Saxena S, Moulé AJ, Bitter HM, Seeley JA, McDermott R, Clarke J, Pines A. Laser-polarized (129)Xe NMR and MRI at ultralow magnetic fields. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 157: 235-41. PMID 12323142 DOI: 10.1006/Jmre.2002.2592 |
0.755 |
|
| 1997 |
Saxena S, Freed JH. Absorption Lineshapes in Two-Dimensional Electron Spin Resonance and the Effects of Slow Motions in Complex Fluids Journal of Magnetic Resonance. 124: 439-454. PMID 9169224 DOI: 10.1006/Jmre.1996.1078 |
0.494 |
|
| 1997 |
Saxena S, Freed JH. Theory of double quantum two-dimensional electron spin resonance with application to distance measurements Journal of Chemical Physics. 107: 1317-1340. DOI: 10.1063/1.474490 |
0.531 |
|
| 1997 |
Saxena S, Freed JH. Two-dimensional electron spin resonance and slow motions Journal of Physical Chemistry A. 101: 7998-8008. DOI: 10.1021/Jp9717047 |
0.525 |
|
| 1997 |
Salikhov K, Schneider D, Saxena S, Freed J. A theoretical approach to the analysis of arbitrary pulses in magnetic resonance (Chem. Phys. Letters 262 (1996) 17) Chemical Physics Letters. 265: 562. DOI: 10.1016/S0009-2614(97)00003-1 |
0.478 |
|
| 1996 |
Salikhov KM, Schneider DJ, Saxena S, Freed JH. A theoretical approach to the analysis of arbitrary pulses in magnetic resonance Chemical Physics Letters. 262: 17-26. DOI: 10.1016/0009-2614(96)01044-5 |
0.489 |
|
| 1996 |
Saxena S, Freed JH. Double quantum two-dimensional Fourier transform electron spin resonance: Distance measurements Chemical Physics Letters. 251: 102-110. DOI: 10.1016/0009-2614(96)00075-9 |
0.546 |
|
| 1996 |
Budil DE, Sanghyuk L, Saxena S, Freed JH. Nonlinear-least-squares analysis of slow-motion EPR spectra in one and two dimensions using a modified levenberg-marquardt algorithm Journal of Magnetic Resonance - Series A. 120: 155-189. DOI: 10.1006/Jmra.1996.0113 |
0.5 |
|
| 1994 |
Crepeau RH, Saxena S, Lee S, Patyal B, Freed JH. Studies on lipid membranes by two-dimensional Fourier transform ESR: Enhancement of resolution to ordering and dynamics Biophysical Journal. 66: 1489-1504. PMID 8061198 DOI: 10.1016/S0006-3495(94)80940-3 |
0.506 |
|
| 1994 |
Lee S, Patyal BR, Saxena S, Crepeau RH, Freed JH. Two-dimensional Fourier-transform electron spin resonance in complex fluids Chemical Physics Letters. 221: 397-406. DOI: 10.1016/0009-2614(94)00281-9 |
0.513 |
|
| Show low-probability matches. |
