Year |
Citation |
Score |
2024 |
Yi X, Fritzsching KJ, Rogawski R, Xu Y, McDermott AE. Contribution of protein conformational heterogeneity to NMR lineshapes at cryogenic temperatures. Proceedings of the National Academy of Sciences of the United States of America. 121: e2301053120. PMID 38346186 DOI: 10.1073/pnas.2301053120 |
0.602 |
|
2023 |
Rogowski R, Sergeyev I, Fritzsching K, McDermott A. Resolution in Cryogenic Solid State NMR: Challenges and Solutions. Protein Science : a Publication of the Protein Society. e4803. PMID 37847566 DOI: 10.1002/pro.4803 |
0.672 |
|
2023 |
Yi X, Fritzsching KJ, Rogawski R, Xu Y, McDermott AE. Contribution of protein conformational heterogeneity to NMR lineshapes at cryogenic temperatures. Biorxiv : the Preprint Server For Biology. PMID 36747795 DOI: 10.1101/2023.01.24.525358 |
0.61 |
|
2023 |
Yang Y, Fritzsching KJ, He S, McDermott AE. Zinc Alters the Supramolecular Organization of Nucleic Acid Complexes with Full-Length TIA1. Biorxiv : the Preprint Server For Biology. PMID 36747652 DOI: 10.1101/2023.01.25.525508 |
0.494 |
|
2022 |
McCoy KM, Fritzsching KJ, McDermott AE. GTP-Bound Escherichia coli FtsZ Filaments Are Composed of Tense Monomers: a Dynamic Nuclear Polarization-Nuclear Magnetic Resonance Study Using Interface Detection. Mbio. e0235822. PMID 36214571 DOI: 10.1128/mbio.02358-22 |
0.534 |
|
2020 |
Fritzsching KJ, Yang Y, Pogue EM, Rayman JB, Kandel ER, McDermott AE. Micellar TIA1 with folded RNA binding domains as a model for reversible stress granule formation. Proceedings of the National Academy of Sciences of the United States of America. PMID 33257579 DOI: 10.1073/pnas.2007423117 |
0.512 |
|
2020 |
Fritzsching KJ, Keeler EG, He C, McDermott AE. Scaled recoupling of chemical shift anisotropies at high magnetic fields under MAS with interspersed C-elements. The Journal of Chemical Physics. 153: 104201. PMID 32933302 DOI: 10.1063/5.0020682 |
0.553 |
|
2019 |
Fritzsching KJ, Duan P, Alberts EM, Tibabuzo Perdomo AM, Kenny P, Wilker JJ, Schmidt-Rohr K. Silk-Like Protein with Persistent Radicals Identified in Oyster Adhesive by Solid-State NMR. Acs Applied Bio Materials. 2: 2840-2852. PMID 35030818 DOI: 10.1021/acsabm.9b00243 |
0.516 |
|
2018 |
Keeler EG, Fritzsching KJ, McDermott AE. Refocusing CSA during magic angle spinning rotating-frame relaxation experiments. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 296: 130-137. PMID 30253322 DOI: 10.1016/J.Jmr.2018.09.004 |
0.546 |
|
2017 |
Fritzsching KJ, Itin B, McDermott AE. N,N-Diethylmethylamine as lineshape standard for NMR above 130 K. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 287: 110-112. PMID 29335163 DOI: 10.1016/J.Jmr.2017.12.021 |
0.565 |
|
2017 |
Fritzsching KJ, Mao K, Schmidt-Rohr K. Avoidance of Density Anomalies as a Structural Principle for Semicrystalline Polymers: The Importance of Chain Ends and Chain Tilt Macromolecules. 50: 1521-1540. DOI: 10.1021/Acs.Macromol.6B02000 |
0.499 |
|
2016 |
Wang H, Feng Z, Wu D, Fritzsching KJ, Rigney M, Zhou J, Jiang Y, Schmidt-Rohr K, Xu B. Enzyme-Regulated Supramolecular Assemblies of Cholesterol Conjugates against Drug-Resistant Ovarian Cancer Cells. Journal of the American Chemical Society. PMID 27529637 DOI: 10.1021/Jacs.6B06075 |
0.456 |
|
2016 |
Comito RJ, Fritzsching KJ, Sundell BJ, Schmidt-Rohr K, Dinca M. Single-Site Heterogeneous Catalysts for Olefin Polymerization Enabled by Cation Exchange in a Metal Organic Framework. Journal of the American Chemical Society. PMID 27443860 DOI: 10.1021/Jacs.6B05200 |
0.486 |
|
2016 |
Burgess SA, Kassie A, Baranowski SA, Fritzsching KJ, Schmidt-Rohr K, Brown CM, Wade CR. Improved Catalytic Activity and Stability of a Palladium Pincer Complex by Incorporation into a Metal-Organic Framework. Journal of the American Chemical Society. PMID 26813149 DOI: 10.1021/Jacs.5B12366 |
0.474 |
|
2016 |
Fritzsching KJ, Hong M, Schmidt-Rohr K. Conformationally selective multidimensional chemical shift ranges in proteins from a PACSY database purged using intrinsic quality criteria. Journal of Biomolecular Nmr. PMID 26787537 DOI: 10.1007/S10858-016-0013-5 |
0.646 |
|
2013 |
Yang Y, Fritzsching KJ, Hong M. Resonance assignment of the NMR spectra of disordered proteins using a multi-objective non-dominated sorting genetic algorithm. Journal of Biomolecular Nmr. 57: 281-96. PMID 24132778 DOI: 10.1007/S10858-013-9788-9 |
0.484 |
|
2013 |
Liao SY, Fritzsching KJ, Hong M. Conformational analysis of the full-length M2 protein of the influenza A virus using solid-state NMR. Protein Science : a Publication of the Protein Society. 22: 1623-38. PMID 24023039 DOI: 10.1002/Pro.2368 |
0.535 |
|
2013 |
Fritzsching KJ, Yang Y, Schmidt-Rohr K, Hong M. Practical use of chemical shift databases for protein solid-state NMR: 2D chemical shift maps and amino-acid assignment with secondary-structure information. Journal of Biomolecular Nmr. 56: 155-67. PMID 23625364 DOI: 10.1007/S10858-013-9732-Z |
0.633 |
|
2013 |
Fritzsching KJ, Kim J, Holland GP. Probing lipid-cholesterol interactions in DOPC/eSM/Chol and DOPC/DPPC/Chol model lipid rafts with DSC and (13)C solid-state NMR. Biochimica Et Biophysica Acta. 1828: 1889-98. PMID 23567917 DOI: 10.1016/J.Bbamem.2013.03.028 |
0.391 |
|
2012 |
Schmidt-Rohr K, Fritzsching KJ, Liao SY, Hong M. Spectral editing of two-dimensional magic-angle-spinning solid-state NMR spectra for protein resonance assignment and structure determination. Journal of Biomolecular Nmr. 54: 343-53. PMID 23053913 DOI: 10.1007/S10858-012-9676-8 |
0.626 |
|
2012 |
Hong M, Fritzsching KJ, Williams JK. Hydrogen-bonding partner of the proton-conducting histidine in the influenza M2 proton channel revealed from 1H chemical shifts. Journal of the American Chemical Society. 134: 14753-5. PMID 22931093 DOI: 10.1021/Ja307453V |
0.578 |
|
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