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For: Theillet FX. In-Cell Structural Biology by NMR: The Benefits of the Atomic Scale. Chem Rev 2022. [PMID: 35357148 DOI: 10.1021/acs.chemrev.1c00937] [Cited by in Crossref: 3] [Cited by in F6Publishing: 4] [Article Influence: 3.0] [Reference Citation Analysis]
Number Citing Articles
1 Lombardo VA, Armesto R, Herrera-estrada I, Binolfi A. High resolution protein in-cell NMR in zebrafish embryos. Journal of Magnetic Resonance Open 2023;16-17:100111. [DOI: 10.1016/j.jmro.2023.100111] [Reference Citation Analysis]
2 Stevanato G, Ding Y, Mamone S, Jagtap AP, Korchak S, Glöggler S. Real-Time Pyruvate Chemical Conversion Monitoring Enabled by PHIP. J Am Chem Soc 2023;145:5864-71. [PMID: 36857108 DOI: 10.1021/jacs.2c13198] [Reference Citation Analysis]
3 Choi AA, Xiang L, Li W, Xu K. Single-molecule displacement mapping indicates unhindered intracellular diffusion of small (<~1 kDa) solutes. bioRxiv 2023:2023. [PMID: 36747694 DOI: 10.1101/2023.01.26.525579] [Reference Citation Analysis]
4 Gao Y, Wang K, Zhang J, Duan X, Sun Q, Men K. Multifunctional nanoparticle for cancer therapy. MedComm (2020) 2023;4:e187. [PMID: 36654533 DOI: 10.1002/mco2.187] [Reference Citation Analysis]
5 Pham LBT, Costantino A, Barbieri L, Calderone V, Luchinat E, Banci L. Direct Expression of Fluorinated Proteins in Human Cells for (19)F In-Cell NMR Spectroscopy. J Am Chem Soc 2023;145:1389-99. [PMID: 36604341 DOI: 10.1021/jacs.2c12086] [Reference Citation Analysis]
6 Gerothanassis IP. Ligand-observed in-tube NMR in natural products research: A review on enzymatic biotransformations, protein-ligand interactions, and in-cell NMR spectroscopy. Arabian Journal of Chemistry 2023. [DOI: 10.1016/j.arabjc.2022.104536] [Reference Citation Analysis]
7 Gerez JA, Prymaczok NC, Kadavath H, Ghosh D, Bütikofer M, Fleischmann Y, Güntert P, Riek R. Protein structure determination in human cells by in-cell NMR and a reporter system to optimize protein delivery or transexpression. Commun Biol 2022;5:1322. [PMID: 36460747 DOI: 10.1038/s42003-022-04251-6] [Cited by in Crossref: 2] [Cited by in F6Publishing: 1] [Article Influence: 2.0] [Reference Citation Analysis]
8 Yamaoki Y, Nagata T, Kondo K, Sakamoto T, Takami S, Katahira M. Shedding light on the base-pair opening dynamics of nucleic acids in living human cells. Nat Commun 2022;13:7143. [PMID: 36446768 DOI: 10.1038/s41467-022-34822-4] [Reference Citation Analysis]
9 Galazzo L, Bordignon E. Electron Paramagnetic Resonance Spectroscopy in structural-dynamic studies of large protein complexes. Progress in Nuclear Magnetic Resonance Spectroscopy 2022. [DOI: 10.1016/j.pnmrs.2022.11.001] [Reference Citation Analysis]
10 Pierro A, Bonucci A, Normanno D, Ansaldi M, Pilet E, Ouari O, Guigliarelli B, Etienne E, Gerbaud G, Magalon A, Belle V, Mileo E. Probing the Structural Dynamics of a Bacterial Chaperone in Its Native Environment by Nitroxide‐Based EPR Spectroscopy. Chemistry A European J 2022. [DOI: 10.1002/chem.202202249] [Reference Citation Analysis]
11 Theillet FX, Luchinat E. In-cell NMR: Why and how? Prog Nucl Magn Reson Spectrosc 2022;132-133:1-112. [PMID: 36496255 DOI: 10.1016/j.pnmrs.2022.04.002] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 1.0] [Reference Citation Analysis]
12 Gorensek-benitez AH, Kirk B, Myers JK. Protein Fibrillation under Crowded Conditions. Biomolecules 2022;12:950. [DOI: 10.3390/biom12070950] [Reference Citation Analysis]