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OpenAlex is a bibliographic catalogue of scientific papers, authors and institutions accessible in open access mode, named after the Library of Alexandria. It's citation coverage is excellent and I hope you will find utility in this listing of citing articles!

If you click the article title, you'll navigate to the article, as listed in CrossRef. If you click the Open Access links, you'll navigate to the "best Open Access location". Clicking the citation count will open this listing for that article. Lastly at the bottom of the page, you'll find basic pagination options.

Requested Article:

Enlarging the Panoply of Site-Directed Spin Labeling Electron Paramagnetic Resonance (SDSL-EPR): Sensitive and Selective Spin-Labeling of Tyrosine Using an Isoindoline-Based Nitroxide
Elisabetta Mileo, Émilien Étienne, Marlène Martinho, et al.
Bioconjugate Chemistry (2013) Vol. 24, Iss. 6, pp. 1110-1117
Closed Access | Times Cited: 43

Showing 1-25 of 43 citing articles:

Advances in Chemical Protein Modification
Omar Boutureira, Gonçalo J. L. Bernardes
Chemical Reviews (2015) Vol. 115, Iss. 5, pp. 2174-2195
Open Access | Times Cited: 1008
Introducing Protein Intrinsic Disorder
Johnny Habchi, Péter Tompa, Sonia Longhi, et al.
Chemical Reviews (2014) Vol. 114, Iss. 13, pp. 6561-6588
Open Access | Times Cited: 703
Sterically shielded spin labels for in-cell EPR spectroscopy: Analysis of stability in reducing environment
Anil P. Jagtap, Ivan Krstić, Nitin C. Kunjir, et al.
Free Radical Research (2014) Vol. 49, Iss. 1, pp. 78-85
Closed Access | Times Cited: 153
Site-Selective Functionalization of Methionine Residues via Photoredox Catalysis
Junyong Kim, Beryl X. Li, Richard Y.‐C. Huang, et al.
Journal of the American Chemical Society (2020) Vol. 142, Iss. 51, pp. 21260-21266
Open Access | Times Cited: 120
A Bioresistant Nitroxide Spin Label for In‐Cell EPR Spectroscopy: In Vitro and In Oocytes Protein Structural Dynamics Studies
Ganesan Karthikeyan, Alessio Bonucci, Gilles Casano, et al.
Angewandte Chemie International Edition (2017) Vol. 57, Iss. 5, pp. 1366-1370
Closed Access | Times Cited: 103
Nitroxide spin labels and EPR spectroscopy: A powerful association for protein dynamics studies
Francesco Torricella, Annalisa Pierro, Elisabetta Mileo, et al.
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics (2021) Vol. 1869, Iss. 7, pp. 140653-140653
Open Access | Times Cited: 82
Intrinsically disordered proteins of viruses: Involvement in the mechanism of cell regulation and pathogenesis
Pushpendra Mani Mishra, Navneet C. Verma, Chethana Rao, et al.
Progress in molecular biology and translational science (2020), pp. 1-78
Open Access | Times Cited: 76
In‐Cell EPR: Progress towards Structural Studies Inside Cells
Alessio Bonucci, Olivier Ouari, Bruno Guigliarelli, et al.
ChemBioChem (2019) Vol. 21, Iss. 4, pp. 451-460
Open Access | Times Cited: 69
Exploring intrinsically disordered proteins using site-directed spin labeling electron paramagnetic resonance spectroscopy
Nolwenn Le Breton, Marlène Martinho, Elisabetta Mileo, et al.
Frontiers in Molecular Biosciences (2015) Vol. 2
Open Access | Times Cited: 54
A molecular engineering toolbox for the structural biologist
Galia T. Debelouchina, Tom W. Muir
Quarterly Reviews of Biophysics (2017) Vol. 50
Open Access | Times Cited: 54
Expanding the diversity of nitroxide‐based paramagnetic probes conjugated to non‐canonical amino acids for SDSL‐EPR applications
Maxime Bizet, Áron Balázsi, Frédéric Biaso, et al.
ChemBioChem (2025)
Open Access
Development and Application of Spin Traps, Spin Probes, and Spin Labels
Elena G. Bagryanskaya, Olesya A. Krumkacheva, Matvey V. Fedin, et al.
Methods in enzymology on CD-ROM/Methods in enzymology (2015), pp. 365-396
Closed Access | Times Cited: 46
Site-directed spin labeling of 2′-amino groups in RNA with isoindoline nitroxides that are resistant to reduction
Subham Saha, Anil P. Jagtap, Snorri Th. Sigurdsson
Chemical Communications (2015) Vol. 51, Iss. 66, pp. 13142-13145
Closed Access | Times Cited: 43
SimLabel: a graphical user interface to simulate continuous wave EPR spectra from site‐directed spin labeling experiments
Émilien Étienne, Nolwenn Le Breton, Marlène Martinho, et al.
Magnetic Resonance in Chemistry (2017) Vol. 55, Iss. 8, pp. 714-719
Closed Access | Times Cited: 38
EPR of site-directed spin-labeled proteins: A powerful tool to study structural flexibility
Inés García‐Rubio
Archives of Biochemistry and Biophysics (2020) Vol. 684, pp. 108323-108323
Open Access | Times Cited: 30
In-cell investigation of the conformational landscape of the GTPase UreG by SDSL-EPR
Annalisa Pierro, Ketty C. Tamburrini, Hugo Le Guenno, et al.
iScience (2023) Vol. 26, Iss. 10, pp. 107855-107855
Open Access | Times Cited: 9
Orthogonal Tyrosine and Cysteine Site-Directed Spin Labeling for Dipolar Pulse EPR Spectroscopy on Proteins
Christoph Gmeiner, Daniel Klose, Elisabetta Mileo, et al.
The Journal of Physical Chemistry Letters (2017) Vol. 8, Iss. 19, pp. 4852-4857
Closed Access | Times Cited: 31
A Bioresistant Nitroxide Spin Label for In‐Cell EPR Spectroscopy: In Vitro and In Oocytes Protein Structural Dynamics Studies
Ganesan Karthikeyan, Alessio Bonucci, Gilles Casano, et al.
Angewandte Chemie (2017) Vol. 130, Iss. 5, pp. 1380-1384
Closed Access | Times Cited: 30
Toward increased concentration sensitivity for continuous wave EPR investigations of spin-labeled biological macromolecules at high fields
Likai Song, Zhanglong Liu, Pavanjeet Kaur, et al.
Journal of Magnetic Resonance (2016) Vol. 265, pp. 188-196
Open Access | Times Cited: 27
Isoindoline‐Based Nitroxides as Bioresistant Spin Labels for Protein Labeling through Cysteines and Alkyne‐Bearing Noncanonical Amino Acids
Theresa Braun, Pia Widder, Uwe Osswald, et al.
ChemBioChem (2019) Vol. 21, Iss. 7, pp. 958-962
Open Access | Times Cited: 26
Dynamics of the intrinsically disordered protein CP12 in its association with GAPDH in the green alga Chlamydomonas reinhardtii: a fuzzy complex
Elisabetta Mileo, Magali Lorenzi, Jenny Erales, et al.
Molecular BioSystems (2013) Vol. 9, Iss. 11, pp. 2869-2869
Closed Access | Times Cited: 28
Protein Spin Labeling with a Photocaged Nitroxide Using Diels–Alder Chemistry
Anandi Kugele, Bjarne Silkenath, J Langer, et al.
ChemBioChem (2019) Vol. 20, Iss. 19, pp. 2479-2484
Open Access | Times Cited: 24
Impact of Cellular Crowding on Protein Structural Dynamics Investigated by EPR Spectroscopy
Annalisa Pierro, Alessio Bonucci, Axel Magalon, et al.
Chemical Reviews (2024) Vol. 124, Iss. 17, pp. 9873-9898
Closed Access | Times Cited: 2
Guidelines for the Simulations of Nitroxide X-Band cw EPR Spectra from Site-Directed Spin Labeling Experiments Using SimLabel
Émilien Étienne, Annalisa Pierro, Ketty C. Tamburrini, et al.
Molecules (2023) Vol. 28, Iss. 3, pp. 1348-1348
Open Access | Times Cited: 6
Continuous wave W- and D-Band EPR spectroscopy offer “sweet-spots” for characterizing conformational changes and dynamics in intrinsically disordered proteins
Thomas M. Casey, Zhanglong Liu, Jackie M. Esquiaqui, et al.
Biochemical and Biophysical Research Communications (2014) Vol. 450, Iss. 1, pp. 723-728
Open Access | Times Cited: 20
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