OpenAlex Citation Counts

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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:

Probing Protein Conformation in Cells by EPR Distance Measurements using Gd3+ Spin Labeling
Andrea Martorana, Giuliano Bellapadrona, Akiva Feintuch, et al.
Journal of the American Chemical Society (2014) Vol. 136, Iss. 38, pp. 13458-13465
Closed Access | Times Cited: 201

Showing 1-25 of 201 citing articles:

Structural disorder of monomeric α-synuclein persists in mammalian cells
François‐Xavier Theillet, Andrés Binolfi, Beata Bekei, et al.
Nature (2016) Vol. 530, Iss. 7588, pp. 45-50
Open Access | Times Cited: 796

Intracellular Delivery by Membrane Disruption: Mechanisms, Strategies, and Concepts
Martin P. Stewart, Róbert Langer, Klavs F. Jensen
Chemical Reviews (2018) Vol. 118, Iss. 16, pp. 7409-7531
Open Access | Times Cited: 594

Dynamic nuclear polarization for sensitivity enhancement in modern solid-state NMR
Aany Sofia Lilly Thankamony, Johannes Wittmann, Monu Kaushik, et al.
Progress in Nuclear Magnetic Resonance Spectroscopy (2017) Vol. 102-103, pp. 120-195
Open Access | Times Cited: 510

Dynamic Nuclear Polarization for Sensitivity Enhancement in Biomolecular Solid-State NMR
Thomas Biedenbänder, Victoria Aladin, Siavash Saeidpour, et al.
Chemical Reviews (2022) Vol. 122, Iss. 10, pp. 9738-9794
Closed Access | Times Cited: 99

In-Cell Structural Biology by NMR: The Benefits of the Atomic Scale
François‐Xavier Theillet
Chemical Reviews (2022) Vol. 122, Iss. 10, pp. 9497-9570
Open Access | Times Cited: 80

Ultrafast Bioorthogonal Spin-Labeling and Distance Measurements in Mammalian Cells Using Small, Genetically Encoded Tetrazine Amino Acids
Subhashis Jana, Eric G.B. Evans, Hyo Sang Jang, et al.
Journal of the American Chemical Society (2023) Vol. 145, Iss. 27, pp. 14608-14620
Open Access | Times Cited: 42

Single-molecule scale magnetic resonance spectroscopy using quantum diamond sensors
Jiangfeng Du, Fazhan Shi, Xi Kong, et al.
Reviews of Modern Physics (2024) Vol. 96, Iss. 2
Closed Access | Times Cited: 20

Gd(III)-PyMTA Label Is Suitable for In-Cell EPR
Mian Qi, Andreas Groß, Gunnar Jeschke, et al.
Journal of the American Chemical Society (2014) Vol. 136, Iss. 43, pp. 15366-15378
Closed Access | Times Cited: 166

Versatile Trityl Spin Labels for Nanometer Distance Measurements on Biomolecules In Vitro and within Cells
Jean Jacques Jassoy, Andreas Berndhäuser, Fraser Duthie, et al.
Angewandte Chemie International Edition (2016) Vol. 56, Iss. 1, pp. 177-181
Closed Access | Times Cited: 132

Site-directed spin labeling of proteins for distance measurements in vitro and in cells
Patrick Roser, Moritz J. Schmidt, Malte Drescher, et al.
Organic & Biomolecular Chemistry (2016) Vol. 14, Iss. 24, pp. 5468-5476
Open Access | Times Cited: 106

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

3D structure determination of a protein in living cells using paramagnetic NMR spectroscopy
Binbin Pan, Feng Yang, Yansheng Ye, et al.
Chemical Communications (2016) Vol. 52, Iss. 67, pp. 10237-10240
Open Access | Times Cited: 102

Distance Measurement on an Endogenous Membrane Transporter in E. coli Cells and Native Membranes Using EPR Spectroscopy
Benesh Joseph, Arthur Sikora, Enrica Bordignon, et al.
Angewandte Chemie International Edition (2015) Vol. 54, Iss. 21, pp. 6196-6199
Open Access | Times Cited: 100

Gd(iii)–Gd(iii) EPR distance measurements – the range of accessible distances and the impact of zero field splitting
Arina Dalaloyan, Mian Qi, Sharon Ruthstein, et al.
Physical Chemistry Chemical Physics (2015) Vol. 17, Iss. 28, pp. 18464-18476
Closed Access | Times Cited: 95

Gd(III)–Gd(III) distance measurements with chirp pump pulses
Andrin Doll, Mian Qi, Nino Wili, et al.
Journal of Magnetic Resonance (2015) Vol. 259, pp. 153-162
Closed Access | Times Cited: 95

A Reactive, Rigid GdIII Labeling Tag for In‐Cell EPR Distance Measurements in Proteins
Yin Yang, Feng Yang, Yanjun Gong, et al.
Angewandte Chemie International Edition (2017) Vol. 56, Iss. 11, pp. 2914-2918
Closed Access | Times Cited: 95

Structural Biology outside the box — inside the cell
Jürgen M. Plitzko, Benjamin Schuler, Philipp Selenko
Current Opinion in Structural Biology (2017) Vol. 46, pp. 110-121
Open Access | Times Cited: 90

Ligand Induced Conformational Changes of a Membrane Transporter in E. coli Cells Observed with DEER/PELDOR
Benesh Joseph, Arthur Sikora, David S. Cafiso
Journal of the American Chemical Society (2016) Vol. 138, Iss. 6, pp. 1844-1847
Open Access | Times Cited: 89

In-Cell Protein Structures from 2D NMR Experiments
Thomas Müntener, Daniel Häußinger, Philipp Selenko, et al.
The Journal of Physical Chemistry Letters (2016) Vol. 7, Iss. 14, pp. 2821-2825
Closed Access | Times Cited: 88

SLIM: A Short‐Linked, Highly Redox‐Stable Trityl Label for High‐Sensitivity In‐Cell EPR Distance Measurements
Nico Fleck, Caspar A. Heubach, Tobias Hett, et al.
Angewandte Chemie International Edition (2020) Vol. 59, Iss. 24, pp. 9767-9772
Open Access | Times Cited: 88

Gd(iii) and Mn(ii) complexes for dynamic nuclear polarization: small molecular chelate polarizing agents and applications with site-directed spin labeling of proteins
Monu Kaushik, Thorsten Bahrenberg, Thach V. Can, et al.
Physical Chemistry Chemical Physics (2016) Vol. 18, Iss. 39, pp. 27205-27218
Open Access | Times Cited: 86

In-Cell NMR in Human Cells: Direct Protein Expression Allows Structural Studies of Protein Folding and Maturation
Enrico Luchinat, Lucia Banci
Accounts of Chemical Research (2018) Vol. 51, Iss. 6, pp. 1550-1557
Open Access | Times Cited: 86

In-Cell Trityl–Trityl Distance Measurements on Proteins
Yin Yang, Binbin Pan, Xiaoli Tan, et al.
The Journal of Physical Chemistry Letters (2020) Vol. 11, Iss. 3, pp. 1141-1147
Open Access | Times Cited: 76

Exploring protein conformations in vitro and in cell with EPR distance measurements
Daniella Goldfarb
Current Opinion in Structural Biology (2022) Vol. 75, pp. 102398-102398
Open Access | Times Cited: 61

Exploring the dynamics and structure of PpiB in living Escherichia coli cells using electron paramagnetic resonance spectroscopy
Yasmin Ben‐Ishay, Yoav Barak, Akiva Feintuch, et al.
Protein Science (2024) Vol. 33, Iss. 3
Open Access | Times Cited: 12

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