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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:

Mitigating local over-fitting during single particle reconstruction with SIDESPLITTER
Kailash Ramlaul, Colin M. Palmer, Takanori Nakane, et al.
Journal of Structural Biology (2020) Vol. 211, Iss. 2, pp. 107545-107545
Open Access | Times Cited: 100

Showing 1-25 of 100 citing articles:

Non-uniform refinement: adaptive regularization improves single-particle cryo-EM reconstruction
Ali Punjani, Haowei Zhang, David J. Fleet
Nature Methods (2020) Vol. 17, Iss. 12, pp. 1214-1221
Open Access | Times Cited: 1310
SARS-CoV-2 RBD antibodies that maximize breadth and resistance to escape
Tyler N. Starr, Nadine Czudnochowski, Zhuoming Liu, et al.
Nature (2021) Vol. 597, Iss. 7874, pp. 97-102
Open Access | Times Cited: 502
Multi-particle cryo-EM refinement with M visualizes ribosome-antibiotic complex at 3.5 Å in cells
Dimitry Tegunov, Liang Xue, Christian Dienemann, et al.
Nature Methods (2021) Vol. 18, Iss. 2, pp. 186-193
Open Access | Times Cited: 404
Molecular basis of β-arrestin coupling to formoterol-bound β1-adrenoceptor
Yang Lee, Tony Warne, Rony Nehmé, et al.
Nature (2020) Vol. 583, Iss. 7818, pp. 862-866
Open Access | Times Cited: 234
Structure of the SARS-CoV-2 RNA-dependent RNA polymerase in the presence of favipiravir-RTP
Katerina Naydenova, Kyle Muir, Long-Fei Wu, et al.
Proceedings of the National Academy of Sciences (2021) Vol. 118, Iss. 7
Open Access | Times Cited: 175
Structural basis for channel conduction in the pump-like channelrhodopsin ChRmine
Koichiro Kishi, Yoon Seok Kim, Masahiro Fukuda, et al.
Cell (2022) Vol. 185, Iss. 4, pp. 672-689.e23
Open Access | Times Cited: 109
Structures of human mGlu2 and mGlu7 homo- and heterodimers
Juan Du, Dejian Wang, Hongcheng Fan, et al.
Nature (2021) Vol. 594, Iss. 7864, pp. 589-593
Open Access | Times Cited: 104
Data-driven regularization lowers the size barrier of cryo-EM structure determination
Dari Kimanius, Kiarash Jamali, Max E. Wilkinson, et al.
Nature Methods (2024) Vol. 21, Iss. 7, pp. 1216-1221
Open Access | Times Cited: 59
Membrane phospholipids control gating of the mechanosensitive potassium leak channel TREK1
Philipp A. M. Schmidpeter, John T. Petroff, Leila Khajoueinejad, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 43
Structural insights into the regulation of human serine palmitoyltransferase complexes
Yingdi Wang, Yiming Niu, Zhe Zhang, et al.
Nature Structural & Molecular Biology (2021) Vol. 28, Iss. 3, pp. 240-248
Open Access | Times Cited: 83
Structure and efflux mechanism of the yeast pleiotropic drug resistance transporter Pdr5
Andrzej Harris, Manuel Wagner, Dijun Du, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 82
Structural and mechanistic basis of the EMC-dependent biogenesis of distinct transmembrane clients
Lakshmi E. Miller-Vedam, Bastian Bräuning, Katerina D. Popova, et al.
eLife (2020) Vol. 9
Open Access | Times Cited: 80
Structure and dynamics of the CGRP receptor in apo and peptide-bound forms
Tracy M. Josephs, Matthew J. Belousoff, Yi-Lynn Liang, et al.
Science (2021) Vol. 372, Iss. 6538
Closed Access | Times Cited: 73
Structure of the class D GPCR Ste2 dimer coupled to two G proteins
Vaithish Velazhahan, Ning Ma, Gáspár Pándy‐Szekeres, et al.
Nature (2020) Vol. 589, Iss. 7840, pp. 148-153
Open Access | Times Cited: 72
Structures of the human cholecystokinin 1 (CCK1) receptor bound to Gs and Gq mimetic proteins provide insight into mechanisms of G protein selectivity
Jesse I. Mobbs, Matthew J. Belousoff, Kaleeckal G. Harikumar, et al.
PLoS Biology (2021) Vol. 19, Iss. 6, pp. e3001295-e3001295
Open Access | Times Cited: 71
Structural snapshots of human PepT1 and PepT2 reveal mechanistic insights into substrate and drug transport across epithelial membranes
Maxime Killer, Jiri Wald, Joanna Pieprzyk, et al.
Science Advances (2021) Vol. 7, Iss. 45
Open Access | Times Cited: 70
Differential assembly diversifies GABAA receptor structures and signalling
Andrija Sente, Rooma Desai, Katerina Naydenova, et al.
Nature (2022) Vol. 604, Iss. 7904, pp. 190-194
Open Access | Times Cited: 66
High-throughput cryo-EM structure determination of amyloids
Sofia Lövestam, Sjors H. W. Scheres
Faraday Discussions (2022) Vol. 240, pp. 243-260
Open Access | Times Cited: 46
Structural basis of branch site recognition by the human spliceosome
Jonas Tholen, Michał Rażew, Félix Weis, et al.
Science (2022) Vol. 375, Iss. 6576, pp. 50-57
Open Access | Times Cited: 43
Structure, mechanism and lipid-mediated remodeling of the mammalian Na+/H+ exchanger NHA2
Rei Matsuoka, Roman Fudim, Suk‐Kyeong Jung, et al.
Nature Structural & Molecular Biology (2022) Vol. 29, Iss. 2, pp. 108-120
Open Access | Times Cited: 43
A robust normalized local filter to estimate compositional heterogeneity directly from cryo-EM maps
Björn Forsberg, Pranav N. M. Shah, Alister Burt
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 29
Structural basis for conformational equilibrium of the catalytic spliceosome
Max E. Wilkinson, Sebastian M. Fica, Wojciech P. Galej, et al.
Molecular Cell (2021) Vol. 81, Iss. 7, pp. 1439-1452.e9
Open Access | Times Cited: 51
The structural basis for regulation of the glutathione transporter Ycf1 by regulatory domain phosphorylation
Nitesh Khandelwal, Cinthia Millán, Samantha I. Zangari, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 37
Structure of the type V-C CRISPR-Cas effector enzyme
Nina Kurihara, Ryoya Nakagawa, Hisato Hirano, et al.
Molecular Cell (2022) Vol. 82, Iss. 10, pp. 1865-1877.e4
Open Access | Times Cited: 33
Structural insights into inhibitory mechanism of human excitatory amino acid transporter EAAT2
T. Kato, Tsukasa Kusakizako, Chunhuan Jin, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 33
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