Open Access Helper

OpenAlex Citation Counts

OpenAlex Citations Logo

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:

3D variability analysis: Resolving continuous flexibility and discrete heterogeneity from single particle cryo-EM
Ali Punjani, David J. Fleet
Journal of Structural Biology (2021) Vol. 213, Iss. 2, pp. 107702-107702
Open Access | Times Cited: 817

Showing 1-25 of 817 citing articles:

Atomic structures of respiratory complex III2, complex IV, and supercomplex III2-IV from vascular plants
María Maldonado, Fei Guo, James A. Letts
eLife (2021) Vol. 10
Open Access | Times Cited: 678
CryoDRGN: reconstruction of heterogeneous cryo-EM structures using neural networks
Ellen D. Zhong, Tristan Bepler, Bonnie Berger, et al.
Nature Methods (2021) Vol. 18, Iss. 2, pp. 176-185
Open Access | Times Cited: 496
SARS-CoV-2 variant prediction and antiviral drug design are enabled by RBD in vitro evolution
Jiří Zahradník, Shir Marciano, Maya Shemesh, et al.
Nature Microbiology (2021) Vol. 6, Iss. 9, pp. 1188-1198
Open Access | Times Cited: 379
Structural basis of ribosomal frameshifting during translation of the SARS-CoV-2 RNA genome
Pramod R. Bhatt, Alain Scaiola, Gary Loughran, et al.
Science (2021) Vol. 372, Iss. 6548, pp. 1306-1313
Open Access | Times Cited: 234
Structure of the bacterial ribosome at 2 Å resolution
Zoe L. Watson, Fred R. Ward, Raphaël Méheust, et al.
eLife (2020) Vol. 9
Open Access | Times Cited: 212
3DFlex: determining structure and motion of flexible proteins from cryo-EM
Ali Punjani, David J. Fleet
Nature Methods (2023) Vol. 20, Iss. 6, pp. 860-870
Open Access | Times Cited: 175
Hallucinating symmetric protein assemblies
Basile I. M. Wicky, Lukas F. Milles, Alexis Courbet, et al.
Science (2022) Vol. 378, Iss. 6615, pp. 56-61
Open Access | Times Cited: 157
Activation mechanism of PINK1
Zhong Yan Gan, Sylvie Callegari, Simon A. Cobbold, et al.
Nature (2021) Vol. 602, Iss. 7896, pp. 328-335
Open Access | Times Cited: 130
Cryo-EM structures of the SARS-CoV-2 endoribonuclease Nsp15 reveal insight into nuclease specificity and dynamics
Monica C. Pillon, Meredith N. Frazier, Lucas Dillard, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 118
Structure of a Janus kinase cytokine receptor complex reveals the basis for dimeric activation
Caleb R. Glassman, Naotaka Tsutsumi, Robert A. Saxton, et al.
Science (2022) Vol. 376, Iss. 6589, pp. 163-169
Open Access | Times Cited: 118
Mechanisms of BRCA1–BARD1 nucleosome recognition and ubiquitylation
Qi Hu, Maria Victoria Botuyan, Debiao Zhao, et al.
Nature (2021) Vol. 596, Iss. 7872, pp. 438-443
Open Access | Times Cited: 110
Cryo-EM advances in RNA structure determination
Haiyun Ma, Xinyu Jia, Kaiming Zhang, et al.
Signal Transduction and Targeted Therapy (2022) Vol. 7, Iss. 1
Open Access | Times Cited: 106
Better, Faster, Cheaper: Recent Advances in Cryo–Electron Microscopy
Eugene Chua, Joshua H. Mendez, Micah Rapp, et al.
Annual Review of Biochemistry (2022) Vol. 91, Iss. 1, pp. 1-32
Open Access | Times Cited: 105
R-loop formation and conformational activation mechanisms of Cas9
Martin Pačesa, Luuk Loeff, Irma Querques, et al.
Nature (2022) Vol. 609, Iss. 7925, pp. 191-196
Open Access | Times Cited: 101
Cyclic nucleotide-induced helical structure activates a TIR immune effector
Gaëlle Hogrel, Abbie Guild, Shirley Graham, et al.
Nature (2022) Vol. 608, Iss. 7924, pp. 808-812
Open Access | Times Cited: 96
Cryo-EM structure of the SARS-CoV-2 Omicron spike
Gabriele Cerutti, Yicheng Guo, Lihong Liu, et al.
Cell Reports (2022) Vol. 38, Iss. 9, pp. 110428-110428
Open Access | Times Cited: 95
Mechanism of replication origin melting nucleated by CMG helicase assembly
Jacob S. Lewis, Marta H Gross, Joana S. Sousa, et al.
Nature (2022) Vol. 606, Iss. 7916, pp. 1007-1014
Open Access | Times Cited: 80
Differential activation mechanisms of lipid GPCRs by lysophosphatidic acid and sphingosine 1-phosphate
Shian Liu, Navid Paknejad, Lan Zhu, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 74
Structural basis of regulated m7G tRNA modification by METTL1–WDR4
Jiazhi Li, Longfei Wang, Quentin Hahn, et al.
Nature (2023) Vol. 613, Iss. 7943, pp. 391-397
Closed Access | Times Cited: 63
GPCR activation and GRK2 assembly by a biased intracellular agonist
Jia Duan, Heng Liu, Fenghui Zhao, et al.
Nature (2023) Vol. 620, Iss. 7974, pp. 676-681
Open Access | Times Cited: 56
Sialoglycan binding triggers spike opening in a human coronavirus
Matti F. Pronker, Robert Creutznacher, Ieva Drulyte, et al.
Nature (2023) Vol. 624, Iss. 7990, pp. 201-206
Open Access | Times Cited: 50
Structure, folding and flexibility of co-transcriptional RNA origami
Ewan K.S. McRae, Helena Østergaard Rasmussen, Jianfang Liu, et al.
Nature Nanotechnology (2023) Vol. 18, Iss. 7, pp. 808-817
Open Access | Times Cited: 49
The structural basis for HIV-1 Vif antagonism of human APOBEC3G
Yen-Li Li, Caroline Langley, Caleigh M. Azumaya, et al.
Nature (2023) Vol. 615, Iss. 7953, pp. 728-733
Open Access | Times Cited: 48
Structures of sperm flagellar doublet microtubules expand the genetic spectrum of male infertility
Lunni Zhou, Haobin Liu, Siyu Liu, et al.
Cell (2023) Vol. 186, Iss. 13, pp. 2897-2910.e19
Open Access | Times Cited: 45
Template-assisted covalent modification of DCAF16 underlies activity of BRD4 molecular glue degraders
Yen-Der Li, W Michelle, Muhammad Murtaza Hassan, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 44
Page 1 - Next Page

Scroll to top