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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:

Structure and Function of the Nuclear Pore Complex
Stefan Petrovic, George W. Mobbs, Christopher J. Bley, et al.
Cold Spring Harbor Perspectives in Biology (2022), pp. a041264-a041264
Closed Access | Times Cited: 42

Showing 1-25 of 42 citing articles:

Nuclear transport proteins: structure, function, and disease relevance
Yang Yang, Lu Guo, Lin Chen, et al.
Signal Transduction and Targeted Therapy (2023) Vol. 8, Iss. 1
Open Access | Times Cited: 62
Improving the hole picture: towards a consensus on the mechanism of nuclear transport
David Cowburn, Michael P. Rout
Biochemical Society Transactions (2023) Vol. 51, Iss. 2, pp. 871-886
Open Access | Times Cited: 22
Altered nuclear envelope homeostasis is a key pathogenic event in C9ORF72-linked ALS/FTD
Riccardo Sirtori, Michelle Gregoire, Alicia Collins, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 6
An Efficient Method for Isolating and Purifying Nuclei from Mice Brain for Single-Molecule Imaging Using High-Speed Atomic Force Microscopy
Yujia Qiu, Elma Sakinatus Sajidah, Sota Kondo, et al.
Cells (2024) Vol. 13, Iss. 3, pp. 279-279
Open Access | Times Cited: 5
Nuclear localization signal-tagged systems: relevant nuclear import principles in the context of current therapeutic design
Ritabrita Goswami, Aarohi Gupta, Olga Bednova, et al.
Chemical Society Reviews (2023) Vol. 53, Iss. 1, pp. 204-226
Closed Access | Times Cited: 13
Implications of a multiscale structure of the yeast nuclear pore complex
Christopher W. Akey, Ignacia Echeverria, Christna Ouch, et al.
Molecular Cell (2023) Vol. 83, Iss. 18, pp. 3283-3302.e5
Open Access | Times Cited: 12
Role of mRNA-binding proteins in retinal neovascularization
Pei Lin, Wenye Cao, Xuemei Chen, et al.
Experimental Eye Research (2024) Vol. 242, pp. 109870-109870
Closed Access | Times Cited: 4
Nucleoporin-associated steroid-resistant nephrotic syndrome
Ling Yao, Yuanyuan Li, Ping Wang, et al.
Pediatric Nephrology (2024)
Closed Access | Times Cited: 4
Strategies for the Viral Exploitation of Nuclear Pore Transport Pathways
Xin Zhang, Keesiang Lim, Yujia Qiu, et al.
Viruses (2025) Vol. 17, Iss. 2, pp. 151-151
Open Access
Mechanisms of PP2A-Ankle2 dependent nuclear reassembly after mitosis
Jingjing Li, Xinyue Wang, Laia Jordana, et al.
(2025)
Open Access
Effects of GS-CA1 on nuclear envelope-associated early HIV-1 infection steps
Amita Singh, Victor Fourcassié, Karen Cristine Gonçalves dos Santos, et al.
Frontiers in Virology (2025) Vol. 5
Open Access
Mechanisms of PP2A-Ankle2 dependent nuclear reassembly after mitosis
Jingjing Li, Xinyue Wang, Laia Jordana, et al.
eLife (2025) Vol. 13
Open Access
Correlative In Situ Cryo-ET Reveals Cellular and Viral Remodeling Associated with Selective HIV-1 Core Nuclear Import
Zhen Hou, Y. Shen, Stanley Fronik, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2025)
Open Access
Homeostatic regulation of nucleoporins is a central driver of nuclear pore biogenesis
Stephen Sakuma, Marcela Raı́ces, Ethan Y.S. Zhu, et al.
Cell Reports (2025), pp. 115468-115468
Open Access
ZC3HC1 has functions distinct from TPR and is dispensable for TPR localisation to the nuclear basket
Bethany M Bartlett, Juan Carlos Acosta, Wendy A. Bickmore
Wellcome Open Research (2025) Vol. 10, pp. 188-188
Open Access
Novel biallelicNUP107variants affect the nuclear pore complex and expand the clinical spectrum to include brain malformations
Loisa Dana Bonde, Laura Hecher, Malik Alawi, et al.
Journal of Medical Genetics (2025), pp. jmg-110671
Closed Access
You are who your friends are—nuclear pore proteins as components of chromatin‐binding complexes
Maya Capelson
FEBS Letters (2023) Vol. 597, Iss. 22, pp. 2769-2781
Open Access | Times Cited: 9
Puzzling out nuclear pore complex assembly
Arianna Penzo, Benoı̂t Palancade
FEBS Letters (2023) Vol. 597, Iss. 22, pp. 2705-2727
Open Access | Times Cited: 8
Nucleoporin Nsp1 surveils the phase state of FG-Nups
Tegan A. Otto, Tessa Bergsma, Maurice Dekker, et al.
Cell Reports (2024) Vol. 43, Iss. 10, pp. 114793-114793
Open Access | Times Cited: 3
Nucleoporin Nsp1 surveils the phase state of FG-Nups
Tegan A. Otto, Tessa Bergsma, Maurice Dekker, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 8
RANBP2 evolution and human disease
Sophie Desgraupes, Lucie Etienne, Nathalie J. Arhel
FEBS Letters (2023) Vol. 597, Iss. 20, pp. 2519-2533
Open Access | Times Cited: 8
Nuclear elongation during spermiogenesis depends on physical linkage of nuclear pore complexes to bundled microtubules by Drosophila Mst27D
Pengfei Li, Giovanni Messina, Christian F. Lehner
PLoS Genetics (2023) Vol. 19, Iss. 7, pp. e1010837-e1010837
Open Access | Times Cited: 7
What Is the Role of Nuclear Envelope Proteins in Neurologic Disorders?
Eduardo E. Benarroch
Neurology (2024) Vol. 102, Iss. 5
Closed Access | Times Cited: 2
Nanoimaging of SARS-CoV-2 viral invasion toward the nucleus and genome
Elma Sakinatus Sajidah, Keesiang Lim, Masaharu Hazawa, et al.
Cell Reports Physical Science (2024) Vol. 5, Iss. 9, pp. 102111-102111
Open Access | Times Cited: 2
Particle fusion of super-resolution data reveals the unit structure of Nup96 in Nuclear Pore Complex
Wenxiu Wang, Arjen J. Jakobi, Yule Wu, et al.
Scientific Reports (2023) Vol. 13, Iss. 1
Open Access | Times Cited: 5
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