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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:

Modeling HIV-1 nuclear entry with nucleoporin-gated DNA-origami channels
Qi Shen, Qingzhou Feng, Chunxiang Wu, et al.
Nature Structural & Molecular Biology (2023) Vol. 30, Iss. 4, pp. 425-435
Open Access | Times Cited: 41

Showing 1-25 of 41 citing articles:

HIV-1 capsid shape, orientation, and entropic elasticity regulate translocation into the nuclear pore complex
Arpa Hudait, Gregory A. Voth
Proceedings of the National Academy of Sciences (2024) Vol. 121, Iss. 4
Open Access | Times Cited: 22
Passage of the HIV capsid cracks the nuclear pore
Jan Philipp Kreysing, Maziar Heidari, Vojtěch Žíla, et al.
Cell (2025)
Open Access | Times Cited: 8
Morphology remodelling and membrane channel formation in synthetic cells via reconfigurable DNA nanorafts
Sisi Fan, Shuo Wang, Longjiang Ding, et al.
Nature Materials (2025)
Open Access | Times Cited: 2
The capsid lattice engages a bipartite NUP153 motif to mediate nuclear entry of HIV-1 cores
Qi Shen, Sushila Kumari, Chaoyi Xu, et al.
Proceedings of the National Academy of Sciences (2023) Vol. 120, Iss. 13
Open Access | Times Cited: 33
Capsid–host interactions for HIV-1 ingress
Sooin Jang, Alan Engelman
Microbiology and Molecular Biology Reviews (2023) Vol. 87, Iss. 4
Open Access | Times Cited: 23
HIV-1 Capsid Uncoating Is a Multistep Process That Proceeds through Defect Formation Followed by Disassembly of the Capsid Lattice
Levi B. Gifford, Gregory B. Melikyan
ACS Nano (2024) Vol. 18, Iss. 4, pp. 2928-2947
Open Access | Times Cited: 11
Passage of the HIV capsid cracks the nuclear pore
Jan Philipp Kreysing, Maziar Heidari, Vojtěch Žíla, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Closed Access | Times Cited: 11
Dynamic molecular mechanism of the nuclear pore complex permeability barrier
Toshiya Kozai, Javier Fernández-Martı́nez, Trevor van Eeuwen, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 17
Spatiotemporal binding of cyclophilin A and CPSF6 to capsid regulates HIV-1 nuclear entry and integration
Zachary Ingram, Christopher E. Kline, Alexandra K. Hughson, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 8
MX2 forms nucleoporin-comprising cytoplasmic biomolecular condensates that lure viral capsids
George D. Moschonas, Louis Delhaye, Robin Cooreman, et al.
Cell Host & Microbe (2024) Vol. 32, Iss. 10, pp. 1705-1724.e14
Open Access | Times Cited: 7
Diameter dependence of transport through nuclear pore complex mimics studied using optical nanopores
Nils Klughammer, Anders Barth, Maurice Dekker, et al.
eLife (2024) Vol. 12
Open Access | Times Cited: 5
Channel width modulates the permeability of DNA origami–based nuclear pore mimics
Qingzhou Feng, Martin Saladin, Chunxiang Wu, et al.
Science Advances (2024) Vol. 10, Iss. 46
Open Access | Times Cited: 5
The nuclear localization signal of CPSF6 governs post-nuclear import steps of HIV-1 infection
Nicholas Rohlfes, Rajalingam Radhakrishnan, Parmit K. Singh, et al.
PLoS Pathogens (2025) Vol. 21, Iss. 1, pp. e1012354-e1012354
Open Access
Structural insights into HIV-2 CA lattice formation and FG-pocket binding revealed by single-particle cryo-EM
M. Katherine Cook, Christian Freniere, Chunxiang Wu, et al.
Cell Reports (2025) Vol. 44, Iss. 2, pp. 115245-115245
Closed Access
CPSF6 Promotes HIV-1 Preintegration Complex Function
Evan Chaudhuri, Sooin Jang, Rajasree Chakraborty, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2025)
Open Access
Recent Advances in DNA‐Templated Protein Patterning
Qinglin Xia, Mo Zhou, Kai Jiao, et al.
Small Methods (2025)
Closed Access
Conformational dynamics of the nuclear pore complex central channel
Yu Chen, Guoli Zhou, Miao Yu
Biochemical Society Transactions (2025) Vol. 53, Iss. 01
Closed Access
Spatiotemporal binding of cyclophilin A and CPSF6 to capsid regulates HIV-1 nuclear entry and integration
Zachary Ingram, Christopher E. Kline, Alexandra K. Hughson, et al.
mBio (2025)
Open Access
Novel Function of NUP153 in HNF4α Transcriptional Upregulation Contributes to Promoting HBV Replication
Qianqian Jiang, Zhou Zhao, Xinyu Du, et al.
Journal of Medical Virology (2025) Vol. 97, Iss. 3
Closed 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
Nup358 and Nup153 Facilitate nuclear import of BmNPV nucleocapsids in Bombyx mori cells
Kangping Yin, Tianran Zhang, Jinshan Huang, et al.
Journal of Invertebrate Pathology (2025) Vol. 211, pp. 108318-108318
Closed Access
CPSF6 promotes HIV-1 preintegration complex function
Evan Chaudhuri, Sooin Jang, Rajasree Chakraborty, et al.
Journal of Virology (2025)
Open Access
Unlocking New Frontiers in Cell Signaling and Communication and Fostering New Collaborative Interactions and Scientific Initiatives: Lessons Learned from the International Cellular Communication Network Society (ICCNS) Workshop
Bernard Perbal, Ralf Weiskirchen, Brahim Chaqour
(2025), pp. 1-1
Open Access
Unveiling the complexity: assessing models describing the structure and function of the nuclear pore complex
Coby Rush, Zecheng Jiang, Mark Tingey, et al.
Frontiers in Cell and Developmental Biology (2023) Vol. 11
Open Access | Times Cited: 9
DNA-Origami-Based Precise Molecule Assembly and Their Biological Applications
Guize Li, C.S Chen, Yingying Li, et al.
Nano Letters (2024)
Closed Access | Times Cited: 3
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