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 26-50 of 41 citing articles:

Diameter dependence of transport through nuclear pore complex mimics studied using optical nanopores
Nils Klughammer, Anders Barth, Maurice Dekker, et al.
eLife (2023) Vol. 12
Open Access | Times Cited: 8

HIV-1 Capsid Rapidly Induces Long-Lived CPSF6 Puncta in Non-Dividing Cells, but Similar Puncta Already Exist in Uninfected T-Cells
Anabel Guedán, Megan Burley, Eve R. Caroe, et al.
Viruses (2024) Vol. 16, Iss. 5, pp. 670-670
Open Access | Times Cited: 2

The nuclear localization signal of CPSF6 governs post-nuclear import steps of HIV-1 infection
Nicholas Rohlfes, Rajalingam Radhakrishnan, Parmit K. Singh, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 2

May I Help You with Your Coat? HIV-1 Capsid Uncoating and Reverse Transcription
Laura Arribas, Luis Menéndez‐Arias, Gilberto Betancor
International Journal of Molecular Sciences (2024) Vol. 25, Iss. 13, pp. 7167-7167
Open Access | Times Cited: 2

MX2 restricts HIV-1 and herpes simplex virus type 1 by forming cytoplasmic biomolecular condensates that mimic nuclear pore complexes
George D. Moschonas, Louis Delhaye, Robin Cooreman, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 5

Diameter Dependence of Transport through Nuclear Pore Complex Mimics Studied Using Optical Nanopores
Nils Klughammer, Anders Barth, Maurice Dekker, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 4

Molecular Mechanisms of Nuclear Import of Baculovirus Proteins
Jiale Li, Xing-Yang Wang, Xiao‐Feng Wu
(2024)
Open Access | Times Cited: 1

A new class of capsid-targeting inhibitors that specifically block HIV-1 nuclear import
Aude Boulay, Emmanuel Quevarec, Isabelle Malet, et al.
EMBO Molecular Medicine (2024) Vol. 16, Iss. 11, pp. 2918-2945
Open Access | Times Cited: 1

DNA-Programmed Biomolecular Spatial Pattern Recognition
Yue Wang, Lei Ren, Hongzhen Peng, et al.
Chemosensors (2023) Vol. 11, Iss. 7, pp. 362-362
Open Access | Times Cited: 2

Human Immunodeficiency Virus 1 Capsid Uncoating in the Nucleus Progresses Through Defect Formation in the Capsid Lattice
Levi B. Gifford, Gregory B. Melikyan
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 2

HIV-1 Capsid Shape, Orientation, and Entropic Elasticity Regulate Translocation into the Nuclear Pore Complex
Arpa Hudait, Gregory A. Voth
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 1

Diameter Dependence of Transport through Nuclear Pore Complex Mimics Studied Using Optical Nanopores
Nils Klughammer, Anders Barth, Maurice Dekker, et al.
(2023)
Open Access | Times Cited: 1

HIV-1 Capsid Rapidly Induces Long Lived CPSF6 Puncta in Non-dividing Cells but Similar Puncta Already Exist in Uninfected T-cells
Anabel Guedán, Megan Burley, Eve R. Caroe, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access

Channel width modulates the permeability of DNA origami based nuclear pore mimics
Qingzhou Feng, Martin Saladin, Chunxiang Wu, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access

Label-free imaging of nuclear membrane for analysis of nuclear import of viral complexes
Andrew Ten Eyck, Yen-Cheng Chen, Levi B. Gifford, et al.
Journal of Virological Methods (2023) Vol. 322, pp. 114834-114834
Closed Access

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