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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:

Direct binding of ESCRT protein Chm7 to phosphatidic acid–rich membranes at nuclear envelope herniations
David J. Thaller, Danqing Tong, Christopher J. Marklew, et al.
The Journal of Cell Biology (2021) Vol. 220, Iss. 3
Open Access | Times Cited: 51

Showing 1-25 of 51 citing articles:

The ESCRT Machinery: Remodeling, Repairing, and Sealing Membranes
Yolanda Olmos
Membranes (2022) Vol. 12, Iss. 6, pp. 633-633
Open Access | Times Cited: 54
Biophysical and molecular mechanisms of ESCRT functions, and their implications for disease
Simona M. Migliano, Eva M. Wenzel, Harald Stenmark
Current Opinion in Cell Biology (2022) Vol. 75, pp. 102062-102062
Open Access | Times Cited: 49
The Nuclear Pore Complex: Birth, Life, and Death of a Cellular Behemoth
Elisa Dultz, Matthias Wojtynek, Ohad Medalia, et al.
Cells (2022) Vol. 11, Iss. 9, pp. 1456-1456
Open Access | Times Cited: 44
Phosphatidic acid: from biophysical properties to diverse functions
Hejiang Zhou, Yanwu Huo, Na Yang, et al.
FEBS Journal (2023) Vol. 291, Iss. 9, pp. 1870-1885
Open Access | Times Cited: 39
Lipid saturation controls nuclear envelope function
Anete Romanauska, Alwin Köhler
Nature Cell Biology (2023) Vol. 25, Iss. 9, pp. 1290-1302
Open Access | Times Cited: 39
A membrane-sensing mechanism links lipid metabolism to protein degradation at the nuclear envelope
Shoken Lee, Jake W. Carrasquillo Rodrı́guez, Holly Merta, et al.
The Journal of Cell Biology (2023) Vol. 222, Iss. 9
Open Access | Times Cited: 27
Nuclear and degradative functions of the ESCRT-III pathway: implications for neurodegenerative disease
Olivia Keeley, Alyssa N. Coyne
Nucleus (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 6
ESCRT Is a Great Sealer: Non-Endosomal Function of the ESCRT Machinery in Membrane Repair and Autophagy
Erika Isono
Plant and Cell Physiology (2021) Vol. 62, Iss. 5, pp. 766-774
Closed Access | Times Cited: 35
Distinct EH domains of the endocytic TPLATE complex confer lipid and protein binding
Klaas Yperman, Anna C. Papageorgiou, Romain Merceron, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 33
Phosphatidic acid signaling and function in nuclei
Shuaibing Yao, Sang‐Chul Kim, Jianwu Li, et al.
Progress in Lipid Research (2023) Vol. 93, pp. 101267-101267
Closed Access | Times Cited: 15
Inner nuclear membrane proteins Lem2 and Bqt4 interact with different lipid synthesis enzymes in fission yeast
Yasuhiro Hirano, Yasuha Kinugasa, Yoshino Kubota, et al.
The Journal of Biochemistry (2023) Vol. 174, Iss. 1, pp. 33-46
Open Access | Times Cited: 14
An ESCRT grommet cooperates with a diffusion barrier to maintain nuclear integrity
Nicholas R. Ader, Linda Chen, Ivan V. Surovtsev, et al.
Nature Cell Biology (2023) Vol. 25, Iss. 10, pp. 1465-1477
Open Access | Times Cited: 14
Behind the stoNE wall: a fervent activity for nuclear lipids
Kseniya Samardak, Janélie Bâcle, María Moriel‐Carretero
Biochimie (2024)
Closed Access | Times Cited: 5
Coupling lipid synthesis with nuclear envelope remodeling
Sarah R. Barger, Lauren Penfield, Shirin Bahmanyar
Trends in Biochemical Sciences (2021) Vol. 47, Iss. 1, pp. 52-65
Open Access | Times Cited: 32
Ndc1 drives nuclear pore complex assembly independent of membrane biogenesis to promote nuclear formation and growth
Michael Mauro, Gunta Celma, Vitaly Zimyanin, et al.
eLife (2022) Vol. 11
Open Access | Times Cited: 21
Nuclear lipid droplets – how are they different from their cytoplasmic siblings?
Toyoshi Fujimoto
Journal of Cell Science (2022) Vol. 135, Iss. 5
Open Access | Times Cited: 20
Nuclear envelope budding and its cellular functions
Katharina Keuenhof, Verena Kohler, Filomena Broeskamp, et al.
Nucleus (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 12
SUMOylation at the inner nuclear membrane facilitates nuclear envelope biogenesis during mitosis
Natasha O. Saik, Christopher Ptak, Saif Rehman, et al.
The Journal of Cell Biology (2023) Vol. 222, Iss. 8
Open Access | Times Cited: 12
Host and Viral Factors Involved in Nuclear Egress of Herpes Simplex Virus 1
Jun Arii
Viruses (2021) Vol. 13, Iss. 5, pp. 754-754
Open Access | Times Cited: 27
Genome instability from nuclear catastrophe and DNA damage
Anna Mammel, Emily M. Hatch
Seminars in Cell and Developmental Biology (2021) Vol. 123, pp. 131-139
Open Access | Times Cited: 25
Nuclear envelope assembly relies on CHMP-7 in the absence of BAF–LEM-mediated hole closure
Sarah R. Barger, Lauren Penfield, Shirin Bahmanyar
Journal of Cell Science (2023) Vol. 136, Iss. 21
Open Access | Times Cited: 10
Organelle homeostasis requires ESCRTs
Tsan-Wen Lu, Adam Frost, Frank R. Moss
Current Opinion in Cell Biology (2025) Vol. 93, pp. 102481-102481
Open Access
Quality control mechanisms that protect nuclear envelope identity and function
Philip J. Mannino, C. Patrick Lusk
The Journal of Cell Biology (2022) Vol. 221, Iss. 9
Open Access | Times Cited: 16
The ESCRT machinery directs quality control over inner nuclear membrane architecture
Raakhee Shankar, Molly M. Lettman, William Whisler, et al.
Cell Reports (2022) Vol. 38, Iss. 3, pp. 110263-110263
Open Access | Times Cited: 15
Ceramide synthase homolog Tlc4 maintains nuclear envelope integrity via its Golgi translocation
Yasuhiro Hirano, Yusuke Ohno, Yoshino Kubota, et al.
Journal of Cell Science (2023) Vol. 136, Iss. 10
Open Access | Times Cited: 9
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