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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:

The chaperone DNAJB6 surveils FG-nucleoporins and is required for interphase nuclear pore complex biogenesis
E. F. Elsiena Kuiper, Paola Gallardo, Tessa Bergsma, et al.
Nature Cell Biology (2022) Vol. 24, Iss. 11, pp. 1584-1594
Open Access | Times Cited: 38

Showing 1-25 of 38 citing articles:

Phase separation of intrinsically disordered FG-Nups is driven by highly dynamic FG motifs
Maurice Dekker, E. van der Giessen, Patrick R. Onck
Proceedings of the National Academy of Sciences (2023) Vol. 120, Iss. 25
Open Access | Times Cited: 31
Nuclear-import receptors as gatekeepers of pathological phase transitions in ALS/FTD
Bilal Khalil, Miriam Linsenmeier, Courtney L. Smith, et al.
Molecular Neurodegeneration (2024) Vol. 19, Iss. 1
Open Access | Times Cited: 14
J-domain proteins: From molecular mechanisms to diseases
Jarosław Marszałek, Paolo De Los Rios, Douglas Cyr, et al.
Cell Stress and Chaperones (2024) Vol. 29, Iss. 1, pp. 21-33
Open Access | Times Cited: 9
Nuclear pore dysfunction and disease: a complex opportunity
Charlotte M. Fare, Jeffrey D. Rothstein
Nucleus (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 9
Atypical nuclear envelope condensates linked to neurological disorders reveal nucleoporin-directed chaperone activities
Sarah Prophet, Anthony J. Rampello, Robert F. Niescier, et al.
Nature Cell Biology (2022) Vol. 24, Iss. 11, pp. 1630-1641
Open Access | Times Cited: 35
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
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
DNAJB6 mutants display toxic gain of function through unregulated interaction with Hsp70 chaperones
Meital Abayev-Avraham, Yehuda Salzberg, Dar Gliksberg, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 17
Proxiome assembly of the plant nuclear pore reveals an essential hub for gene expression regulation
Yu Tang, Xiangyun Yang, Aobo Huang, et al.
Nature Plants (2024) Vol. 10, Iss. 6, pp. 1005-1017
Closed Access | Times Cited: 8
DNAJB8 oligomerization is mediated by an aromatic-rich motif that is dispensable for substrate activity
Bryan D. Ryder, Elizaveta Ustyantseva, David R. Boyer, et al.
Structure (2024) Vol. 32, Iss. 6, pp. 662-678.e8
Open Access | Times Cited: 5
UBAP2L ensures homeostasis of nuclear pore complexes at the intact nuclear envelope
Yongrong Liao, Leonid Andronov, Xiao-Tian Liu, et al.
The Journal of Cell Biology (2024) Vol. 223, Iss. 7
Open Access | Times Cited: 4
Unraveling the impact of disrupted nucleocytoplasmic transport systems in C9orf72-associated ALS
Philip McGoldrick, Janice Robertson
Frontiers in Cellular Neuroscience (2023) Vol. 17
Open Access | Times Cited: 10
p97/VCP is required for piecemeal autophagy of aggresomes
Maria Körner, Paul Müller, Hirak Das, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access
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
Metazoan nuclear pore complexes in gene regulation and genome stability
Parisa Nobari, Valérie Doye, Charlène Boumendil
DNA repair (2023) Vol. 130, pp. 103565-103565
Open Access | Times Cited: 7
Tertiary structure and conformational dynamics of the anti-amyloidogenic chaperone DNAJB6b at atomistic resolution
Vasista Adupa, Elizaveta Ustyantseva, Harm H. Kampinga, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 2
TorsinA is essential for neuronal nuclear pore complex localization and maturation
Sumin Kim, Sébastien Phan, Hung Tri Tran, et al.
Nature Cell Biology (2024) Vol. 26, Iss. 9, pp. 1482-1495
Open Access | Times Cited: 2
Cytoplasmic nucleoporin assemblage: the cellular artwork in physiology and disease
Junyan Lin, Izabela Sumara
Nucleus (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 2
DNAJB8 oligomerization is mediated by an aromatic-rich motif that is dispensable for substrate activity
Bryan D. Ryder, Elizaveta Ustyantseva, David R. Boyer, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 6
Coordinating nucleoporin condensation and nuclear pore complex assembly
E. F. Elsiena Kuiper, Sarah Prophet, Christian Schlieker
FEBS Letters (2023) Vol. 597, Iss. 20, pp. 2534-2545
Open Access | Times Cited: 6
Changing the guard—nuclear pore complex quality control
Annemiek C. Veldsink, Paola Gallardo, C. Patrick Lusk, et al.
FEBS Letters (2023) Vol. 597, Iss. 22, pp. 2739-2749
Open Access | Times Cited: 6
TorsinA is essential for the timing and localization of neuronal nuclear pore complex biogenesis
Sumin Kim, Sébastien Phan, Thomas R. Shaw, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 4
DNAJB6 isoform specific knockdown: Therapeutic potential for limb girdle muscular dystrophy D1
Andrew R. Findlay, May M. Paing, Jil Daw, et al.
Molecular Therapy — Nucleic Acids (2023) Vol. 32, pp. 937-948
Open Access | Times Cited: 4
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