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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:

Co-translational assembly orchestrates competing biogenesis pathways
Maximilian Seidel, Anja Becker, Filipa Pereira, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 36

Showing 1-25 of 36 citing articles:

AI-based structure prediction empowers integrative structural analysis of human nuclear pores
Shyamal Mosalaganti, Agnieszka Obarska-Kosińska, Marc Siggel, et al.
Science (2022) Vol. 376, Iss. 6598
Closed Access | Times Cited: 239
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
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
Co-translational binding of importins to nascent proteins
Maximilian Seidel, Natalie Romanov, Agnieszka Obarska-Kosińska, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 20
Hierarchical TAF1-dependent co-translational assembly of the basal transcription factor TFIID
Andrea Bernardini, Pooja Mukherjee, Elisabeth Scheer, et al.
Nature Structural & Molecular Biology (2023) Vol. 30, Iss. 8, pp. 1141-1152
Open Access | Times Cited: 18
mRNA interactions with disordered regions control protein activity
Yang Luo, Supriya Pratihar, Ellen Horste, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 17
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
Large protein complex interfaces have evolved to promote cotranslational assembly
Mihaly Badonyi, Joseph A. Marsh
eLife (2022) Vol. 11
Open Access | Times Cited: 24
Buffering of genetic dominance by allele-specific protein complex assembly
Mihaly Badonyi, Joseph A. Marsh
Science Advances (2023) Vol. 9, Iss. 22
Open Access | Times Cited: 15
Improving the soluble expression of difficult-to-express proteins in prokaryotic expression system via protein engineering and synthetic biology strategies
Jin‐Ping Chen, Jin‐Song Gong, Chang Su, et al.
Metabolic Engineering (2023) Vol. 78, pp. 99-114
Closed Access | Times Cited: 13
YTHDF1 is pivotal for maintenance of cardiac homeostasis
Volha A. Golubeva, Anindhya Sundar Das, Charles P. Rabolli, et al.
Journal of Molecular and Cellular Cardiology (2024) Vol. 193, pp. 25-35
Closed Access | Times Cited: 4
A privileged ER compartment for post-translational heteromeric assembly of an ion channel
Sudharsan Kannan, William Kasberg, Liliana R. Ernandez, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2025)
Open Access
Distinct Cis-Acting Elements Mediate Co-Localization of Mrnas Encoding for Co-Translational Interactors in Cytoplasmic Clusters
Ayala Shiber, Qamar Shade, Mario Pablo Estrada, et al.
(2025)
Closed 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
Translation efficiency covariation across cell types is a conserved organizing principle of mammalian transcriptomes
Yue Liu, Ian Hoskins, Michael Geng, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 3
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
Structural determinants of co-translational protein complex assembly
Saurav Mallik, Johannes Venezian, Arseniy Lobov, et al.
Cell (2024)
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
Diverging co-translational protein complex assembly pathways are governed by interface energy distribution
Johannes Venezian, Hagit Bar-Yosef, Hila Zilberman, et al.
Nature Communications (2024) Vol. 15, Iss. 1
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
Benefits of co‐translational complex assembly for cellular fitness
Krishnendu Khan, Paul L. Fox
BioEssays (2023) Vol. 45, Iss. 5
Open Access | Times Cited: 6
Control of mRNA fate by its encoded nascent polypeptide
Markus Höpfler, Ramanujan S. Hegde
Molecular Cell (2023) Vol. 83, Iss. 16, pp. 2840-2855
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
ATAC and SAGA co-activator complexes utilize co-translational assembly, but their cellular localization properties and functions are distinct
Gizem Yayli, Andrea Bernardini, Paulina Karen Mendoza Sanchez, et al.
Cell Reports (2023) Vol. 42, Iss. 9, pp. 113099-113099
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
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