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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:

SUMO: Glue or Solvent for Phase-Separated Ribonucleoprotein Complexes and Molecular Condensates?
Jan Keiten‐Schmitz, Linda Röder, Eran Hornstein, et al.
Frontiers in Molecular Biosciences (2021) Vol. 8
Open Access | Times Cited: 52

Showing 1-25 of 52 citing articles:

Protein quality control machinery: regulators of condensate architecture and functionality
Anitha Rajendran, Carlos A. Castañeda
Trends in Biochemical Sciences (2025)
Closed Access | Times Cited: 2
SUMO Interacting Motifs: Structure and Function
Tak-Yu Yau, William E. Sander, Christian Eidson, et al.
Cells (2021) Vol. 10, Iss. 11, pp. 2825-2825
Open Access | Times Cited: 57
SUMO-SIM interactions: From structure to biological functions
Jara Lascorz, Joan Codina-Fabra, David Reverter, et al.
Seminars in Cell and Developmental Biology (2021) Vol. 132, pp. 193-202
Closed Access | Times Cited: 57
Sumoylation in Physiology, Pathology and Therapy
Umut Şahin, Hugues de Thé, Valérie Lallemand-Breitenbach
Cells (2022) Vol. 11, Iss. 5, pp. 814-814
Open Access | Times Cited: 52
Morphogen-induced kinase condensates transduce Hh signal by allosterically activating Gli
Yuhong Han, Mengmeng Zhou, Bing Wang, et al.
Science Advances (2025) Vol. 11, Iss. 2
Open Access | Times Cited: 1
SENP6 regulates localization and nuclear condensation of DNA damage response proteins by group deSUMOylation
Laura A. Claessens, Matty Verlaan-de Vries, Ilona J. de Graaf, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 18
Biomolecular Condensates: Structure, Functions, Methods of Research
Natalia A. Gorsheneva, Julia V. Sopova, Vladimir V. Azarov, et al.
Biochemistry (Moscow) (2024) Vol. 89, Iss. S1, pp. S205-S223
Closed Access | Times Cited: 5
Exploring the multifunctionality of SR proteins
Irena Slišković, Hannah Eich, Michaela Müller-McNicoll
Biochemical Society Transactions (2021) Vol. 50, Iss. 1, pp. 187-198
Open Access | Times Cited: 32
Melatonin: Regulation of Biomolecular Condensates in Neurodegenerative Disorders
Doris Loh, Russel J. Reıter
Antioxidants (2021) Vol. 10, Iss. 9, pp. 1483-1483
Open Access | Times Cited: 28
Regulating the p53 Tumor Suppressor Network at PML Biomolecular Condensates
Magdalena C. Liebl, Thomas G. Hofmann
Cancers (2022) Vol. 14, Iss. 19, pp. 4549-4549
Open Access | Times Cited: 19
Phase Separation and Aggregation of a Globular Folded Protein Small Ubiquitin-like Modifier 1 (SUMO1)
S. L. Arora, Debsankar Saha Roy, Sudipta Maiti, et al.
The Journal of Physical Chemistry Letters (2023) Vol. 14, Iss. 40, pp. 9060-9068
Open Access | Times Cited: 11
Telomeric SUMO level influences the choices of APB formation pathways and ALT efficiency
Rongwei Zhao, Allison Wivagg, Rachel M. Lackner, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2025)
Open Access
Transient Pharmacological Inhibition of SUMOylation during Pregnancy Induces Craniofacial Malformations in Offspring Mice
Jorge Mata-Garrido, Isabella Zafferri, Alice Nordlinger, et al.
European Journal of Cell Biology (2025) Vol. 104, Iss. 2, pp. 151480-151480
Open Access
Induced proximity to PML protects TDP-43 from aggregation via SUMO–ubiquitin networks
Kristina Wagner, Jan Keiten‐Schmitz, Bikash Adhikari, et al.
Nature Chemical Biology (2025)
Open Access
Polyubiquitin ligand-induced phase transitions are optimized by spacing between ubiquitin units
Sarasi K. K. Galagedera, Thuy P. Dao, Suzanne E. Enos, et al.
Proceedings of the National Academy of Sciences (2023) Vol. 120, Iss. 42
Open Access | Times Cited: 10
Characterizing the differential distribution and targets of Sumo1 and Sumo2 in the mouse brain
Terry R. Suk, Trina T. Nguyen, Zoe Fisk, et al.
iScience (2023) Vol. 26, Iss. 4, pp. 106350-106350
Open Access | Times Cited: 9
Dynamics of DNA damage-induced nuclear inclusions are regulated by SUMOylation of Btn2
Arun Kumar, Veena Mathew, Peter C. Stirling
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 3
Stress - Regulation of SUMO conjugation and of other Ubiquitin‐Like Modifiers
Dragana Ilic, H Magnussen, Marilyn Tirard
Seminars in Cell and Developmental Biology (2022) Vol. 132, pp. 38-50
Closed Access | Times Cited: 15
Multiplexed Delivery of Synthetic (Un)Conjugatable Ubiquitin and SUMO2 Enables Simultaneous Monitoring of Their Localization and Function in Live Cells
Guy Mann, Pradeep Sadhu, Ashraf Brik
ChemBioChem (2022) Vol. 23, Iss. 11
Open Access | Times Cited: 13
Alternative splicing of the SUMO1/2/3 transcripts affects cellular SUMOylation and produces functionally distinct SUMO protein isoforms
Myriah L. Acuña, Andrea García-Morin, Rebeca Orozco-Sepúlveda, et al.
Scientific Reports (2023) Vol. 13, Iss. 1
Open Access | Times Cited: 7
Phase separation-based visualization of protein–protein interactions and kinase activities in plants
Alaeddine Safi, Wouter Smagghe, Amanda Gonçalves, et al.
The Plant Cell (2023) Vol. 35, Iss. 9, pp. 3280-3302
Open Access | Times Cited: 7
Ubiquitin and SUMO as timers during DNA replication
Rodrigo Martín-Rufo, Guillermo de la Vega-Barranco, Emilio Lecona
Seminars in Cell and Developmental Biology (2022) Vol. 132, pp. 62-73
Open Access | Times Cited: 11
PML Body Biogenesis: A Delicate Balance of Interactions
Sergey A. Silonov, Eugene Y. Smirnov, Irina М. Kuznetsova, et al.
International Journal of Molecular Sciences (2023) Vol. 24, Iss. 23, pp. 16702-16702
Open Access | Times Cited: 6
Crosstalk between Biomolecular Condensates and Proteostasis
Emmanuel Amzallag, Eran Hornstein
Cells (2022) Vol. 11, Iss. 15, pp. 2415-2415
Open Access | Times Cited: 10
CRISPR/Cas9-mediated knockout of the ubiquitin variant UbKEKS reveals a role in regulating nucleolar structures and composition
Julie Frion, Anna Meller, Gwendoline Marbach, et al.
Biology Open (2023) Vol. 12, Iss. 9
Open Access | Times Cited: 5
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