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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:

Converging Small Ubiquitin-like Modifier (SUMO) and Ubiquitin Signaling: Improved Methodology Identifies Co-modified Target Proteins
Sabine A.G. Cuijpers, Edwin Willemstein, Alfred C.O. Vertegaal
Molecular & Cellular Proteomics (2017) Vol. 16, Iss. 12, pp. 2281-2295
Open Access | Times Cited: 24

Showing 24 citing articles:

Crosstalk between Ubiquitination and Other Post-translational Protein Modifications in Plant Immunity
Yi Zhang, Lirong Zeng
Plant Communications (2020) Vol. 1, Iss. 4, pp. 100041-100041
Open Access | Times Cited: 80
Deubiquitinating enzymes and the proteasome regulate preferential sets of ubiquitin substrates
Fredrik Trulsson, Vyacheslav Akimov, Mihaela Robu, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 54
Post‐translational modifications in capsid proteins of recombinant adeno‐associated virus (AAV) 1‐rh10 serotypes
Bertin Mary, Shubham Maurya, Sathyathithan Arumugam, et al.
FEBS Journal (2019) Vol. 286, Iss. 24, pp. 4964-4981
Open Access | Times Cited: 76
The poly-SUMO2/3 protease SENP6 enables assembly of the constitutive centromere-associated network by group deSUMOylation
Frauke Liebelt, Nicolette S. Jansen, Sumit Kumar, et al.
Nature Communications (2019) Vol. 10, Iss. 1
Open Access | Times Cited: 65
Quantitative SUMO proteomics identifies PIAS1 substrates involved in cell migration and motility
Chongyang Li, Francis P. McManus, Cédric Plutoni, et al.
Nature Communications (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 64
SUMO-Targeted Ubiquitin Ligases and Their Functions in Maintaining Genome Stability
Ya‐Chu Chang, Marissa K. Oram, Anja‐Katrin Bielinsky
International Journal of Molecular Sciences (2021) Vol. 22, Iss. 10, pp. 5391-5391
Open Access | Times Cited: 45
Guiding Mitotic Progression by Crosstalk between Post-translational Modifications
Sabine A.G. Cuijpers, Alfred C.O. Vertegaal
Trends in Biochemical Sciences (2018) Vol. 43, Iss. 4, pp. 251-268
Open Access | Times Cited: 53
SUMOylation and the HSF1-Regulated Chaperone Network Converge to Promote Proteostasis in Response to Heat Shock
Frauke Liebelt, Rebecca M. Sebastian, Christopher Moore, et al.
Cell Reports (2019) Vol. 26, Iss. 1, pp. 236-249.e4
Open Access | Times Cited: 49
dsRNAi-mediated silencing of PIAS2beta specifically kills anaplastic carcinomas by mitotic catastrophe
Joana S. Rodrigues, Miguel Chenlo, Susana B. Bravo, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 5
Decoding the PTM-switchboard of Notch
Daniel Antfolk, Christian Antila, Kati Kemppainen, et al.
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research (2019) Vol. 1866, Iss. 12, pp. 118507-118507
Open Access | Times Cited: 40
RNF4—A Paradigm for SUMOylation‐Mediated Ubiquitination
Ramesh Kumar, Kanaga Sabapathy
PROTEOMICS (2019) Vol. 19, Iss. 21-22
Closed Access | Times Cited: 36
SUMO/deSUMOylation of the BRI1 brassinosteroid receptor modulates plant growth responses to temperature
Maria Augusta Naranjo-Arcos, Moumita Srivastava, Florian Deligne, et al.
Proceedings of the National Academy of Sciences (2023) Vol. 120, Iss. 4
Open Access | Times Cited: 12
MS‐based strategies for identification of protein SUMOylation modification
Zenghua Sheng, Xixi Wang, Yanni Ma, et al.
Electrophoresis (2019) Vol. 40, Iss. 21, pp. 2877-2887
Open Access | Times Cited: 21
How Does SUMO Participate in Spindle Organization?
Ariane Abrieu, Dimitris Liakopoulos
Cells (2019) Vol. 8, Iss. 8, pp. 801-801
Open Access | Times Cited: 17
Interplay between ubiquitylation and SUMOylation: Empowered by phase separation
Jianping Jin
Journal of Biological Chemistry (2019) Vol. 294, Iss. 42, pp. 15235-15236
Open Access | Times Cited: 17
Poly-SUMO-2/3 chain modification of Nuf2 facilitates CENP-E kinetochore localization and chromosome congression during mitosis
Divya Subramonian, Te-An Chen, Nicholas Paolini, et al.
Cell Cycle (2021) Vol. 20, Iss. 9, pp. 855-873
Open Access | Times Cited: 13
Site-specific proteomic strategies to identify ubiquitin and SUMO modifications: Challenges and opportunities
Fredrik Trulsson, Alfred C.O. Vertegaal
Seminars in Cell and Developmental Biology (2021) Vol. 132, pp. 97-108
Open Access | Times Cited: 13
BRCA1/BARD1 ubiquitinates PCNA in unperturbed conditions to promote replication fork stability and continuous DNA synthesis
Daniel Salas‐Lloret, Néstor García‐Rodríguez, Lisanne Giebel, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 4
Proteomic strategies for characterizing ubiquitin-like modifications
Chongyang Li, Trent Nelson, Alfred C.O. Vertegaal, et al.
Nature Reviews Methods Primers (2021) Vol. 1, Iss. 1
Closed Access | Times Cited: 10
Identification of Novel Gene Variants for Autism Spectrum Disorders in the Lebanese Population Using Whole-Exome Sequencing
Perla Gerges, Tania Bitar, Frédéric Laumonnier, et al.
Genes (2022) Vol. 13, Iss. 2, pp. 186-186
Open Access | Times Cited: 7
Ubiquitination of angiotensin-converting enzyme 2 contributes to the development of pulmonary arterial hypertension mediated by neural precursor cell–expressed developmentally down-regulated gene 4-Like
Rui Wang, Rui Wang, Siqi Zhou, et al.
Respiratory Research (2024) Vol. 25, Iss. 1
Open Access | Times Cited: 1
Variation in expression of small ubiquitin-like modifiers in injured sciatic nerve of mice
Dianying Zhang, Kai Yu, Zhong Yang, et al.
Neural Regeneration Research (2019) Vol. 14, Iss. 8, pp. 1455-1455
Open Access | Times Cited: 5
Quantitative proteomics identifies novel PIAS1 substrates involved in cell migration and motility
Chongyang Li, Francis P. McManus, Cédric Plutoni, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2019)
Open Access
SUMO/deSUMOylation of the BRI1 brassinosteroid receptor modulates plant growth responses to temperature
Maria Augusta Naranjo-Arcos, Moumita Srivastava, Mansi Bhardwarj, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access
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