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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:

Relation Between Stress Granules and Cytoplasmic Protein Aggregates Linked to Neurodegenerative Diseases
Ioana Dobra, Serhii Pankivskyi, Anastasiia Samsonova, et al.
Current Neurology and Neuroscience Reports (2018) Vol. 18, Iss. 12
Closed Access | Times Cited: 48

Showing 1-25 of 48 citing articles:

Gut Microbiota and Dysbiosis in Alzheimer’s Disease: Implications for Pathogenesis and Treatment
Shan Liu, Jiguo Gao, Mingqin Zhu, et al.
Molecular Neurobiology (2020) Vol. 57, Iss. 12, pp. 5026-5043
Open Access | Times Cited: 344
Liquid–Liquid Phase Separation and Its Mechanistic Role in Pathological Protein Aggregation
W. Michael Babinchak, Witold K. Surewicz
Journal of Molecular Biology (2020) Vol. 432, Iss. 7, pp. 1910-1925
Open Access | Times Cited: 235
Stress granule homeostasis is modulated by TRIM21-mediated ubiquitination of G3BP1 and autophagy-dependent elimination of stress granules
Cuiwei Yang, Zhangshun Wang, Yingjin Kang, et al.
Autophagy (2023) Vol. 19, Iss. 7, pp. 1934-1951
Open Access | Times Cited: 54
Biomolecular condensates in neurodegeneration and cancer
Stephanie Spannl, Maria Tereshchenko, Giovanni J. Mastromarco, et al.
Traffic (2019) Vol. 20, Iss. 12, pp. 890-911
Open Access | Times Cited: 101
Recent Developments in the Field of Intrinsically Disordered Proteins: Intrinsic Disorder–Based Emergence in Cellular Biology in Light of the Physiological and Pathological Liquid–Liquid Phase Transitions
Vladimir N. Uversky
Annual Review of Biophysics (2021) Vol. 50, Iss. 1, pp. 135-156
Closed Access | Times Cited: 85
New pathologic mechanisms in nucleotide repeat expansion disorders
Caitlin M. Rodriguez, Peter K. Todd
Neurobiology of Disease (2019) Vol. 130, pp. 104515-104515
Open Access | Times Cited: 77
Huntington’s disease mice and human brain tissue exhibit increased G3BP1 granules and TDP43 mislocalization
Isabella Sanchez, Thai B. Nguyen, Whitney England, et al.
Journal of Clinical Investigation (2021) Vol. 131, Iss. 12
Open Access | Times Cited: 57
Stress granules: functions and mechanisms in cancer
Huan Zhou, Jing Luo, Kelin Mou, et al.
Cell & Bioscience (2023) Vol. 13, Iss. 1
Open Access | Times Cited: 29
Intrinsic Disorder-Based Emergence in Cellular Biology: Physiological and Pathological Liquid-Liquid Phase Transitions in Cells
April L. Darling, Boris Y. Zaslavsky, Vladimir N. Uversky
Polymers (2019) Vol. 11, Iss. 6, pp. 990-990
Open Access | Times Cited: 74
Targeting stress granules: A novel therapeutic strategy for human diseases
Fei Wang, Juan Li, Shengjie Fan, et al.
Pharmacological Research (2020) Vol. 161, pp. 105143-105143
Open Access | Times Cited: 56
The cooperative binding of TDP-43 to GU-rich RNA repeats antagonizes TDP-43 aggregation
Juan Carlos Rengifo-Gonzalez, Krystel El Hage, Marie‐Jeanne Clément, et al.
eLife (2021) Vol. 10
Open Access | Times Cited: 56
Translational Repression of G3BP in Cancer and Germ Cells Suppresses Stress Granules and Enhances Stress Tolerance
Anna K. Lee, Jonathon Klein, Klementina Fon Tacer, et al.
Molecular Cell (2020) Vol. 79, Iss. 4, pp. 645-659.e9
Open Access | Times Cited: 51
α-Synuclein emulsifies TDP-43 prion-like domain—RNA liquid droplets to promote heterotypic amyloid fibrils
Shailendra Dhakal, Malay Mondal, Azin Mirzazadeh, et al.
Communications Biology (2023) Vol. 6, Iss. 1
Open Access | Times Cited: 22
Amyloids, amorphous aggregates and assemblies of peptides – Assessing aggregation
Maja Juković, Ivana Ratkaj, Daniela Kalafatović, et al.
Biophysical Chemistry (2024) Vol. 308, pp. 107202-107202
Closed Access | Times Cited: 7
Strategies for Success. Viral Infections and Membraneless Organelles
Aracelly Gaete-Argel, Chantal L. Márquez, Gonzalo P. Barriga, et al.
Frontiers in Cellular and Infection Microbiology (2019) Vol. 9
Open Access | Times Cited: 53
Core autophagy genes and human diseases
Yan Zhao, Hong Zhang
Current Opinion in Cell Biology (2019) Vol. 61, pp. 117-125
Closed Access | Times Cited: 48
Supramolecular Fuzziness of Intracellular Liquid Droplets: Liquid–Liquid Phase Transitions, Membrane-Less Organelles, and Intrinsic Disorder
Vladimir N. Uversky
Molecules (2019) Vol. 24, Iss. 18, pp. 3265-3265
Open Access | Times Cited: 39
Tau oligomers mediate aggregation of RNA‐binding proteins Musashi1 and Musashi2 inducing Lamin alteration
Mauro Montalbano, Salomé McAllen, Urmi Sengupta, et al.
Aging Cell (2019) Vol. 18, Iss. 6
Open Access | Times Cited: 36
Melatonin: Regulation of Biomolecular Condensates in Neurodegenerative Disorders
Doris Loh, Rüssel J. Reiter
Antioxidants (2021) Vol. 10, Iss. 9, pp. 1483-1483
Open Access | Times Cited: 30
The Role of Ubiquitin in Regulating Stress Granule Dynamics
Laura J. Krause, María Georgina Herrera, Konstanze F. Winklhofer
Frontiers in Physiology (2022) Vol. 13
Open Access | Times Cited: 21
Neuronal RNA granules are ribosome complexes stalled at the pre-translocation state
Kalle Kipper, Abbas Mansour, Arto Pulk
Journal of Molecular Biology (2022) Vol. 434, Iss. 20, pp. 167801-167801
Open Access | Times Cited: 17
TIA1‐Mediated Stress Granules Promote the Neuroinflammation and Demyelination in Experimental Autoimmune Encephalomyelitis through Upregulating IL‐31RA Signaling
Xin Hua, Lingting Jin, Zheyu Fang, et al.
Advanced Science (2025)
Open Access
Aggregates associated with amyotrophic lateral sclerosis sequester the actin-binding protein profilin 2
Sabrina Kubinski, Laura R. Claus, Tobias Schüning, et al.
Human Molecular Genetics (2025)
Closed Access
Two Birds With One Stone: RNA Virus Strategies to Manipulate G3BP1 and Other Stress Granule Components
Moh Egy Rahman Firdaus, Eliana Dukhno, Ritoo Kapoor, et al.
Wiley Interdisciplinary Reviews - RNA (2025) Vol. 16, Iss. 2
Open Access
Neuromelanin granules of the substantia nigra: proteomic profile provides links to tyrosine hydroxylase, stress granules and lysosomes
Maximilian Wulf, Katalin Barkovits, Karin Schork, et al.
Journal of Neural Transmission (2022) Vol. 129, Iss. 10, pp. 1257-1270
Open Access | Times Cited: 16
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