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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:

Spatiotemporal Proteomic Analysis of Stress Granule Disassembly Using APEX Reveals Regulation by SUMOylation and Links to ALS Pathogenesis
Hagai Marmor-Kollet, Aviad Siany, Nancy Kedersha, et al.
Molecular Cell (2020) Vol. 80, Iss. 5, pp. 876-891.e6
Open Access | Times Cited: 208

Showing 1-25 of 208 citing articles:

OpenCell: Endogenous tagging for the cartography of human cellular organization
Nathan Cho, Keith C. Cheveralls, Andreas‐David Brunner, et al.
Science (2022) Vol. 375, Iss. 6585
Open Access | Times Cited: 363
Molecular mechanisms of stress granule assembly and disassembly
Sarah Hofmann, Nancy Kedersha, Paul Anderson, et al.
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research (2020) Vol. 1868, Iss. 1, pp. 118876-118876
Open Access | Times Cited: 272
Signalling mechanisms and cellular functions of SUMO
Alfred C.O. Vertegaal
Nature Reviews Molecular Cell Biology (2022) Vol. 23, Iss. 11, pp. 715-731
Closed Access | Times Cited: 207
Protein posttranslational modifications in health and diseases: Functions, regulatory mechanisms, and therapeutic implications
Qian Zhong, Xina Xiao, Yijie Qiu, et al.
MedComm (2023) Vol. 4, Iss. 3
Open Access | Times Cited: 117
The Integral Role of RNA in Stress Granule Formation and Function
Danae Campos-Melo, Zachary C. E. Hawley, Cristian A. Droppelmann, et al.
Frontiers in Cell and Developmental Biology (2021) Vol. 9
Open Access | Times Cited: 105
Stressful steps: Progress and challenges in understanding stress-induced mRNA condensation and accumulation in stress granules
Hendrik Glauninger, Caitlin J. Wong Hickernell, Jared A.M. Bard, et al.
Molecular Cell (2022) Vol. 82, Iss. 14, pp. 2544-2556
Open Access | Times Cited: 93
Liquid–liquid phase separation as an organizing principle of intracellular space: overview of the evolution of the cell compartmentalization concept
Iuliia A. Antifeeva, Alexander V. Fonin, Anna S. Fefilova, et al.
Cellular and Molecular Life Sciences (2022) Vol. 79, Iss. 5
Closed Access | Times Cited: 78
Molecular and environmental determinants of biomolecular condensate formation
José A. Villegas, Meta Heidenreich, Emmanuel D. Levy
Nature Chemical Biology (2022) Vol. 18, Iss. 12, pp. 1319-1329
Closed Access | Times Cited: 76
Dynamic mapping of proteome trafficking within and between living cells by TransitID
Wei Qin, Joleen S. Cheah, Charles Xu, et al.
Cell (2023) Vol. 186, Iss. 15, pp. 3307-3324.e30
Open Access | Times Cited: 72
A New Phase of Networking: The Molecular Composition and Regulatory Dynamics of Mammalian Stress Granules
Seán Millar, Jie Huang, Karl J. Schreiber, et al.
Chemical Reviews (2023) Vol. 123, Iss. 14, pp. 9036-9064
Open Access | Times Cited: 62
Stress-related biomolecular condensates in plants
Jorge Solís-Miranda, Monika Chodasiewicz, Aleksandra Skirycz, et al.
The Plant Cell (2023) Vol. 35, Iss. 9, pp. 3187-3204
Open Access | Times Cited: 48
Plant Stress Granules: Trends and Beyond
Israel Maruri‐López, Nicolás E. Figueroa, Itzell Eurídice Hernández-Sánchez, et al.
Frontiers in Plant Science (2021) Vol. 12
Open Access | Times Cited: 69
Tudor staphylococcal nuclease is a docking platform for stress granule components and is essential for SnRK1 activation in Arabidopsis
Emilio Gutiérrez-Beltrán, Pernilla H Elander, Kerstin Dalman, et al.
The EMBO Journal (2021) Vol. 40, Iss. 17
Open Access | Times Cited: 64
Sexually dimorphic RNA helicases DDX3X and DDX3Y differentially regulate RNA metabolism through phase separation
Hui Shen, Amber Yanas, Michael C. Owens, et al.
Molecular Cell (2022) Vol. 82, Iss. 14, pp. 2588-2603.e9
Open Access | Times Cited: 61
Post-translational modifications on RNA-binding proteins: accelerators, brakes, or passengers in neurodegeneration?
Erin L. Sternburg, Lara A. Gruijs da Silva, Dorothee Dormann
Trends in Biochemical Sciences (2021) Vol. 47, Iss. 1, pp. 6-22
Closed Access | Times Cited: 59
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
Precision analysis of mutant U2AF1 activity reveals deployment of stress granules in myeloid malignancies
Giulia Biancon, Poorval Joshi, Joshua T. Zimmer, et al.
Molecular Cell (2022) Vol. 82, Iss. 6, pp. 1107-1122.e7
Open Access | Times Cited: 56
SENP1 Decreases RNF168 Phase Separation to Promote DNA Damage Repair and Drug Resistance in Colon Cancer
Min Wei, Xinping Huang, Liming Liao, et al.
Cancer Research (2023) Vol. 83, Iss. 17, pp. 2908-2923
Closed Access | Times Cited: 41
Human senataxin is a bona fide R-loop resolving enzyme and transcription termination factor
Zdenka Hašanová, Veronika Klapstova, Odil Porrúa, et al.
Nucleic Acids Research (2023) Vol. 51, Iss. 6, pp. 2818-2837
Open Access | Times Cited: 40
Stress granule formation inhibits stress-induced apoptosis by selectively sequestering executioner caspases
Daichi Fujikawa, Takanori Nakamura, Daisuke Yoshioka, et al.
Current Biology (2023) Vol. 33, Iss. 10, pp. 1967-1981.e8
Open Access | Times Cited: 36
Diverse CMT2 neuropathies are linked to aberrant G3BP interactions in stress granules
Qinqin Cui, Hongyun Bi, Zhanyun Lv, et al.
Cell (2023) Vol. 186, Iss. 4, pp. 803-820.e25
Open Access | Times Cited: 35
Pro-Viral and Anti-Viral Roles of the RNA-Binding Protein G3BP1
Aravinth Kumar Jayabalan, Diane E. Griffin, Anthony K. L. Leung
Viruses (2023) Vol. 15, Iss. 2, pp. 449-449
Open Access | Times Cited: 24
TRIM25 predominately associates with anti-viral stress granules
Zehua Shang, Sitao Zhang, Jinrui Wang, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 10
µMap proximity labeling in living cells reveals stress granule disassembly mechanisms
Chenmengxiao Pan, Steve D. Knutson, Sean W. Huth, et al.
Nature Chemical Biology (2024)
Closed Access | Times Cited: 10
Stress granule and P-body clearance: Seeking coherence in acts of disappearance
J. Ross Buchan
Seminars in Cell and Developmental Biology (2024) Vol. 159-160, pp. 10-26
Closed Access | Times Cited: 8
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