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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:

Ubiquitination is essential for recovery of cellular activities after heat shock
Brian A. Maxwell, Youngdae Gwon, Ashutosh Mishra, et al.
Science (2021) Vol. 372, Iss. 6549
Open Access | Times Cited: 139

Showing 1-25 of 139 citing articles:

Ubiquitination of G3BP1 mediates stress granule disassembly in a context-specific manner
Youngdae Gwon, Brian A. Maxwell, Regina‐Maria Kolaitis, et al.
Science (2021) Vol. 372, Iss. 6549
Open Access | Times Cited: 240
Liquid-Liquid Phase Separation of TDP-43 and FUS in Physiology and Pathology of Neurodegenerative Diseases
Jenny L. Carey, Lin Guo
Frontiers in Molecular Biosciences (2022) Vol. 9
Open Access | Times Cited: 100
Heat-shock chaperone HSPB1 regulates cytoplasmic TDP-43 phase separation and liquid-to-gel transition
Shan Lu, Jiaojiao Hu, Olubankole Aladesuyi Arogundade, et al.
Nature Cell Biology (2022) Vol. 24, Iss. 9, pp. 1378-1393
Open Access | Times Cited: 94
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
Mammalian oocytes store mRNAs in a mitochondria-associated membraneless compartment
Shiya Cheng, Gerrit Altmeppen, Chun So, et al.
Science (2022) Vol. 378, Iss. 6617
Closed Access | Times Cited: 90
The structural context of posttranslational modifications at a proteome-wide scale
Isabell Bludau, Sander Willems, Wenfeng Zeng, et al.
PLoS Biology (2022) Vol. 20, Iss. 5, pp. e3001636-e3001636
Open Access | Times Cited: 84
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 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: 50
Heat Shock Response and Heat Shock Proteins: Current Understanding and Future Opportunities in Human Diseases
Manish Singh, Yoonhwa Shin, Songhyun Ju, et al.
International Journal of Molecular Sciences (2024) Vol. 25, Iss. 8, pp. 4209-4209
Open Access | Times Cited: 39
Identification of small molecule inhibitors of G3BP-driven stress granule formation
Brian D. Freibaum, James Messing, Haruko Nakamura, et al.
The Journal of Cell Biology (2024) Vol. 223, Iss. 3
Open Access | Times Cited: 22
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
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
Effects of pH alterations on stress- and aging-induced protein phase separation
Xuejiao Jin, Min Zhou, Shuxin Chen, et al.
Cellular and Molecular Life Sciences (2022) Vol. 79, Iss. 7
Open Access | Times Cited: 49
Intracellular localization of the proteasome in response to stress conditions
Cordula Enenkel, Ryu Won Kang, Florian Wilfling, et al.
Journal of Biological Chemistry (2022) Vol. 298, Iss. 7, pp. 102083-102083
Open Access | Times Cited: 42
The ubiquitin codes in cellular stress responses
Xiangpeng Sheng, Zhixiong Xia, Hanting Yang, et al.
Protein & Cell (2023) Vol. 15, Iss. 3, pp. 157-190
Open Access | Times Cited: 37
Proteotoxic stress and the ubiquitin proteasome system
Rachel Kandel, Jasmine Jung, Sonya E. Neal
Seminars in Cell and Developmental Biology (2023) Vol. 156, pp. 107-120
Open Access | Times Cited: 33
A Functional Map of the Human Intrinsically Disordered Proteome
Iva Pritišanac, T. Reid Alderson, Đesika Kolarić, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Closed 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
Dysregulation of stress granule dynamics by DCTN1 deficiency exacerbates TDP-43 pathology in Drosophila models of ALS/FTD
Tetsuhiro Ueda, Toshihide Takeuchi, Nobuhiro Fujikake, et al.
Acta Neuropathologica Communications (2024) Vol. 12, Iss. 1
Open Access | Times Cited: 9
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
Chaperone regulation of biomolecular condensates
Jared A.M. Bard, D. Allan Drummond
Frontiers in Biophysics (2024) Vol. 2
Open Access | Times Cited: 8
Role of stress granules in tumorigenesis and cancer therapy
Tiansheng Li, Zhaoyang Zeng, Chunmei Fan, et al.
Biochimica et Biophysica Acta (BBA) - Reviews on Cancer (2023) Vol. 1878, Iss. 6, pp. 189006-189006
Closed Access | Times Cited: 22
Acute and chronic impacts of heat stress on planetary health
Vanitha Sampath, Omar Shalakhti, Erika Veidis, et al.
Allergy (2023) Vol. 78, Iss. 8, pp. 2109-2120
Open Access | Times Cited: 20
Targeting the NEDP1 enzyme to ameliorate ALS phenotypes through stress granule disassembly
Toufic Kassouf, Rohit Shrivastava, Igor Meszka, et al.
Science Advances (2023) Vol. 9, Iss. 13
Open Access | Times Cited: 17
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