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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:

ULK1 and ULK2 Regulate Stress Granule Disassembly Through Phosphorylation and Activation of VCP/p97
Bo Wang, Brian A. Maxwell, Joung Hyuck Joo, et al.
Molecular Cell (2019) Vol. 74, Iss. 4, pp. 742-757.e8
Open Access | Times Cited: 158

Showing 1-25 of 158 citing articles:

Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition)1
Daniel J. Klionsky, Amal Kamal Abdel‐Aziz, Sara Abdelfatah, et al.
Autophagy (2021) Vol. 17, Iss. 1, pp. 1-382
Open Access | Times Cited: 1984
The LC3-conjugation machinery specifies the loading of RNA-binding proteins into extracellular vesicles
Andrew M. Leidal, Hector H. Huang, Timothy Marsh, et al.
Nature Cell Biology (2020) Vol. 22, Iss. 2, pp. 187-199
Open Access | Times Cited: 388
Beyond aggregation: Pathological phase transitions in neurodegenerative disease
Cécile Mathieu, Rohit V. Pappu, J. Paul Taylor
Science (2020) Vol. 370, Iss. 6512, pp. 56-60
Open Access | Times Cited: 331
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
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
FUS and TDP-43 Phases in Health and Disease
Bede Portz, Bo Lim Lee, James Shorter
Trends in Biochemical Sciences (2021) Vol. 46, Iss. 7, pp. 550-563
Open Access | Times Cited: 226
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
Repair or Lysophagy: Dealing with Damaged Lysosomes
Chrisovalantis Papadopoulos, Bojana Kravić, Hemmo Meyer
Journal of Molecular Biology (2019) Vol. 432, Iss. 1, pp. 231-239
Closed Access | Times Cited: 160
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
AMPK/ULK1-mediated phosphorylation of Parkin ACT domain mediates an early step in mitophagy
Chien‐Min Hung, Portia S. Lombardo, Nazma Malik, et al.
Science Advances (2021) Vol. 7, Iss. 15
Open Access | Times Cited: 115
VCP/p97 regulates Beclin-1-dependent autophagy initiation
Sandra Malmgren Hill, Lidia Wróbel, Avraham Ashkenazi, et al.
Nature Chemical Biology (2021) Vol. 17, Iss. 4, pp. 448-455
Closed Access | Times Cited: 104
ULK1-mediated metabolic reprogramming regulates Vps34 lipid kinase activity by its lactylation
Mengshu Jia, Yue Xiao, Weixia Sun, et al.
Science Advances (2023) Vol. 9, Iss. 22
Open Access | Times Cited: 78
QKI shuttles internal m7G-modified transcripts into stress granules and modulates mRNA metabolism
Zhicong Zhao, Ying Qing, Lei Dong, et al.
Cell (2023) Vol. 186, Iss. 15, pp. 3208-3226.e27
Open Access | Times Cited: 77
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
Liquid–liquid phase separation in autophagy
Nobuo N. Noda, Zheng Wang, Hong Zhang
The Journal of Cell Biology (2020) Vol. 219, Iss. 8
Open Access | Times Cited: 135
The Nuclear SUMO-Targeted Ubiquitin Quality Control Network Regulates the Dynamics of Cytoplasmic Stress Granules
Jan Keiten‐Schmitz, Kristina Wagner, Tanja Piller, et al.
Molecular Cell (2020) Vol. 79, Iss. 1, pp. 54-67.e7
Closed Access | Times Cited: 101
Cellular stress leads to the formation of membraneless stress assemblies in eukaryotic cells
Wessel van Leeuwen, Cathérine Rabouille
Traffic (2019) Vol. 20, Iss. 9, pp. 623-638
Open Access | Times Cited: 92
Cancer Cells Upregulate NRF2 Signaling to Adapt to Autophagy Inhibition
Christina G. Towers, Brent E. Fitzwalter, Daniel P. Regan, et al.
Developmental Cell (2019) Vol. 50, Iss. 6, pp. 690-703.e6
Open Access | Times Cited: 86
Combating deleterious phase transitions in neurodegenerative disease
April L. Darling, James Shorter
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research (2021) Vol. 1868, Iss. 5, pp. 118984-118984
Open Access | Times Cited: 80
Spatiotemporally-resolved mapping of RNA binding proteins via functional proximity labeling reveals a mitochondrial mRNA anchor promoting stress recovery
Wei Qin, Samuel A. Myers, Dominique K. Carey, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 65
Stress granules and mTOR are regulated by membrane atg8ylation during lysosomal damage
Jingyue Jia, Fulong Wang, Zambarlal Bhujabal, et al.
The Journal of Cell Biology (2022) Vol. 221, Iss. 11
Open Access | Times Cited: 53
Autophagy and beyond: Unraveling the complexity of UNC-51-like kinase 1 (ULK1) from biological functions to therapeutic implications
Ling Zou, Minru Liao, Yongqi Zhen, et al.
Acta Pharmaceutica Sinica B (2022) Vol. 12, Iss. 10, pp. 3743-3782
Open Access | Times Cited: 49
Friend or foe: The role of stress granule in neurodegenerative disease
Qinqin Cui, Zhongyi Liu, Ge Bai
Neuron (2024) Vol. 112, Iss. 15, pp. 2464-2485
Closed Access | Times Cited: 12
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
Physiological functions of ULK1/2
Gautam Pareek, Mondira Kundu
Journal of Molecular Biology (2024) Vol. 436, Iss. 15, pp. 168472-168472
Open Access | Times Cited: 9
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