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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:

Stress Granules and Processing Bodies in Translational Control
Pavel Ivanov, Nancy Kedersha, Paul Anderson
Cold Spring Harbor Perspectives in Biology (2018) Vol. 11, Iss. 5, pp. a032813-a032813
Open Access | Times Cited: 410

Showing 1-25 of 410 citing articles:

A SARS-CoV-2 protein interaction map reveals targets for drug repurposing
David E. Gordon, Gwendolyn Μ. Jang, Mehdi Bouhaddou, et al.
Nature (2020) Vol. 583, Iss. 7816, pp. 459-468
Open Access | Times Cited: 4457
LNCcation: lncRNA localization and function
Mary Catherine Bridges, Amanda C. Daulagala, Antonis Kourtidis
The Journal of Cell Biology (2020) Vol. 220, Iss. 2
Open Access | Times Cited: 1132
G3BP1 Is a Tunable Switch that Triggers Phase Separation to Assemble Stress Granules
Peiguo Yang, Cécile Mathieu, Regina‐Maria Kolaitis, et al.
Cell (2020) Vol. 181, Iss. 2, pp. 325-345.e28
Open Access | Times Cited: 993
Competing Protein-RNA Interaction Networks Control Multiphase Intracellular Organization
David W. Sanders, Nancy Kedersha, Daniel S.W. Lee, et al.
Cell (2020) Vol. 181, Iss. 2, pp. 306-324.e28
Open Access | Times Cited: 716
Role of eIF2α Kinases in Translational Control and Adaptation to Cellular Stress
Ronald C. Wek
Cold Spring Harbor Perspectives in Biology (2018) Vol. 10, Iss. 7, pp. a032870-a032870
Open Access | Times Cited: 433
A SARS-CoV-2-Human Protein-Protein Interaction Map Reveals Drug Targets and Potential Drug-Repurposing
David E. Gordon, Gwendolyn Μ. Jang, Mehdi Bouhaddou, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2020)
Open Access | Times Cited: 433
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: 394
Properties of Stress Granule and P-Body Proteomes
Ji‐Young Youn, Boris J.A. Dyakov, Jianping Zhang, et al.
Molecular Cell (2019) Vol. 76, Iss. 2, pp. 286-294
Open Access | Times Cited: 364
Mammalian stress granules and P bodies at a glance
Claire L. Riggs, Nancy Kedersha, Pavel Ivanov, et al.
Journal of Cell Science (2020) Vol. 133, Iss. 16
Open Access | Times Cited: 306
A guide to membraneless organelles and their various roles in gene regulation
Tetsuro Hirose, Kensuke Ninomiya, Shinichi Nakagawa, et al.
Nature Reviews Molecular Cell Biology (2022) Vol. 24, Iss. 4, pp. 288-304
Closed Access | Times Cited: 297
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: 278
m6A-binding YTHDF proteins promote stress granule formation
Ye Fu, Xiaowei Zhuang
Nature Chemical Biology (2020) Vol. 16, Iss. 9, pp. 955-963
Open Access | Times Cited: 265
Single-Molecule Imaging Reveals Translation of mRNAs Localized to Stress Granules
Daniel Matějů, Bastian Eichenberger, Franka Voigt, et al.
Cell (2020) Vol. 183, Iss. 7, pp. 1801-1812.e13
Open Access | Times Cited: 258
Modulation of RNA Condensation by the DEAD-Box Protein eIF4A
Devin Tauber, Gabriel Tauber, Anthony Khong, et al.
Cell (2020) Vol. 180, Iss. 3, pp. 411-426.e16
Open Access | Times Cited: 251
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: 209
Principles of Translational Control
John W.B. Hershey, Nahum Sonenberg, Michael B. Mathews
Cold Spring Harbor Perspectives in Biology (2018) Vol. 11, Iss. 9, pp. a032607-a032607
Open Access | Times Cited: 180
Translational Control under Stress: Reshaping the Translatome
Vivek M. Advani, Pavel Ivanov
BioEssays (2019) Vol. 41, Iss. 5
Open Access | Times Cited: 180
Translational Control in Virus-Infected Cells
Noam Stern‐Ginossar, Sunnie R. Thompson, Michael B. Mathews, et al.
Cold Spring Harbor Perspectives in Biology (2018) Vol. 11, Iss. 3, pp. a033001-a033001
Open Access | Times Cited: 167
Chromatin mechanics dictates subdiffusion and coarsening dynamics of embedded condensates
Daniel S.W. Lee, Ned S. Wingreen, Clifford P. Brangwynne
Nature Physics (2021) Vol. 17, Iss. 4, pp. 531-538
Open Access | Times Cited: 141
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: 94
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: 93
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: 82
LncRNAs in human cancers: signal from noise
Sara Adnane, Alessandro Marino, Eleonora Leucci
Trends in Cell Biology (2022) Vol. 32, Iss. 7, pp. 565-573
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: 63
Stress granules plug and stabilize damaged endolysosomal membranes
Claudio Bussi, Agustín Mangiarotti, Christian Vanhille-Campos, et al.
Nature (2023) Vol. 623, Iss. 7989, pp. 1062-1069
Open Access | Times Cited: 56
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