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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:

Different Material States of Pub1 Condensates Define Distinct Modes of Stress Adaptation and Recovery
Sonja Kroschwald, Matthias C. Munder, Shovamayee Maharana, et al.
Cell Reports (2018) Vol. 23, Iss. 11, pp. 3327-3339
Open Access | Times Cited: 229

Showing 1-25 of 229 citing articles:

Considerations and Challenges in Studying Liquid-Liquid Phase Separation and Biomolecular Condensates
Simon Alberti, Amy Gladfelter, Tanja Mittag
Cell (2019) Vol. 176, Iss. 3, pp. 419-434
Open Access | Times Cited: 2381
Biomolecular condensates at the nexus of cellular stress, protein aggregation disease and ageing
Simon Alberti, Anthony A. Hyman
Nature Reviews Molecular Cell Biology (2021) Vol. 22, Iss. 3, pp. 196-213
Closed Access | Times Cited: 872
Physical Principles Underlying the Complex Biology of Intracellular Phase Transitions
Jeong‐Mo Choi, Alex S. Holehouse, Rohit V. Pappu
Annual Review of Biophysics (2020) Vol. 49, Iss. 1, pp. 107-133
Open Access | Times Cited: 803
Liquid–Liquid Phase Separation in Disease
Simon Alberti, Dorothee Dormann
Annual Review of Genetics (2019) Vol. 53, Iss. 1, pp. 171-194
Open Access | Times Cited: 772
The molecular language of membraneless organelles
Edward Gomes, James Shorter
Journal of Biological Chemistry (2018) Vol. 294, Iss. 18, pp. 7115-7127
Open Access | Times Cited: 711
Biomolecular Phase Separation: From Molecular Driving Forces to Macroscopic Properties
Gregory L. Dignon, Robert B. Best, Jeetain Mittal
Annual Review of Physical Chemistry (2020) Vol. 71, Iss. 1, pp. 53-75
Open Access | Times Cited: 552
A conceptual framework for understanding phase separation and addressing open questions and challenges
Tanja Mittag, Rohit V. Pappu
Molecular Cell (2022) Vol. 82, Iss. 12, pp. 2201-2214
Open Access | Times Cited: 500
Who's In and Who's Out—Compositional Control of Biomolecular Condensates
Jonathon A. Ditlev, Lindsay B. Case, Michael K. Rosen
Journal of Molecular Biology (2018) Vol. 430, Iss. 23, pp. 4666-4684
Open Access | Times Cited: 341
TDP-43 α-helical structure tunes liquid–liquid phase separation and function
Alexander E. Conicella, Gregory L. Dignon, Gül H. Zerze, et al.
Proceedings of the National Academy of Sciences (2020) Vol. 117, Iss. 11, pp. 5883-5894
Open Access | Times Cited: 330
Temperature-Controlled Liquid–Liquid Phase Separation of Disordered Proteins
Gregory L. Dignon, Wenwei Zheng, Young C. Kim, et al.
ACS Central Science (2019) Vol. 5, Iss. 5, pp. 821-830
Open Access | Times Cited: 278
Nucleo-cytoplasmic Partitioning of ARF Proteins Controls Auxin Responses in Arabidopsis thaliana
Samantha K. Powers, Alex S. Holehouse, David A. Korasick, et al.
Molecular Cell (2019) Vol. 76, Iss. 1, pp. 177-190.e5
Open Access | Times Cited: 234
Prion-like low-complexity sequences: Key regulators of protein solubility and phase behavior
Titus M. Franzmann, Simon Alberti
Journal of Biological Chemistry (2018) Vol. 294, Iss. 18, pp. 7128-7136
Open Access | Times Cited: 208
Condensation of Ded1p Promotes a Translational Switch from Housekeeping to Stress Protein Production
Christiane Iserman, Christine Desroches Altamirano, Ceciel Jegers, et al.
Cell (2020) Vol. 181, Iss. 4, pp. 818-831.e19
Open Access | Times Cited: 203
Phase Separation of Intrinsically Disordered Proteins
Ammon E. Posey, Alex S. Holehouse, Rohit V. Pappu
Methods in enzymology on CD-ROM/Methods in enzymology (2018), pp. 1-30
Closed Access | Times Cited: 194
Cellular sensing by phase separation: Using the process, not just the products
Haneul Yoo, Catherine G. Triandafillou, D. Allan Drummond
Journal of Biological Chemistry (2019) Vol. 294, Iss. 18, pp. 7151-7159
Open Access | Times Cited: 180
Hydrogen bond guidance and aromatic stacking drive liquid-liquid phase separation of intrinsically disordered histidine-rich peptides
Bartosz Gabryelczyk, Hao Cai, Xiangyan Shi, et al.
Nature Communications (2019) Vol. 10, Iss. 1
Open Access | Times Cited: 176
Protein Phase Separation as a Stress Survival Strategy
Titus M. Franzmann, Simon Alberti
Cold Spring Harbor Perspectives in Biology (2019) Vol. 11, Iss. 6, pp. a034058-a034058
Open Access | Times Cited: 148
Stress‐induced mRNP granules: Form and function of processing bodies and stress granules
Anna R. Guzikowski, Yang S. Chen, Brian M. Zid
Wiley Interdisciplinary Reviews - RNA (2019) Vol. 10, Iss. 3
Open Access | Times Cited: 148
ROS regulated reversible protein phase separation synchronizes plant flowering
Xiaozhen Huang, Shudong Chen, Weiping Li, et al.
Nature Chemical Biology (2021) Vol. 17, Iss. 5, pp. 549-557
Closed Access | Times Cited: 144
It’s not just a phase: function and characteristics of RNA-binding proteins in phase separation
Hannah J. Wiedner, Jimena Giudice
Nature Structural & Molecular Biology (2021) Vol. 28, Iss. 6, pp. 465-473
Open Access | Times Cited: 142
A brief guideline for studies of phase-separated biomolecular condensates
Yifei Gao, Xi Li, Pilong Li, et al.
Nature Chemical Biology (2022) Vol. 18, Iss. 12, pp. 1307-1318
Closed Access | Times Cited: 107
Post-translational modifications in liquid-liquid phase separation: a comprehensive review
Jingxian Li, Mengdi Zhang, Weirui Ma, et al.
Molecular Biomedicine (2022) Vol. 3, Iss. 1
Open Access | Times Cited: 103
Phase separation of protein mixtures is driven by the interplay of homotypic and heterotypic interactions
Mina Farag, Wade M. Borcherds, Anne Bremer, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 98
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
Chaperones directly and efficiently disperse stress-triggered biomolecular condensates
Haneul Yoo, Jared A.M. Bard, Evgeny V. Pilipenko, et al.
Molecular Cell (2022) Vol. 82, Iss. 4, pp. 741-755.e11
Open Access | Times Cited: 90
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