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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-Triggered Phase Separation Is an Adaptive, Evolutionarily Tuned Response
Joshua A. Riback, Christopher D. Katanski, Jamie L. Kear‐Scott, et al.
Cell (2017) Vol. 168, Iss. 6, pp. 1028-1040.e19
Open Access | Times Cited: 851

Showing 26-50 of 851 citing articles:

Phase Separation and Neurodegenerative Diseases: A Disturbance in the Force
Aurélie Zbinden, Manuela Pérez‐Berlanga, Pierre De Rossi, et al.
Developmental Cell (2020) Vol. 55, Iss. 1, pp. 45-68
Open Access | Times Cited: 384
Relationship of Sequence and Phase Separation in Protein Low-Complexity Regions
Erik Martin, Tanja Mittag
Biochemistry (2018) Vol. 57, Iss. 17, pp. 2478-2487
Open Access | Times Cited: 382
Relation between single-molecule properties and phase behavior of intrinsically disordered proteins
Gregory L. Dignon, Wenwei Zheng, Robert B. Best, et al.
Proceedings of the National Academy of Sciences (2018) Vol. 115, Iss. 40, pp. 9929-9934
Open Access | Times Cited: 378
Intrinsically disordered sequences enable modulation of protein phase separation through distributed tyrosine motifs
Yuan Lin, Simon L. Currie, Michael K. Rosen
Journal of Biological Chemistry (2017) Vol. 292, Iss. 46, pp. 19110-19120
Open Access | Times Cited: 377
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
The causes of evolvability and their evolution
Joshua L. Payne, Andreas Wagner
Nature Reviews Genetics (2018) Vol. 20, Iss. 1, pp. 24-38
Open Access | Times Cited: 324
Probing and engineering liquid-phase organelles
Dan Bracha, Mackenzie T. Walls, Clifford P. Brangwynne
Nature Biotechnology (2019) Vol. 37, Iss. 12, pp. 1435-1445
Closed Access | Times Cited: 303
Identifying sequence perturbations to an intrinsically disordered protein that determine its phase-separation behavior
Benjamin S. Schuster, Gregory L. Dignon, Wai Shing Tang, et al.
Proceedings of the National Academy of Sciences (2020) Vol. 117, Iss. 21, pp. 11421-11431
Open Access | Times Cited: 286
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
Liquid-liquid phase separation in biology: mechanisms, physiological functions and human diseases
Hong Zhang, Ji Xiong, Pilong Li, et al.
Science China Life Sciences (2020) Vol. 63, Iss. 7, pp. 953-985
Closed Access | Times Cited: 262
Arabidopsis FLL2 promotes liquid–liquid phase separation of polyadenylation complexes
Xiaofeng Fang, Liang Wang, Ryo Ishikawa, et al.
Nature (2019) Vol. 569, Iss. 7755, pp. 265-269
Open Access | Times Cited: 261
Physics-driven coarse-grained model for biomolecular phase separation with near-quantitative accuracy
Jerelle A. Joseph, Aleks Reinhardt, Anne Aguirre, et al.
Nature Computational Science (2021) Vol. 1, Iss. 11, pp. 732-743
Open Access | Times Cited: 260
Acetylation of intrinsically disordered regions regulates phase separation
Makoto Saito, Daniel Heß, Jan Eglinger, et al.
Nature Chemical Biology (2018) Vol. 15, Iss. 1, pp. 51-61
Closed Access | Times Cited: 252
How do intrinsically disordered protein regions encode a driving force for liquid–liquid phase separation?
Wade M. Borcherds, Anne Bremer, Madeleine B. Borgia, et al.
Current Opinion in Structural Biology (2020) Vol. 67, pp. 41-50
Open Access | Times Cited: 252
Biomolecular Condensates and Cancer
Ann Boija, Isaac A. Klein, Richard A. Young
Cancer Cell (2021) Vol. 39, Iss. 2, pp. 174-192
Open Access | Times Cited: 246
Functional Implications of Intracellular Phase Transitions
Alex S. Holehouse, Rohit V. Pappu
Biochemistry (2018) Vol. 57, Iss. 17, pp. 2415-2423
Open Access | Times Cited: 237
The molecular basis for cellular function of intrinsically disordered protein regions
Alex S. Holehouse, Birthe B. Kragelund
Nature Reviews Molecular Cell Biology (2023) Vol. 25, Iss. 3, pp. 187-211
Open Access | Times Cited: 237
Phase Transitions of Associative Biomacromolecules
Rohit V. Pappu, Samuel R. Cohen, Furqan Dar, et al.
Chemical Reviews (2023) Vol. 123, Iss. 14, pp. 8945-8987
Closed Access | Times Cited: 236
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
TAR DNA-binding protein 43 (TDP-43) liquid–liquid phase separation is mediated by just a few aromatic residues
Hao-Ru Li, Wan‐Chin Chiang, Po-Chun Chou, et al.
Journal of Biological Chemistry (2018) Vol. 293, Iss. 16, pp. 6090-6098
Open Access | Times Cited: 233
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: 230
Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water
Joshua A. Riback, Micayla A. Bowman, Adam M. Zmyslowski, et al.
Science (2017) Vol. 358, Iss. 6360, pp. 238-241
Open Access | Times Cited: 229
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: 228
Intrinsically disordered protein regions and phase separation: sequence determinants of assembly or lack thereof
Erik Martin, Alex S. Holehouse
Emerging Topics in Life Sciences (2020) Vol. 4, Iss. 3, pp. 307-329
Closed Access | Times Cited: 225
Advances in Understanding Stimulus-Responsive Phase Behavior of Intrinsically Disordered Protein Polymers
Kiersten M. Ruff, Stefan Roberts, Ashutosh Chilkoti, et al.
Journal of Molecular Biology (2018) Vol. 430, Iss. 23, pp. 4619-4635
Open Access | Times Cited: 218

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