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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:

The Role of Post-Translational Modifications on Prion-Like Aggregation and Liquid-Phase Separation of FUS
Shannon N. Rhoads, Zachary Monahan, Debra Yee, et al.
International Journal of Molecular Sciences (2018) Vol. 19, Iss. 3, pp. 886-886
Open Access | Times Cited: 109

Showing 1-25 of 109 citing articles:

Intrinsically Disordered Proteins and Their “Mysterious” (Meta)Physics
Vladimir N. Uversky
Frontiers in Physics (2019) Vol. 7
Open Access | Times Cited: 466
Friend or foe—Post-translational modifications as regulators of phase separation and RNP granule dynamics
Mario Hofweber, Dorothee Dormann
Journal of Biological Chemistry (2018) Vol. 294, Iss. 18, pp. 7137-7150
Open Access | Times Cited: 338
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
The Role of Post-Translational Modifications in the Phase Transitions of Intrinsically Disordered Proteins
Izzy Owen, Frank Shewmaker
International Journal of Molecular Sciences (2019) Vol. 20, Iss. 21, pp. 5501-5501
Open Access | Times Cited: 192
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
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: 102
Current State and Future Directions in the Therapy of ALS
Laura Tzeplaeff, Sibylle Wilfling, Maria Viktoria Requardt, et al.
Cells (2023) Vol. 12, Iss. 11, pp. 1523-1523
Open Access | Times Cited: 59
Chemically Informed Coarse-Graining of Electrostatic Forces in Charge-Rich Biomolecular Condensates
Andrés R. Tejedor, Anne Aguirre Gonzalez, Maria Julia Maristany, et al.
ACS Central Science (2025) Vol. 11, Iss. 2, pp. 302-321
Open Access | Times Cited: 2
Cellular consequences of arginine methylation
Benjamin M. Lorton, David Shechter
Cellular and Molecular Life Sciences (2019) Vol. 76, Iss. 15, pp. 2933-2956
Open Access | Times Cited: 132
Molecular and Cellular Mechanisms Affected in ALS
Laura Le Gall, Ekene Anakor, Owen Connolly, et al.
Journal of Personalized Medicine (2020) Vol. 10, Iss. 3, pp. 101-101
Open Access | Times Cited: 112
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: 81
RNA and liquid-liquid phase separation
Qi Guo, Xiangmin Shi, Xiangting Wang
Non-coding RNA Research (2021) Vol. 6, Iss. 2, pp. 92-99
Open Access | Times Cited: 81
Fused in Sarcoma: Properties, Self-Assembly and Correlation with Neurodegenerative Diseases
Chen Chen, Xiufang Ding, Nimrah Akram, et al.
Molecules (2019) Vol. 24, Iss. 8, pp. 1622-1622
Open Access | Times Cited: 80
Post-translational modifications: Regulators of neurodegenerative proteinopathies
Rohan Gupta, Mehar Sahu, Devesh Srivastava, et al.
Ageing Research Reviews (2021) Vol. 68, pp. 101336-101336
Closed Access | Times Cited: 79
A predictive coarse-grained model for position-specific effects of post-translational modifications
Theodora Myrto Perdikari, Nina Jovic, Gregory L. Dignon, et al.
Biophysical Journal (2021) Vol. 120, Iss. 7, pp. 1187-1197
Open Access | Times Cited: 68
Deubiquitinating enzymes (DUBs): decipher underlying basis of neurodegenerative diseases
Baohua Liu, Jing Ruan, Meng Chen, et al.
Molecular Psychiatry (2021) Vol. 27, Iss. 1, pp. 259-268
Closed Access | Times Cited: 62
‘RNA modulation of transport properties and stability in phase-separated condensates
Andrés R. Tejedor, Adiran Garaizar, Jorge Ramı́rez, et al.
Biophysical Journal (2021) Vol. 120, Iss. 23, pp. 5169-5186
Open Access | Times Cited: 61
Protein structural transitions critically transform the network connectivity and viscoelasticity of RNA-binding protein condensates but RNA can prevent it
Andrés R. Tejedor, Ignacio Sanchez‐Burgos, Maria Estevez-Espinosa, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 45
RNA length has a non-trivial effect in the stability of biomolecular condensates formed by RNA-binding proteins
Ignacio Sanchez‐Burgos, Jorge R. Espinosa, Jerelle A. Joseph, et al.
PLoS Computational Biology (2022) Vol. 18, Iss. 2, pp. e1009810-e1009810
Open Access | Times Cited: 44
Interplay between posttranslational modifications and liquid‒liquid phase separation in tumors
Xiaojun Yan, Meng Zhang, Donglai Wang
Cancer Letters (2024) Vol. 584, pp. 216614-216614
Closed Access | Times Cited: 11
Aberrant Phase Transitions: Side Effects and Novel Therapeutic Strategies in Human Disease
Veronica Verdile, Elisa De Paola, Maria Paola Paronetto
Frontiers in Genetics (2019) Vol. 10
Open Access | Times Cited: 64
Salt dependent phase behavior of intrinsically disordered proteins from a coarse-grained model with explicit water and ions
Adiran Garaizar, Jorge R. Espinosa
The Journal of Chemical Physics (2021) Vol. 155, Iss. 12, pp. 125103-125103
Closed Access | Times Cited: 56
Expansion of Intrinsically Disordered Proteins Increases the Range of Stability of Liquid–Liquid Phase Separation
Adiran Garaizar, Ignacio Sanchez‐Burgos, Rosana Collepardo‐Guevara, et al.
Molecules (2020) Vol. 25, Iss. 20, pp. 4705-4705
Open Access | Times Cited: 55
The physics of liquid-to-solid transitions in multi-domain protein condensates
Srivastav Ranganathan, Eugene I. Shakhnovich
Biophysical Journal (2022) Vol. 121, Iss. 14, pp. 2751-2766
Open Access | Times Cited: 34
Location and Concentration of Aromatic‐Rich Segments Dictates the Percolating Inter‐Molecular Network and Viscoelastic Properties of Ageing Condensates
S. Blazquez, Ignacio Sanchez‐Burgos, Jorge Ramı́rez, et al.
Advanced Science (2023) Vol. 10, Iss. 25
Open Access | Times Cited: 21
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