
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:
What are the distinguishing features and size requirements of biomolecular condensates and their implications for RNA-containing condensates?
Julie D. Forman‐Kay, Jonathon A. Ditlev, Michael L. Nosella, et al.
RNA (2021) Vol. 28, Iss. 1, pp. 36-47
Open Access | Times Cited: 40
Julie D. Forman‐Kay, Jonathon A. Ditlev, Michael L. Nosella, et al.
RNA (2021) Vol. 28, Iss. 1, pp. 36-47
Open Access | Times Cited: 40
Showing 1-25 of 40 citing articles:
Learning the chemical grammar of biomolecular condensates
Henry R. Kilgore, Richard A. Young
Nature Chemical Biology (2022) Vol. 18, Iss. 12, pp. 1298-1306
Open Access | Times Cited: 115
Henry R. Kilgore, Richard A. Young
Nature Chemical Biology (2022) Vol. 18, Iss. 12, pp. 1298-1306
Open Access | Times Cited: 115
Formation, function, and pathology of RNP granules
Nina Ripin, Roy Parker
Cell (2023) Vol. 186, Iss. 22, pp. 4737-4756
Closed Access | Times Cited: 75
Nina Ripin, Roy Parker
Cell (2023) Vol. 186, Iss. 22, pp. 4737-4756
Closed Access | Times Cited: 75
RNA granules: functional compartments or incidental condensates?
Andrea Putnam, Laura Thomas, Géraldine Seydoux
Genes & Development (2023) Vol. 37, Iss. 9-10, pp. 354-376
Open Access | Times Cited: 57
Andrea Putnam, Laura Thomas, Géraldine Seydoux
Genes & Development (2023) Vol. 37, Iss. 9-10, pp. 354-376
Open Access | Times Cited: 57
Distinct chemical environments in biomolecular condensates
Henry R. Kilgore, Peter G. Mikhael, Kalon J. Overholt, et al.
Nature Chemical Biology (2023) Vol. 20, Iss. 3, pp. 291-301
Closed Access | Times Cited: 48
Henry R. Kilgore, Peter G. Mikhael, Kalon J. Overholt, et al.
Nature Chemical Biology (2023) Vol. 20, Iss. 3, pp. 291-301
Closed Access | Times Cited: 48
Fundamental Aspects of Phase-Separated Biomolecular Condensates
Huan‐Xiang Zhou, Divya Kota, Sanbo Qin, et al.
Chemical Reviews (2024) Vol. 124, Iss. 13, pp. 8550-8595
Closed Access | Times Cited: 22
Huan‐Xiang Zhou, Divya Kota, Sanbo Qin, et al.
Chemical Reviews (2024) Vol. 124, Iss. 13, pp. 8550-8595
Closed Access | Times Cited: 22
Intrinsically disordered regions that drive phase separation form a robustly distinct protein class
Ayyam Y. Ibrahim, Nathan P. Khaodeuanepheng, Dhanush L. Amarasekara, et al.
Journal of Biological Chemistry (2022) Vol. 299, Iss. 1, pp. 102801-102801
Open Access | Times Cited: 55
Ayyam Y. Ibrahim, Nathan P. Khaodeuanepheng, Dhanush L. Amarasekara, et al.
Journal of Biological Chemistry (2022) Vol. 299, Iss. 1, pp. 102801-102801
Open Access | Times Cited: 55
Label-Free Techniques for Probing Biomolecular Condensates
Khalid A. Ibrahim, Akhil S. Naidu, Helena Miljkovic, et al.
ACS Nano (2024) Vol. 18, Iss. 16, pp. 10738-10757
Closed Access | Times Cited: 11
Khalid A. Ibrahim, Akhil S. Naidu, Helena Miljkovic, et al.
ACS Nano (2024) Vol. 18, Iss. 16, pp. 10738-10757
Closed Access | Times Cited: 11
A Functional Map of the Human Intrinsically Disordered Proteome
Iva Pritišanac, T. Reid Alderson, Đesika Kolarić, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Closed Access | Times Cited: 10
Iva Pritišanac, T. Reid Alderson, Đesika Kolarić, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Closed Access | Times Cited: 10
A biophysical basis for the spreading behavior and limited diffusion of Xist
Mingrui Ding, Danni Wang, Hui Chen, et al.
Cell (2025)
Closed Access | Times Cited: 1
Mingrui Ding, Danni Wang, Hui Chen, et al.
Cell (2025)
Closed Access | Times Cited: 1
Protein interactions, calcium, phosphorylation, and cholesterol modulate CFTR cluster formation on membranes
Yimei Wan, R.D.A. Hudson, Jordyn Smith, et al.
Proceedings of the National Academy of Sciences (2025) Vol. 122, Iss. 11
Open Access | Times Cited: 1
Yimei Wan, R.D.A. Hudson, Jordyn Smith, et al.
Proceedings of the National Academy of Sciences (2025) Vol. 122, Iss. 11
Open Access | Times Cited: 1
The dynamic clustering of insulin receptor underlies its signaling and is disrupted in insulin resistance
Alessandra Dall’Agnese, Jesse M. Platt, Ming Zheng, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 27
Alessandra Dall’Agnese, Jesse M. Platt, Ming Zheng, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 27
Dual DNA/RNA-binding factor regulates dynamics of hnRNP splicing condensates
Mukulika Ray, Julia Zaborowsky, Pranav Mahableshwarkar, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 5
Mukulika Ray, Julia Zaborowsky, Pranav Mahableshwarkar, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 5
Activation of L-lactate oxidase by the formation of enzyme assemblies through liquid–liquid phase separation
Tomoto Ura, Ako Kagawa, Nanako Sakakibara, et al.
Scientific Reports (2023) Vol. 13, Iss. 1
Open Access | Times Cited: 11
Tomoto Ura, Ako Kagawa, Nanako Sakakibara, et al.
Scientific Reports (2023) Vol. 13, Iss. 1
Open Access | Times Cited: 11
Spectrin condensates provide a nidus for assembling the periodic axonal structure
Nicholas P. Boyer, Rohan Sharma, Theresa Wiesner, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 4
Nicholas P. Boyer, Rohan Sharma, Theresa Wiesner, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 4
An RNA-centric view of transcription and genome organization
Jonathan E. Henninger, Richard A. Young
Molecular Cell (2024) Vol. 84, Iss. 19, pp. 3627-3643
Closed Access | Times Cited: 4
Jonathan E. Henninger, Richard A. Young
Molecular Cell (2024) Vol. 84, Iss. 19, pp. 3627-3643
Closed Access | Times Cited: 4
Bclaf1 biomolecular condensates protect nuclear PTK2 from ubiquitin-proteasome system promoting cardiomyocyte survival during oxidative stress
Isabela Aparecida Moretto, Beatriz Rodrigues, Pedro Víctor-Carvalho, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2025)
Open Access
Isabela Aparecida Moretto, Beatriz Rodrigues, Pedro Víctor-Carvalho, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2025)
Open Access
Purification of Low‐Complexity Domain Proteins FUS, EWSR1, and Their Fusions
Jesse Altemus, Michelle A. Lay, Valery F. Thompson, et al.
Current Protocols (2025) Vol. 5, Iss. 4
Open Access
Jesse Altemus, Michelle A. Lay, Valery F. Thompson, et al.
Current Protocols (2025) Vol. 5, Iss. 4
Open Access
Determining the Role of Electrostatics in the Making and Breaking of the Caprin1–ATP Nanocondensate
Maria Tsanai, Teresa Head‐Gordon
The Journal of Physical Chemistry B (2025)
Closed Access
Maria Tsanai, Teresa Head‐Gordon
The Journal of Physical Chemistry B (2025)
Closed Access
The Material Properties of the Cell Nucleus: A Matter of Scale
Maud Hertzog, Fabian Erdel
Cells (2023) Vol. 12, Iss. 15, pp. 1958-1958
Open Access | Times Cited: 10
Maud Hertzog, Fabian Erdel
Cells (2023) Vol. 12, Iss. 15, pp. 1958-1958
Open Access | Times Cited: 10
Hydrodynamic Radii of Intrinsically Disordered Proteins: Fast Prediction by Minimum Dissipation Approximation and Experimental Validation
Radost Waszkiewicz, Agnieszka Michaś, Michał K. Białobrzewski, et al.
The Journal of Physical Chemistry Letters (2024) Vol. 15, Iss. 19, pp. 5024-5033
Open Access | Times Cited: 3
Radost Waszkiewicz, Agnieszka Michaś, Michał K. Białobrzewski, et al.
The Journal of Physical Chemistry Letters (2024) Vol. 15, Iss. 19, pp. 5024-5033
Open Access | Times Cited: 3
Perspective: fluorescence lifetime imaging and single-molecule spectroscopy for studying biological condensates
Maria Loidolt-Krüger
Methods in microscopy (2025)
Closed Access
Maria Loidolt-Krüger
Methods in microscopy (2025)
Closed Access
Polymer-engineered condensates for enzyme activation
Tomoto Ura, Toya Yoshida, Tsutomu Mikawa, et al.
Polymer Journal (2025)
Open Access
Tomoto Ura, Toya Yoshida, Tsutomu Mikawa, et al.
Polymer Journal (2025)
Open Access
Seeing Biomolecular Condensates Through the Lens of Viruses
Alexander Borodavka, Julia Acker
Annual Review of Virology (2023) Vol. 10, Iss. 1, pp. 163-182
Open Access | Times Cited: 9
Alexander Borodavka, Julia Acker
Annual Review of Virology (2023) Vol. 10, Iss. 1, pp. 163-182
Open Access | Times Cited: 9
Intrinsically disordered plant protein PARCL colocalizes with RNA in phase-separated condensates whose formation can be regulated by mutating the PLD
Anna Ostendorp, Steffen Ostendorp, Yuan Zhou, et al.
Journal of Biological Chemistry (2022) Vol. 298, Iss. 12, pp. 102631-102631
Open Access | Times Cited: 13
Anna Ostendorp, Steffen Ostendorp, Yuan Zhou, et al.
Journal of Biological Chemistry (2022) Vol. 298, Iss. 12, pp. 102631-102631
Open Access | Times Cited: 13
From the Catastrophic Objective Irreproducibility of Cancer Research and Unavoidable Failures of Molecular Targeted Therapies to the Sparkling Hope of Supramolecular Targeted Strategies
И. В. Алексеенко, L. G. Kondratyeva, И. П. Чернов, et al.
International Journal of Molecular Sciences (2023) Vol. 24, Iss. 3, pp. 2796-2796
Open Access | Times Cited: 7
И. В. Алексеенко, L. G. Kondratyeva, И. П. Чернов, et al.
International Journal of Molecular Sciences (2023) Vol. 24, Iss. 3, pp. 2796-2796
Open Access | Times Cited: 7