Open Access Helper

OpenAlex Citation Counts

OpenAlex Citations Logo

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:

Surface Electrostatics Govern the Emulsion Stability of Biomolecular Condensates
Timothy J. Welsh, Georg Krainer, Jorge R. Espinosa, et al.
Nano Letters (2022) Vol. 22, Iss. 2, pp. 612-621
Open Access | Times Cited: 110

Showing 1-25 of 110 citing articles:

Active coacervate droplets are protocells that grow and resist Ostwald ripening
Karina K. Nakashima, Merlijn H. I. van Haren, Alain A. M. André, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 133
Aging can transform single-component protein condensates into multiphase architectures
Adiran Garaizar, Jorge R. Espinosa, Jerelle A. Joseph, et al.
Proceedings of the National Academy of Sciences (2022) Vol. 119, Iss. 26
Open Access | Times Cited: 70
Interface of biomolecular condensates modulates redox reactions
Yifan Dai, Christian F. Chamberlayne, Marco S. Messina, et al.
Chem (2023) Vol. 9, Iss. 6, pp. 1594-1609
Open Access | Times Cited: 65
Coacervate Droplets for Synthetic Cells
Zi Lin, Thomas Beneyton, Jean‐Christophe Baret, et al.
Small Methods (2023) Vol. 7, Iss. 12
Open Access | Times Cited: 41
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: 12
Quantifying viscosity and surface tension of multicomponent protein-nucleic acid condensates
Ibraheem Alshareedah, George M. Thurston, Priya R. Banerjee
Biophysical Journal (2021) Vol. 120, Iss. 7, pp. 1161-1169
Open Access | Times Cited: 83
Amphiphilic proteins coassemble into multiphasic condensates and act as biomolecular surfactants
Fleurie M. Kelley, Bruna Favetta, Roshan Mammen Regy, et al.
Proceedings of the National Academy of Sciences (2021) Vol. 118, Iss. 51
Open Access | Times Cited: 61
Coacervate formation studied by explicit solvent coarse-grain molecular dynamics with the Martini model
Maria Tsanai, Pim W. J. M. Frederix, Carsten Schroer, et al.
Chemical Science (2021) Vol. 12, Iss. 24, pp. 8521-8530
Open Access | Times Cited: 59
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: 40
RNA at the surface of phase-separated condensates impacts their size and number
Audrey Cochard, Marina Garcia-Jove Navarro, Leonard Piroska, et al.
Biophysical Journal (2022) Vol. 121, Iss. 9, pp. 1675-1690
Open Access | Times Cited: 39
Time-Dependent Material Properties of Aging Biomolecular Condensates from Different Viscoelasticity Measurements in Molecular Dynamics Simulations
Andrés R. Tejedor, Rosana Collepardo‐Guevara, Jorge Ramı́rez, et al.
The Journal of Physical Chemistry B (2023) Vol. 127, Iss. 20, pp. 4441-4459
Open Access | Times Cited: 29
Thermodynamic origins of two-component multiphase condensates of proteins
Pin Yu Chew, Jerelle A. Joseph, Rosana Collepardo‐Guevara, et al.
Chemical Science (2023) Vol. 14, Iss. 7, pp. 1820-1836
Open Access | Times Cited: 24
Direct digital sensing of protein biomarkers in solution
Georg Krainer, Kadi L. Saar, William E. Arter, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 22
Highly Charged Proteins and Their Repulsive Interactions Antagonize Biomolecular Condensation
Cheng Tan, Ai Niitsu, Yuji Sugita
JACS Au (2023) Vol. 3, Iss. 3, pp. 834-848
Open Access | Times Cited: 20
The role of biomolecular condensates in protein aggregation
Brent S. Visser, Wojciech P. Lipiński, Evan Spruijt
Nature Reviews Chemistry (2024) Vol. 8, Iss. 9, pp. 686-700
Closed Access | Times Cited: 9
Probing the surface charge of condensates using microelectrophoresis
Merlijn H. I. van Haren, Brent S. Visser, Evan Spruijt
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 8
Biomolecular condensates sustain pH gradients at equilibrium driven by charge neutralisation
Hannes Ausserwöger, Rob Scrutton, Tomas Šneideris, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 8
Biomolecular condensates can function as inherent catalysts
Xiao Guo, Mina Farag, Naixin Qian, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 8
Biomolecular condensates regulate cellular electrochemical equilibria
Yifan Dai, Zhengqing Zhou, Yu Wen, et al.
Cell (2024)
Closed Access | Times Cited: 8
Emerging experimental methods to study the thermodynamics of biomolecular condensate formation
Soumik Ray, Alexander K. Buell
The Journal of Chemical Physics (2024) Vol. 160, Iss. 9
Open Access | Times Cited: 7
Biomolecular Condensates are Characterized by Interphase Electric Potentials
Ammon E. Posey, A Bremer, Nadia A. Erkamp, et al.
Journal of the American Chemical Society (2024)
Closed Access | Times Cited: 7
Differential Effects of Sequence-Local versus Nonlocal Charge Patterns on Phase Separation and Conformational Dimensions of Polyampholytes as Model Intrinsically Disordered Proteins
Tanmoy Pal, Jonas Wessén, Suman Das, et al.
The Journal of Physical Chemistry Letters (2024) Vol. 15, Iss. 32, pp. 8248-8256
Open Access | Times Cited: 6
Thermal aggregation of immunoglobulin G depending on the charge state of protein–polyelectrolyte complexes
Akira Nomoto, Kentaro Shiraki
International Journal of Biological Macromolecules (2025), pp. 139500-139500
Closed Access
Charge Arrangement Determines the Sensitivity of Aggregation Patterns between Peptide-Chains to the Surrounding Ionic Environment
Lei Bao, Wen-Bin Kang, Ben‐Chao Zhu, et al.
Journal of Chemical Information and Modeling (2025)
Closed Access
Decoding Phase Separation of Prion-Like Domains through Data-Driven Scaling Laws
Maria Julia Maristany, Anne Aguirre Gonzalez, Jorge R. Espinosa, et al.
(2025)
Open Access
Page 1 - Next Page

Scroll to top