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:

Hydrophobicity of arginine leads to reentrant liquid-liquid phase separation behaviors of arginine-rich proteins
Yuri Hong, Saeed Najafi, Thomas M. Casey, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 97

Showing 1-25 of 97 citing articles:

Liquid–Liquid Phase Separation Modifies the Dynamic Properties of Intrinsically Disordered Proteins
Serafima Guseva, Vincent Schnapka, Wiktor Adamski, et al.
Journal of the American Chemical Society (2023) Vol. 145, Iss. 19, pp. 10548-10563
Open Access | Times Cited: 59

Molecular Crowding: The History and Development of a Scientific Paradigm
Caterina Alfano, Yann Fichou, Klaus Huber, et al.
Chemical Reviews (2024) Vol. 124, Iss. 6, pp. 3186-3219
Open Access | Times Cited: 38

Emergent microenvironments of nucleoli
Matthew R. King, Kiersten M. Ruff, Rohit V. Pappu
Nucleus (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 23

Single-fluorogen imaging reveals distinct environmental and structural features of biomolecular condensates
Tingting Wu, Matthew R. King, Yuanxin Qiu, et al.
Nature Physics (2025)
Open Access | Times Cited: 3

Peptide-Mediated Liquid-Liquid Phase Separation and Biomolecular Condensates
Guangle Li, Chengqian Yuan, Xuehai Yan
Soft Matter (2025) Vol. 21, Iss. 10, pp. 1781-1812
Closed Access | Times Cited: 2

Binary peptide coacervates as an active model for biomolecular condensates
Shoupeng Cao, Peng Zhou, Guizhi Shen, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access | Times Cited: 2

Biological importance of arginine: A comprehensive review of the roles in structure, disorder, and functionality of peptides and proteins
Munishwar N. Gupta, Vladimir N. Uversky
International Journal of Biological Macromolecules (2023) Vol. 257, pp. 128646-128646
Open Access | Times Cited: 35

Cross-Talk of Cation−π Interactions with Electrostatic and Aromatic Interactions: A Salt-Dependent Trade-off in Biomolecular Condensates
Milan Kumar Hazra, Yaakov Levy
The Journal of Physical Chemistry Letters (2023) Vol. 14, Iss. 38, pp. 8460-8469
Open Access | Times Cited: 26

Aromatic Residues in Proteins: Re-Evaluating the Geometry and Energetics of π–π, Cation−π, and CH−π Interactions
Rivka Calinsky, Yaakov Levy
The Journal of Physical Chemistry B (2024) Vol. 128, Iss. 36, pp. 8687-8700
Open Access | Times Cited: 9

pH-Responsive Phase Separation Dynamics of Intrinsically Disordered Peptides
Manali Nandy, Ketan A. Ganar, Hans Ippel, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2025)
Open Access | Times Cited: 1

Context dependence in assembly code for supramolecular peptide materials and systems
Kübra Kaygisiz, Deborah Sementa, Vignesh Athiyarath, et al.
Nature Reviews Materials (2025)
Closed Access | Times Cited: 1

Peptide Coacervates: Formation, Mechanism, and Biological Applications
Jiewei Yuan, Y. Richard Yang, Kehua Dai, et al.
ACS Applied Materials & Interfaces (2025)
Closed Access | Times Cited: 1

Single fluorogen imaging reveals distinct environmental and structural features of biomolecular condensates
Tingting Wu, Matthew R. King, Yuanxin Qiu, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 23

Polyelectrolyte-multivalent molecule complexes: physicochemical properties and applications
Santiago E. Herrera, Maximiliano L. Agazzi, Eugenia Apuzzo, et al.
Soft Matter (2023) Vol. 19, Iss. 11, pp. 2013-2041
Closed Access | Times Cited: 22

Protein compactness and interaction valency define the architecture of a biomolecular condensate across scales
Anton A. Polyansky, Laura D. Gallego, Roman G. Efremov, et al.
eLife (2023) Vol. 12
Open Access | Times Cited: 20

Structure‐Property Relationships Governing Membrane‐Penetrating Behaviour of Complex Coacervates
Tiemei Lu, Xinyu Hu, Merlijn H. I. van Haren, et al.
Small (2023) Vol. 19, Iss. 38
Open Access | Times Cited: 17

Complex Coacervate-Based Materials for Biomedicine: Recent Advancements and Future Prospects
Partha Sarathi Roy
Industrial & Engineering Chemistry Research (2024) Vol. 63, Iss. 13, pp. 5414-5487
Closed Access | Times Cited: 8

Phase-separating peptide coacervates with programmable material properties for universal intracellular delivery of macromolecules
Yue Sun, Xi Wu, Jianguo Li, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 8

Decoding Phase Separation of Prion-Like Domains through Data-Driven Scaling Laws
Maria Julia Maristany, Anne Aguirre Gonzalez, Jorge R. Espinosa, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 14

Aromatic and arginine content drives multiphasic condensation of protein-RNA mixtures
Pin Yu Chew, Jerelle A. Joseph, Rosana Collepardo‐Guevara, et al.
Biophysical Journal (2023)
Open Access | Times Cited: 13

Decoding Phase Separation of Prion-Like Domains through Data-Driven Scaling Laws
Maria Julia Maristany, Anne Aguirre Gonzalez, Jorge R. Espinosa, et al.
eLife (2024)
Open Access | Times Cited: 4

Influence of the backbone chemistry and ionic functional groups of five pairs of oppositely charged polyelectrolytes on complex coacervation
Yuri Hong, Surim Yoo, Jihoon Han, et al.
Communications Chemistry (2024) Vol. 7, Iss. 1
Open Access | Times Cited: 4

Phase separation and ageing of glycine-rich protein from tick adhesive
Ketan A. Ganar, Manali Nandy, Polina Turbina, et al.
Nature Chemistry (2024)
Open Access | Times Cited: 4

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