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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:

Reentrant liquid condensate phase of proteins is stabilized by hydrophobic and non-ionic interactions
Georg Krainer, Timothy J. Welsh, Jerelle A. Joseph, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 394

Showing 1-25 of 394 citing articles:

Accurate model of liquid–liquid phase behavior of intrinsically disordered proteins from optimization of single-chain properties
Giulio Tesei, Thea K. Schulze, Ramón Crehuet, et al.
Proceedings of the National Academy of Sciences (2021) Vol. 118, Iss. 44
Open Access | Times Cited: 289
Widespread occurrence of the droplet state of proteins in the human proteome
Maarten C. Hardenberg, Attila Horváth, Viktor Ambrus, et al.
Proceedings of the National Academy of Sciences (2020) Vol. 117, Iss. 52, pp. 33254-33262
Open Access | Times Cited: 286
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
Liquid network connectivity regulates the stability and composition of biomolecular condensates with many components
Jorge R. Espinosa, Jerelle A. Joseph, Ignacio Sanchez‐Burgos, et al.
Proceedings of the National Academy of Sciences (2020) Vol. 117, Iss. 24, pp. 13238-13247
Open Access | Times Cited: 243
Modulating biomolecular condensates: a novel approach to drug discovery
Diana M. Mitrea, Matthäus Mittasch, Beatriz Ferreira Gomes, et al.
Nature Reviews Drug Discovery (2022) Vol. 21, Iss. 11, pp. 841-862
Open Access | Times Cited: 236
Improved coarse‐grained model for studying sequence dependent phase separation of disordered proteins
Roshan Mammen Regy, J Thompson, Young C. Kim, et al.
Protein Science (2021) Vol. 30, Iss. 7, pp. 1371-1379
Open Access | Times Cited: 183
Learning the molecular grammar of protein condensates from sequence determinants and embeddings
Kadi L. Saar, Alexey S. Morgunov, Runzhang Qi, et al.
Proceedings of the National Academy of Sciences (2021) Vol. 118, Iss. 15
Open Access | Times Cited: 170
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: 125
Conformational Expansion of Tau in Condensates Promotes Irreversible Aggregation
Jitao Wen, Liu Hong, Georg Krainer, et al.
Journal of the American Chemical Society (2021) Vol. 143, Iss. 33, pp. 13056-13064
Open Access | Times Cited: 123
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: 116
Modulating α-Synuclein Liquid–Liquid Phase Separation
Ajay Singh Sawner, Soumik Ray, Preeti Yadav, et al.
Biochemistry (2021) Vol. 60, Iss. 48, pp. 3676-3696
Closed Access | Times Cited: 114
A multi-step nucleation process determines the kinetics of prion-like domain phase separation
Erik Martin, Tyler S. Harmon, Jesse B. Hopkins, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 110
Engineering synthetic biomolecular condensates
Yifan Dai, Lingchong You, Ashutosh Chilkoti
Nature Reviews Bioengineering (2023) Vol. 1, Iss. 7, pp. 466-480
Open Access | Times Cited: 101
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
Liquid-liquid phase separation of RBGD2/4 is required for heat stress resistance in Arabidopsis
Shaobo Zhu, Jinge Gu, Juanjuan Yao, et al.
Developmental Cell (2022) Vol. 57, Iss. 5, pp. 583-597.e6
Open Access | Times Cited: 93
Amyloid formation as a protein phase transition
Thomas C. T. Michaels, Daoyuan Qian, Anđela Šarić, et al.
Nature Reviews Physics (2023) Vol. 5, Iss. 7, pp. 379-397
Closed Access | Times Cited: 83
Protein condensation diseases: therapeutic opportunities
Michele Vendruscolo, Mónika Fuxreiter
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 81
Biomolecular condensates formed by designer minimalistic peptides
Avigail Baruch Leshem, Sian Sloan‐Dennison, Tlalit Massarano, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 79
Intermolecular interactions underlie protein/peptide phase separation irrespective of sequence and structure at crowded milieu
Manisha Poudyal, Komal Patel, Laxmikant Gadhe, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 78
Molecular and environmental determinants of biomolecular condensate formation
José A. Villegas, Meta Heidenreich, Emmanuel D. Levy
Nature Chemical Biology (2022) Vol. 18, Iss. 12, pp. 1319-1329
Closed Access | Times Cited: 77
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: 76
The liquid-to-solid transition of FUS is promoted by the condensate surface
Yi Shen, Anqi Chen, Wenyun Wang, et al.
Proceedings of the National Academy of Sciences (2023) Vol. 120, Iss. 33
Open Access | Times Cited: 75
Spatiotemporal modulations in heterotypic condensates of prion and α-synuclein control phase transitions and amyloid conversion
Aishwarya Agarwal, Lisha Arora, K. Sandeep, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 71
A New Phase of Networking: The Molecular Composition and Regulatory Dynamics of Mammalian Stress Granules
Seán Millar, Jie Huang, Karl J. Schreiber, et al.
Chemical Reviews (2023) Vol. 123, Iss. 14, pp. 9036-9064
Open Access | Times Cited: 63
Spontaneous nucleation and fast aggregate-dependent proliferation of α-synuclein aggregates within liquid condensates at neutral pH
Samuel Dada, Maarten C. Hardenberg, Zenon Toprakcioglu, et al.
Proceedings of the National Academy of Sciences (2023) Vol. 120, Iss. 9
Open Access | Times Cited: 58
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