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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:

Liquid–Liquid Phase Separation in Disease
Simon Alberti, Dorothee Dormann
Annual Review of Genetics (2019) Vol. 53, Iss. 1, pp. 171-194
Open Access | Times Cited: 772

Showing 26-50 of 772 citing articles:

Unraveling Molecular Interactions in Liquid–Liquid Phase Separation of Disordered Proteins by Atomistic Simulations
Matteo Paloni, Rémy Bailly, Luca Ciandrini, et al.
The Journal of Physical Chemistry B (2020) Vol. 124, Iss. 41, pp. 9009-9016
Open Access | Times Cited: 141
Conformational Dynamics of Intrinsically Disordered Proteins Regulate Biomolecular Condensate Chemistry
Anton Abyzov, Martin Blackledge, Markus Zweckstetter
Chemical Reviews (2022) Vol. 122, Iss. 6, pp. 6719-6748
Open Access | Times Cited: 137
CCT2 is an aggrephagy receptor for clearance of solid protein aggregates
Xinyu Ma, Caijing Lu, Yuting Chen, et al.
Cell (2022) Vol. 185, Iss. 8, pp. 1325-1345.e22
Open Access | Times Cited: 129
Disease‐linked TDP‐43 hyperphosphorylation suppresses TDP‐43 condensation and aggregation
Lara A. Gruijs da Silva, Francesca Simonetti, Saskia Hutten, et al.
The EMBO Journal (2022) Vol. 41, Iss. 8
Open Access | Times Cited: 128
RNA-induced liquid phase separation of SARS-CoV-2 nucleocapsid protein facilitates NF-κB hyper-activation and inflammation
Yaoxing Wu, Ling Ma, Sihui Cai, et al.
Signal Transduction and Targeted Therapy (2021) Vol. 6, Iss. 1
Open Access | Times Cited: 127
Generic nature of the condensed states of proteins
Mónika Fuxreiter, Michele Vendruscolo
Nature Cell Biology (2021) Vol. 23, Iss. 6, pp. 587-594
Closed Access | Times Cited: 126
Systematic identification of conditionally folded intrinsically disordered regions by AlphaFold2
T. Reid Alderson, Iva Pritišanac, Đesika Kolarić, et al.
Proceedings of the National Academy of Sciences (2023) Vol. 120, Iss. 44
Open Access | Times Cited: 122
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
The key role of solvent in condensation: Mapping water in liquid-liquid phase-separated FUS
Jonas Ahlers, Ellen M. Adams, Verian Bader, et al.
Biophysical Journal (2021) Vol. 120, Iss. 7, pp. 1266-1275
Open Access | Times Cited: 110
Targeting androgen receptor phase separation to overcome antiandrogen resistance
Jingjing Xie, Hao He, Wenna Kong, et al.
Nature Chemical Biology (2022) Vol. 18, Iss. 12, pp. 1341-1350
Closed Access | Times Cited: 95
The material properties of a bacterial-derived biomolecular condensate tune biological function in natural and synthetic systems
Keren Lasker, Steven Boeynaems, Vinson Lam, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 86
Macromolecular condensation buffers intracellular water potential
Joseph L. Watson, Estere Seinkmane, Christine T. Styles, et al.
Nature (2023) Vol. 623, Iss. 7988, pp. 842-852
Open Access | Times Cited: 86
Expanding the molecular language of protein liquid–liquid phase separation
Shiv Rekhi, Cristobal Garcia Garcia, Mayur Barai, et al.
Nature Chemistry (2024) Vol. 16, Iss. 7, pp. 1113-1124
Open Access | Times Cited: 85
Liquid-liquid Phase Separation of α-Synuclein: A New Mechanistic Insight for α-Synuclein Aggregation Associated with Parkinson's Disease Pathogenesis
Semanti Mukherjee, Arunima Sakunthala, Laxmikant Gadhe, et al.
Journal of Molecular Biology (2022) Vol. 435, Iss. 1, pp. 167713-167713
Open 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
LncRNAs in human cancers: signal from noise
Sara Adnane, Alessandro Marino, Eleonora Leucci
Trends in Cell Biology (2022) Vol. 32, Iss. 7, pp. 565-573
Open 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
Game changers in science and technology - now and beyond
Ulrich A. K. Betz, Loukik Arora, R.A. Assal, et al.
Technological Forecasting and Social Change (2023) Vol. 193, pp. 122588-122588
Open Access | Times Cited: 74
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
Mass photometric detection and quantification of nanoscale α-synuclein phase separation
Soumik Ray, Thomas O. Mason, Lars Boyens‐Thiele, et al.
Nature Chemistry (2023) Vol. 15, Iss. 9, pp. 1306-1316
Open Access | Times Cited: 68
Cellular functions of eukaryotic RNA helicases and their links to human diseases
Katherine E. Bohnsack, Soon Yi, Sarah Venus, et al.
Nature Reviews Molecular Cell Biology (2023) Vol. 24, Iss. 10, pp. 749-769
Closed Access | Times Cited: 67
Evidence for widespread cytoplasmic structuring into mesoscale condensates
Felix C. Keber, Thao Nguyen, Andrea Mariossi, et al.
Nature Cell Biology (2024) Vol. 26, Iss. 3, pp. 346-352
Closed Access | Times Cited: 36
Macromolecular Crowding, Phase Separation, and Homeostasis in the Orchestration of Bacterial Cellular Functions
Begoña Monterroso, William Margolin, Arnold J. Boersma, et al.
Chemical Reviews (2024) Vol. 124, Iss. 4, pp. 1899-1949
Open Access | Times Cited: 34
Protein misfolding and amyloid nucleation through liquid–liquid phase separation
S. Mukherjee, Manisha Poudyal, K. Dave, et al.
Chemical Society Reviews (2024) Vol. 53, Iss. 10, pp. 4976-5013
Closed Access | Times Cited: 25

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