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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:

Intrinsically disordered proteins in crowded milieu: when chaos prevails within the cellular gumbo
Alexander V. Fonin, April L. Darling, Irina М. Kuznetsova, et al.
Cellular and Molecular Life Sciences (2018) Vol. 75, Iss. 21, pp. 3907-3929
Open Access | Times Cited: 93

Showing 1-25 of 93 citing articles:

Liquid–Liquid Phase Separation in Crowded Environments
Alain A.M. André, Evan Spruijt
International Journal of Molecular Sciences (2020) Vol. 21, Iss. 16, pp. 5908-5908
Open Access | Times Cited: 242
The role of liquid–liquid phase separation in regulating enzyme activity
Brian G. O’Flynn, Tanja Mittag
Current Opinion in Cell Biology (2021) Vol. 69, pp. 70-79
Open Access | Times Cited: 144
NMR Provides Unique Insight into the Functional Dynamics and Interactions of Intrinsically Disordered Proteins
Aldo R. Camacho‐Zarco, Vincent Schnapka, Serafima Guseva, et al.
Chemical Reviews (2022) Vol. 122, Iss. 10, pp. 9331-9356
Open Access | Times Cited: 95
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: 37
Bridging protein structure, dynamics, and function using hydrogen/deuterium‐exchange mass spectrometry
Edgar A. Hodge, Mark A. Benhaim, Kelly K. Lee
Protein Science (2019) Vol. 29, Iss. 4, pp. 843-855
Open Access | Times Cited: 104
OASL phase condensation induces amyloid-like fibrillation of RIPK3 to promote virus-induced necroptosis
Shin-Ae Lee, Lin-Chun Chang, WooRam Jung, et al.
Nature Cell Biology (2023) Vol. 25, Iss. 1, pp. 92-107
Open Access | Times Cited: 32
Protein Disorder in Plant Stress Adaptation: From Late Embryogenesis Abundant to Other Intrinsically Disordered Proteins
An‐Shan Hsiao
International Journal of Molecular Sciences (2024) Vol. 25, Iss. 2, pp. 1178-1178
Open Access | Times Cited: 11
Features of molecular recognition of intrinsically disordered proteins via coupled folding and binding
Jing Yang, Meng Gao, J. Xiong, et al.
Protein Science (2019) Vol. 28, Iss. 11, pp. 1952-1965
Open Access | Times Cited: 76
The more the merrier: effects of macromolecular crowding on the structure and dynamics of biological membranes
Maryna Löwe, Milara Kalacheva, Arnold J. Boersma, et al.
FEBS Journal (2020) Vol. 287, Iss. 23, pp. 5039-5067
Open Access | Times Cited: 69
Fundamental Challenges and Outlook in Simulating Liquid–Liquid Phase Separation of Intrinsically Disordered Proteins
Khandekar Jishan Bari, Dube Dheeraj Prakashchand
The Journal of Physical Chemistry Letters (2021) Vol. 12, Iss. 6, pp. 1644-1656
Closed Access | Times Cited: 46
Aberrant liquid-liquid phase separation and amyloid aggregation of proteins related to neurodegenerative diseases
Azeem Ahmad, Vladimir N. Uversky, Rizwan Hasan Khan
International Journal of Biological Macromolecules (2022) Vol. 220, pp. 703-720
Closed Access | Times Cited: 36
Single Molecule FRET: A Powerful Tool to Study Intrinsically Disordered Proteins
Sharonda LeBlanc, Prakash Kulkarni, Keith Weninger
Biomolecules (2018) Vol. 8, Iss. 4, pp. 140-140
Open Access | Times Cited: 54
Structure, Activity, and Dynamics of Human Serum Albumin in a Crowded Pluronic F127 Hydrogel
Atanu Nandy, Subhajit Chakraborty, Somen Nandi, et al.
The Journal of Physical Chemistry B (2019) Vol. 123, Iss. 16, pp. 3397-3408
Closed Access | Times Cited: 47
Modeling Crowded Environment in Molecular Simulations
Natalia Ostrowska, Michael Feig, Joanna Trylska
Frontiers in Molecular Biosciences (2019) Vol. 6
Open Access | Times Cited: 44
Proteasome Activation to Combat Proteotoxicity
Corey L. Jones, Jetze J. Tepe
Molecules (2019) Vol. 24, Iss. 15, pp. 2841-2841
Open Access | Times Cited: 40
Influence of size and charge of unstructured polypeptides on pharmacokinetics and biodistribution of targeted fusion proteins
Fabian Brandl, Hannes Merten, Martina Zimmermann, et al.
Journal of Controlled Release (2019) Vol. 307, pp. 379-392
Closed Access | Times Cited: 35
Crowding Effects on the Structure and Dynamics of the Intrinsically Disordered Nuclear Chromatin Protein NUPR1
Alessio Bonucci, Martina Palomino‐Schätzlein, Paula Malo de Molina, et al.
Frontiers in Molecular Biosciences (2021) Vol. 8
Open Access | Times Cited: 26
Unveiling induced folding of intrinsically disordered proteins – Protein engineering, frustration and emerging themes
Francesca Malagrinò, Awa Diop, Livia Pagano, et al.
Current Opinion in Structural Biology (2021) Vol. 72, pp. 153-160
Open Access | Times Cited: 25
Role of the Psi Packaging Signal and Dimerization Initiation Sequence in the Organization of Rous Sarcoma Virus Gag-gRNA Co-Condensates
Gregory S. Lambert, Rebecca J. Kaddis Maldonado, Leslie J. Parent
Viruses (2025) Vol. 17, Iss. 1, pp. 97-97
Open Access
Liquid-liquid phase separation of intrinsically disordered proteins: Effect of osmolytes and crowders
G Priyanka, E Jawahar Raj, N. Prakash Prabhu
Progress in molecular biology and translational science (2025), pp. 249-269
Closed Access
A Deep Learning Method for Predicting Interactions for Intrinsically Disordered Regions of Proteins
Kartik Majila, Varun Ullanat, Shruthi Viswanath
(2025)
Closed Access
Targeting Proteostasis Pathways for Cancer Therapy
Xiaofeng Dai, Ruohan Lyu, Guanqun Ge
Journal of Pharmaceutical Analysis (2025), pp. 101287-101287
Open Access
Intrinsic Disorder in Protein Interaction Networks Linking Cancer with Metabolic Diseases
Veda Naga Priya Vangala, Vladimir N. Uversky
Computational Biology and Chemistry (2025) Vol. 118, pp. 108493-108493
Closed Access
Intrinsic Disorder and Phase Separation Coordinate Exocytosis, Motility, and Chromatin Remodeling in the Human Acrosomal Proteome
Shivam Shukla, Sean S. Lastorka, Vladimir N. Uversky
Proteomes (2025) Vol. 13, Iss. 2, pp. 16-16
Open Access
The Functionally Important N-Terminal Half of Fission Yeast Mid1p Anillin Is Intrinsically Disordered and Undergoes Phase Separation
Moon Chatterjee, Thomas D. Pollard
Biochemistry (2019) Vol. 58, Iss. 27, pp. 3031-3041
Open Access | Times Cited: 27
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