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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:

How do intrinsically disordered protein regions encode a driving force for liquid–liquid phase separation?
Wade M. Borcherds, Anne Bremer, Madeleine B. Borgia, et al.
Current Opinion in Structural Biology (2020) Vol. 67, pp. 41-50
Open Access | Times Cited: 247

Showing 1-25 of 247 citing articles:

AlphaFold2 and the future of structural biology
Patrick Cramer
Nature Structural & Molecular Biology (2021) Vol. 28, Iss. 9, pp. 704-705
Closed Access | Times Cited: 299
On the role of phase separation in the biogenesis of membraneless compartments
Andrea Musacchio
The EMBO Journal (2022) Vol. 41, Iss. 5
Open Access | Times Cited: 158
Liquid–liquid phase separation in tumor biology
Xuhui Tong, Rong Tang, Jin Xu, et al.
Signal Transduction and Targeted Therapy (2022) Vol. 7, Iss. 1
Open Access | Times Cited: 136
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: 117
ER-phagy: mechanisms, regulation, and diseases connected to the lysosomal clearance of the endoplasmic reticulum
Fulvio Reggiori, Maurizio Molinari
Physiological Reviews (2022) Vol. 102, Iss. 3, pp. 1393-1448
Open Access | Times Cited: 111
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: 82
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: 77
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: 77
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: 56
Local environment in biomolecular condensates modulates enzymatic activity across length scales
Marcos Gil-García, Ana I. Benítez‐Mateos, M Papp, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 30
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
Precise prediction of phase-separation key residues by machine learning
Jun Sun, Jiale Qu, Cai Zhao, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 22
Disordered regions of condensate-promoting proteins have distinct molecular signatures associated with cellular function
Shubham Vashishtha, Benjamin R. Sabari
Journal of Molecular Biology (2025), pp. 168953-168953
Closed Access | Times Cited: 3
Regulation of liquid–liquid phase separation with focus on post-translational modifications
Yun-Yi Luo, Jun Wu, Yanmei Li
Chemical Communications (2021) Vol. 57, Iss. 98, pp. 13275-13287
Closed Access | Times Cited: 85
Biomolecular condensates at sites of DNA damage: More than just a phase
Vincent Spegg, Matthias Altmeyer
DNA repair (2021) Vol. 106, pp. 103179-103179
Open Access | Times Cited: 78
Conformational ensembles of intrinsically disordered proteins and flexible multidomain proteins
F. Emil Thomasen, Kresten Lindorff‐Larsen
Biochemical Society Transactions (2022) Vol. 50, Iss. 1, pp. 541-554
Open Access | Times Cited: 69
The intrinsically disorderly story of Ki-67
Lucy Remnant, Natalia Y. Kochanova, Caitlin Reid, et al.
Open Biology (2021) Vol. 11, Iss. 8
Open Access | Times Cited: 68
Histone H2B.8 compacts flowering plant sperm through chromatin phase separation
Toby Buttress, Shengbo He, Liang Wang, et al.
Nature (2022) Vol. 611, Iss. 7936, pp. 614-622
Open Access | Times Cited: 54
Implementation of residue-level coarse-grained models in GENESIS for large-scale molecular dynamics simulations
Cheng Tan, Jaewoon Jung, Chigusa Kobayashi, et al.
PLoS Computational Biology (2022) Vol. 18, Iss. 4, pp. e1009578-e1009578
Open Access | Times Cited: 53
Multivalent interactions between molecular components involved in fast endophilin mediated endocytosis drive protein phase separation
Samsuzzoha Mondal, Karthik Narayan, Samuel Botterbusch, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 53
Biological soft matter: intrinsically disordered proteins in liquid–liquid phase separation and biomolecular condensates
Alexander V. Fonin, Iuliia A. Antifeeva, Irina М. Kuznetsova, et al.
Essays in Biochemistry (2022) Vol. 66, Iss. 7, pp. 831-847
Closed Access | Times Cited: 44
Direct Observation of “Elongated” Conformational States in α‐Synuclein upon Liquid‐Liquid Phase Separation
Daniele Ubbiali, Marta Fratini, Lolita Piersimoni, et al.
Angewandte Chemie International Edition (2022) Vol. 61, Iss. 46
Open Access | Times Cited: 43
Systematic identification of conditionally folded intrinsically disordered regions by AlphaFold2
T. Reid Alderson, Iva Pritišanac, Đesika Kolarić, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 41
IDPConformerGenerator: A Flexible Software Suite for Sampling the Conformational Space of Disordered Protein States
João M. C. Teixeira, Zi Hao Liu, Ashley Namini, et al.
The Journal of Physical Chemistry A (2022) Vol. 126, Iss. 35, pp. 5985-6003
Open Access | Times Cited: 39
Biomolecular condensates modulate membrane lipid packing and hydration
Agustín Mangiarotti, Macarena Siri, Nicky W. Tam, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 39
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