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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 of the microtubule-binding repeats of the Alzheimer-related protein Tau
Susmitha Ambadipudi, Jacek Biernat, Dietmar Riedel, et al.
Nature Communications (2017) Vol. 8, Iss. 1
Open Access | Times Cited: 708

Showing 26-50 of 708 citing articles:

Theories for Sequence-Dependent Phase Behaviors of Biomolecular Condensates
Yi‐Hsuan Lin, Julie D. Forman‐Kay, Hue Sun Chan
Biochemistry (2018) Vol. 57, Iss. 17, pp. 2499-2508
Closed Access | Times Cited: 224
Lysine/RNA-interactions drive and regulate biomolecular condensation
Tina Ukmar, Saskia Hutten, Matthew P. Grieshop, et al.
Nature Communications (2019) Vol. 10, Iss. 1
Open Access | Times Cited: 221
Matter over mind: Liquid phase separation and neurodegeneration
Shana Elbaum‐Garfinkle
Journal of Biological Chemistry (2019) Vol. 294, Iss. 18, pp. 7160-7168
Open Access | Times Cited: 218
Formation of biological condensates via phase separation: Characteristics, analytical methods, and physiological implications
Zhe Feng, Xudong Chen, Xiandeng Wu, et al.
Journal of Biological Chemistry (2019) Vol. 294, Iss. 40, pp. 14823-14835
Open Access | Times Cited: 212
Liquid–liquid phase separation of tau protein: The crucial role of electrostatic interactions
Solomiia Boyko, Xu Qi, Tien‐Hao Chen, et al.
Journal of Biological Chemistry (2019) Vol. 294, Iss. 29, pp. 11054-11059
Open Access | Times Cited: 209
Mechanisms of Cell-to-Cell Transmission of Pathological Tau
Garrett S. Gibbons, Virginia M.‐Y. Lee, John Q. Trojanowski
JAMA Neurology (2018) Vol. 76, Iss. 1, pp. 101-101
Open Access | Times Cited: 200
Microtubules gate tau condensation to spatially regulate microtubule functions
Ruensern Tan, Aileen J. Lam, Tracy Tan, et al.
Nature Cell Biology (2019) Vol. 21, Iss. 9, pp. 1078-1085
Open Access | Times Cited: 191
Bridging biophysics and neurology: aberrant phase transitions in neurodegenerative disease
Natalia B. Nedelsky, J. Paul Taylor
Nature Reviews Neurology (2019) Vol. 15, Iss. 5, pp. 272-286
Closed Access | Times Cited: 187
Humanization of the entire murine Mapt gene provides a murine model of pathological human tau propagation
Takashi Saito, Naomi Mihira, Yukio Matsuba, et al.
Journal of Biological Chemistry (2019) Vol. 294, Iss. 34, pp. 12754-12765
Open Access | Times Cited: 183
Tau aggregates are RNA-protein assemblies that mislocalize multiple nuclear speckle components
Evan Lester, Felicia K. Ooi, Nadine Bakkar, et al.
Neuron (2021) Vol. 109, Iss. 10, pp. 1675-1691.e9
Open Access | Times Cited: 167
Liquid–Liquid Phase Separation by Intrinsically Disordered Protein Regions of Viruses: Roles in Viral Life Cycle and Control of Virus–Host Interactions
Stefania Brocca, Rita Grandori, Sonia Longhi, et al.
International Journal of Molecular Sciences (2020) Vol. 21, Iss. 23, pp. 9045-9045
Open Access | Times Cited: 157
Cell‐Inspired All‐Aqueous Microfluidics: From Intracellular Liquid–Liquid Phase Separation toward Advanced Biomaterials
Qingming Ma, Yang Song, Wentao Sun, et al.
Advanced Science (2020) Vol. 7, Iss. 7
Open Access | Times Cited: 155
Tau-Mediated Disruption of the Spliceosome Triggers Cryptic RNA Splicing and Neurodegeneration in Alzheimer’s Disease
Yi‐Chen Hsieh, Caiwei Guo, Hari Krishna Yalamanchili, et al.
Cell Reports (2019) Vol. 29, Iss. 2, pp. 301-316.e10
Open Access | Times Cited: 154
Dehydration entropy drives liquid-liquid phase separation by molecular crowding
Sohee Park, Ryan P. Barnes, Yanxian Lin, et al.
Communications Chemistry (2020) Vol. 3, Iss. 1
Open Access | Times Cited: 153
Phase separation in immune signalling
Qian Xiao, Ceara K. McAtee, Xiaolei Su
Nature reviews. Immunology (2021) Vol. 22, Iss. 3, pp. 188-199
Open Access | Times Cited: 150
Prediction of liquid–liquid phase separating proteins using machine learning
Xiaoquan Chu, Tanlin Sun, Qian Li, et al.
BMC Bioinformatics (2022) Vol. 23, Iss. 1
Open Access | Times Cited: 146
It’s not just a phase: function and characteristics of RNA-binding proteins in phase separation
Hannah J. Wiedner, Jimena Giudice
Nature Structural & Molecular Biology (2021) Vol. 28, Iss. 6, pp. 465-473
Open Access | Times Cited: 142
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
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
Alpha-synuclein research: defining strategic moves in the battle against Parkinson’s disease
Luís M. A. Oliveira, Thomas Gasser, Robert H. Edwards, et al.
npj Parkinson s Disease (2021) Vol. 7, Iss. 1
Open Access | Times Cited: 115
Revisiting the grammar of Tau aggregation and pathology formation: how new insights from brain pathology are shaping how we study and target Tauopathies
Galina Limorenko, Hilal A. Lashuel
Chemical Society Reviews (2021) Vol. 51, Iss. 2, pp. 513-565
Open Access | Times Cited: 115
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
Tau liquid–liquid phase separation in neurodegenerative diseases
Solomiia Boyko, Witold K. Surewicz
Trends in Cell Biology (2022) Vol. 32, Iss. 7, pp. 611-623
Open Access | Times Cited: 113
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
Molecular interactions contributing to FUS SYGQ LC-RGG phase separation and co-partitioning with RNA polymerase II heptads
Anastasia C. Murthy, Wai Shing Tang, Nina Jovic, et al.
Nature Structural & Molecular Biology (2021) Vol. 28, Iss. 11, pp. 923-935
Open Access | Times Cited: 109

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