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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:

Phase Separation and Neurodegenerative Diseases: A Disturbance in the Force
Aurélie Zbinden, Manuela Pérez‐Berlanga, Pierre De Rossi, et al.
Developmental Cell (2020) Vol. 55, Iss. 1, pp. 45-68
Open Access | Times Cited: 372

Showing 1-25 of 372 citing articles:

Liquid–liquid phase separation in human health and diseases
Bin Wang, Lei Zhang, Tong Dai, et al.
Signal Transduction and Targeted Therapy (2021) Vol. 6, Iss. 1
Open Access | Times Cited: 437
Phase separation of FSP1 promotes ferroptosis
Toshitaka Nakamura, Clara Hipp, André Mourão, et al.
Nature (2023) Vol. 619, Iss. 7969, pp. 371-377
Open Access | Times Cited: 165
Amyloid-type Protein Aggregation and Prion-like Properties of Amyloids
Dieter Willbold, Birgit Strodel, Gunnar F. Schröder, et al.
Chemical Reviews (2021) Vol. 121, Iss. 13, pp. 8285-8307
Open Access | Times Cited: 152
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: 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: 140
Stress granules, RNA-binding proteins and polyglutamine diseases: too much aggregation?
Adriana Marcelo, Rebekah Koppenol, Luís Pereira de Almeida, et al.
Cell Death and Disease (2021) Vol. 12, Iss. 6
Open Access | Times Cited: 132
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: 131
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: 130
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: 120
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: 113
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: 111
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: 111
Liquid–Liquid Phase Separation in Chromatin
Karsten Rippe
Cold Spring Harbor Perspectives in Biology (2021) Vol. 14, Iss. 2, pp. a040683-a040683
Open Access | Times Cited: 108
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
The interface of condensates of the hnRNPA1 low-complexity domain promotes formation of amyloid fibrils
Miriam Linsenmeier, Lenka Faltova, Chiara Morelli, et al.
Nature Chemistry (2023) Vol. 15, Iss. 10, pp. 1340-1349
Open Access | Times Cited: 75
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: 64
Stress granules plug and stabilize damaged endolysosomal membranes
Claudio Bussi, Agustín Mangiarotti, Christian Vanhille-Campos, et al.
Nature (2023) Vol. 623, Iss. 7989, pp. 1062-1069
Open Access | Times Cited: 50
Interaction modules that impart specificity to disordered protein
Kateřina Čermáková, H. Courtney Hodges
Trends in Biochemical Sciences (2023) Vol. 48, Iss. 5, pp. 477-490
Open Access | Times Cited: 45
Loss of TDP‐43 oligomerization or RNA binding elicits distinct aggregation patterns
Manuela Pérez‐Berlanga, Vera I. Wiersma, Aurélie Zbinden, et al.
The EMBO Journal (2023) Vol. 42, Iss. 17
Open Access | Times Cited: 43
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: 23
Fundamental Aspects of Phase-Separated Biomolecular Condensates
Huan‐Xiang Zhou, Divya Kota, Sanbo Qin, et al.
Chemical Reviews (2024) Vol. 124, Iss. 13, pp. 8550-8595
Closed Access | Times Cited: 22
The six brain‐specific TAU isoforms and their role in Alzheimer's disease and related neurodegenerative dementia syndromes
Sarah Buchholz, Hans Zempel
Alzheimer s & Dementia (2024) Vol. 20, Iss. 5, pp. 3606-3628
Open Access | Times Cited: 19
The role of biomolecular condensates in protein aggregation
Brent S. Visser, Wojciech P. Lipiński, Evan Spruijt
Nature Reviews Chemistry (2024) Vol. 8, Iss. 9, pp. 686-700
Closed Access | Times Cited: 19
High-throughput and proteome-wide discovery of endogenous biomolecular condensates
Pengjie Li, Peng Chen, Fukang Qi, et al.
Nature Chemistry (2024) Vol. 16, Iss. 7, pp. 1101-1112
Closed Access | Times Cited: 15
Structured protein domains enter the spotlight: modulators of biomolecular condensate form and function
Nathaniel Hess, Jerelle A. Joseph
Trends in Biochemical Sciences (2025)
Open Access | Times Cited: 3
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