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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:

hnRNPDL Phase Separation Is Regulated by Alternative Splicing and Disease-Causing Mutations Accelerate Its Aggregation
Cristina Batlle, Peiguo Yang, Maura Coughlin, et al.
Cell Reports (2020) Vol. 30, Iss. 4, pp. 1117-1128.e5
Open Access | Times Cited: 63

Showing 1-25 of 63 citing articles:

Phase Separation as a Missing Mechanism for Interpretation of Disease Mutations
Brian Tsang, Iva Pritišanac, Stephen W. Scherer, et al.
Cell (2020) Vol. 183, Iss. 7, pp. 1742-1756
Open Access | Times Cited: 226
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
Protein condensation diseases: therapeutic opportunities
Michele Vendruscolo, Mónika Fuxreiter
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 81
Relevance of Electrostatic Charges in Compactness, Aggregation, and Phase Separation of Intrinsically Disordered Proteins
Greta Bianchi, Sonia Longhi, Rita Grandori, et al.
International Journal of Molecular Sciences (2020) Vol. 21, Iss. 17, pp. 6208-6208
Open Access | Times Cited: 96
Genetic variation associated with condensate dysregulation in disease
Salman F. Banani, Lena K. Afeyan, Susana Wilson Hawken, et al.
Developmental Cell (2022) Vol. 57, Iss. 14, pp. 1776-1788.e8
Open Access | Times Cited: 64
Tau interactome and RNA binding proteins in neurodegenerative diseases
Tomas Kavanagh, Aditi Halder, Eleanor Drummond
Molecular Neurodegeneration (2022) Vol. 17, Iss. 1
Open Access | Times Cited: 62
PhaSepDB in 2022: annotating phase separation-related proteins with droplet states, co-phase separation partners and other experimental information
Chao Hou, Xinxin Wang, Haotai Xie, et al.
Nucleic Acids Research (2022) Vol. 51, Iss. D1, pp. D460-D465
Open Access | Times Cited: 46
The function of alternative splicing in the proteome: rewiring protein interactomes to put old functions into new contexts
Peter Kjer-Hansen, Robert J. Weatheritt
Nature Structural & Molecular Biology (2023) Vol. 30, Iss. 12, pp. 1844-1856
Closed Access | Times Cited: 28
Splicing regulation through biomolecular condensates and membraneless organelles
Jimena Giudice, Hao Jiang
Nature Reviews Molecular Cell Biology (2024) Vol. 25, Iss. 9, pp. 683-700
Closed Access | Times Cited: 17
CIDE proteins and their regulatory mechanisms in lipid droplet fusion and growth
Li Xu, Li-Zhen Li, Lingzhi Wu, et al.
FEBS Letters (2024) Vol. 598, Iss. 10, pp. 1154-1169
Open Access | Times Cited: 12
Interplay between posttranslational modifications and liquid‒liquid phase separation in tumors
Xiaojun Yan, Meng Zhang, Donglai Wang
Cancer Letters (2024) Vol. 584, pp. 216614-216614
Closed Access | Times Cited: 11
Mis-splicing of a neuronal microexon promotes CPEB4 aggregation in ASD
Carla Garcia‐Cabau, Anna Bartomeu, Giulio Tesei, et al.
Nature (2024) Vol. 637, Iss. 8045, pp. 496-503
Open Access | Times Cited: 11
Regulation of biomolecular condensate dynamics by signaling
Carla Garcia‐Cabau, Xavier Salvatella
Current Opinion in Cell Biology (2021) Vol. 69, pp. 111-119
Closed Access | Times Cited: 50
Heterozygous frameshift variants in HNRNPA2B1 cause early-onset oculopharyngeal muscular dystrophy
Hong Joo Kim, Payam Mohassel, Sandra Donkervoort, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 32
Cryo-EM structure of hnRNPDL-2 fibrils, a functional amyloid associated with limb-girdle muscular dystrophy D3
Javier García‐Pardo, Andrea Bartolomé-Nafría, Antonio Chaves-Sanjuán, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 21
Role of RNA Binding Proteins with prion-like domains in muscle and neuromuscular diseases
Gina Picchiarelli, Luc Dupuis
Cell Stress (2020) Vol. 4, Iss. 4, pp. 76-91
Open Access | Times Cited: 48
Investigating the ACE2 polymorphisms in COVID‐19 susceptibility: An in silico analysis
Nasser Pouladi, Sepehr Abdolahi
Molecular Genetics & Genomic Medicine (2021) Vol. 9, Iss. 6
Open Access | Times Cited: 38
A gel-like condensation of Cidec generates lipid-permeable plates for lipid droplet fusion
Xuchao Lyu, Jia Wang, Jianqin Wang, et al.
Developmental Cell (2021) Vol. 56, Iss. 18, pp. 2592-2606.e7
Open Access | Times Cited: 36
The return of the rings: Evolutionary convergence of aromatic residues in the intrinsically disordered regions of RNA‐binding proteins for liquid–liquid phase separation
Wen‐Lin Ho, Jie‐rong Huang
Protein Science (2022) Vol. 31, Iss. 5
Open Access | Times Cited: 18
Biomolecular Condensation: A New Phase in Cancer Research
Anupam K. Chakravarty, Daniel J. McGrail, Thomas M. Lozanoski, et al.
Cancer Discovery (2022) Vol. 12, Iss. 9, pp. 2031-2043
Open Access | Times Cited: 17
Kinetic stabilization of translation-repression condensates by a neuron-specific microexon
Carla Garcia‐Cabau, Anna Bartomeu, Giulio Tesei, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 10
Viral amyloids: New opportunities for antiviral therapeutic strategies
Frank Gondelaud, Pierre‐Yves Lozach, Sonia Longhi
Current Opinion in Structural Biology (2023) Vol. 83, pp. 102706-102706
Open Access | Times Cited: 10
Cryo-EM structures of functional and pathological amyloid ribonucleoprotein assemblies
Javier García‐Pardo, Salvador Ventura
Trends in Biochemical Sciences (2023) Vol. 49, Iss. 2, pp. 119-133
Open Access | Times Cited: 10
Virus-like particles of retroviral origin in protein aggregation and neurodegenerative diseases
Serena Carra, Balázs Fábián, Hamed Taghavi, et al.
Molecular Aspects of Medicine (2025) Vol. 103, pp. 101369-101369
Open Access
AMYCO: evaluation of mutational impact on prion-like proteins aggregation propensity
Valentín Iglesias, Oscar Conchillo‐Solé, Cristina Batlle, et al.
BMC Bioinformatics (2019) Vol. 20, Iss. 1
Open Access | Times Cited: 28
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