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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:

CD-CODE: crowdsourcing condensate database and encyclopedia
Nadia Rostam, Soumyadeep Ghosh, Chi Fung Willis Chow, et al.
Nature Methods (2023) Vol. 20, Iss. 5, pp. 673-676
Open Access | Times Cited: 33

Showing 1-25 of 33 citing articles:

Conformational ensembles of the human intrinsically disordered proteome
Giulio Tesei, Anna Ida Trolle, Nicolas Jonsson, et al.
Nature (2024) Vol. 626, Iss. 8000, pp. 897-904
Closed Access | Times Cited: 134
RNA granules: functional compartments or incidental condensates?
Andrea Putnam, Laura Thomas, Géraldine Seydoux
Genes & Development (2023) Vol. 37, Iss. 9-10, pp. 354-376
Open Access | Times Cited: 57
MolPhase, an advanced prediction algorithm for protein phase separation
Qiyu Liang, Nana Peng, Yi Xie, et al.
The EMBO Journal (2024) Vol. 43, Iss. 9, pp. 1898-1918
Open Access | Times Cited: 19
Protein codes promote selective subcellular compartmentalization
Henry R. Kilgore, Itamar Chinn, Peter G. Mikhael, et al.
Science (2025)
Closed Access | Times Cited: 7
A Functional Map of the Human Intrinsically Disordered Proteome
Iva Pritišanac, T. Reid Alderson, Đesika Kolarić, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Closed Access | Times Cited: 10
Multimodal cell maps as a foundation for structural and functional genomics
Leah V. Schaffer, Mengzhou Hu, Gege Qian, et al.
Nature (2025)
Open Access | Times Cited: 1
Protein codes promote selective subcellular compartmentalization
Henry R. Kilgore, Itamar Chinn, Peter G. Mikhael, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 4
Glycogen phase separation drives macromolecular rearrangement and asymmetric division inE. coli
Yashna Thappeta, Silvia J. Cañas-Duarte, Till Kallem, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 4
Preserving condensate structure and composition by lowering sequence complexity
Amogh Sood, Bin Zhang
Biophysical Journal (2024) Vol. 123, Iss. 13, pp. 1815-1826
Open Access | Times Cited: 4
Aggregation of the amyloid-β peptide (Aβ40) within condensates generated through liquid–liquid phase separation
Owen M. Morris, Zenon Toprakcioglu, Alexander Röntgen, et al.
Scientific Reports (2024) Vol. 14, Iss. 1
Open Access | Times Cited: 4
catGRANULE 2.0: accurate predictions of liquid-liquid phase separating proteins at single amino acid resolution
Michele Monti, Jonathan Fiorentino, Dimitrios Miltiadis-Vrachnos, et al.
Genome biology (2025) Vol. 26, Iss. 1
Open Access
Beyond peptide targeting sequences: machine learning of cellular condensate localization
Jonathon A. Ditlev, Julie D. Forman‐Kay
Cell Research (2025)
Closed Access
Protein Language Model Identifies Disordered, Conserved Motifs Driving Phase Separation
Yumeng Zhang, Jared Zheng, Bin Zhang
(2025)
Open Access
Protein Language Model Identifies Disordered, Conserved Motifs Driving Phase Separation
Yumeng Zhang, Jared Zheng, Bin Zhang
(2025)
Open Access
AlphaFold2-based prediction of the co-condensation propensity of proteins
Shengyu Zhang, Christine Lim, Martina Occhetta, et al.
Proceedings of the National Academy of Sciences (2024) Vol. 121, Iss. 34
Open Access | Times Cited: 3
PICNIC accurately predicts condensate-forming proteins regardless of their structural disorder across organisms
Anna Hadarovich, Hari Singh, Soumyadeep Ghosh, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 3
PICNIC accurately predicts condensate-forming proteins regardless of their structural disorder across organisms
Anna Hadarovich, Hari Singh, Soumyadeep Ghosh, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 5
Sequence, Structure and Functional space of Drosophila de novo proteins
Lasse Middendorf, Bharat Ravi Iyengar, Lars A. Eicholt
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1
Functional characteristics and computational model of abundant hyperactive loci in the human genome
Sanjarbek Hudaiberdiev, Ivan Ovcharenko
eLife (2024) Vol. 13
Open Access | Times Cited: 1
Evolutionary analysis of ZAP and its cofactors identifies intrinsically disordered regions as central elements in host-pathogen interactions
Rachele Cagliani, Diego Forni, Alessandra Mozzi, et al.
Computational and Structural Biotechnology Journal (2024) Vol. 23, pp. 3143-3154
Open Access | Times Cited: 1
Sequence, Structure, and Functional Space of Drosophila De Novo Proteins
Lasse Middendorf, Bharat Ravi Iyengar, Lars A. Eicholt
Genome Biology and Evolution (2024) Vol. 16, Iss. 8
Open Access | Times Cited: 1
Functional characteristics and computational model of abundant hyperactive loci in the human genome
Sanjarbek Hudaiberdiev, Ivan Ovcharenko
(2024)
Open Access | Times Cited: 1
The evolution and exploration of intrinsically disordered and phase-separated protein states
Chi Fung Willis Chow, Ágnes Tóth-Petróczy
Elsevier eBooks (2024), pp. 353-379
Closed Access | Times Cited: 1
Aggregation of the Amyloid-β Peptide (Aβ40) within Condensates Generated through Liquid-Liquid Phase Separation
Owen M. Morris, Zenon Toprakcioglu, Alexander Röntgen, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 2
Functional characteristics and computational model of abundant hyperactive loci in the human genome
Sanjarbek Hudaiberdiev, Ivan Ovcharenko
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 1
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