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:

The next wave of interactomics: Mapping the SLiM-based interactions of the intrinsically disordered proteome
Norman E. Davey, Leandro Simonetti, Ylva Ivarsson
Current Opinion in Structural Biology (2023) Vol. 80, pp. 102593-102593
Open Access | Times Cited: 29

Showing 1-25 of 29 citing articles:

The molecular basis for cellular function of intrinsically disordered protein regions
Alex S. Holehouse, Birthe B. Kragelund
Nature Reviews Molecular Cell Biology (2023) Vol. 25, Iss. 3, pp. 187-211
Open Access | Times Cited: 180

ELM—the Eukaryotic Linear Motif resource—2024 update
Manjeet Kumar, Sushama Michael, Jesús Alvarado-Valverde, et al.
Nucleic Acids Research (2023) Vol. 52, Iss. D1, pp. D442-D455
Open Access | Times Cited: 39

Direct prediction of intermolecular interactions driven by disordered regions
Garrett M. Ginell, Ryan J. Emenecker, Jeffrey M. Lotthammer, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 11

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: 9

Protein binding and folding through an evolutionary lens
Per Jemth
Current Opinion in Structural Biology (2025) Vol. 90, pp. 102980-102980
Open Access

Molecular determinants of condensate composition
Alex S. Holehouse, Simon Alberti
Molecular Cell (2025) Vol. 85, Iss. 2, pp. 290-308
Open Access

A quantitative intracellular peptide binding assay reveals recognition determinants and context dependence of short linear motifs
Mythili S. Subbanna, Matthew J. Winters, Mihkel Örd, et al.
Journal of Biological Chemistry (2025), pp. 108225-108225
Open Access

Sequence- and chemical specificity define the functional landscape of intrinsically disordered regions
Iris Langstein-Skora, Andrea Schmid, Frauke Huth, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Closed Access | Times Cited: 34

Pathogenic mutations of human phosphorylation sites affect protein–protein interactions
Trëndelina Rrustemi, Katrina Meyer, Yvette Roske, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 5

Key Proteomics Tools for Fundamental and Applied Microalgal Research
Maxence Plouviez, Éric Dubreucq
Proteomes (2024) Vol. 12, Iss. 2, pp. 13-13
Open Access | Times Cited: 4

Diversity of short linear interaction motifs in SARS-CoV-2 nucleocapsid protein
Peter Schuck, Huaying Zhao
mBio (2023) Vol. 14, Iss. 6
Open Access | Times Cited: 8

A Native Mass Spectrometry Approach to Qualitatively Elucidate Interfacial Epitopes of Transient Protein-Protein Interactions
Clinton G. L. Veale, Abir Chakraborty, Richwell Mhlanga, et al.
Chemical Communications (2024) Vol. 60, Iss. 45, pp. 5844-5847
Open Access | Times Cited: 2

Growing ecosystem of deep learning methods for modeling protein–protein interactions
Julia R. Rogers, Gergő Nikolényi, Mohammed AlQuraishi
Protein Engineering Design and Selection (2023) Vol. 36
Open Access | Times Cited: 5

Uncovering domain motif interactions using high‐throughput protein–protein interaction detection methods
Sobia Idrees, Keshav Raj Paudel, Tayyaba Sadaf, et al.
FEBS Letters (2024) Vol. 598, Iss. 7, pp. 725-742
Open Access | Times Cited: 1

FaSTPACE: a fast and scalable tool for peptide alignment and consensus extraction
Hazem M. Kotb, Norman E. Davey
NAR Genomics and Bioinformatics (2024) Vol. 6, Iss. 3
Open Access | Times Cited: 1

The Proteomic Analysis of Cancer-Related Alterations in the Human Unfoldome
Victor Paromov, Vladimir N. Uversky, Ayorinde Cooley, et al.
International Journal of Molecular Sciences (2024) Vol. 25, Iss. 3, pp. 1552-1552
Open Access | Times Cited: 1

Mass spectrometry-based methods for characterizing transient protein–protein interactions
Clinton G. L. Veale, David J. Clarke
Trends in Chemistry (2024) Vol. 6, Iss. 7, pp. 377-391
Closed Access | Times Cited: 1

A quantitative intracellular peptide binding assay reveals recognition determinants and context dependence of short linear motifs
Mythili S. Subbanna, Matthew J. Winters, Mihkel Örd, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1

Novel Insights into Phytoplasma Effectors
Karla Gisel Carreón-Anguiano, Sara Elena Vila-Luna, Luis Sáenz-Carbonell, et al.
Horticulturae (2023) Vol. 9, Iss. 11, pp. 1228-1228
Open Access | Times Cited: 4

Pathogenic mutations of human phosphorylation sites affect protein-protein interactions
Trëndelina Rrustemi, Katrina Meyer, Yvette Roske, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 2

Diversity of Short Linear Interaction Motifs in SARS-CoV-2 Nucleocapsid Protein
Peter Schuck, Huaying Zhao
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 2

Benchmarking computational tools for de novo motif discovery
Leandro Simonetti, Ylva Ivarsson, Norman E. Davey
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access

Massively parallel screening of TIR-derived peptides reveals vast TLR-targeting immunomodulatory peptides
Yun Lim, Tae Kyeom Kang, Meong Il Kim, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access

Defining short linear motif binding determinants by phage-based multiplexed deep mutational scanning
Caroline Benz, Lars Maasen, Leandro Simonetti, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access

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