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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:

A mutational atlas for Parkin proteostasis
Lene Clausen, Vasileios Voutsinos, Matteo Cagiada, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 19

Showing 19 citing articles:

ProteinGym: Large-Scale Benchmarks for Protein Design and Fitness Prediction
Pascal Notin, Aaron W. Kollasch, Daniel P. Ritter, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 77
Site-saturation mutagenesis of 500 human protein domains
Antoni Beltran, Xuege Jiang, Yue Shen, et al.
Nature (2025)
Open Access | Times Cited: 1
Site saturation mutagenesis of 500 human protein domains reveals the contribution of protein destabilization to genetic disease
Antoni Beltran, Xuege Jiang, Yue Shen, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 8
Deep mutational scanning reveals a correlation between degradation and toxicity of thousands of aspartoacylase variants
Martin Grønbæk-Thygesen, Vasileios Voutsinos, Kristoffer E. Johansson, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 6
Importance of an N-terminal structural switch in the distinction between small RNA-bound and free ARGONAUTE
Simon Bressendorff, Ida Marie Zobbe Sjøgaard, Andreas Prestel, et al.
Nature Structural & Molecular Biology (2025)
Closed Access
Computational Study of the Activation Mechanism of Wild-Type Parkin and Its Clinically Relevant Mutant
Zeynep Nur Cinviz, Özge Şensoy
ACS Chemical Neuroscience (2025)
Closed Access
PRKN-linked familial Parkinson’s disease: cellular and molecular mechanisms of disease-linked variants
Lene Clausen, Justyna Okarmus, Vasileios Voutsinos, et al.
Cellular and Molecular Life Sciences (2024) Vol. 81, Iss. 1
Open Access | Times Cited: 5
Structural Basis for the Pathogenicity of Parkin Catalytic Domain Mutants
Julian P. Wagner, Véronique Sauvé, Anshu Saran, et al.
Journal of Biological Chemistry (2024), pp. 108051-108051
Closed Access | Times Cited: 1
A side-by-side comparison of variant function measurements using deep mutational scanning and base editing
Ivan Sokirniy, Haider Inam, Marta Tomaszkiewicz, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
Systematic characterization of indel variants using a yeast-based protein folding sensor
Sven Larsen-Ledet, Søren Lindemose, Aleksandra Panfilova, et al.
(2024)
Closed Access
Understanding the Pathogenicity of Parkin Catalytic Domain Mutants
Julian P. Wagner, Véronique Sauvé, Kalle Gehring
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
Disentangling the mutational effects on protein stability and interaction of human MLH1
Sven Larsen-Ledet, Amelie Stein
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
Naturally occurring hyperactive variants of human parkin
Tahrima Saiha Huq, Jean Luo, Rayan Fakih, et al.
Communications Biology (2024) Vol. 7, Iss. 1
Open Access
Structural and Functional Characterization of the Most Frequent Pathogenic PRKN Substitution p.R275W
Bernardo A. Bustillos, Liam T. Cocker, Matt Coban, et al.
Cells (2024) Vol. 13, Iss. 18, pp. 1540-1540
Open Access
Cooperative Substructure and Energetics of Allosteric Regulation of the Catalytic Core of the E3 Ubiquitin Ligase Parkin by Phosphorylated Ubiquitin
Xiang Ye, Sravya Kotaru, Rosana Lopes, et al.
Biomolecules (2024) Vol. 14, Iss. 10, pp. 1338-1338
Open Access
Therapeutic potential of Parkin and its regulation in Parkinson’s disease
Narukkottil Safreena, Indu R. Nair, Goutam Chandra
Biochemical Pharmacology (2024) Vol. 230, pp. 116600-116600
Closed Access
A pharmacological chaperone stabilizer rescues the expression of the vast majority of pathogenic variants in a G protein-coupled receptor
Taylor L. Mighell, Ben Lehner
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
Effects of residue substitutions on the cellular abundance of proteins
Thea K. Schulze, Kresten Lindorff‐Larsen
(2024)
Open Access
Effects of residue substitutions on the cellular abundance of proteins
Thea K. Schulze, Kresten Lindorff‐Larsen
(2024)
Open Access
Systematic characterization of indel variants using a yeast-based protein folding sensor
Sven Larsen-Ledet, Søren Lindemose, Aleksandra Panfilova, et al.
Structure (2024)
Closed Access
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