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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:

Real‐Time and Label‐Free Measurement of Deubiquitinase Activity with a MspA Nanopore
Spencer A. Shorkey, Jiale Du, Ryan Pham, et al.
ChemBioChem (2021) Vol. 22, Iss. 17, pp. 2688-2692
Open Access | Times Cited: 17

Showing 17 citing articles:

Detection of phosphorylation post-translational modifications along single peptides with nanopores
Ian C. Nova, Justas Ritmejeris, Henry Brinkerhoff, et al.
Nature Biotechnology (2023) Vol. 42, Iss. 5, pp. 710-714
Closed Access | Times Cited: 49
Nanopore discrimination of rare earth elements
Wen Sun, Yunqi Xiao, Kefan Wang, et al.
Nature Nanotechnology (2025)
Closed Access | Times Cited: 2
Machine Learning Assisted Simultaneous Structural Profiling of Differently Charged Proteins in a Mycobacterium smegmatis Porin A (MspA) Electroosmotic Trap
Yao Liu, Kefan Wang, Yuqin Wang, et al.
Journal of the American Chemical Society (2022) Vol. 144, Iss. 2, pp. 757-768
Closed Access | Times Cited: 49
Quantification of Protein Glycosylation Using Nanopores
Roderick Corstiaan Abraham Versloot, Florian Leonardus Rudolfus Lucas, Liubov Yakovlieva, et al.
Nano Letters (2022) Vol. 22, Iss. 13, pp. 5357-5364
Open Access | Times Cited: 46
Protein Sizing with 15 nm Conical Biological Nanopore YaxAB
Sabine Straathof, Giovanni Di Muccio, Maaruthy Yelleswarapu, et al.
ACS Nano (2023) Vol. 17, Iss. 14, pp. 13685-13699
Open Access | Times Cited: 22
A cryptic K48 ubiquitin chain binding site on UCH37 is required for its role in proteasomal degradation
Jiale Du, Sándor Babik, Yanfeng Li, et al.
eLife (2022) Vol. 11
Open Access | Times Cited: 20
Nanopore sensing of protein and peptide conformation for point-of-care applications
Laura Ratinho, N. Helge Meyer, Sandra J. Greive, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access
Obtaining Narrow Distributions of Single-Molecule Peptide Signals Enables Sensitive Peptide Discrimination with α-Hemolysin Nanopores
Xing Wei, Jiaqi Wen, Hao Wu, et al.
Journal of the American Chemical Society (2025)
Closed Access
Protein Profiling by Nanopore-Based Technology
Fu-Na Meng, Xin Li, Na Zou, et al.
Analytical Chemistry (2025)
Closed Access
Site‐Specific Introduction of Bioorthogonal Handles to Nanopores by Genetic Code Expansion
Jing Yang, Kefan Wang, Shanyu Zhang, et al.
Angewandte Chemie International Edition (2023) Vol. 62, Iss. 21
Closed Access | Times Cited: 9
Enzymology on an Electrode and in a Nanopore: Analysis Algorithms, Enzyme Kinetics, and Perspectives
V.V. Shumyantseva, Alexey V. Kuzikov, Rami A. Masamrekh, et al.
BioNanoScience (2022) Vol. 12, Iss. 4, pp. 1341-1355
Closed Access | Times Cited: 10
Tuning single-molecule ClyA nanopore tweezers for real-time tracking of the conformational dynamics of West Nile viral NS2B/NS3 protease
Spencer A. Shorkey, Yumeng Zhang, Jacqueline Sharp, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1
Nanopore single-molecule detection of bleomycin via dumbbell DNA scission
Ting Li, Xinying Li, Xiaoxue Li, et al.
Microchemical Journal (2021) Vol. 170, pp. 106738-106738
Closed Access | Times Cited: 6
Mapping phosphorylation post-translational modifications along single peptides with nanopores
Ian C. Nova, Justas Ritmejeris, Henry Brinkerhoff, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 3
A Novel Bi-Directional Channel for Nutrient Uptake across Mycobacterial Outer Envelope
Lei Liu, Chongzheng Wen, Xiaoying Cai, et al.
Microorganisms (2024) Vol. 12, Iss. 9, pp. 1827-1827
Open Access
A Cryptic K48 Ubiquitin Chain Binding Site on UCH37 is Required for its Role in Proteasomal Degradation
Jiale Du, Sándor Babik, Yanfeng Li, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2021)
Open Access | Times Cited: 1
Site‐Specific Introduction of Bioorthogonal Handles to Nanopores by Genetic Code Expansion
Jing Yang, Kefan Wang, Shanyu Zhang, et al.
Angewandte Chemie (2023) Vol. 135, Iss. 21
Closed Access
A Cryptic K48 Ubiquitin Chain Binding Site on UCH37 is Required for its Role in Proteasomal Degradation
Jiale Du, Sándor Babik, Yanfeng Li, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2021) Vol. 1
Closed Access
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