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:

Optimization of sortase A ligation for flexible engineering of complex protein systems
Jess Li, Yue Zhang, Olivier Soubias, et al.
Journal of Biological Chemistry (2020) Vol. 295, Iss. 9, pp. 2664-2675
Open Access | Times Cited: 41

Showing 1-25 of 41 citing articles:

Challenges in the use of sortase and other peptide ligases for site-specific protein modification
Holly E. Morgan, W. Bruce Turnbull, Michael E. Webb
Chemical Society Reviews (2022) Vol. 51, Iss. 10, pp. 4121-4145
Open Access | Times Cited: 80

NMR illuminates intrinsic disorder
H. Jane Dyson, Peter E. Wright
Current Opinion in Structural Biology (2021) Vol. 70, pp. 44-52
Open Access | Times Cited: 74

Protein Engineering Strategies for Improved Pharmacokinetics
Aurélie Rondon, Sohaib Mahri, Francisco Morales-Yánez, et al.
Advanced Functional Materials (2021) Vol. 31, Iss. 44
Open Access | Times Cited: 49

Lipid Nanodiscs for High-Resolution NMR Studies of Membrane Proteins
Umut Günsel, Franz Hagn
Chemical Reviews (2021) Vol. 122, Iss. 10, pp. 9395-9421
Closed Access | Times Cited: 44

A simple protocol for the production of highly deuterated proteins for biophysical studies
Jess Li, R. Andrew Byrd
Journal of Biological Chemistry (2022) Vol. 298, Iss. 8, pp. 102253-102253
Open Access | Times Cited: 21

Selective deuteration of an RNA:RNA complex for structural analysis using small-angle scattering
Aldrex Munsayac, Wellington Leite, Jesse B. Hopkins, et al.
Structure (2025)
Closed Access

Enzymatic assembly for CRISPR split-Cas9 system: The emergence of a Sortase-based split-Cas9 technology
Seyed Hossein Helalat, Helga Thora Kristinsdóttir, Astrid Dolinger Petersen, et al.
International Journal of Biological Macromolecules (2025) Vol. 306, pp. 141583-141583
Open Access

Advances in the chemical synthesis of human proteoforms
Ziyi Yang, Yingqi Xiao, Yang Shi, et al.
Science China Life Sciences (2025)
Closed Access

Sortase A-Based Post-translational Modifications on Encapsulin Nanocompartments
Seyed Hossein Helalat, Rodrigo Coronel Téllez, Ehsan Ansari Dezfouli, et al.
Biomacromolecules (2024) Vol. 25, Iss. 5, pp. 2762-2769
Open Access | Times Cited: 3

Sequence variation in the β7–β8 loop of bacterial class A sortase enzymes alters substrate selectivity
Isabel M. Piper, Sarah A. Struyvenberg, Jordan D. Valgardson, et al.
Journal of Biological Chemistry (2021) Vol. 297, Iss. 2, pp. 100981-100981
Open Access | Times Cited: 17

EPISOMAL VECTORS FOR STABLE PRODUCTION OF RECOMBINANT PROTEINS AND ENGINEERED ANTIBODIES
Ian Fallahee, Daniel Hawiger
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 2

The Transpeptidase Sortase A Binds Nucleic Acids and Mediates Mammalian Cell Labeling
Yingzheng Liu, Zhike Lu, Panfeng Wu, et al.
Advanced Science (2024) Vol. 11, Iss. 21
Open Access | Times Cited: 2

Archaeal Connectase is a specific and efficient protein ligase related to proteasome β subunits
Adrian Fuchs, Moritz Ammelburg, Jörg Martin, et al.
Proceedings of the National Academy of Sciences (2021) Vol. 118, Iss. 11
Open Access | Times Cited: 15

Segmental and site-specific isotope labelling strategies for structural analysis of posttranslationally modified proteins
Dominik P. Vogl, Anne C. Conibear, Christian F. W. Becker
RSC Chemical Biology (2021) Vol. 2, Iss. 5, pp. 1441-1461
Open Access | Times Cited: 14

Sortase-Mediated Site-Specific Conjugation and 89Zr-Radiolabeling of Designed Ankyrin Repeat Proteins for PET
Rachael Fay, I Törö, Anna-Lena Schinke, et al.
Molecular Pharmaceutics (2022) Vol. 19, Iss. 10, pp. 3576-3585
Closed Access | Times Cited: 9

Deciphering the Structure and Formation of Amyloids in Neurodegenerative Diseases With Chemical Biology Tools
Isabelle Landrieu, Elian Dupré, Davy Sinnaeve, et al.
Frontiers in Chemistry (2022) Vol. 10
Open Access | Times Cited: 9

Enzymatic Spin-Labeling of Protein N- and C-Termini for Electron Paramagnetic Resonance Spectroscopy
Robert Dunleavy, Siddarth Chandrasekaran, Brian R. Crane
Bioconjugate Chemistry (2023)
Open Access | Times Cited: 5

Reversed Proteolysis—Proteases as Peptide Ligases
Peter Goettig
Catalysts (2020) Vol. 11, Iss. 1, pp. 33-33
Open Access | Times Cited: 12

Peptide and protein engineering by modification of backbone and sidechain functional groups
Shadi Kordbacheh, Andrea M. Kasko
Polymer International (2021) Vol. 70, Iss. 7, pp. 889-896
Closed Access | Times Cited: 11

The Chemistry of Creating Chemically Programmed Antibodies (cPAbs): Site-Specific Bioconjugation of Small Molecules
Omozojie P. Aigbogun, Christopher P. Phenix, Ed S. Krol, et al.
Molecular Pharmaceutics (2023) Vol. 20, Iss. 2, pp. 853-874
Closed Access | Times Cited: 4

The PH domain in the ArfGAP ASAP1 drives catalytic activation through an unprecedented allosteric mechanism
Olivier Soubias, Samuel Foley, Xiaoying Jian, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1

Repurposing Amide Bond-Forming Enzymes for Non-native Protein Modification
Tong Zhu, Bian Wu
ACS Catalysis (2024) Vol. 14, Iss. 21, pp. 15811-15826
Closed Access | Times Cited: 1

Improvement of Modular Protein Display Efficiency in SpyTag-Implemented Norovirus-like Particles
Jirayu Boonyakida, Indra Memdi Khoris, Fahmida Nasrin, et al.
Biomacromolecules (2022) Vol. 24, Iss. 1, pp. 308-318
Closed Access | Times Cited: 6

Site-Specific C-Terminal Fluorescent Labeling of Tau Protein
Louise C. Bryan, Saurabh Awasthi, Yuanjie Li, et al.
ACS Omega (2022) Vol. 7, Iss. 50, pp. 47009-47014
Open Access | Times Cited: 4

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