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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:

Robust De Novo-Designed Homotetrameric Coiled Coils
Caitlin L. Edgell, Nigel J. Savery, Derek N. Woolfson
Biochemistry (2020) Vol. 59, Iss. 10, pp. 1087-1092
Open Access | Times Cited: 14

Showing 14 citing articles:

Understanding a protein fold: The physics, chemistry, and biology of α-helical coiled coils
Derek N. Woolfson
Journal of Biological Chemistry (2023) Vol. 299, Iss. 4, pp. 104579-104579
Open Access | Times Cited: 53
Assembling membraneless organelles from de novo designed proteins
Alexander T. Hilditch, Andrey Romanyuk, Stephen Cross, et al.
Nature Chemistry (2023) Vol. 16, Iss. 1, pp. 89-97
Open Access | Times Cited: 34
Self-assembly and regulation of protein cages from pre-organised coiled-coil modules
Fabio Lapenta, Jana Aupič, Marco Vezzoli, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 39
De novo designed peptides for cellular delivery and subcellular localisation
Guto G. Rhys, Jessica A. Cross, William Dawson, et al.
Nature Chemical Biology (2022) Vol. 18, Iss. 9, pp. 999-1004
Open Access | Times Cited: 27
Structural details of helix-mediated TDP-43 C-terminal domain multimerization
Azamat Rizuan, Jayakrishna Kanhangad Shenoy, Priyesh Mohanty, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 4
Structural duality enables a single protein to act as a toxin–antidote pair for meiotic drive
Hua Yu, Jianxiu Zhang, Ming Yang, et al.
Proceedings of the National Academy of Sciences (2024) Vol. 121, Iss. 45
Closed Access | Times Cited: 2
Design, synthesis, and characterization of protein origami based on self-assembly of a brick and staple artificial protein pair
Laureen Moreaud, Sébastien Viollet, Agathe Urvoas, et al.
Proceedings of the National Academy of Sciences (2023) Vol. 120, Iss. 11
Open Access | Times Cited: 5
Recent Progress Using De Novo Design to Study Protein Structure, Design and Binding Interactions
Juan Ferrando, Lee A. Solomon
Life (2021) Vol. 11, Iss. 3, pp. 225-225
Open Access | Times Cited: 15
Hydrodynamic Mixing Tunes the Stiffness of Proteoglycan‐Mimicking Physical Hydrogels
James P. Warren, Danielle Miles, Nikil Kapur, et al.
Advanced Healthcare Materials (2021) Vol. 10, Iss. 11
Open Access | Times Cited: 10
Expanding the versatility of natural and de novo designed coiled coils and helical bundles
Mohammad ElGamacy, Birte Hernandez Alvarez
Current Opinion in Structural Biology (2021) Vol. 68, pp. 224-234
Closed Access | Times Cited: 9
Exchange, promiscuity, and orthogonality in de novo designed coiled-coil peptide assemblies
Kathleen W. Kurgan, Freddie J. O. Martin, William Dawson, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
Exchange, promiscuity, and orthogonality in de novo designed coiled-coil peptide assemblies
Kathleen W. Kurgan, Freddie J. O. Martin, William Dawson, et al.
Chemical Science (2024)
Open Access
Assembling membraneless organelles fromde novodesigned proteins
Alexander T. Hilditch, Andrey Romanyuk, Stephen Cross, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 1
SalmonellaYqiC exerts its function through an oligomeric state
Wei‐Chun Huang, W.-T. Chen, Yueh‐Chen Chen, et al.
Protein Science (2023) Vol. 32, Iss. 10
Open Access | Times Cited: 1
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