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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:

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: 31

Showing 1-25 of 31 citing articles:

Engineering synthetic biomolecular condensates
Yifan Dai, Lingchong You, Ashutosh Chilkoti
Nature Reviews Bioengineering (2023) Vol. 1, Iss. 7, pp. 466-480
Open Access | Times Cited: 101
De novo protein design—From new structures to programmable functions
Tanja Kortemme
Cell (2024) Vol. 187, Iss. 3, pp. 526-544
Open Access | Times Cited: 87
Benchmarking AlphaFold2 on peptide structure prediction
Eli Fritz McDonald, Taylor Jones, Lars Plate, et al.
Structure (2022) Vol. 31, Iss. 1, pp. 111-119.e2
Open Access | Times Cited: 80
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: 63
De novo design of modular peptide-binding proteins by superhelical matching
Kejia Wu, Hua Bai, Ya‐Ting Chang, et al.
Nature (2023) Vol. 616, Iss. 7957, pp. 581-589
Open Access | Times Cited: 50
Rationally seeded computational protein design of ɑ-helical barrels
Katherine I. Albanese, Rokas Petrenas, Fabio Pirro, et al.
Nature Chemical Biology (2024) Vol. 20, Iss. 8, pp. 991-999
Open Access | Times Cited: 10
Homochiral versus Heterochiral Dimeric Helical Foldamer Bundles: Chlorinated‐Solvent‐Dependent Self‐Sorting
Friedericke S. Menke, Barbara Wicher, Victor Maurizot, et al.
Angewandte Chemie International Edition (2023) Vol. 62, Iss. 12
Open Access | Times Cited: 20
A de novo designed coiled coil-based switch regulates the microtubule motor kinesin-1
Jessica A. Cross, William Dawson, Shivam Shukla, et al.
Nature Chemical Biology (2024) Vol. 20, Iss. 7, pp. 916-923
Open Access | Times Cited: 6
From peptides to proteins: coiled-coil tetramers to single-chain 4-helix bundles
Elise A. Naudin, Katherine I. Albanese, Abigail J. Smith, et al.
Chemical Science (2022) Vol. 13, Iss. 38, pp. 11330-11340
Open Access | Times Cited: 19
Computational protein design
Katherine I. Albanese, Sophie Barbe, Derek N. Woolfson, et al.
Nature Reviews Methods Primers (2025) Vol. 5, Iss. 1
Open Access
Assessment of the Topology and Oligomerisation States of Coiled Coils Using Metadynamics with Conformational Restraints
Evangelia Notari, Christopher W. Wood, Julien Michel
Journal of Chemical Theory and Computation (2025)
Open Access
From prediction to design: Revealing the mechanisms of umami peptides using interpretable deep learning, quantum chemical simulations, and module substitution
Lijun Su, Zongwei Ma, Huizhuo Ji, et al.
Food Chemistry (2025), pp. 144301-144301
Closed Access
De Novo Design of Parallel and Antiparallel A3B3 Heterohexameric α-Helical Barrels
J Chubb, Katherine I. Albanese, Alison Rodger, et al.
Biochemistry (2025)
Open Access
An abiotic, tetrameric, eight-helix bundle
Friedericke S. Menke, Barbara Wicher, Lars Allmendinger, et al.
Chemical Science (2023) Vol. 14, Iss. 14, pp. 3742-3751
Open Access | Times Cited: 9
The art of designed coiled-coils for the regulation of mammalian cells
Tjaša Plaper, Erik Rihtar, Taja Železnik Ramuta, et al.
Cell chemical biology (2024) Vol. 31, Iss. 8, pp. 1460-1472
Open Access | Times Cited: 2
De novo design of monomeric helical bundles for pH‐controlled membrane lysis
Nicolas Goldbach, Issa Benna, Basile I. M. Wicky, et al.
Protein Science (2023) Vol. 32, Iss. 11
Open Access | Times Cited: 6
Affinity-based drug delivery systems for the central nervous system: exploiting molecular interactions for local, precise targeting
Pablo Ramos Ferrer, Shelly E. Sakiyama‐Elbert
Journal of Neural Engineering (2024) Vol. 21, Iss. 4, pp. 041004-041004
Closed Access | Times Cited: 2
Homochirale versus heterochirale dimere helikale Foldamerbündel: chlorierte Lösungsmittel‐abhängige Selbstsortierung
Friedericke S. Menke, Barbara Wicher, Victor Maurizot, et al.
Angewandte Chemie (2023) Vol. 135, Iss. 12
Open Access | Times Cited: 5
Adjusting Heterodimeric Coiled-Coils (K/E Zipper) to Connect Autophagy-Inducing Peptide with Cell-Penetrating Peptide
Yoshiyuki Hakata, Kazuma Yamashita, Sonoko Hashimoto, et al.
Pharmaceutics (2023) Vol. 15, Iss. 4, pp. 1048-1048
Open Access | Times Cited: 4
The application and prospects of drug delivery systems in idiopathic pulmonary fibrosis
Xi Zhang, Ling Zhang, Jia-Hua Tian, et al.
Biomaterials Advances (2024) Vol. 168, pp. 214123-214123
Closed Access | Times Cited: 1
Interface-aware molecular generative framework for protein–protein interaction modulators
Jianmin Wang, Jiashun Mao, Chunyan Li, et al.
Journal of Cheminformatics (2024) Vol. 16, Iss. 1
Open Access | Times Cited: 1
Interface-aware molecular generative framework for protein-protein interaction modulators
Jianmin Wang, Jiashun Mao, Chunyan Li, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 3
Design and Selection of Heterodimerizing Helical Hairpins for Synthetic Biology
Abigail J. Smith, Elise A. Naudin, Caitlin L. Edgell, et al.
ACS Synthetic Biology (2023) Vol. 12, Iss. 6, pp. 1845-1858
Open Access | Times Cited: 1
Rationally seeded computational protein design
Katherine I. Albanese, Rokas Petrenas, Fabio Pirro, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 1
Configuration of two cysteine residues in a ring within a stapled Bim peptide affects the secondary structure and apoptotic activity
Shengli Zhou, Fuka Nishimura, Kazuhaya Wada, et al.
Bioorganic & Medicinal Chemistry Letters (2024) Vol. 112, pp. 129915-129915
Closed Access
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