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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:

Community-Wide Experimental Evaluation of the PROSS Stability-Design Method
Yoav Peleg, Renaud Vincentelli, Brett M. Collins, et al.
Journal of Molecular Biology (2021) Vol. 433, Iss. 13, pp. 166964-166964
Open Access | Times Cited: 52

Showing 1-25 of 52 citing articles:

Mega-scale experimental analysis of protein folding stability in biology and design
Kotaro Tsuboyama, Justas Dauparas, Jonathan H. Chen, et al.
Nature (2023) Vol. 620, Iss. 7973, pp. 434-444
Open Access | Times Cited: 158
Opportunities and challenges in design and optimization of protein function
Dina Listov, Casper A. Goverde, Bruno E. Correia, et al.
Nature Reviews Molecular Cell Biology (2024) Vol. 25, Iss. 8, pp. 639-653
Closed Access | Times Cited: 33
Stable and Functionally Diverse Versatile Peroxidases Designed Directly from Sequences
S. Barber-Zucker, Vladimir Mindel, Eva García-Ruiz, et al.
Journal of the American Chemical Society (2022) Vol. 144, Iss. 8, pp. 3564-3571
Open Access | Times Cited: 47
A concise guide to choosing suitable gene expression systems for recombinant protein production
Anja Schütz, Frank Bernhard, Nicholas S. Berrow, et al.
STAR Protocols (2023) Vol. 4, Iss. 4, pp. 102572-102572
Open Access | Times Cited: 29
Advancing Enzyme’s Stability and Catalytic Efficiency through Synergy of Force-Field Calculations, Evolutionary Analysis, and Machine Learning
Antonín Kunka, Sérgio M. Marques, Martin Havlasek, et al.
ACS Catalysis (2023) Vol. 13, Iss. 19, pp. 12506-12518
Open Access | Times Cited: 27
Recent advances in recombinant production of soluble proteins in E. coli
Ario de Marco
Microbial Cell Factories (2025) Vol. 24, Iss. 1
Open Access
Stabilized designs of the malaria adhesin protein PvRBP2b for use as a potential diagnostic for Plasmodium vivax
D Jaison, Lucas Krauss, Lauren M. Smith, et al.
Journal of Biological Chemistry (2025), pp. 108290-108290
Open Access
Designed High-Redox Potential Laccases Exhibit High Functional Diversity
S. Barber-Zucker, Ivan Mateljak, Moshe Goldsmith, et al.
ACS Catalysis (2022) Vol. 12, Iss. 21, pp. 13164-13173
Open Access | Times Cited: 34
Tools for computational design and high-throughput screening of therapeutic enzymes
Michal Vasina, Jan Velecký, Joan Planas-Iglesias, et al.
Advanced Drug Delivery Reviews (2022) Vol. 183, pp. 114143-114143
Closed Access | Times Cited: 33
Principles and practical applications of structure-based vaccine design
Patrick O. Byrne, Jason S. McLellan
Current Opinion in Immunology (2022) Vol. 77, pp. 102209-102209
Open Access | Times Cited: 33
Functionally Diverse Peroxygenases by AlphaFold2, Design, and Signal Peptide Shuffling
Judith Münch, N.L. Dietz, S. Barber-Zucker, et al.
ACS Catalysis (2024) Vol. 14, Iss. 7, pp. 4738-4748
Open Access | Times Cited: 5
Recombinant expression of insoluble enzymes in Escherichia coli: a systematic review of experimental design and its manufacturing implications
Suraj Mital, Graham Christie, Duygu Dikicioǧlu
Microbial Cell Factories (2021) Vol. 20, Iss. 1
Open Access | Times Cited: 38
Enhancing thermostability of lipase from Pseudomonas alcaligenes for producing l-menthol by the CREATE strategy
Zhonglang Yu, Haoran Yu, Jinling Xu, et al.
Catalysis Science & Technology (2022) Vol. 12, Iss. 8, pp. 2531-2541
Closed Access | Times Cited: 24
Mega-scale experimental analysis of protein folding stability in biology and protein design
Kotaro Tsuboyama, Justas Dauparas, Jonathan H. Chen, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 23
Interrogation and validation of the interactome of neuronal Munc18-interacting Mint proteins with AlphaFold2
Saroja Weeratunga, Rachel S. Gormal, Meihan Liu, et al.
Journal of Biological Chemistry (2023) Vol. 300, Iss. 1, pp. 105541-105541
Open Access | Times Cited: 12
Design of a stable human acid‐β‐glucosidase: towards improved Gaucher disease therapy and mutation classification
Šárka Pokorná, Olga Khersonsky, Rosalie Lipsh‐Sokolik, et al.
FEBS Journal (2023) Vol. 290, Iss. 13, pp. 3383-3399
Open Access | Times Cited: 10
Efficient Exploration of Sequence Space by Sequence-Guided Protein Engineering and Design
Ben E. Clifton, Dan Kozome, Paola Laurino
Biochemistry (2022) Vol. 62, Iss. 2, pp. 210-220
Open Access | Times Cited: 15
Improving the secretion of designed protein assemblies through negative design of cryptic transmembrane domains
Jing Yang Wang, Alena Khmelinskaia, William Sheffler, et al.
Proceedings of the National Academy of Sciences (2023) Vol. 120, Iss. 11
Open Access | Times Cited: 9
Click, Compute, Create: A Review of Web‐based Tools for Enzyme Engineering
Adrian Tripp, Markus Braun, Florian Wieser, et al.
ChemBioChem (2024)
Open Access | Times Cited: 2
One‐shot design elevates functional expression levels of a voltage‐gated potassium channel
Jonathan J. Weinstein, Chandamita Saikia, Izhar Karbat, et al.
Protein Science (2024) Vol. 33, Iss. 6
Open Access | Times Cited: 2
Enhancement of tryptophan 2-monooxygenase thermostability by semi-rational enzyme engineering: A strategic design to minimize experimental investigation
Sirus Kongjaroon, Narin Lawan, Duangthip Trisrivirat, et al.
RSC Chemical Biology (2024) Vol. 5, Iss. 10, pp. 989-1001
Open Access | Times Cited: 2
What Have We Learned from Design of Function in Large Proteins?
Olga Khersonsky, Sarel J. Fleishman
BioDesign Research (2022) Vol. 2022
Open Access | Times Cited: 14
Structure-Based Design of Xanthine-Benzimidazole Derivatives as Novel and Potent Tryptophan Hydroxylase Inhibitors
Edgar Specker, Susann Matthes, Radosław Wesołowski, et al.
Journal of Medicinal Chemistry (2022) Vol. 65, Iss. 16, pp. 11126-11149
Closed Access | Times Cited: 11
Logistic Regression-Guided Identification of Cofactor Specificity-Contributing Residues in Enzyme with Sequence Datasets Partitioned by Catalytic Properties
Sou Sugiki, Teppei Niide, Yoshihiro Toya, et al.
ACS Synthetic Biology (2022) Vol. 11, Iss. 12, pp. 3973-3985
Open Access | Times Cited: 10
Increased Thermostability of an Engineered Flavin-Containing Monooxygenase to Remediate Trimethylamine in Fish Protein Hydrolysates
Marianne Goris, Isabel Cea‐Rama, Pål Puntervoll, et al.
Applied and Environmental Microbiology (2023) Vol. 89, Iss. 6
Open Access | Times Cited: 5
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