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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:

Computational Design of Synthetic Enzymes
Valerie Vaissier Welborn, Teresa Head‐Gordon
Chemical Reviews (2018) Vol. 119, Iss. 11, pp. 6613-6630
Open Access | Times Cited: 172

Showing 26-50 of 172 citing articles:

Catalytic Principles from Natural Enzymes and Translational Design Strategies for Synthetic Catalysts
Wan‐Lu Li, Teresa Head‐Gordon
ACS Central Science (2020) Vol. 7, Iss. 1, pp. 72-80
Open Access | Times Cited: 61
DenseCPD: Improving the Accuracy of Neural-Network-Based Computational Protein Sequence Design with DenseNet
Yifei Qi, John Z. H. Zhang
Journal of Chemical Information and Modeling (2020) Vol. 60, Iss. 3, pp. 1245-1252
Open Access | Times Cited: 59
Recent advances in artificial enzyme cascades for the production of value-added chemicals
Zilong Wang, Balaji Sundara Sekar, Zhi Li
Bioresource Technology (2020) Vol. 323, pp. 124551-124551
Closed Access | Times Cited: 53
Chemical modification of enzymes to improve biocatalytic performance
Pritam Giri, Amol D. Pagar, Mahesh D. Patil, et al.
Biotechnology Advances (2021) Vol. 53, pp. 107868-107868
Closed Access | Times Cited: 51
Interplay of water and a supramolecular capsule for catalysis of reductive elimination reaction from gold
Valerie Vaissier Welborn, Wan‐Lu Li, Teresa Head‐Gordon
Nature Communications (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 49
Enhancing computational enzyme design by a maximum entropy strategy
Wen Jun Xie, Mojgan Asadi, Arieh Warshel
Proceedings of the National Academy of Sciences (2022) Vol. 119, Iss. 7
Open Access | Times Cited: 29
Bioprospecting of microbial enzymes: current trends in industry and healthcare
Eswar Rao Tatta, Madangchanok Imchen, Jamseel Moopantakath, et al.
Applied Microbiology and Biotechnology (2022) Vol. 106, Iss. 5-6, pp. 1813-1835
Closed Access | Times Cited: 26
Computational design of highly efficient thermostable MHET hydrolases and dual enzyme system for PET recycling
Jun Zhang, Hongzhao Wang, Zhaorong Luo, et al.
Communications Biology (2023) Vol. 6, Iss. 1
Open Access | Times Cited: 19
Heme-Dependent Supramolecular Nanocatalysts: A Review
Yuanxi Liu, Zhen‐Gang Wang
ACS Nano (2023) Vol. 17, Iss. 14, pp. 13000-13016
Closed Access | Times Cited: 18
Hexachlorobenzene (HCB) adsorption onto the surfaces of C60, C59Si, and C59Ge: Insight from DFT, QTAIM, and NCI
Mohsen Doust Mohammadi, Hewa Y. Abdullah, Hitler Louis, et al.
Chemical Physics Impact (2023) Vol. 6, pp. 100234-100234
Open Access | Times Cited: 16
Ceria-Based Nanozymes in Point-of-Care Diagnosis: An Emerging Futuristic Approach for Biosensing
Ruixue Wang, Yuanyuan Du, Ying Fu, et al.
ACS Sensors (2023) Vol. 8, Iss. 12, pp. 4442-4467
Closed Access | Times Cited: 15
Manipulation of Diatomic Molecules with Oriented External Electric Fields: Linear Correlations in Atomic Properties Lead to Nonlinear Molecular Responses
Shahin Sowlati‐Hashjin, Mikko Karttunen, Chérif F. Matta
The Journal of Physical Chemistry A (2020) Vol. 124, Iss. 23, pp. 4720-4731
Open Access | Times Cited: 39
Design of Artificial Enzymes: Insights into Protein Scaffolds
Stefanie Hanreich, Elisa Bonandi, Ivana Drienovská
ChemBioChem (2022) Vol. 24, Iss. 6
Open Access | Times Cited: 22
Understanding Charge Dynamics in Dense Electronic Manifolds in Complex Environments
Fulvio Perrella, Alessio Petrone, Nadia Rega
Journal of Chemical Theory and Computation (2023) Vol. 19, Iss. 2, pp. 626-639
Open Access | Times Cited: 12
Electric field–assisted anion-π catalysis on carbon nanotubes in electrochemical microfluidic devices
M. Ángeles Gutiérrez López, Rojan Ali, Mei‐Ling Tan, et al.
Science Advances (2023) Vol. 9, Iss. 41
Open Access | Times Cited: 12
Harnessing generative AI to decode enzyme catalysis and evolution for enhanced engineering
Wen Jun Xie, Arieh Warshel
National Science Review (2023) Vol. 10, Iss. 12
Open Access | Times Cited: 11
Diels–Alder Reactions in Water Are Determined by Microsolvation
Luis Ruiz Pestana, Hongxia Hao, Teresa Head‐Gordon
Nano Letters (2019) Vol. 20, Iss. 1, pp. 606-611
Open Access | Times Cited: 41
The Role of Electrostatics in Enzymes: Do Biomolecular Force Fields Reflect Protein Electric Fields?
Richard T. Bradshaw, Jacek Dziedzic, Chris‐Kriton Skylaris, et al.
Journal of Chemical Information and Modeling (2020) Vol. 60, Iss. 6, pp. 3131-3144
Open Access | Times Cited: 37
An isolated water droplet in the aqueous solution of a supramolecular tetrahedral cage
Federico Sebastiani, Trandon A. Bender, Simone Pezzotti, et al.
Proceedings of the National Academy of Sciences (2020) Vol. 117, Iss. 52, pp. 32954-32961
Open Access | Times Cited: 37
A Critical Evaluation of Vibrational Stark Effect (VSE) Probes with the Local Vibrational Mode Theory
Niraj Verma, Peng Tao, Wenli Zou, et al.
Sensors (2020) Vol. 20, Iss. 8, pp. 2358-2358
Open Access | Times Cited: 36
Enhancing ade novoenzyme activity by computationally-focused ultra-low-throughput screening
Valeria A. Risso, Adrian Romero‐Rivera, Luis I. Gutierrez-Rus, et al.
Chemical Science (2020) Vol. 11, Iss. 24, pp. 6134-6148
Open Access | Times Cited: 35
Supramolecular enzyme-mimicking catalysts self-assembled from peptides
Qing Liu, Akinori Kuzuya, Zhen‐Gang Wang
iScience (2022) Vol. 26, Iss. 1, pp. 105831-105831
Open Access | Times Cited: 18
Hydrophobicity-Based Force Field In Enzymes
Irena Roterman, Leszek Konieczny, Katarzyna Stąpor, et al.
ACS Omega (2024)
Open Access | Times Cited: 3
Minimalist de Novo Design of Protein Catalysts
Liam R. Marshall, Oleksii Zozulia, Zsofia Lengyel‐Zhand, et al.
ACS Catalysis (2019) Vol. 9, Iss. 10, pp. 9265-9275
Open Access | Times Cited: 33
Globally optimal catalytic fields for a Diels–Alder reaction
Mark Dittner, Bernd Hartke
The Journal of Chemical Physics (2020) Vol. 152, Iss. 11
Closed Access | Times Cited: 29

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