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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 51-75 of 172 citing articles:

Artificial enzymes bringing together computational design and directed evolution
Beatriz de Pina Mariz, Sara Carvalho, Íris L. Batalha, et al.
Organic & Biomolecular Chemistry (2021) Vol. 19, Iss. 9, pp. 1915-1925
Closed Access | Times Cited: 25
Fast and Simple Evaluation of the Catalysis and Selectivity Induced by External Electric Fields
Pau Besalú‐Sala, Miquel Solà, Josep M. Luis, et al.
ACS Catalysis (2021) Vol. 11, Iss. 23, pp. 14467-14479
Open Access | Times Cited: 25
Biocatalytic Baeyer–Villiger Reactions: Uncovering the Source of Regioselectivity at Each Evolutionary Stage of a Mutant with Scrutiny of Fleeting Chiral Intermediates
Yijie Dong, Tang Li, Shiqing Zhang, et al.
ACS Catalysis (2022) Vol. 12, Iss. 6, pp. 3669-3680
Closed Access | Times Cited: 17
Switchable Enzyme-mimicking catalysts Self-Assembled from de novo designed peptides and DNA G-quadruplex/hemin complex
Qiao Teng, Haifeng Wu, Hao Sun, et al.
Journal of Colloid and Interface Science (2022) Vol. 628, pp. 1004-1011
Closed Access | Times Cited: 17
Role of Enzyme and Active Site Conformational Dynamics in the Catalysis by α-Amylase Explored with QM/MM Molecular Dynamics
Rui P. P. Neves, Pedro Alexandrino Fernandes, Maria J. Ramos
Journal of Chemical Information and Modeling (2022) Vol. 62, Iss. 15, pp. 3638-3650
Open Access | Times Cited: 16
Modern computational methods for rational enzyme engineering
Pedro Ferreira, Pedro Alexandrino Fernandes, Maria J. Ramos
Chem Catalysis (2022) Vol. 2, Iss. 10, pp. 2481-2498
Open Access | Times Cited: 16
Natural Evolution Provides Strong Hints about Laboratory Evolution of Designer Enzymes
Wen Jun Xie, Arieh Warshel
Proceedings of the National Academy of Sciences (2022) Vol. 119, Iss. 31
Open Access | Times Cited: 15
Reactivity and Selectivity of the Diels–Alder Reaction of Anthracene in [Pd6L4]12+ Supramolecular Cages: A Computational Study
Xin‐Rui Mao, Qian Wang, Shuping Zhuo, et al.
Inorganic Chemistry (2023) Vol. 62, Iss. 10, pp. 4330-4340
Closed Access | Times Cited: 9
Mutexa: A Computational Ecosystem for Intelligent Protein Engineering
Zhongyue Yang, Qianzhen Shao, Yaoyukun Jiang, et al.
Journal of Chemical Theory and Computation (2023) Vol. 19, Iss. 21, pp. 7459-7477
Open Access | Times Cited: 9
A simple and consistent quantum‐chemical fragmentation scheme for proteins that includes two‐body contributions
Johannes R. Vornweg, Mario Wolter, Christoph R. Jacob
Journal of Computational Chemistry (2023) Vol. 44, Iss. 18, pp. 1634-1644
Open Access | Times Cited: 8
QM/MM Modeling Aided Enzyme Engineering in Natural Products Biosynthesis
Fan Zhang, Tao Zeng, Ruibo Wu
Journal of Chemical Information and Modeling (2023) Vol. 63, Iss. 16, pp. 5018-5034
Closed Access | Times Cited: 8
Mechanisms and Opportunities for Rational In Silico Design of Enzymes to Degrade Per- and Polyfluoroalkyl Substances (PFAS)
Melissa Marciesky, Diana S. Aga, Ian Bradley, et al.
Journal of Chemical Information and Modeling (2023) Vol. 63, Iss. 23, pp. 7299-7319
Open Access | Times Cited: 8
Optimizing the Solvent Reorganization Free Energy by Metal Substitution for Nanocage Catalysis
Wan‐Lu Li, Hongxia Hao, Teresa Head‐Gordon
ACS Catalysis (2022) Vol. 12, Iss. 7, pp. 3782-3788
Open Access | Times Cited: 14
Molecular Dynamics-Derived Descriptor Informs the Impact of Mutation on the Catalytic Turnover Number in Lactonase Across Substrates
Yaoyukun Jiang, Bailu Yan, Yu Chen, et al.
The Journal of Physical Chemistry B (2022) Vol. 126, Iss. 13, pp. 2486-2495
Closed Access | Times Cited: 13
Ultrafast photo-induced processes in complex environments: The role of accuracy in excited-state energy potentials and initial conditions
Alessio Petrone, Fulvio Perrella, Federico Coppola, et al.
Chemical Physics Reviews (2022) Vol. 3, Iss. 2
Open Access | Times Cited: 13
CO bonding in hexa‐ and pentacoordinate carboxy‐neuroglobin: A quantum mechanics/molecular mechanics and local vibrational mode study
Marek Freindorf, Alexis Antoinette Ann Delgado, Elfi Kraka
Journal of Computational Chemistry (2022) Vol. 43, Iss. 25, pp. 1725-1746
Closed Access | Times Cited: 13
Chemical transformations and transport phenomena at interfaces
Hongxia Hao, Luis Ruiz Pestana, Jin Qian, et al.
Wiley Interdisciplinary Reviews Computational Molecular Science (2022) Vol. 13, Iss. 2
Open Access | Times Cited: 13
Chicken fat for catalysis: a scaffold is as important for molecular complexes for energy transformations as it is for enzymes in catalytic function
Joseph A. Laureanti, Molly O’Hagan, Wendy J. Shaw
Sustainable Energy & Fuels (2019) Vol. 3, Iss. 12, pp. 3260-3278
Closed Access | Times Cited: 22
Unraveling the energetic significance of chemical events in enzyme catalysis via machine-learning based regression approach
Zilin Song, Hong-Yu Zhou, Hao Tian, et al.
Communications Chemistry (2020) Vol. 3, Iss. 1
Open Access | Times Cited: 20
Going Beyond the Local Catalytic Activity Space of Chitinase Using a Simulation-Based Iterative Saturation Mutagenesis Strategy
Jinlong Li, Sijia Wang, Cui Liu, et al.
ACS Catalysis (2022) Vol. 12, Iss. 16, pp. 10235-10244
Closed Access | Times Cited: 12
Prediction of Enzyme Catalysis by Computing Reaction Energy Barriers via Steered QM/MM Molecular Dynamics Simulations and Machine Learning
Daniel Platero-Rochart, Tatyana Krivobokova, Michael Gastegger, et al.
Journal of Chemical Information and Modeling (2023) Vol. 63, Iss. 15, pp. 4623-4632
Closed Access | Times Cited: 6
Enzymes to unravel bioproducts architecture
Claire Bourlieu‐Lacanal, Thierry Astruc, Sophie Barbe, et al.
Biotechnology Advances (2020) Vol. 41, pp. 107546-107546
Open Access | Times Cited: 19
Geometry of Charge Density as a Reporter on the Role of the Protein Scaffold in Enzymatic Catalysis: Electrostatic Preorganization and Beyond
Mark E. Eberhart, Timothy Wilson, Nathaniel W. Johnston, et al.
Journal of Chemical Theory and Computation (2022) Vol. 19, Iss. 3, pp. 694-704
Open Access | Times Cited: 11
A protein sequence fitness function for identifying natural and nonnatural proteins
Rahul Kaushik, Kam Y. J. Zhang
Proteins Structure Function and Bioinformatics (2020) Vol. 88, Iss. 10, pp. 1271-1284
Open Access | Times Cited: 17
Physics-Based Computational Protein Design: An Update
David Mignon, Karen Druart, Eleni Michael, et al.
The Journal of Physical Chemistry A (2020) Vol. 124, Iss. 51, pp. 10637-10648
Closed Access | Times Cited: 17

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