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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:

Equatorial Active Site Compaction and Electrostatic Reorganization in Catechol-O-methyltransferase
Sylwia Czarnota, Linus O. Johannissen, Nicola J. Baxter, et al.
ACS Catalysis (2019) Vol. 9, Iss. 5, pp. 4394-4401
Open Access | Times Cited: 22

Showing 22 citing articles:

Recent developments in molecular docking technology applied in food science: a review
Xuan Tao, Yukun Huang, Chong Wang, et al.
International Journal of Food Science & Technology (2019) Vol. 55, Iss. 1, pp. 33-45
Closed Access | Times Cited: 163
Methyltransferases: Functions and Applications
Eman M. M. Abdelraheem, Benjamin Thair, Romina Fernández Varela, et al.
ChemBioChem (2022) Vol. 23, Iss. 18
Open Access | Times Cited: 80
Synthetic Reagents for Enzyme‐Catalyzed Methylation
Xiaojin Wen, Florian Leisinger, Viviane Leopold, et al.
Angewandte Chemie International Edition (2022) Vol. 61, Iss. 41
Open Access | Times Cited: 35
Protein Dynamics and Enzymatic Catalysis
Steven D. Schwartz
The Journal of Physical Chemistry B (2023) Vol. 127, Iss. 12, pp. 2649-2660
Open Access | Times Cited: 31
Bridging the gap between theory and treatment: Transition metal complexes as successful candidates in medicine
Sara Abdolmaleki, Alireza Aliabadi, Samad Khaksar
Coordination Chemistry Reviews (2025) Vol. 531, pp. 216477-216477
Closed Access
Characterization of two O-methyltransferases involved in the biosynthesis of O-methylated catechins in tea plant
Ji-Qiang Jin, Fu-Rong Qu, Huisi Huang, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 18
Functional roles of enzyme dynamics in accelerating active site chemistry: Emerging techniques and changing concepts
Shuaihua Gao, Judith P. Klinman
Current Opinion in Structural Biology (2022) Vol. 75, pp. 102434-102434
Open Access | Times Cited: 25
Enzymatic Fluoromethylation Enabled by the S-Adenosylmethionine Analog Te-Adenosyl-L-(fluoromethyl)homotellurocysteine
Syam Sundar Neti, Bo Wang, David F. Iwig, et al.
ACS Central Science (2023) Vol. 9, Iss. 5, pp. 905-914
Open Access | Times Cited: 13
Quantum Mechanical Description of Electrostatics Provides a Unified Picture of Catalytic Action Across Methyltransferases
Zhongyue Yang, Fang Liu, Adam H. Steeves, et al.
The Journal of Physical Chemistry Letters (2019) Vol. 10, Iss. 13, pp. 3779-3787
Open Access | Times Cited: 26
Hydrogen–Deuterium Exchange within Adenosine Deaminase, a TIM Barrel Hydrolase, Identifies Networks for Thermal Activation of Catalysis
Shuaihua Gao, Emily J. Thompson, Samuel L. Barrow, et al.
Journal of the American Chemical Society (2020) Vol. 142, Iss. 47, pp. 19936-19949
Open Access | Times Cited: 25
Hydrogen deuterium exchange defines catalytically linked regions of protein flexibility in the catechol O -methyltransferase reaction
Jianyu Zhang, Jeremy L. Balsbaugh, Shuaihua Gao, et al.
Proceedings of the National Academy of Sciences (2020) Vol. 117, Iss. 20, pp. 10797-10805
Open Access | Times Cited: 24
Computationally designedp-coumaric acid analogs: searching for neuroprotective antioxidants
Miguel Reina, Eduardo Gabriel Guzmán‐López, Isabella Romeo, et al.
New Journal of Chemistry (2021) Vol. 45, Iss. 32, pp. 14369-14380
Closed Access | Times Cited: 14
Structural and Computational Analyses of the Unique Interactions of Opicapone in the Binding Pocket of Catechol O-Methyltransferase: A Crystallographic Study and Fragment Molecular Orbital Analyses
Katsuki Takebe, Mamoru Suzuki, Takao Kuwada-Kusunose, et al.
Journal of Chemical Information and Modeling (2023) Vol. 63, Iss. 14, pp. 4468-4476
Closed Access | Times Cited: 5
The Catechol O-Methyltransferase Inhibitor Entacapone in the Treatment of Parkinson’s Disease: Personal Reflections on a First-in-Class Drug Development Programme 40 Years On
Pekka T. Männistö, Tapani Keränen, Kari Reinikainen, et al.
Neurology and Therapy (2024) Vol. 13, Iss. 4, pp. 1039-1054
Open Access | Times Cited: 1
Metalloenzyme mechanisms correlated to their turnover number and metal lability
Caio B. Castro, Millena P. Ferreira, Caterina G. C. Marques Netto
Current Research in Chemical Biology (2021) Vol. 1, pp. 100004-100004
Open Access | Times Cited: 11
Examining the Origin of Catalytic Power of Catechol O-Methyltransferase
Xi Chen, Steven D. Schwartz
ACS Catalysis (2019) Vol. 9, Iss. 11, pp. 9870-9879
Open Access | Times Cited: 13
Regioselectivity Inversion of an O‐Methyltransferase via Semi‐rational Mutagenesis Combined with Metal Ion Substitution
Ying Su, Hai‐Peng Li, Man Zhang, et al.
ChemCatChem (2022) Vol. 14, Iss. 23
Closed Access | Times Cited: 7
Crystal Structure and Regiospecificity of Catechol O-Methyltransferase from Niastella koreensis
Seul Hoo Lee, Bongsang Kim, Kyung‐Jin Kim
Journal of Agricultural and Food Chemistry (2021) Vol. 69, Iss. 8, pp. 2531-2538
Closed Access | Times Cited: 9
Discovery of Small Molecules as Membrane-Bound Catechol-O-methyltransferase Inhibitors with Interest in Parkinson’s Disease: Pharmacophore Modeling, Molecular Docking and In Vitro Experimental Validation Studies
Pedro Cruz-Vicente, Ana M. Gonçalves, Octávio Ferreira, et al.
Pharmaceuticals (2021) Vol. 15, Iss. 1, pp. 51-51
Open Access | Times Cited: 7
Multisubstrate‐based system: a kinetic mechanism study of catechol‐O‐methyltransferase
Fangyuan Wang, Xianglu Zhou, Haonan Wang, et al.
FEBS Journal (2024)
Closed Access
Nano-second protein dynamics of key residue at Position 38 in catechol-O-methyltransferase system: a time-resolved fluorescence study
Fan Liu, Jianyu Zhang
The Journal of Biochemistry (2020) Vol. 168, Iss. 4, pp. 417-425
Closed Access | Times Cited: 4
Transition-State Vibrational Analysis and Isotope Effects for COMT-Catalyzed Methyl Transfer
Maite Roca, Ian H. Williams
Journal of the American Chemical Society (2020) Vol. 142, Iss. 36, pp. 15548-15559
Open Access | Times Cited: 4
Synthetic Reagents for Enzyme‐Catalyzed Methylation
Xiaojin Wen, Florian Leisinger, Viviane Leopold, et al.
Angewandte Chemie (2022) Vol. 134, Iss. 41
Closed Access | Times Cited: 2
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