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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:

Does Substrate Positioning Affect the Selectivity and Reactivity in the Hectochlorin Biosynthesis Halogenase?
Amy Timmins, Nicholas Fowler, Jim Warwicker, et al.
Frontiers in Chemistry (2018) Vol. 6
Open Access | Times Cited: 45

Showing 1-25 of 45 citing articles:

Enzyme function prediction using contrastive learning
Tianhao Yu, Haiyang Cui, Jianan Canal Li, et al.
Science (2023) Vol. 379, Iss. 6639, pp. 1358-1363
Closed Access | Times Cited: 164
The Diversity of Cyanobacterial Toxins on Structural Characterization, Distribution and Identification: A Systematic Review
Xingde Du, Haohao Liu, Le Yuan, et al.
Toxins (2019) Vol. 11, Iss. 9, pp. 530-530
Open Access | Times Cited: 153
Second‐Coordination Sphere Effects on Selectivity and Specificity of Heme and Nonheme Iron Enzymes
Sam P. de Visser
Chemistry - A European Journal (2019) Vol. 26, Iss. 24, pp. 5308-5327
Open Access | Times Cited: 94
Catalytic Mechanism of Aromatic Nitration by Cytochrome P450 TxtE: Involvement of a Ferric-Peroxynitrite Intermediate
Savvas Louka, Sarah M. Barry, Derren J. Heyes, et al.
Journal of the American Chemical Society (2020) Vol. 142, Iss. 37, pp. 15764-15779
Open Access | Times Cited: 81
Inspiration from Nature: Influence of Engineered Ligand Scaffolds and Auxiliary Factors on the Reactivity of Biomimetic Oxidants
Gourab Mukherjee, Jagnyesh Kumar Satpathy, Umesh Kumar Bagha, et al.
ACS Catalysis (2021) Vol. 11, Iss. 15, pp. 9761-9797
Closed Access | Times Cited: 73
What Drives Radical Halogenation versus Hydroxylation in Mononuclear Nonheme Iron Complexes? A Combined Experimental and Computational Study
Emilie F. Gérard, Vishal Yadav, David P. Goldberg, et al.
Journal of the American Chemical Society (2022) Vol. 144, Iss. 24, pp. 10752-10767
Open Access | Times Cited: 43
Multiscale QM/MM modelling of catalytic systems with ChemShell
You Lü, Kakali Sen, Chin W. Yong, et al.
Physical Chemistry Chemical Physics (2023) Vol. 25, Iss. 33, pp. 21816-21835
Open Access | Times Cited: 29
Mechanistic Insights into Substrate Positioning That Distinguish Non-heme Fe(II)/α-Ketoglutarate-Dependent Halogenases and Hydroxylases
David W. Kastner, Aditya Nandy, Rimsha Mehmood, et al.
ACS Catalysis (2023) Vol. 13, Iss. 4, pp. 2489-2501
Closed Access | Times Cited: 27
A Comparative Review on the Catalytic Mechanism of Nonheme Iron Hydroxylases and Halogenases
Amy Timmins, Sam P. de Visser
Catalysts (2018) Vol. 8, Iss. 8, pp. 314-314
Open Access | Times Cited: 68
Negative catalysis / non-Bell-Evans-Polanyi reactivity by metalloenzymes: Examples from mononuclear heme and non-heme iron oxygenases
Sam P. de Visser, Yen‐Ting Lin, Hafiz Saqib Ali, et al.
Coordination Chemistry Reviews (2021) Vol. 439, pp. 213914-213914
Closed Access | Times Cited: 49
How Do Electrostatic Perturbations of the Protein Affect the Bifurcation Pathways of Substrate Hydroxylation versus Desaturation in the Nonheme Iron-Dependent Viomycin Biosynthesis Enzyme?
Hafiz Saqib Ali, Richard H. Henchman, Jim Warwicker, et al.
The Journal of Physical Chemistry A (2021) Vol. 125, Iss. 8, pp. 1720-1737
Closed Access | Times Cited: 42
How Is Substrate Halogenation Triggered by the Vanadium Haloperoxidase from Curvularia inaequalis?
Emilie F. Gérard, Thirakorn Mokkawes, Linus O. Johannissen, et al.
ACS Catalysis (2023) Vol. 13, Iss. 12, pp. 8247-8261
Open Access | Times Cited: 17
Unusual catalytic strategy by non-heme Fe(ii)/2-oxoglutarate-dependent aspartyl hydroxylase AspH
Anandhu Krishnan, Sodiq O. Waheed, Ann Varghese, et al.
Chemical Science (2024) Vol. 15, Iss. 10, pp. 3466-3484
Open Access | Times Cited: 6
Conformational Isomerization of the Fe(III)–OH Species Enables Selective Halogenation in Carrier-Protein-Independent Halogenase BesD and Hydroxylase-Evolved Halogenase
Xin Zhang, Yifan Li, Wenli Yuan, et al.
ACS Catalysis (2024) Vol. 14, Iss. 12, pp. 9342-9353
Closed Access | Times Cited: 6
Lignin Biodegradation by a Cytochrome P450 Enzyme: A Computational Study into Syringol Activation by GcoA
Hafiz Saqib Ali, Richard H. Henchman, Sam P. de Visser
Chemistry - A European Journal (2020) Vol. 26, Iss. 57, pp. 13093-13102
Open Access | Times Cited: 43
Determining the Inherent Selectivity for Carbon Radical Hydroxylation versus Halogenation with FeIII(OH)(X) Complexes: Relevance to the Rebound Step in Non-heme Iron Halogenases
Vishal Yadav, Rodolfo J. Rodriguez, Maxime A. Siegler, et al.
Journal of the American Chemical Society (2020) Vol. 142, Iss. 16, pp. 7259-7264
Open Access | Times Cited: 41
Spectroscopically Guided Simulations Reveal Distinct Strategies for Positioning Substrates to Achieve Selectivity in Nonheme Fe(II)/α-Ketoglutarate-Dependent Halogenases
Rimsha Mehmood, Vyshnavi Vennelakanti, Heather J. Kulik
ACS Catalysis (2021) Vol. 11, Iss. 19, pp. 12394-12408
Closed Access | Times Cited: 34
Re‐Programming and Optimization of aL‐Prolinecis‐4‐Hydroxylase for thecis‐3‐Halogenation of its Native Substrate
Athena Papadopoulou, Jasmin Meierhofer, Fabian Meyer, et al.
ChemCatChem (2021) Vol. 13, Iss. 18, pp. 3914-3919
Open Access | Times Cited: 32
Properties of the Reactants and Their Interactions within and with the Enzyme Binding Cavity Determine Reaction Selectivities. The Case of Fe(II)/2‐Oxoglutarate Dependent Enzymes
Zuzanna Wojdyła, Tomasz Borowski
Chemistry - A European Journal (2022) Vol. 28, Iss. 18
Closed Access | Times Cited: 23
The Protein’s Role in Substrate Positioning and Reactivity for Biosynthetic Enzyme Complexes: The Case of SyrB2/SyrB1
Rimsha Mehmood, Helena W. Qi, Adam H. Steeves, et al.
ACS Catalysis (2019) Vol. 9, Iss. 6, pp. 4930-4943
Open Access | Times Cited: 39
Catalytic divergencies in the mechanism of L-arginine hydroxylating nonheme iron enzymes
Hafiz Saqib Ali, Sam P. de Visser
Frontiers in Chemistry (2024) Vol. 12
Open Access | Times Cited: 3
Bioengineering of Cytochrome P450 OleTJE: How Does Substrate Positioning Affect the Product Distributions?
Fabián G. Cantú Reinhard, Yen‐Ting Lin, Agnieszka Stańczak, et al.
Molecules (2020) Vol. 25, Iss. 11, pp. 2675-2675
Open Access | Times Cited: 29
Halogenases for biosynthetic pathway engineering: Toward new routes to naturals and non-naturals
Binuraj R. K. Menon, Daniel Richmond, Navya Menon
Catalysis Reviews (2020) Vol. 64, Iss. 3, pp. 533-591
Open Access | Times Cited: 28
Electrostatically Regulated Active Site Assembly Governs Reactivity in Nonheme Iron Halogenases
Elizabeth R. Smithwick, R. Hunter Wilson, Sourav Chatterjee, et al.
ACS Catalysis (2023) Vol. 13, Iss. 20, pp. 13743-13755
Open Access | Times Cited: 9
Can a Mononuclear Iron(III)‐Superoxo Active Site Catalyze the Decarboxylation of Dodecanoic Acid in UndA to Produce Biofuels?
Yen‐Ting Lin, Agnieszka Stańczak, Yulian T. Manchev, et al.
Chemistry - A European Journal (2019) Vol. 26, Iss. 10, pp. 2233-2242
Open Access | Times Cited: 29
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