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.

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Showing 1-25 of 27 citing articles:

The Quantum Chemical Cluster Approach in Biocatalysis
Xiang Sheng, Fahmi Himo
Accounts of Chemical Research (2023) Vol. 56, Iss. 8, pp. 938-947
Open Access | Times Cited: 54

An Active Site Tyr Residue Guides the Regioselectivity of Lysine Hydroxylation by Nonheme Iron Lysine-4-hydroxylase Enzymes through Proton-Coupled Electron Transfer
Yuanxin Cao, Sam Hay, Sam P. de Visser
Journal of the American Chemical Society (2024) Vol. 146, Iss. 17, pp. 11726-11739
Open Access | Times Cited: 10

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

Computer-aided understanding and engineering of enzymatic selectivity
Lunjie Wu, Lei Qin, Yao Nie, et al.
Biotechnology Advances (2021) Vol. 54, pp. 107793-107793
Closed Access | Times Cited: 43

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: 41

Yeast Platforms for Production and Screening of Bioactive Derivatives of Rauwolscine
Samuel A. Bradley, Frederik G. Hansson, Beata Joanna Lehka, et al.
ACS Synthetic Biology (2024) Vol. 13, Iss. 5, pp. 1498-1512
Closed Access | Times Cited: 3

The role of biocatalysis in the asymmetric synthesis of alkaloids – an update
Emmanuel Cigan, Bettina Eggbauer, Joerg H. Schrittwieser, et al.
RSC Advances (2021) Vol. 11, Iss. 45, pp. 28223-28270
Open Access | Times Cited: 26

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

Metabolic engineering of yeast for de novo production of kratom monoterpene indole alkaloids
M Holtz, Daniela Rago, Ida Nedermark, et al.
Metabolic Engineering (2024) Vol. 86, pp. 135-146
Closed Access | Times Cited: 2

Directed Biosynthesis of New to Nature Alkaloids in a Heterologous Nicotiana benthamiana Expression Host
Marianna Boccia, Dagny Grzech, Adriana A. Lopes, et al.
Frontiers in Plant Science (2022) Vol. 13
Open Access | Times Cited: 10

Pentafluorophenol (C6F5OH) Catalyzed Pictet‐Spengler Reaction: A Facile and Metal‐Free Approach Towards Tetrahydro‐β‐Carbolines
Rina Mahato, Chinmoy Kumar Hazra
Chemistry - A European Journal (2023) Vol. 29, Iss. 27
Closed Access | Times Cited: 5

Highly Acidic Electron-Rich Brønsted Acids Accelerate Asymmetric Pictet–Spengler Reactions by Virtue of Stabilizing Cation–π Interactions
Manuel J. Scharf, Nobuya Tsuji, Monika M. Lindner, et al.
Journal of the American Chemical Society (2024)
Open Access | Times Cited: 1

Computational Study of Mechanism and Enantioselectivity of Imine Reductase from Amycolatopsis orientalis
Mario Prejanò, Xiang Sheng, Fahmi Himo
ChemistryOpen (2021) Vol. 11, Iss. 1
Open Access | Times Cited: 9

Construction of an artificial phosphoketolase pathway that efficiently catabolizes multiple carbon sources to acetyl-CoA
Yiqun Yang, Yuwan Liu, Haodong Zhao, et al.
PLoS Biology (2023) Vol. 21, Iss. 9, pp. e3002285-e3002285
Open Access | Times Cited: 3

Chemoenzymatic synthesis of natural products using plant biocatalysts
Helena H. Chubatsu Nunes, Trinh-Don Nguyen, Thu‐Thuy T. Dang
Current Opinion in Green and Sustainable Chemistry (2022) Vol. 35, pp. 100627-100627
Closed Access | Times Cited: 5

Gene coexpression networks allow the discovery of two strictosidine synthases underlying monoterpene indole alkaloid biosynthesis in Uncaria rhynchophylla
Chengxi Jiang, Jia-xing Yu, Xuan Fei, et al.
International Journal of Biological Macromolecules (2022) Vol. 226, pp. 1360-1373
Closed Access | Times Cited: 5

Elucidation of the 1-phenethylisoquinoline pathway from an endemic conifer Cephalotaxus hainanensis
Fei Qiao, Yuedong He, Yuhao Zhang, et al.
Proceedings of the National Academy of Sciences (2022) Vol. 120, Iss. 1
Open Access | Times Cited: 5

Binding order and apparent binding affinity in the bisubstrate activity of strictosidine synthase
Kulhar Nitin, Eerappa Rajakumara
Journal of Biomolecular Structure and Dynamics (2023) Vol. 41, Iss. 24, pp. 15634-15646
Closed Access | Times Cited: 2

Proxy-approach in understanding the bisubstrate activity of strictosidine synthases
Kulhar Nitin, Eerappa Rajakumara
International Journal of Biological Macromolecules (2024) Vol. 262, pp. 130091-130091
Closed Access

Computational mechanistic investigation of the kinetic resolution of α-methyl-phenylacetaldehyde by norcoclaurine synthase
Shiqing Zhang, Chenghua Zhang, Aijing Guo, et al.
Communications Chemistry (2024) Vol. 7, Iss. 1
Open Access

Study of stereocontrol in enzymatic reactions using atomic models and computational methods
Daniel Platero-Rochart, Pedro A. Sánchez‐Murcia
Elsevier eBooks (2024), pp. 65-99
Closed Access

Metabolic engineering of yeast forde novoproduction of kratom monoterpene indole alkaloids
M Holtz, Daniela Rago, Ida Nedermark, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access

β-Methyltryptamine Provoking the Crucial Role of Strictosidine Synthase Tyr151-OH for Its Stereoselective Pictet−Spengler Reactions to Tryptoline-type Alkaloids
Haicheng Liu, Santosh Panjikar, Xiang Sheng, et al.
ACS Chemical Biology (2022) Vol. 17, Iss. 1, pp. 187-197
Closed Access | Times Cited: 3

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