OpenAlex Citation Counts

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:

Stairway to Stereoisomers: Engineering Short‐ and Medium‐Chain Ketoreductases To Produce Chiral Alcohols
Anirudh P. Shanbhag
ChemBioChem (2023) Vol. 24, Iss. 6
Closed Access | Times Cited: 16

Showing 16 citing articles:

Microbial alcohol dehydrogenases: recent developments and applications in asymmetric synthesis
Anju Chadha, Santosh Kumar Padhi, S. Stella, et al.
Organic & Biomolecular Chemistry (2023) Vol. 22, Iss. 2, pp. 228-251
Closed Access | Times Cited: 17

Classification and functional origins of stereocomplementary alcohol dehydrogenases for asymmetric synthesis of chiral secondary alcohols: A review
Lu Zhang, Zewen Sun, Guochao Xu, et al.
International Journal of Biological Macromolecules (2024) Vol. 270, pp. 132238-132238
Closed Access | Times Cited: 7

Enantioselective transformation of phytoplankton-derived dihydroxypropanesulfonate by marine bacteria
Le Liu, Xiang Gao, Changjie Dong, et al.
The ISME Journal (2024) Vol. 18, Iss. 1
Open Access | Times Cited: 4

Unraveling the substrate-binding pocket: Endowing carbonyl reductase BaSDRX with intriguing inconsistent stereoselectivity towards similar structured β-Ketoesters
Aipeng Li, Shuqi Guo, Xinying Wang, et al.
International Journal of Biological Macromolecules (2025) Vol. 306, pp. 141591-141591
Closed Access

SubTuner leverages physics-based modeling to complement AI in enzyme engineering toward non-native substrates
Qianzhen Shao, Asher C. Hollenbeak, Yaoyukun Jiang, et al.
Chem Catalysis (2025), pp. 101334-101334
Closed Access

Reduction of C=O to CH-OH Using Enzymes and Microorganisms
Federico Rossi, Matteo Aleotti, Mélanie Hall
Elsevier eBooks (2025)
Closed Access

The Molecular Basis of Catalysis by SDR Family Members Ketoacyl‐ACP Reductase FabG and Enoyl‐ACP Reductase FabI in Type‐II Fatty Acid Biosynthesis
Jiashen Zhou, Lin Zhang, Yiran Wang, et al.
Angewandte Chemie International Edition (2023) Vol. 62, Iss. 46
Open Access | Times Cited: 10

Directed Evolution and Immobilization of Lactobacillus brevis Alcohol Dehydrogenase for Chemo‐Enzymatic Synthesis of Rivastigmine
Guorong Su, Ran Lu, Chang Liu, et al.
Chemistry - A European Journal (2024) Vol. 30, Iss. 32
Closed Access | Times Cited: 3

Biocatalysis with Unconventional Yeasts
Cecilia Andreu, Marcel·lí del Olmo
Catalysts (2024) Vol. 14, Iss. 11, pp. 767-767
Open Access | Times Cited: 1

Design of a Self-Sufficient Whole-Cell Cascade for the Production of (R)-Citronellal from Geraniol
Guoxiang Ma, Xiangyu Zhu, Dongxin Zhang, et al.
Journal of Agricultural and Food Chemistry (2024) Vol. 72, Iss. 47, pp. 26305-26315
Closed Access | Times Cited: 1

Two anti‐Prelog NAD‐Dependent Alcohol Dehydrogenases with Broad Substrate Scope and Excellent Enantioselectivity
Matteo Damian, Francesco G. Mutti
European Journal of Organic Chemistry (2023) Vol. 26, Iss. 47
Open Access | Times Cited: 2

Asymmetric Synthesis of Chiral Benzoins Enabled by Engineered Ketoreductase-Catalyzed Stereoselective Reduction of Benzils
Yangtian Ye, Yuan Tao, Pan Hu, et al.
ACS Sustainable Chemistry & Engineering (2024) Vol. 12, Iss. 31, pp. 11605-11612
Closed Access

Substrate expansion of Geotrichum candidum alcohol dehydrogenase towards diaryl ketones by mutation
Zhongyao Tang, Yui Takagi, Afifa Ayu Koesoema, et al.
Applied Microbiology and Biotechnology (2024) Vol. 108, Iss. 1
Open Access

Reducing the vicissitudes of heterologous prochiral substrate catalysis by alcohol dehydrogenases through machine learning algorithms
Arindam Ghatak, Anirudh P. Shanbhag, Santanu Datta
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access

Reducing the vicissitudes of heterologous prochiral substrate catalysis by alcohol dehydrogenases through machine learning algorithms
Arindam Ghatak, Anirudh P. Shanbhag, Santanu Datta
Biochemical and Biophysical Research Communications (2023) Vol. 691, pp. 149298-149298
Open Access

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Requested Article:

Showing 16 citing articles:

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