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:

Multifunctional biocatalyst for conjugate reduction and reductive amination
Thomas W. Thorpe, James R. Marshall, Vanessa Harawa, et al.
Nature (2022) Vol. 604, Iss. 7904, pp. 86-91
Open Access | Times Cited: 93

Showing 1-25 of 93 citing articles:

Enantioconvergent Cu-catalysed N-alkylation of aliphatic amines
Ji‐Jun Chen, Jia‐Heng Fang, Xuan‐Yi Du, et al.
Nature (2023) Vol. 618, Iss. 7964, pp. 294-300
Closed Access | Times Cited: 83

Discovery of an Imine Reductase for Reductive Amination of Carbonyl Compounds with Sterically Challenging Amines
Fei‐Fei Chen, Xuefeng He, Xin-Xin Zhu, et al.
Journal of the American Chemical Society (2023) Vol. 145, Iss. 7, pp. 4015-4025
Closed Access | Times Cited: 43

General (hetero)polyaryl amine synthesis via multicomponent cycloaromatization of amines
Lebin Su, Jianyu Dong, Yangyang Shen, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access | Times Cited: 1

Reductive aminations by imine reductases: from milligrams to tons
Amelia K. Gilio, Thomas W. Thorpe, Nicholas J. Turner, et al.
Chemical Science (2022) Vol. 13, Iss. 17, pp. 4697-4713
Open Access | Times Cited: 54

Emerging Technologies for Biocatalysis in the Pharmaceutical Industry
Russell D. Lewis, Scott P. France, Carlos A. Martínez
ACS Catalysis (2023) Vol. 13, Iss. 8, pp. 5571-5577
Open Access | Times Cited: 25

Biocatalytic reductive aminations with NAD(P)H-dependent enzymes: enzyme discovery, engineering and synthetic applications
Bo Yuan, Dameng Yang, Ge Qu, et al.
Chemical Society Reviews (2023) Vol. 53, Iss. 1, pp. 227-262
Closed Access | Times Cited: 23

Multifunctional Biocatalysts for Organic Synthesis
Thomas W. Thorpe, James R. Marshall, Nicholas J. Turner
Journal of the American Chemical Society (2024) Vol. 146, Iss. 12, pp. 7876-7884
Open Access | Times Cited: 9

Modular Access to Chiral Amines via Imine Reductase-Based Photoenzymatic Catalysis
Bin Chen, Renjie Li, Jianqiang Feng, et al.
Journal of the American Chemical Society (2024) Vol. 146, Iss. 20, pp. 14278-14286
Closed Access | Times Cited: 7

Unlocking New Reactivities in Enzymes by Iminium Catalysis
Guangcai Xu, Gerrit J. Poelarends
Angewandte Chemie International Edition (2022) Vol. 61, Iss. 30
Open Access | Times Cited: 29

Engineered Imine Reductase for Larotrectinib Intermediate Manufacture
Qi Chen, Bo-Bo Li, Lilan Zhang, et al.
ACS Catalysis (2022) Vol. 12, Iss. 23, pp. 14795-14803
Closed Access | Times Cited: 29

Synthesis of Stereoenriched Piperidines via Chemo-Enzymatic Dearomatization of Activated Pyridines
Vanessa Harawa, Thomas W. Thorpe, James R. Marshall, et al.
Journal of the American Chemical Society (2022) Vol. 144, Iss. 46, pp. 21088-21095
Open Access | Times Cited: 27

Active and stable alcohol dehydrogenase-assembled hydrogels via synergistic bridging of triazoles and metal ions
Qiang Chen, Ge Qu, Xu Li, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 17

One-Pot Chemoenzymatic Cascade for the Enantioselective C(1)-Allylation of Tetrahydroisoquinolines
Jack J. Sangster, Rebecca E. Ruscoe, Sebastian C. Cosgrove, et al.
Journal of the American Chemical Society (2023) Vol. 145, Iss. 8, pp. 4431-4437
Open Access | Times Cited: 16

Structure-guided semi-rational design of an imine reductase for enantio-complementary synthesis of pyrrolidinamine
Jun Zhang, Yaqing Ma, Fangfang Zhu, et al.
Chemical Science (2023) Vol. 14, Iss. 16, pp. 4265-4272
Open Access | Times Cited: 15

Imine Reductases and Reductive Aminases in Organic Synthesis
Godwin A. Aleku
ACS Catalysis (2024), pp. 14308-14329
Open Access | Times Cited: 5

Access to Axially Chiral Biaryl Benzylamines via Ancestral Enzyme-Enabled Reductive Amination Desymmetrization
W. Jim Zheng, Xinxin Zhu, Zheng Zhu, et al.
ACS Catalysis (2025) Vol. 15, Iss. 3, pp. 1522-1531
Closed Access

Mutagenesis of a Single Site Inverts the Stereopreference of Imine Reductase
Yitong Li, Yunyun Yang, Mengting Zhang, et al.
ACS Catalysis (2025) Vol. 15, Iss. 3, pp. 2192-2199
Closed Access

Biocatalytic enantioselective formation and ring-opening of oxetanes
Xia Hua, Yuanfei Wang, Xiao Jin, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access

Direct carbonyl reductive functionalizations by diphenylphosphine oxide
Feng Liu, Jianyu Dong, Ruofei Cheng, et al.
Science Advances (2025) Vol. 11, Iss. 6
Open Access

Biocatalytic Reduction of Double Carbon-Nitrogen Bonds Toward Chiral Amines
J. González-Rodríguez, Florian Rudroff
Elsevier eBooks (2025)
Closed Access

OSCAR: an extensive repository of chemically and functionally diverse organocatalysts
Simone Gallarati, Puck van Gerwen, Rubén Laplaza, et al.
Chemical Science (2022) Vol. 13, Iss. 46, pp. 13782-13794
Open Access | Times Cited: 24

Recent advances in oxidase biocatalysts: Enzyme discovery, cascade reactions and scale up
Rachel S. Heath, Nicholas J. Turner
Current Opinion in Green and Sustainable Chemistry (2022) Vol. 38, pp. 100693-100693
Open Access | Times Cited: 23

Redox Out of the Box: Catalytic Versatility Across NAD(P)H‐Dependent Oxidoreductases
Sebastian Roth, Richard Niese, Michael Müller, et al.
Angewandte Chemie International Edition (2023) Vol. 63, Iss. 13
Open Access | Times Cited: 13

Catch-and-Release: The Assembly, Immobilization, and Recycling of Redox-Reversible Artificial Metalloenzymes
Alex H. Miller, E.V. Blagova, Benjamin Large, et al.
ACS Catalysis (2024) Vol. 14, Iss. 5, pp. 3218-3227
Open Access | Times Cited: 4

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