Open Access Helper

OpenAlex Citation Counts

OpenAlex Citations Logo

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:

Mechanism-guided tunnel engineering to increase the efficiency of a flavin-dependent halogenase
Kridsadakorn Prakinee, Aisaraphon Phintha, Surawit Visitsatthawong, et al.
Nature Catalysis (2022) Vol. 5, Iss. 6, pp. 534-544
Closed Access | Times Cited: 80

Showing 1-25 of 80 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: 158
Discovery and mechanism-guided engineering of BHET hydrolases for improved PET recycling and upcycling
Anni Li, Yijie Sheng, Haiyang Cui, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 49
Flexibility Regulation of Loops Surrounding the Tunnel Entrance in Cytochrome P450 Enhanced Substrate Access Substantially
Zhongyu Li, Shuaiqi Meng, Kaili Nie, et al.
ACS Catalysis (2022) Vol. 12, Iss. 20, pp. 12800-12808
Closed Access | Times Cited: 42
Selective C−H Halogenation of Alkenes and Alkynes Using Flavin‐Dependent Halogenases
Yuhua Jiang, Ahram Kim, Cahmlo Olive, et al.
Angewandte Chemie International Edition (2024) Vol. 63, Iss. 13
Open Access | Times Cited: 8
Navigating the landscape of enzyme design: from molecular simulations to machine learning
Jiahui Zhou, Meilan Huang
Chemical Society Reviews (2024) Vol. 53, Iss. 16, pp. 8202-8239
Open Access | Times Cited: 8
Crystallographic and Thermodynamic Evidence of Negative Coupling in the Flavin-Dependent Tryptophan Halogenases AbeH and BorH
Md Ashaduzzaman, Kazi Lingkon, Aravinda J. De Silva, et al.
ACS Omega (2025)
Open Access
The Single‐Component Flavin Reductase/Flavin‐Dependent Halogenase AetF is a Versatile Catalyst for Selective Bromination and Iodination of Arenes and Olefins**
Yuhua Jiang, Harrison M. Snodgrass, Yasmine S. Zubi, et al.
Angewandte Chemie International Edition (2022) Vol. 61, Iss. 51
Open Access | Times Cited: 27
Enzymatic Halogenation of Terminal Alkynes
April L. Lukowski, Felix M. Hubert, Thuan-Ethan Ngo, et al.
Journal of the American Chemical Society (2023) Vol. 145, Iss. 34, pp. 18716-18721
Open Access | Times Cited: 18
Unifying and versatile features of flavin-dependent monooxygenases: Diverse catalysis by a common C4a-(hydro)peroxyflavin
Aisaraphon Phintha, Pimchai Chaiyen
Journal of Biological Chemistry (2023) Vol. 299, Iss. 12, pp. 105413-105413
Open Access | Times Cited: 14
Harnessing solvation-guided engineering to enhance deep eutectic solvent resistance and thermostability in enzymes
Yijie Sheng, Haiyang Cui, Xinyue Wang, et al.
Green Chemistry (2024) Vol. 26, Iss. 16, pp. 9132-9141
Closed Access | Times Cited: 5
Site-selective chlorination of pyrrolic heterocycles by flavin dependent enzyme PrnC
GuangRong Peh, Terence Tay, Lee Ling Tan, et al.
Communications Chemistry (2024) Vol. 7, Iss. 1
Open Access | Times Cited: 4
Engineering of 4-hydroxyphenylacetate 3-hydroxylase derived from Pseudomonas aeruginosa for the ortho-hydroxylation of ferulic acid
Ping Sun, Pu Zheng, Pengcheng Chen, et al.
International Journal of Biological Macromolecules (2024) Vol. 264, pp. 130545-130545
Closed Access | Times Cited: 4
On the Mechanisms of Hypohalous Acid Formation and Electrophilic Halogenation by Non‐Native Halogenases
Kridsadakorn Prakinee, Narin Lawan, Aisaraphon Phintha, et al.
Angewandte Chemie International Edition (2024) Vol. 63, Iss. 24
Open Access | Times Cited: 4
Engineering the next-generation synthetic cell factory driven by protein engineering
Ailin Guan, Zixi He, Xin Wang, et al.
Biotechnology Advances (2024) Vol. 73, pp. 108366-108366
Closed Access | Times Cited: 4
Identifying and Engineering Flavin Dependent Halogenases for Selective Biocatalysis
Jared C. Lewis
Accounts of Chemical Research (2024) Vol. 57, Iss. 15, pp. 2067-2079
Open Access | Times Cited: 4
Structural basis of regioselective tryptophan dibromination by the single-component flavin-dependent halogenase AetF
Simon Gäfe, Hartmut H. Niemann
Acta Crystallographica Section D Structural Biology (2023) Vol. 79, Iss. 7, pp. 596-609
Open Access | Times Cited: 13
Halogenases for the synthesis of small molecules
Eimear Hegarty, Johannes Büchler, Rebecca Buller
Current Opinion in Green and Sustainable Chemistry (2023) Vol. 41, pp. 100784-100784
Open Access | Times Cited: 11
Computer-Aided Tunnel Engineering: A Promising Strategy for Improving Lipase Applications in Esterification Reactions
Wenya Chong, Qi Yuan, Liran Ji, et al.
ACS Catalysis (2023) Vol. 14, Iss. 1, pp. 67-83
Closed Access | Times Cited: 11
Structural and functional insights into the self-sufficient flavin-dependent halogenase
Longhai Dai, Hao Li, Si Dai, et al.
International Journal of Biological Macromolecules (2024) Vol. 260, pp. 129312-129312
Closed Access | Times Cited: 3
Deciphering the Key Loop: Enhancing l-Threonine Transaldolase’s Catalytic Potential
Zhiwen Xi, Jingxin Rao, Xinyi Zhang, et al.
ACS Catalysis (2024) Vol. 14, Iss. 14, pp. 10462-10474
Closed Access | Times Cited: 3
Tunnel engineering of gas-converting enzymes for inhibitor retardation and substrate acceleration
Suk Min Kim, Sung Heuck Kang, Byoung Wook Jeon, et al.
Bioresource Technology (2023) Vol. 394, pp. 130248-130248
Open Access | Times Cited: 10
Asymmetric catalysis by flavin‐dependent halogenases
Yuhua Jiang, Jared C. Lewis
Chirality (2023) Vol. 35, Iss. 8, pp. 452-460
Open Access | Times Cited: 9
Enzymatic Peptide and Protein Bromination: The BromoTrp Tag
Nicolai Montua, Paula Thye, Pia Hartwig, et al.
Angewandte Chemie International Edition (2023) Vol. 63, Iss. 5
Open Access | Times Cited: 8
A high catalytic efficiency and chemotolerant formate dehydrogenase from Bacillus simplex
Rattima Boonkumkrong, Paweenapon Chunthaboon, Pobthum Munkajohnpong, et al.
Biotechnology Journal (2024) Vol. 19, Iss. 1
Closed Access | Times Cited: 2
Empowering Protein Engineering through Recombination of Beneficial Substitutions
Xinyue Wang, Anni Li, Xiujuan Li, et al.
Chemistry - A European Journal (2024) Vol. 30, Iss. 16
Closed Access | Times Cited: 2
Page 1 - Next Page

Scroll to top