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:

Structure-based protein engineering enables prenyl donor switching of a fungal aromatic prenyltransferase
Peter Mai, Georg Zocher, Thilo Stehle, et al.
Organic & Biomolecular Chemistry (2018) Vol. 16, Iss. 40, pp. 7461-7469
Closed Access | Times Cited: 21

Showing 21 citing articles:

Enzymatic studies on aromatic prenyltransferases
Takahiro Mori
Journal of Natural Medicines (2020) Vol. 74, Iss. 3, pp. 501-512
Open Access | Times Cited: 58

Global genome mining-driven discovery of an unusual biosynthetic logic for fungal polyketide–terpenoid hybrids
Dexiu Yan, Yudai Matsuda
Chemical Science (2024) Vol. 15, Iss. 8, pp. 3011-3017
Open Access | Times Cited: 7

Biocatalytic Friedel‐Crafts Reactions
Reuben B. Leveson‐Gower, Gérard Roelfes
ChemCatChem (2022) Vol. 14, Iss. 18
Open Access | Times Cited: 25

Prenylation: A Critical Step for Biomanufacturing of Prenylated Aromatic Natural Products
Ting An, Xudong Feng, Chun Li
Journal of Agricultural and Food Chemistry (2023) Vol. 71, Iss. 5, pp. 2211-2233
Closed Access | Times Cited: 16

Structural insights into the diverse prenylating capabilities of DMATS prenyltransferases
Evan T. Miller, Oleg V. Tsodikov, Sylvie Garneau‐Tsodikova
Natural Product Reports (2023) Vol. 41, Iss. 1, pp. 113-147
Closed Access | Times Cited: 14

Switching Prenyl Donor Specificities of Cyanobactin Prenyltransferases
Yuchen Zhang, K. Hamada, Masayuki Satake, et al.
Journal of the American Chemical Society (2023) Vol. 145, Iss. 44, pp. 23893-23898
Closed Access | Times Cited: 13

Understanding and Engineering of C4 Indole Prenyltransferase FgaPT2 by Theoretical Study and Mutation Experiments
Yihan Liu, Yongpeng Yao, Kiran Siddique, et al.
ACS Catalysis (2025), pp. 4921-4933
Closed Access

A Gatekeeper Residue Controls Aromatic Acceptor Specificity of the PHB-Type UbiA Prenyltransferases
Erlan Yang, Yongpeng Yao, Yihan Liu, et al.
ACS Catalysis (2023) Vol. 13, Iss. 20, pp. 13717-13728
Closed Access | Times Cited: 9

Complete Decoration of the Indolyl Residue in cyclo-l-Trp-l-Trp with Geranyl Moieties by Using Engineered Dimethylallyl Transferases
Ge Liao, Peter Mai, Jie Fan, et al.
Organic Letters (2018) Vol. 20, Iss. 22, pp. 7201-7205
Closed Access | Times Cited: 21

Synthetic biology, combinatorial biosynthesis, and chemo‑enzymatic synthesis of isoprenoids
Alexandra A. Malico, Miles A Calzini, Anuran K Gayen, et al.
Journal of Industrial Microbiology & Biotechnology (2020) Vol. 47, Iss. 9-10, pp. 675-702
Open Access | Times Cited: 20

Promiscuous Enzymes for Residue‐Specific Peptide and Protein Late‐Stage Functionalization
Ashley K. Alexander, Sherif I. Elshahawi
ChemBioChem (2023) Vol. 24, Iss. 17
Open Access | Times Cited: 6

Biochemical and Mechanistic Characterization of the Fungal Reverse N-1-Dimethylallyltryptophan Synthase DMATS1Ff
Immo Burkhardt, Zhongfeng Ye, Slavica Janevska, et al.
ACS Chemical Biology (2019) Vol. 14, Iss. 12, pp. 2922-2931
Closed Access | Times Cited: 15

Reprogramming Substrate and Catalytic Promiscuity of Tryptophan Prenyltransferases
E. Ostertag, Liujuan Zheng, K. Broger, et al.
Journal of Molecular Biology (2020) Vol. 433, Iss. 2, pp. 166726-166726
Closed Access | Times Cited: 14

A Single Amino Acid Switch Alters the Prenyl Donor Specificity of a Fungal Aromatic Prenyltransferase toward Biflavonoids
Yuanyuan Xu, Dan Li, Gui‐Shan Tan, et al.
Organic Letters (2020) Vol. 23, Iss. 2, pp. 497-502
Closed Access | Times Cited: 13

Rational Engineered C-Acyltransferase Transforms Sterically Demanding Acyl Donors
Anna Żądło‐Dobrowolska, Lucas Hammerer, Tea Pavkov‐Keller, et al.
ACS Catalysis (2019) Vol. 10, Iss. 2, pp. 1094-1101
Open Access | Times Cited: 13

Substrate‐Multiplexed Assessment of Aromatic Prenyltransferase Activity
Peyton M. Higgins, Nicolette G. Wehrli, Andrew R. Buller
ChemBioChem (2024) Vol. 26, Iss. 1
Open Access | Times Cited: 1

Novel strategy to produce prenylated resveratrol by prenyltransferase iacE and evaluation of neuroprotective mechanisms
Ting Zhou, Bao Yang
Biochemical and Biophysical Research Communications (2022) Vol. 609, pp. 127-133
Closed Access | Times Cited: 6

Crystal structures of a 6-dimethylallyltryptophan synthase, IptA: Insights into substrate tolerance and enhancement of prenyltransferase activity
Hironori Suemune, Doukan Nishimura, Kenjiro Mizutani, et al.
Biochemical and Biophysical Research Communications (2022) Vol. 593, pp. 144-150
Open Access | Times Cited: 5

Combining mutagenesis on Glu281 of prenyltransferase NovQ and metabolic engineering strategies for the increased prenylated activity towards menadione
Wenfeng Ni, Zhiming Zheng, Hui Liu, et al.
Applied Microbiology and Biotechnology (2020) Vol. 104, Iss. 10, pp. 4371-4382
Closed Access | Times Cited: 6

Correction to: Combining mutagenesis on Glu281 of prenyltransferase NovQ and metabolic engineering strategies for the increased prenylated activity towards menadione
Wenfeng Ni, Zhiming Zheng, Hui Liu, et al.
Applied Microbiology and Biotechnology (2020) Vol. 104, Iss. 10, pp. 4629-4630
Open Access | Times Cited: 2

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