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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:

Sabatier Principle for Rationalizing Enzymatic Hydrolysis of a Synthetic Polyester
Jenny Arnling Bååth, Kenneth Jensen, Kim Borch, et al.
JACS Au (2022) Vol. 2, Iss. 5, pp. 1223-1231
Open Access | Times Cited: 52

Showing 1-25 of 52 citing articles:

Enzymes’ Power for Plastics Degradation
Vincent Tournier, Sophie Duquesne, Frédérique Guillamot, et al.
Chemical Reviews (2023) Vol. 123, Iss. 9, pp. 5612-5701
Closed Access | Times Cited: 229
Assessment of Four Engineered PET Degrading Enzymes Considering Large-Scale Industrial Applications
Grégory Arnal, Julien Anglade, Sabine Gavalda, et al.
ACS Catalysis (2023) Vol. 13, Iss. 20, pp. 13156-13166
Open Access | Times Cited: 82
Microbial Enzyme Biotechnology to Reach Plastic Waste Circularity: Current Status, Problems and Perspectives
Marco Orlando, Gianluca Molla, Pietro Castellani, et al.
International Journal of Molecular Sciences (2023) Vol. 24, Iss. 4, pp. 3877-3877
Open Access | Times Cited: 43
Dynamic Docking-Assisted Engineering of Hydrolases for Efficient PET Depolymerization
Yi Zheng, Qingbin Li, Pan Liu, et al.
ACS Catalysis (2024) Vol. 14, Iss. 5, pp. 3627-3639
Closed Access | Times Cited: 14
Natural and engineered enzymes for polyester degradation: a review
Rey‐Ting Guo, Xian Li, Yu Yang, et al.
Environmental Chemistry Letters (2024) Vol. 22, Iss. 3, pp. 1275-1296
Open Access | Times Cited: 13
Concentration‐Dependent Inhibition of Mesophilic PETases on Poly(ethylene terephthalate) Can Be Eliminated by Enzyme Engineering
Luisana Avilán, Bruce R. Lichtenstein, Gerhard König, et al.
ChemSusChem (2023) Vol. 16, Iss. 8
Open Access | Times Cited: 30
Efficient polyethylene terephthalate degradation at moderate temperature: a protein engineering study of LC‐cutinase highlights the key role of residue 243
Valentina Pirillo, Marco Orlando, Caren Battaglia, et al.
FEBS Journal (2023) Vol. 290, Iss. 12, pp. 3185-3202
Open Access | Times Cited: 29
Validated High-Throughput Screening System for Directed Evolution of Nylon-Depolymerizing Enzymes
Hendrik Puetz, Christoph Janknecht, Francisca Contreras, et al.
ACS Sustainable Chemistry & Engineering (2023) Vol. 11, Iss. 43, pp. 15513-15522
Open Access | Times Cited: 20
Recent advances in the biodegradation of polyethylene terephthalate with cutinase-like enzymes
Beibei Sui, Tao Wang, Jingxiang Fang, et al.
Frontiers in Microbiology (2023) Vol. 14
Open Access | Times Cited: 19
The reaction mechanism of the Ideonella sakaiensis PETase enzyme
Tucker Burgin, Benjamin C. Pollard, Brandon C. Knott, et al.
Communications Chemistry (2024) Vol. 7, Iss. 1
Open Access | Times Cited: 9
Relationships of crystallinity and reaction rates for enzymatic degradation of poly (ethylene terephthalate), PET
Sune Schubert, Thore Bach Thomsen, Kristine S. Clausen, et al.
ChemSusChem (2024) Vol. 17, Iss. 10
Open Access | Times Cited: 8
Applying the Sabatier Principle to Decipher the Surface-Structure-Dependent Catalysis of Different Starch Granules by Pullulanase
Yu Wang, Yu Tian, Andrew Philip Rennison, et al.
JACS Au (2025)
Open Access
Combined Adsorption and Michaelis–Menten Approach Reveals Predominant Enzymatic Depolymerization of Crystalline Poly(ethylene terephthalate) by Humicola insolens Cutinase in the Solution Phase
Suprio Kamal, Kiersten Carew, Ji Qin, et al.
ACS Sustainable Chemistry & Engineering (2025)
Closed Access
Efficient depolymerization of polyethylene terephthalate (PET) and polyethylene furanoate by engineered PET hydrolase Cut190
Fusako Kawai, Yoshitomo Furushima, N. Mochizuki, et al.
AMB Express (2022) Vol. 12, Iss. 1
Open Access | Times Cited: 28
Protein-plastic interactions: The driving forces behind the high affinity of a carbohydrate-binding module for polyethylene terephthalate
Andrew Philip Rennison, Peter Westh, Marie Sofie Møller
The Science of The Total Environment (2023) Vol. 870, pp. 161948-161948
Open Access | Times Cited: 19
Biochemical Characterization and NMR Study of a PET-Hydrolyzing Cutinase from Fusarium solani pisi
Kristina Naasen Hellesnes, Shunmathi Vijayaraj, Peter Fojan, et al.
Biochemistry (2023) Vol. 62, Iss. 8, pp. 1369-1375
Open Access | Times Cited: 16
Thermodynamic principle to enhance enzymatic activity using the substrate affinity
Hideshi Ooka, Yoko Chiba, Ryuhei Nakamura
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 16
Interfacial Catalysis during Amylolytic Degradation of Starch Granules: Current Understanding and Kinetic Approaches
Yu Tian, Yu Wang, Yuyue Zhong, et al.
Molecules (2023) Vol. 28, Iss. 9, pp. 3799-3799
Open Access | Times Cited: 14
Catalytic degradation of microplastics
Елена Ефременко, Ilya Lyagin, Olga Maslova, et al.
Russian Chemical Reviews (2023) Vol. 92, Iss. 2, pp. RCR5069-RCR5069
Closed Access | Times Cited: 14
A versatile microbial platform as a tunable whole-cell chemical sensor
Javier M Hernández-Sancho, Arnaud Boudigou, Maria V G Alván-Vargas, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 4
Efficient polyethylene terephthalate biodegradation by an engineered Ideonella sakaiensis PETase with a fixed substrate-binding W156 residue
Qingdian Yin, Jiaxing Zhang, Sen Ma, et al.
Green Chemistry (2023) Vol. 26, Iss. 5, pp. 2560-2570
Closed Access | Times Cited: 13
Unveiling PET Hydrolase Surface Dynamics through Fluorescence Microscopy
Andrew Philip Rennison, Aimilia Nousi, Peter Westh, et al.
ChemBioChem (2024) Vol. 25, Iss. 5
Open Access | Times Cited: 3
Mimicking the enzymatic plant cell wall hydrolysis mechanism for the degradation of polyethylene terephthalate
George Taxeidis, Efstratios Nikolaivits, Jasmina Nikodinović‐Runić, et al.
Environmental Pollution (2024) Vol. 356, pp. 124347-124347
Closed Access | Times Cited: 3
Conversion of polyethylene terephthalate into pure terephthalic acid through synergy between a solid-degrading cutinase and a reaction intermediate-hydrolysing carboxylesterase
Arpita Mrigwani, Bhishem Thakur, Purnananda Guptasarma
Green Chemistry (2022) Vol. 24, Iss. 17, pp. 6707-6719
Open Access | Times Cited: 20
A new continuous assay for quantitative assessment of enzymatic degradation of poly(ethylene terephthalate) (PET)
Thore Bach Thomsen, Sune Schubert, Cameron J. Hunt, et al.
Enzyme and Microbial Technology (2022) Vol. 162, pp. 110142-110142
Open Access | Times Cited: 15
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