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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:

An ancient family of lytic polysaccharide monooxygenases with roles in arthropod development and biomass digestion
Federico Sabbadin, G.R. Hemsworth, Luisa Ciano, et al.
Nature Communications (2018) Vol. 9, Iss. 1
Open Access | Times Cited: 249

Showing 1-25 of 249 citing articles:

Lignocellulose degradation: An overview of fungi and fungal enzymes involved in lignocellulose degradation
Martina Andlar, Tonči Rezić, Nenad Marđetko, et al.
Engineering in Life Sciences (2018) Vol. 18, Iss. 11, pp. 768-778
Open Access | Times Cited: 466
Enzymatic Modifications of Chitin, Chitosan, and Chitooligosaccharides
Michał B. Kaczmarek, Katarzyna Struszczyk‐Świta, Xingkang Li, et al.
Frontiers in Bioengineering and Biotechnology (2019) Vol. 7
Open Access | Times Cited: 328
Oxidoreductases and Reactive Oxygen Species in Conversion of Lignocellulosic Biomass
Bastien Bissaro, Anikó Várnai, Åsmund K. Røhr, et al.
Microbiology and Molecular Biology Reviews (2018) Vol. 82, Iss. 4
Open Access | Times Cited: 252
Molecular architecture of softwood revealed by solid-state NMR
Oliver M. Terrett, Jan J. Łyczakowski, Li Yu, et al.
Nature Communications (2019) Vol. 10, Iss. 1
Open Access | Times Cited: 214
AA16, a new lytic polysaccharide monooxygenase family identified in fungal secretomes
Camille Filiatrault-Chastel, David Navarro, Mireille Haon, et al.
Biotechnology for Biofuels (2019) Vol. 12, Iss. 1
Open Access | Times Cited: 174
Enzymatic processing of lignocellulosic biomass: principles, recent advances and perspectives
Heidi Østby, Line Degn Hansen, Svein Jarle Horn, et al.
Journal of Industrial Microbiology & Biotechnology (2020) Vol. 47, Iss. 9-10, pp. 623-657
Open Access | Times Cited: 170
Bioethanol production from waste lignocelluloses: A review on microbial degradation potential
Rajesh Kumar Prasad, Soumya Chatterjee, Pranab Behari Mazumder, et al.
Chemosphere (2019) Vol. 231, pp. 588-606
Closed Access | Times Cited: 169
Secreted pectin monooxygenases drive plant infection by pathogenic oomycetes
Federico Sabbadin, S. Urresti, Bernard Henrissat, et al.
Science (2021) Vol. 373, Iss. 6556, pp. 774-779
Open Access | Times Cited: 163
On the functional characterization of lytic polysaccharide monooxygenases (LPMOs)
Vincent G. H. Eijsink, Dejan Petrović, Zarah Forsberg, et al.
Biotechnology for Biofuels (2019) Vol. 12, Iss. 1
Open Access | Times Cited: 154
Expanding the catalytic landscape of metalloenzymes with lytic polysaccharide monooxygenases
Alessia Munzone, Vincent G. H. Eijsink, Jean‐Guy Berrin, et al.
Nature Reviews Chemistry (2024)
Closed Access | Times Cited: 28
Bracing copper for the catalytic oxidation of C–H bonds
Luisa Ciano, G.J. Davies, William B. Tolman, et al.
Nature Catalysis (2018) Vol. 1, Iss. 8, pp. 571-577
Closed Access | Times Cited: 161
The continuing expansion of CAZymes and their families
Marie-Line Garron, Bernard Henrissat
Current Opinion in Chemical Biology (2019) Vol. 53, pp. 82-87
Closed Access | Times Cited: 138
Polysaccharide degradation by lytic polysaccharide monooxygenases
Zarah Forsberg, Morten Sørlie, Dejan Petrović, et al.
Current Opinion in Structural Biology (2019) Vol. 59, pp. 54-64
Open Access | Times Cited: 136
Molecular mechanism of the chitinolytic peroxygenase reaction
Bastien Bissaro, Bennett R. Streit, Ingvild Isaksen, et al.
Proceedings of the National Academy of Sciences (2020) Vol. 117, Iss. 3, pp. 1504-1513
Open Access | Times Cited: 119
Distinct Substrate Specificities and Electron-Donating Systems of Fungal Lytic Polysaccharide Monooxygenases
Matthias Frommhagen, Adrie H. Westphal, Willem J. H. van Berkel, et al.
Frontiers in Microbiology (2018) Vol. 9
Open Access | Times Cited: 109
Recent insights into lytic polysaccharide monooxygenases (LPMOs)
Tobias Tandrup, Kristian E. H. Frandsen, Katja S. Johansen, et al.
Biochemical Society Transactions (2018) Vol. 46, Iss. 6, pp. 1431-1447
Closed Access | Times Cited: 102
Kinetic insights into the peroxygenase activity of cellulose-active lytic polysaccharide monooxygenases (LPMOs)
Riin Kont, Bastien Bissaro, Vincent G. H. Eijsink, et al.
Nature Communications (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 93
Unraveling the roles of the reductant and free copper ions in LPMO kinetics
Anton A. Stepnov, Zarah Forsberg, Morten Sørlie, et al.
Biotechnology for Biofuels (2021) Vol. 14, Iss. 1
Open Access | Times Cited: 92
On the expansion of biological functions of lytic polysaccharide monooxygenases
Theruvothu Madathil Vandhana, Jean-Lou Reyre, Dangudubiyyam Sushmaa, et al.
New Phytologist (2021) Vol. 233, Iss. 6, pp. 2380-2396
Open Access | Times Cited: 88
Gut anatomical properties and microbial functional assembly promote lignocellulose deconstruction and colony subsistence of a wood-feeding beetle
Javier A. Ceja-Navarro, Ulaş Karaöz, Markus Bill, et al.
Nature Microbiology (2019) Vol. 4, Iss. 5, pp. 864-875
Open Access | Times Cited: 82
Role and significance of lytic polysaccharide monooxygenases (LPMOs) in lignocellulose deconstruction
Reeta Rani Singhania, Pooja Dixit, Anil Kumar Patel, et al.
Bioresource Technology (2021) Vol. 335, pp. 125261-125261
Closed Access | Times Cited: 82
Formation of a Copper(II)–Tyrosyl Complex at the Active Site of Lytic Polysaccharide Monooxygenases Following Oxidation by H2O2
Alessandro Paradisi, Esther M. Johnston, Morten Tovborg, et al.
Journal of the American Chemical Society (2019) Vol. 141, Iss. 46, pp. 18585-18599
Open Access | Times Cited: 77
Enzymatic Hydroxylations of sp3-Carbons
Judith Münch, Pascal Püllmann, Wuyuan Zhang, et al.
ACS Catalysis (2021) Vol. 11, Iss. 15, pp. 9168-9203
Open Access | Times Cited: 74
Integrative omics analysis of the termite gut system adaptation to Miscanthus diet identifies lignocellulose degradation enzymes
Magdalena Całusińska, Martyna Marynowska, Marie Bertucci, et al.
Communications Biology (2020) Vol. 3, Iss. 1
Open Access | Times Cited: 72
Enzyme mediated multi-product process: A concept of bio-based refinery
Bikash Kumar, Pradeep Verma
Industrial Crops and Products (2020) Vol. 154, pp. 112607-112607
Closed Access | Times Cited: 71
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