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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:

Engineered N-acetylhexosamine-active enzymes in glycoscience
Kristýna Slámová, Pavla Bojarová
Biochimica et Biophysica Acta (BBA) - General Subjects (2017) Vol. 1861, Iss. 8, pp. 2070-2087
Closed Access | Times Cited: 25

Showing 25 citing articles:

“Sweet Flavonoids”: Glycosidase-Catalyzed Modifications
Kristýna Slámová, Jana Kapešová, Kateřina Valentová
International Journal of Molecular Sciences (2018) Vol. 19, Iss. 7, pp. 2126-2126
Open Access | Times Cited: 176
Secretome analysis of the chitinolytic machinery of Chitiniphilus shinanonensis and its implication in chitooligosaccharide production
T. Swaroopa Rani, Daisuke Takahashi, Saumashish Mukherjee, et al.
Carbohydrate Polymers (2025), pp. 123272-123272
Closed Access
Revisiting glycoside hydrolase family 20 β-N-acetyl-d-hexosaminidases: Crystal structures, physiological substrates and specific inhibitors
Tian Liu, Yanwei Duan, Qing Yang
Biotechnology Advances (2018) Vol. 36, Iss. 4, pp. 1127-1138
Closed Access | Times Cited: 38
Glycosynthase reaction meets the flow: Continuous synthesis of lacto‐N‐triose II by engineered β‐hexosaminidase immobilized on solid support
Lucija Ruzic, Juan M. Bolívar, Bernd Nidetzky
Biotechnology and Bioengineering (2020) Vol. 117, Iss. 5, pp. 1597-1602
Open Access | Times Cited: 35
Biocompatible glyconanomaterials based on HPMA-copolymer for specific targeting of galectin-3
Pavla Bojarová, Marina Rodrigues Tavares, Dominic Laaf, et al.
Journal of Nanobiotechnology (2018) Vol. 16, Iss. 1
Open Access | Times Cited: 33
Discovery of human hexosaminidase inhibitors by in situ screening of a library of mono- and divalent pyrrolidine iminosugars
Valeria Pingitore, Macarena Martı́nez-Bailén, Ana T. Carmona, et al.
Bioorganic Chemistry (2022) Vol. 120, pp. 105650-105650
Open Access | Times Cited: 16
Loop Protein Engineering for Improved Transglycosylation Activity of a β‐N‐Acetylhexosaminidase
Shariza Jamek, Jan Muschiol, Jesper Holck, et al.
ChemBioChem (2018) Vol. 19, Iss. 17, pp. 1858-1865
Closed Access | Times Cited: 31
The β-N-Acetylhexosaminidase in the Synthesis of Bioactive Glycans: Protein and Reaction Engineering
Pavla Bojarová, Natalia Kulik, Michaela Hovorková, et al.
Molecules (2019) Vol. 24, Iss. 3, pp. 599-599
Open Access | Times Cited: 25
β-N-Acetylhexosaminidases for Carbohydrate Synthesis via Trans-Glycosylation
Jan Muschiol, M. Paul Vuillemin, Anne S. Meyer, et al.
Catalysts (2020) Vol. 10, Iss. 4, pp. 365-365
Open Access | Times Cited: 25
β-N-Acetylhexosaminidases—the wizards of glycosylation
Pavla Bojarová, Jan Bruthans, Vladimı́r Křen
Applied Microbiology and Biotechnology (2019) Vol. 103, Iss. 19, pp. 7869-7881
Closed Access | Times Cited: 24
A chemo-enzymatic approach for the synthesis of human milk oligosaccharide backbone structures
Jan Muschiol, Anne S. Meyer
Zeitschrift für Naturforschung C (2018) Vol. 74, Iss. 3-4, pp. 85-89
Open Access | Times Cited: 18
Selective β-N-acetylhexosaminidase from Aspergillus versicolor—a tool for producing bioactive carbohydrates
Pavla Bojarová, Natalia Kulik, Kristýna Slámová, et al.
Applied Microbiology and Biotechnology (2019) Vol. 103, Iss. 4, pp. 1737-1753
Closed Access | Times Cited: 18
Glycosphingolipids: From metabolism to chemoenzymatic total synthesis
Mitra K. F. Bonab, Zhongwu Guo, Qingjiang Li
Organic & Biomolecular Chemistry (2024) Vol. 22, Iss. 33, pp. 6665-6683
Open Access | Times Cited: 1
Identification and Characterization of a β-N-Acetylhexosaminidase with a Biosynthetic Activity from the Marine Bacterium Paraglaciecola hydrolytica S66T
Triinu Visnapuu, David Tezé, Christian Kjeldsen, et al.
International Journal of Molecular Sciences (2020) Vol. 21, Iss. 2, pp. 417-417
Open Access | Times Cited: 15
Enzymatic Synthesis of Glycans and Glycoconjugates
Thomas Rexer, Dominic Laaf, Johannes Gottschalk, et al.
Advances in biochemical engineering, biotechnology (2020), pp. 231-280
Closed Access | Times Cited: 15
A Novel GH Family 20 β-N-acetylhexosaminidase With Both Chitosanase and Chitinase Activity From Aspergillus oryzae
Tianle Qu, Chunyue Zhang, Zhen Qin, et al.
Frontiers in Molecular Biosciences (2021) Vol. 8
Open Access | Times Cited: 12
The molecular structure of the glycoside hydrolase domain of Cwp19 from Clostridium difficile
W.J. Bradshaw, Jonathan M. Kirby, April K. Roberts, et al.
FEBS Journal (2017) Vol. 284, Iss. 24, pp. 4343-4357
Open Access | Times Cited: 13
Crystal structure of native β‐N‐acetylhexosaminidase isolated from Aspergillus oryzae sheds light onto its substrate specificity, high stability, and regulation by propeptide
Jana Škerlová, Jan Bláha, Petr Pachl, et al.
FEBS Journal (2017) Vol. 285, Iss. 3, pp. 580-598
Open Access | Times Cited: 13
Acceptor Specificity of β-N-Acetylhexosaminidase from Talaromyces flavus: A Rational Explanation
Cecilia García‐Oliva, Pilar Hoyos, Lucie Petrásková, et al.
International Journal of Molecular Sciences (2019) Vol. 20, Iss. 24, pp. 6181-6181
Open Access | Times Cited: 13
Transglycosidase activity of glycosynthase-type mutants of a fungal GH20 β-N-acetylhexosaminidase
Jana Kapešová, Lucie Petrásková, Natalia Kulik, et al.
International Journal of Biological Macromolecules (2020) Vol. 161, pp. 1206-1215
Closed Access | Times Cited: 11
How Site‐Directed Mutagenesis Boosted Selectivity of a Promiscuous Enzyme
Pavlína Nekvasilová, Natalia Kulik, Nikola Rychlá, et al.
Advanced Synthesis & Catalysis (2020) Vol. 362, Iss. 19, pp. 4138-4150
Closed Access | Times Cited: 8
Potent GH20 N-Acetyl-β-d-hexosaminidase Inhibitors: N-Substituted 3-acetamido-4-amino-5-hydroxymethyl-cyclopentanediols
Patrick Weber, Seyed A. Nasseri, Bettina M. Pabst, et al.
Molecules (2018) Vol. 23, Iss. 3, pp. 708-708
Open Access | Times Cited: 8
Enhanced production of N-acetyl-glucosaminidase by marine Aeromonas caviae CHZ306 in bioreactor
Flávio Augusto Cardozo, Valker Araujo Feitosa, Carlos Mendonça, et al.
Brazilian Journal of Microbiology (2023) Vol. 54, Iss. 3, pp. 1533-1545
Open Access | Times Cited: 1
Mutation Hotspot for Changing the Substrate Specificity of β-N-Acetylhexosaminidase: A Library of GlcNAcases
Pavlína Nekvasilová, Natalia Kulik, Michael Kotik, et al.
International Journal of Molecular Sciences (2022) Vol. 23, Iss. 20, pp. 12456-12456
Open Access | Times Cited: 1
Nucleotide binding as an allosteric regulatory mechanism for Akkermansia muciniphila β-N-acetylhexosaminidase Am2136
Chang-Cheng Li, Huan Yi, Yan-Mei Wang, et al.
Gut Microbes (2022) Vol. 14, Iss. 1
Open Access
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