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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:

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

Showing 25 citing articles:

Advanced glycosidases as ingenious biosynthetic instruments
Zuzana Mészáros, Pavlína Nekvasilová, Pavla Bojarová, et al.
Biotechnology Advances (2021) Vol. 49, pp. 107733-107733
Closed Access | Times Cited: 33
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
Glycopolymers for Efficient Inhibition of Galectin-3: In Vitro Proof of Efficacy Using Suppression of T Lymphocyte Apoptosis and Tumor Cell Migration
Marcela Filipová, Pavla Bojarová, Marina Rodrigues Tavares, et al.
Biomacromolecules (2020) Vol. 21, Iss. 8, pp. 3122-3133
Closed Access | Times Cited: 28
High-Affinity N-(2-Hydroxypropyl)methacrylamide Copolymers with Tailored N-Acetyllactosamine Presentation Discriminate between Galectins
Marina Rodrigues Tavares, M Blahová, Lieselotte Sedláková, et al.
Biomacromolecules (2020) Vol. 21, Iss. 2, pp. 641-652
Closed Access | Times Cited: 26
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
Immunoprotective neo-glycoproteins: Chemoenzymatic synthesis of multivalent glycomimetics for inhibition of cancer-related galectin-3
Viktoria Heine, Michaela Hovorková, Miluše Vlachová, et al.
European Journal of Medicinal Chemistry (2021) Vol. 220, pp. 113500-113500
Closed Access | Times Cited: 21
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
Production of Lacto-N-triose II and Lacto-N-neotetraose from Chitin by a Novel β-N-Acetylhexosaminidase Expressed in Pichia pastoris
Yihao Liu, Qiaojuan Yan, Junwen Ma, et al.
ACS Sustainable Chemistry & Engineering (2020) Vol. 8, Iss. 41, pp. 15466-15474
Closed Access | Times Cited: 17
Engineered Glycosidases for the Synthesis of Analogs of Human Milk Oligosaccharides
Pavlína Nekvasilová, Michaela Hovorková, Zuzana Mészáros, et al.
International Journal of Molecular Sciences (2022) Vol. 23, Iss. 8, pp. 4106-4106
Open Access | Times Cited: 9
Glycosidase‐Catalyzed Synthesis of Glycosyl Esters and Phenolic Glycosides of Aromatic Acids
Ivan Bassanini, Jana Kapešová, Lucie Petrásková, et al.
Advanced Synthesis & Catalysis (2019) Vol. 361, Iss. 11, pp. 2627-2637
Open Access | Times Cited: 16
Oligosaccharide Ligands of Galectin-4 and Its Subunits: Multivalency Scores Highly
Kristýna Slámová, Jakub Červený, Zuzana Mészáros, et al.
Molecules (2023) Vol. 28, Iss. 10, pp. 4039-4039
Open Access | Times Cited: 4
Advanced high-affinity glycoconjugate ligands of galectins
Michaela Hovorková, Jakub Červený, Ladislav Bumba, et al.
Bioorganic Chemistry (2022) Vol. 131, pp. 106279-106279
Open Access | Times Cited: 8
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
A novel enzymatic tool for transferring GalNAc moiety onto challenging acceptors
Pavlína Nekvasilová, Iveta Andreasová, Lucie Petrásková, et al.
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics (2019) Vol. 1868, Iss. 2, pp. 140319-140319
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
Cross-Linking Effects Dictate the Preference of Galectins to Bind LacNAc-Decorated HPMA Copolymers
Sara Bertuzzi, Ana Gimeno, Ane Martínez-Castillo, et al.
International Journal of Molecular Sciences (2021) Vol. 22, Iss. 11, pp. 6000-6000
Open Access | Times Cited: 8
Mutagenesis of Catalytic Nucleophile of β‐Galactosidase Retains Residual Hydrolytic Activity and Affords a Transgalactosidase
Michaela Hovorková, Natalia Kulik, Dorota Konvalinková, et al.
ChemCatChem (2021) Vol. 13, Iss. 21, pp. 4532-4542
Closed Access | Times Cited: 7
Reprint of: Advanced glycosidases as ingenious biosynthetic instruments
Zuzana Mészáros, Pavlína Nekvasilová, Pavla Bojarová, et al.
Biotechnology Advances (2021) Vol. 51, pp. 107820-107820
Closed Access | Times Cited: 5
Reversible Lectin Binding to Glycan-Functionalized Graphene
Tereza Koukalová, Petr Kovaříček, Pavla Bojarová, et al.
International Journal of Molecular Sciences (2021) Vol. 22, Iss. 13, pp. 6661-6661
Open Access | Times Cited: 3
Chemo-Enzymatic Production of 4-Nitrophenyl-2-acetamido-2-deoxy-α-D-galactopyranoside Using Immobilized β-N-Acetylhexosaminidase
Helena Hronská, Vladimı́r Štefuca, Ema Ondrejková, et al.
Catalysts (2022) Vol. 12, Iss. 5, pp. 474-474
Open Access | Times Cited: 2
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
Glycosylation, Sulfation and Phosphorylation
Vladimı́r Křen
(2020), pp. 363-407
Closed Access
Characterization of a β‐N‐acetylhexosaminidase with transglycosylation activity from Metarhizium sp. A34
Masahiro Kurakake, Yukari Amai
Journal of Food Science (2022) Vol. 87, Iss. 4, pp. 1466-1474
Closed Access
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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