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IUBMB Life|November 9, 2022
Involvement of sialoglycans in SARS-COV-2 infection: Opportunities and challenges for glyco-based inhibitorsSakonwan Kuhaudomlarp, Anne Imberty
Viruses|September 28, 2023
Bridging the Gap: Can COVID-19 Research Help Combat African Swine Fever?Danaya Pakotiprapha, Sakonwan Kuhaudomlarp, Ruchanok Tinikul, et al.
Methods in Molecular Biology (Clifton, N.J.)|April 20, 2020
LecA (PA-IL): A Galactose-Binding Lectin from Pseudomonas aeruginosaSakonwan Kuhaudomlarp, Emilie Gillon, Annabelle Varrot, et al.
Protein and Peptide Letters|August 12, 2017
Glycan Phosphorylases in Multi-Enzyme Synthetic ProcessesGiulia Pergolizzi, Sakonwan Kuhaudomlarp, Eeshan Kalita, et al.
The Journal of Biological Chemistry|March 2, 2019
Unraveling the subtleties of β-(1→3)-glucan phosphorylase specificity in the GH94, GH149, and GH161 glycoside hydrolase familiesSakonwan Kuhaudomlarp, Giulia Pergolizzi, Nicola J Patron, et al.
Proteins|May 29, 2019
The structure of a GH149 β-(1 → 3) glucan phosphorylase reveals a new surface oligosaccharide binding site and additional domains that are absent in the disaccharide-specific GH94 glucose-β-(1 → 3)-glucose (laminaribiose) phosphorylaseSakonwan Kuhaudomlarp, Clare E M Stevenson, David M Lawson, et al.
Angewandte Chemie (International Ed. in English)|October 29, 2021
Druggable Allosteric Sites in β-Propeller LectinsElena Shanina, Sakonwan Kuhaudomlarp, Kanhaya Lal, et al.
The Journal of Biological Chemistry|January 11, 2018
Identification of <i>Euglena gracilis</i> β-1,3-glucan phosphorylase and establishment of a new glycoside hydrolase (GH) family GH149Sakonwan Kuhaudomlarp, Nicola J Patron, Bernard Henrissat, et al.
Methods in Enzymology|September 23, 2017
Profiling of Sugar NucleotidesMartin Rejzek, Lionel Hill, Edward S Hems, et al.
Chembiochem : a European Journal of Chemical Biology|October 29, 2019
Preparative and Kinetic Analysis of β-1,4- and β-1,3-Glucan Phosphorylases Informs Access to Human Milk Oligosaccharide Fragments and Analogues ThereofRavindra Pal Singh, Giulia Pergolizzi, Sergey A Nepogodiev, et al.
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