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Sergio Galan Bartual on Muck Rack

Sergio Galan Bartual

As seen in: Nature, BioRxiv
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Articles

Multi-domain O-GlcNAcase structures reveal allosteric regulatory mechanisms

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By Sara Hansen, Sergio Galan Bartual, Huijie Yuan, Olawale G. Raimi
| BioRxiv
Abstract Nucleocytoplasmic protein O-GlcNAcylation is an essential modification catalysed by O-GlcNAc transferase (OGT) and reversed by O-GlcNAc hydrolase (OGA), a multi-domain enzyme that also contains a C-terminal pseudo-histone acetyltransferase (pHAT) domain. OGA and OGT are tightly regulated using O-GlcNAc-dependent feedback mechanisms that are largely unknown.
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Exploiting O-GlcNAc Transferase promiscuity to dissect site-specific O-GlcNAcylation

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By Conor Mitchell, Sergio Galan Bartual, Andrew Trevelyan Ferenbach
| BioRxiv
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Genetic recoding to dissect the roles of site-specific protein O-GlcNAcylation

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By Andrii Gorelik, Joby Varghese, Sergio Galan Bartual, Vladimir S. Borodkin
| Nature Verified
Abstract Modification of specific Ser and Thr residues of nucleocytoplasmic proteins with O-GlcNAc, catalyzed by O-GlcNAc transferase (OGT), is an abundant posttranslational event essential for proper animal development and is dysregulated in various diseases. Due to the rapid concurrent removal by the single O-GlcNAcase (OGA), precise functional dissection of site-specific O-GlcNAc modification in vivo is currently not possible without affecting the entire O-GlcNAc proteome.
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