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September 28, 2024iScienceOpen Access

Self-regulation of MGAT4A and MGAT4B activity toward glycoproteins through interaction of lectin domain with their own N-glycans

Naoko Osada Sushil K. Mishra Miyako Nakano Yuko Tokoro Masamichi Nagae Robert J. Doerksen Yasuhiko Kizuka

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Abstract

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-Acetylglucosaminyltransferases-IVa (GnT-IVa or MGAT4A) and -IVb (MGAT4B) are glycosyltransferase isozymes synthesizing the β1,4-GlcNAc branch in

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Cite This Study

Osada et al. (2024) studied this question.

synapsesocial.com/papers/68e57180b6db643587511fed https://doi.org/10.1016/j.isci.2024.111066

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Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

1Evolutionary analyses of the animal glycosyltransferase family 54 reveals two β1,4-N-acetylglucosaminyltransferase familiesOriginal Research · 2025 · 3 citations
2Upregulation of GnT-IVa and Its Critical Roles in ATRA-Induced Differentiation of Acute Promyelocytic Leukemia CellsOriginal Research · 2026
3Delving into human α1,4-galactosyltransferase acceptor specificity: the role of enzyme dimerization2024
4Neuroblastoma cell growth and invasiveness is modulated by the activity of N-acetylglucosaminyltransferase-IIIOriginal Research · 2026 · 1 citations
5A Bioorthogonal Precision Tool for human N-acetylglucosaminyltransferase V2024

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Iterative Bump-and-Hole Engineering Creates a Bioorthogonal Reporter for <i>N</i> -Acetylglucosaminyltransferase I2026

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