1H, 13C, 15N resonance assignments and secondary structure of yeast oligosaccharyltransferase subunit Ost4 and its functionally important mutant Ost4V23D
Author:
Funder
National Science Foundation
Publisher
Springer Science and Business Media LLC
Subject
Biochemistry,Structural Biology
Link
https://link.springer.com/content/pdf/10.1007/s12104-020-09946-7.pdf
Reference19 articles.
1. Bai L, Wang T, Zhao G, Kovach A, Li H (2018) The atomic structure of a eukaryotic oligosaccharyltransferase complex. Nature 555:328–333. doi:https://doi.org/10.1038/nature25755
2. Chaudhary B, Mazumder S, Mohanty S (2017) Production and biophysical characterization of a mini-membrane protein, Ost4V23D: A functionally important mutant of yeast oligosaccharyltransferase subunit Ost4p. Protein Expr Purif 139:43–48. doi:https://doi.org/10.1016/j.pep.2017.07.009
3. Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6:277–293
4. Freeze HH (1998) Disorders in protein glycosylation and potential therapy: Tip of an iceberg? J Pediatr 133:593–600. doi:https://doi.org/10.1016/S0022-3476(98)70096-4
5. Gayen S, Kang C (2011) Solution structure of a human minimembrane protein Ost4, a subunit of the oligosaccharyltransferase complex. Biochem Biophys Res Commun 409:572–576. doi:https://doi.org/10.1016/j.bbrc.2011.05.050
Cited by 3 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
1. Evolutionary rate covariation is pervasive between glycosylation pathways and points to potential disease modifiers;PLOS Genetics;2024-09-11
2. Reconstitution and resonance assignments of yeast OST subunit Ost4 and its critical mutant Ost4V23D in liposomes by solid-state NMR;Journal of Biomolecular NMR;2024-02-29
3. NMR and MD simulations reveal the impact of the V23D mutation on the function of yeast oligosaccharyltransferase subunit Ost4;Glycobiology;2021-01-12
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