Cytoplasmic glycoengineering enables biosynthesis of nanoscale glycoprotein assemblies

Established bacterial glycoengineering platforms limit access to protein and glycan substrates. Here the authors design a cytoplasmic protein glycosylation system, Glycoli, to generate a variety of multivalent glycostructures.

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Autores principales:	Hanne L. P. Tytgat, Chia-wei Lin, Mikail D. Levasseur, Markus B. Tomek, Christoph Rutschmann, Jacqueline Mock, Nora Liebscher, Naohiro Terasaka, Yusuke Azuma, Michael Wetter, Martin F. Bachmann, Donald Hilvert, Markus Aebi, Timothy G. Keys
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/ac3f91e741e14ae68b947f045f6333f3
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spelling	oai:doaj.org-article:ac3f91e741e14ae68b947f045f6333f32021-12-02T14:39:40ZCytoplasmic glycoengineering enables biosynthesis of nanoscale glycoprotein assemblies10.1038/s41467-019-13283-22041-1723https://doaj.org/article/ac3f91e741e14ae68b947f045f6333f32019-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-13283-2https://doaj.org/toc/2041-1723Established bacterial glycoengineering platforms limit access to protein and glycan substrates. Here the authors design a cytoplasmic protein glycosylation system, Glycoli, to generate a variety of multivalent glycostructures.Hanne L. P. TytgatChia-wei LinMikail D. LevasseurMarkus B. TomekChristoph RutschmannJacqueline MockNora LiebscherNaohiro TerasakaYusuke AzumaMichael WetterMartin F. BachmannDonald HilvertMarkus AebiTimothy G. KeysNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-10 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Hanne L. P. Tytgat Chia-wei Lin Mikail D. Levasseur Markus B. Tomek Christoph Rutschmann Jacqueline Mock Nora Liebscher Naohiro Terasaka Yusuke Azuma Michael Wetter Martin F. Bachmann Donald Hilvert Markus Aebi Timothy G. Keys Cytoplasmic glycoengineering enables biosynthesis of nanoscale glycoprotein assemblies
description	Established bacterial glycoengineering platforms limit access to protein and glycan substrates. Here the authors design a cytoplasmic protein glycosylation system, Glycoli, to generate a variety of multivalent glycostructures.
format	article
author	Hanne L. P. Tytgat Chia-wei Lin Mikail D. Levasseur Markus B. Tomek Christoph Rutschmann Jacqueline Mock Nora Liebscher Naohiro Terasaka Yusuke Azuma Michael Wetter Martin F. Bachmann Donald Hilvert Markus Aebi Timothy G. Keys
author_facet	Hanne L. P. Tytgat Chia-wei Lin Mikail D. Levasseur Markus B. Tomek Christoph Rutschmann Jacqueline Mock Nora Liebscher Naohiro Terasaka Yusuke Azuma Michael Wetter Martin F. Bachmann Donald Hilvert Markus Aebi Timothy G. Keys
author_sort	Hanne L. P. Tytgat
title	Cytoplasmic glycoengineering enables biosynthesis of nanoscale glycoprotein assemblies
title_short	Cytoplasmic glycoengineering enables biosynthesis of nanoscale glycoprotein assemblies
title_full	Cytoplasmic glycoengineering enables biosynthesis of nanoscale glycoprotein assemblies
title_fullStr	Cytoplasmic glycoengineering enables biosynthesis of nanoscale glycoprotein assemblies
title_full_unstemmed	Cytoplasmic glycoengineering enables biosynthesis of nanoscale glycoprotein assemblies
title_sort	cytoplasmic glycoengineering enables biosynthesis of nanoscale glycoprotein assemblies
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/ac3f91e741e14ae68b947f045f6333f3
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Cytoplasmic glycoengineering enables biosynthesis of nanoscale glycoprotein assemblies

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