A cell-free biosynthesis platform for modular construction of protein glycosylation pathways

Constructing biosynthetic pathways to study and engineer glycoprotein structures is difficult. Here, the authors use GlycoPRIME, a cell-free workflow for mixing-and-matching glycosylation enzymes, to evaluate 37 putative glycosylation pathways and discover routes to 18 new glycoprotein structures

Guardado en:

Detalles Bibliográficos
Autores principales:	Weston Kightlinger, Katherine E. Duncker, Ashvita Ramesh, Ariel H. Thames, Aravind Natarajan, Jessica C. Stark, Allen Yang, Liang Lin, Milan Mrksich, Matthew P. DeLisa, Michael C. Jewett
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/3ed28a4885534b4f9dbe3db52b4d222c
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:3ed28a4885534b4f9dbe3db52b4d222c
record_format	dspace
spelling	oai:doaj.org-article:3ed28a4885534b4f9dbe3db52b4d222c2021-12-02T16:50:57ZA cell-free biosynthesis platform for modular construction of protein glycosylation pathways10.1038/s41467-019-12024-92041-1723https://doaj.org/article/3ed28a4885534b4f9dbe3db52b4d222c2019-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-12024-9https://doaj.org/toc/2041-1723Constructing biosynthetic pathways to study and engineer glycoprotein structures is difficult. Here, the authors use GlycoPRIME, a cell-free workflow for mixing-and-matching glycosylation enzymes, to evaluate 37 putative glycosylation pathways and discover routes to 18 new glycoprotein structuresWeston KightlingerKatherine E. DunckerAshvita RameshAriel H. ThamesAravind NatarajanJessica C. StarkAllen YangLiang LinMilan MrksichMatthew P. DeLisaMichael C. JewettNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-13 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Weston Kightlinger Katherine E. Duncker Ashvita Ramesh Ariel H. Thames Aravind Natarajan Jessica C. Stark Allen Yang Liang Lin Milan Mrksich Matthew P. DeLisa Michael C. Jewett A cell-free biosynthesis platform for modular construction of protein glycosylation pathways
description	Constructing biosynthetic pathways to study and engineer glycoprotein structures is difficult. Here, the authors use GlycoPRIME, a cell-free workflow for mixing-and-matching glycosylation enzymes, to evaluate 37 putative glycosylation pathways and discover routes to 18 new glycoprotein structures
format	article
author	Weston Kightlinger Katherine E. Duncker Ashvita Ramesh Ariel H. Thames Aravind Natarajan Jessica C. Stark Allen Yang Liang Lin Milan Mrksich Matthew P. DeLisa Michael C. Jewett
author_facet	Weston Kightlinger Katherine E. Duncker Ashvita Ramesh Ariel H. Thames Aravind Natarajan Jessica C. Stark Allen Yang Liang Lin Milan Mrksich Matthew P. DeLisa Michael C. Jewett
author_sort	Weston Kightlinger
title	A cell-free biosynthesis platform for modular construction of protein glycosylation pathways
title_short	A cell-free biosynthesis platform for modular construction of protein glycosylation pathways
title_full	A cell-free biosynthesis platform for modular construction of protein glycosylation pathways
title_fullStr	A cell-free biosynthesis platform for modular construction of protein glycosylation pathways
title_full_unstemmed	A cell-free biosynthesis platform for modular construction of protein glycosylation pathways
title_sort	cell-free biosynthesis platform for modular construction of protein glycosylation pathways
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/3ed28a4885534b4f9dbe3db52b4d222c
work_keys_str_mv	AT westonkightlinger acellfreebiosynthesisplatformformodularconstructionofproteinglycosylationpathways AT katherineeduncker acellfreebiosynthesisplatformformodularconstructionofproteinglycosylationpathways AT ashvitaramesh acellfreebiosynthesisplatformformodularconstructionofproteinglycosylationpathways AT arielhthames acellfreebiosynthesisplatformformodularconstructionofproteinglycosylationpathways AT aravindnatarajan acellfreebiosynthesisplatformformodularconstructionofproteinglycosylationpathways AT jessicacstark acellfreebiosynthesisplatformformodularconstructionofproteinglycosylationpathways AT allenyang acellfreebiosynthesisplatformformodularconstructionofproteinglycosylationpathways AT lianglin acellfreebiosynthesisplatformformodularconstructionofproteinglycosylationpathways AT milanmrksich acellfreebiosynthesisplatformformodularconstructionofproteinglycosylationpathways AT matthewpdelisa acellfreebiosynthesisplatformformodularconstructionofproteinglycosylationpathways AT michaelcjewett acellfreebiosynthesisplatformformodularconstructionofproteinglycosylationpathways AT westonkightlinger cellfreebiosynthesisplatformformodularconstructionofproteinglycosylationpathways AT katherineeduncker cellfreebiosynthesisplatformformodularconstructionofproteinglycosylationpathways AT ashvitaramesh cellfreebiosynthesisplatformformodularconstructionofproteinglycosylationpathways AT arielhthames cellfreebiosynthesisplatformformodularconstructionofproteinglycosylationpathways AT aravindnatarajan cellfreebiosynthesisplatformformodularconstructionofproteinglycosylationpathways AT jessicacstark cellfreebiosynthesisplatformformodularconstructionofproteinglycosylationpathways AT allenyang cellfreebiosynthesisplatformformodularconstructionofproteinglycosylationpathways AT lianglin cellfreebiosynthesisplatformformodularconstructionofproteinglycosylationpathways AT milanmrksich cellfreebiosynthesisplatformformodularconstructionofproteinglycosylationpathways AT matthewpdelisa cellfreebiosynthesisplatformformodularconstructionofproteinglycosylationpathways AT michaelcjewett cellfreebiosynthesisplatformformodularconstructionofproteinglycosylationpathways
_version_	1718382971748089856

A cell-free biosynthesis platform for modular construction of protein glycosylation pathways

Ejemplares similares