Dissecting Context-Specific Galectin Binding Using Glycoengineered Cell Libraries

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Standard

Dissecting Context-Specific Galectin Binding Using Glycoengineered Cell Libraries. / Nielsen, Mathias Ingemann; Wandall, Hans H.

Galectins : Methods and Protocols. Humana Press, 2022. s. 205-214 (Methods in Molecular Biology, Bind 2442).

Publikation: Bidrag til bog/antologi/rapport › Bidrag til bog/antologi › Forskning › fagfællebedømt

Harvard

Nielsen, MI & Wandall, HH 2022, Dissecting Context-Specific Galectin Binding Using Glycoengineered Cell Libraries. i Galectins : Methods and Protocols. Humana Press, Methods in Molecular Biology, bind 2442, s. 205-214. https://doi.org/10.1007/978-1-0716-2055-7_12

APA

Nielsen, M. I., & Wandall, H. H. (2022). Dissecting Context-Specific Galectin Binding Using Glycoengineered Cell Libraries. I Galectins : Methods and Protocols (s. 205-214). Humana Press. Methods in Molecular Biology Bind 2442 https://doi.org/10.1007/978-1-0716-2055-7_12

Vancouver

Nielsen MI, Wandall HH. Dissecting Context-Specific Galectin Binding Using Glycoengineered Cell Libraries. I Galectins : Methods and Protocols. Humana Press. 2022. s. 205-214. (Methods in Molecular Biology, Bind 2442). https://doi.org/10.1007/978-1-0716-2055-7_12

Author

Nielsen, Mathias Ingemann ; Wandall, Hans H. / Dissecting Context-Specific Galectin Binding Using Glycoengineered Cell Libraries. Galectins : Methods and Protocols. Humana Press, 2022. s. 205-214 (Methods in Molecular Biology, Bind 2442).

Bibtex

@inbook{dd1d8110891747378d406abe3935e46f,
title = "Dissecting Context-Specific Galectin Binding Using Glycoengineered Cell Libraries",
abstract = "The family of galectins has critical functions in a wide range of biological processes, primarily based on their broad interactions with proteins carrying β-galactoside-containing glycans. To understand the diversity of functions governed by galectins, it is essential to define the binding specificity of the carbohydrate recognition domain (CRDs) of the individual galectins. The binding specificity of galectins has primarily been examined with glycoarrays, but now the ability to probe and dissect binding to defined glycans in the context of a cellular membrane is facilitated by the generations of glycoengineered cell libraries with defined glyco-phenotypes. The following section will show how galectin specificities can be probed in the natural context of cellular surfaces using glycoengineered cell libraries, and how binding to glycoproteins can be measured in solution with fluorescence anisotropy.",
keywords = "Carbohydrate binding proteins, Galectin, Gene editing, Glycoengineering, Glycogenes, Glycosylation, Glycosyltransferases, Substrate specificity",
author = "Nielsen, {Mathias Ingemann} and Wandall, {Hans H.}",
note = "Publisher Copyright: {\textcopyright} 2022, Springer Science+Business Media, LLC, part of Springer Nature.",
year = "2022",
doi = "10.1007/978-1-0716-2055-7_12",
language = "English",
isbn = "978-1-0716-2054-0",
series = "Methods in Molecular Biology",
publisher = "Humana Press",
pages = "205--214",
booktitle = "Galectins",
address = "United States",

}

RIS

TY - CHAP

T1 - Dissecting Context-Specific Galectin Binding Using Glycoengineered Cell Libraries

AU - Nielsen, Mathias Ingemann

AU - Wandall, Hans H.

N1 - Publisher Copyright: © 2022, Springer Science+Business Media, LLC, part of Springer Nature.

PY - 2022

Y1 - 2022

N2 - The family of galectins has critical functions in a wide range of biological processes, primarily based on their broad interactions with proteins carrying β-galactoside-containing glycans. To understand the diversity of functions governed by galectins, it is essential to define the binding specificity of the carbohydrate recognition domain (CRDs) of the individual galectins. The binding specificity of galectins has primarily been examined with glycoarrays, but now the ability to probe and dissect binding to defined glycans in the context of a cellular membrane is facilitated by the generations of glycoengineered cell libraries with defined glyco-phenotypes. The following section will show how galectin specificities can be probed in the natural context of cellular surfaces using glycoengineered cell libraries, and how binding to glycoproteins can be measured in solution with fluorescence anisotropy.

AB - The family of galectins has critical functions in a wide range of biological processes, primarily based on their broad interactions with proteins carrying β-galactoside-containing glycans. To understand the diversity of functions governed by galectins, it is essential to define the binding specificity of the carbohydrate recognition domain (CRDs) of the individual galectins. The binding specificity of galectins has primarily been examined with glycoarrays, but now the ability to probe and dissect binding to defined glycans in the context of a cellular membrane is facilitated by the generations of glycoengineered cell libraries with defined glyco-phenotypes. The following section will show how galectin specificities can be probed in the natural context of cellular surfaces using glycoengineered cell libraries, and how binding to glycoproteins can be measured in solution with fluorescence anisotropy.

KW - Carbohydrate binding proteins

KW - Galectin

KW - Gene editing

KW - Glycoengineering

KW - Glycogenes

KW - Glycosylation

KW - Glycosyltransferases

KW - Substrate specificity

U2 - 10.1007/978-1-0716-2055-7_12

DO - 10.1007/978-1-0716-2055-7_12

M3 - Book chapter

C2 - 35320528

AN - SCOPUS:85126840389

SN - 978-1-0716-2054-0

T3 - Methods in Molecular Biology

SP - 205

EP - 214

BT - Galectins

PB - Humana Press

ER -

ID: 305715154