Enhancing the thermostability and activity of glycosyltransferase UGT76G1 via computational design
- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- Extent
-
1 Online-Ressource.
- Language
-
Englisch
- Bibliographic citation
-
Enhancing the thermostability and activity of glycosyltransferase UGT76G1 via computational design ; volume:6 ; number:1 ; day:6 ; month:12 ; year:2023 ; pages:1-10 ; date:12.2023
Communications chemistry ; 6, Heft 1 (6.12.2023), 1-10, 12.2023
- Classification
-
Chemie
- Creator
-
Go, Seong-Ryeong
Lee, Su-Jin
Ahn, Woo-Chan
Park, Kwang-Hyun
Woo, Eui-Jeon
- Contributor
-
SpringerLink (Online service)
- DOI
-
10.1038/s42004-023-01070-6
- URN
-
urn:nbn:de:101:1-2024022214060128296835
- Rights
-
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
14.08.2025, 10:50 AM CEST
Data provider
This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Go, Seong-Ryeong
- Lee, Su-Jin
- Ahn, Woo-Chan
- Park, Kwang-Hyun
- Woo, Eui-Jeon
- SpringerLink (Online service)
Other Objects (12)
Enhancing the thermostability and activity of uronate dehydrogenase from Agrobacterium tumefaciens LBA4404 by semi-rational engineering
Thermostability of enzymes
Thermostability and excision activity of polymorphic forms of hOGG1
Development of computational approaches for knowledge-driven protein engineering aimed at improving thermostability
Glycosyltransferase efficiently controls phenylpropanoid pathway
Determinants for the improved thermostability of a mesophilic family 11 xylanase predicted by computational methods
Thermostability in endoglucanases is fold-specific
Consistent mutational paths predict eukaryotic thermostability
Cellulase protein engineering towards improved thermostability
Novel cytotoxic glycosyltransferase effectors of Legionella
A unique self-truncation of bacterial GH5 endoglucanases leads to enhanced activity and thermostability
Health enhancing physical activity
Enhancing the thermostability and activity of uronate dehydrogenase from Agrobacterium tumefaciens LBA4404 by semi-rational engineering
Thermostability of enzymes
Thermostability and excision activity of polymorphic forms of hOGG1
Development of computational approaches for knowledge-driven protein engineering aimed at improving thermostability
Glycosyltransferase efficiently controls phenylpropanoid pathway
Determinants for the improved thermostability of a mesophilic family 11 xylanase predicted by computational methods
Thermostability in endoglucanases is fold-specific
Consistent mutational paths predict eukaryotic thermostability
Cellulase protein engineering towards improved thermostability
Novel cytotoxic glycosyltransferase effectors of Legionella
A unique self-truncation of bacterial GH5 endoglucanases leads to enhanced activity and thermostability
Health enhancing physical activity
Enhancing the thermostability and activity of uronate dehydrogenase from Agrobacterium tumefaciens LBA4404 by semi-rational engineering
Thermostability of enzymes
Thermostability and excision activity of polymorphic forms of hOGG1
Development of computational approaches for knowledge-driven protein engineering aimed at improving thermostability
Glycosyltransferase efficiently controls phenylpropanoid pathway
Determinants for the improved thermostability of a mesophilic family 11 xylanase predicted by computational methods
Thermostability in endoglucanases is fold-specific
Consistent mutational paths predict eukaryotic thermostability
Cellulase protein engineering towards improved thermostability
Novel cytotoxic glycosyltransferase effectors of Legionella
A unique self-truncation of bacterial GH5 endoglucanases leads to enhanced activity and thermostability