Exploration of the Transglycosylation Activity of Barley Limit Dextrinase for Production of Novel Glycoconjugates

Autor: Malene Bech Vester-Christensen, Jesper Holck, Martin Rejzek, Léa Perrin, Morten Tovborg, Birte Svensson, Robert A. Field, Marie Sofie Møller

Publikováno v: Molecules, Vol 28, Iss 10, p 4111 (2023)

A few α-glucan debranching enzymes (DBEs) of the large glycoside hydrolase family 13 (GH13), also known as the α-amylase family, have been shown to catalyze transglycosylation as well as hydrolysis. However, little is known about their acceptor and

Externí odkaz: https://doaj.org/article/620f05c062cd4838b1d09b34822420f3

Optimizing selectivity of anion hydrophobic multimodal chromatography for purification of a single-chain variable fragment

Autor: Malene Bech Vester-Christensen, Jens Jacob Hansen, Maria B. Dainiak, Ileana Rodríguez León, Leif Bülow, Laila I. Sakhnini, Anja K. Pedersen, Per Jr Greisen

Publikováno v: Eng Life Sci

Single-chain variable fragments (scFv) are widely used in several fields. However, they can be challenging to purify unless using expensive Protein L-based affinity adsorbents or affinity tags. In this work, a purification process for a scFv using mi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d43786f784cc4d5267dc45d8b0181e90
https://pubmed.ncbi.nlm.nih.gov/32625026

Crystal Structure of Barley Limit Dextrinase-Limit Dextrinase Inhibitor (LD-LDI) Complex Reveals Insights into Mechanism and Diversity of Cereal Type Inhibitors

Autor: Maher Abou Hachem, Marie Sofie Møller, Anette Henriksen, Johanne Mørch Jensen, Birte Svensson, Malene Bech Vester-Christensen

Publikováno v: Møller, M S, Vester-Christensen, M B, Jensen, J M, Abou Hachem, M, Henriksen, A & Svensson, B 2015, ' Crystal Structure of Barley Limit Dextrinase-Limit Dextrinase Inhibitor (LD-LDI) Complex Reveals Insights into Mechanism and Diversity of Cereal Type Inhibitors ', Journal of Biological Chemistry, vol. 290, no. 20, pp. 12614-12629 . https://doi.org/10.1074/jbc.M115.642777

Molecular details underlying regulation of starch mobilization in cereal seed endosperm remain unknown despite the paramount role of this process in plant growth. The structure of the complex between the starch debranching enzyme barley limit dextrin

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7eed948771a991548312b484bb46604d
https://doi.org/10.1074/jbc.m115.642777

Enhanced Mass Spectrometric Mapping of the Human GalNAc-type O-Glycoproteome with SimpleCells

Autor: Malene Bech Vester-Christensen, Eric P. Bennett, Steven B. Levery, Henrik Clausen, Sergey Y. Vakhrushev, Catharina Steentoft

Publikováno v: Molecular & Cellular Proteomics. 12:932-944

Characterizing protein GalNAc-type O-glycosylation has long been a major challenge, and as a result, our understanding of this glycoproteome is particularly poor. Recently, we presented a novel strategy for high throughput identification of O-GalNAc

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c2f59e24280c6a3bfc86df553cc1ba74
https://doi.org/10.1074/mcp.o112.021972

A Systematic Study of Site-specific GalNAc-type O-Glycosylation Modulating Proprotein Convertase Processing

Autor: Malene Bech Vester-Christensen, Katrine T. Schjoldager, Henrik Clausen, Søren Brunak, Christoffer K. Goth, Thomas Nordahl Petersen, Steven B. Levery, Eric P. Bennett

Publikováno v: Journal of Biological Chemistry. 286:40122-40132

Site-specific GalNAc-type O-glycosylation is emerging as an important co-regulator of proprotein convertase (PC) processing of proteins. PC processing is crucial in regulating many fundamental biological pathways and O-glycans in or immediately adjac

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3170281add05794572c364419f7ca6cf
https://doi.org/10.1074/jbc.m111.287912