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Difference between revisions of "User:Marie Sofie Moeller"
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| − | + | In 2013 Marie Sofie Møller completed her PhD under the supervision of ^^^Birte Svensson^^^ and Maher Abou Hachem at the Technical University of Denmark. She has mainly been focusing on structure-function relationship studies of glycoside hydrolases from family [[GH13]]. At the Carlsberg Research Laboratory under supervision by Anette Henriksen, she has been determining several structures of GH13_13 barley limit dextrinase including the first structure of an ɑ-glucan debranching enzyme in complex with a natural substrate, i.e. a branched maltooligosaccharide (limit dextrin). Furthermore, she has determined the complex structure between barley limit dextrinase and its endogenous inhibitor, a 13.4 kDa cereal type inhibitor. The study of the latter complex resulted in a spin-off project, which she got granted by an individual postdoc grant from the Independent Research Fund Denmark. The project was carried out in the laboratory of Ingemar André at Lund University, Sweden. The spin-off project focused on understanding the high-affinity (pM) using computational redesign. | |
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| + | In 2016 she returned to the Technical University of Denmark, where she holds a position as Assistant Professor in the group of ^^^Birte Svensson^^^. She is currently working on a project on low affinity protein-carbohydrate interactions focusing on carbohydrate binding module families [[CBM10]] and [[CBM45]]. The CBM10s studied originate from a [[GH5]] subfamily 8 mannanase from a marine bacterium, while the CBM45s originate from a glucan, water dikinase from potato. | ||
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<biblio> | <biblio> | ||
| − | # | + | #Jensen2011 pmid=21539920 |
| + | #Moeller2012a pmid=22949184 | ||
| + | #Moeller2012b pmid=22685275 | ||
| + | #Moeller2015a pmid=25562209 | ||
| + | #Moeller2015b pmid=25792743 | ||
| + | #Moeller2016a pmid=27137180 | ||
| + | #Moeller2016b pmid=27450115 | ||
| + | #Moeller2017 pmid=28411221 | ||
| + | #Wilkens2018 pmid=30483298 | ||
| + | #Holck2019 pmid=31558605 | ||
| + | #Andersen2019 pmid=31676454 | ||
</biblio> | </biblio> | ||
<!-- Do not remove this Category tag --> | <!-- Do not remove this Category tag --> | ||
[[Category:Contributors|Moeller,Marie-Sofie]] | [[Category:Contributors|Moeller,Marie-Sofie]] | ||
Revision as of 05:18, 6 November 2019
In 2013 Marie Sofie Møller completed her PhD under the supervision of ^^^Birte Svensson^^^ and Maher Abou Hachem at the Technical University of Denmark. She has mainly been focusing on structure-function relationship studies of glycoside hydrolases from family GH13. At the Carlsberg Research Laboratory under supervision by Anette Henriksen, she has been determining several structures of GH13_13 barley limit dextrinase including the first structure of an ɑ-glucan debranching enzyme in complex with a natural substrate, i.e. a branched maltooligosaccharide (limit dextrin). Furthermore, she has determined the complex structure between barley limit dextrinase and its endogenous inhibitor, a 13.4 kDa cereal type inhibitor. The study of the latter complex resulted in a spin-off project, which she got granted by an individual postdoc grant from the Independent Research Fund Denmark. The project was carried out in the laboratory of Ingemar André at Lund University, Sweden. The spin-off project focused on understanding the high-affinity (pM) using computational redesign.
In 2016 she returned to the Technical University of Denmark, where she holds a position as Assistant Professor in the group of ^^^Birte Svensson^^^. She is currently working on a project on low affinity protein-carbohydrate interactions focusing on carbohydrate binding module families CBM10 and CBM45. The CBM10s studied originate from a GH5 subfamily 8 mannanase from a marine bacterium, while the CBM45s originate from a glucan, water dikinase from potato.
- Jensen JM, Vester-Christensen MB, Møller MS, Bønsager BC, Christensen HE, Hachem MA, and Svensson B. (2011). Efficient secretory expression of functional barley limit dextrinase inhibitor by high cell-density fermentation of Pichia pastoris. Protein Expr Purif. 2011;79(2):217-22. DOI:10.1016/j.pep.2011.04.009 |
- Møller MS, Abou Hachem M, Svensson B, and Henriksen A. (2012). Structure of the starch-debranching enzyme barley limit dextrinase reveals homology of the N-terminal domain to CBM21. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012;68(Pt 9):1008-12. DOI:10.1107/S1744309112031004 |
- Møller MS, Fredslund F, Majumder A, Nakai H, Poulsen JC, Lo Leggio L, Svensson B, and Abou Hachem M. (2012). Enzymology and structure of the GH13_31 glucan 1,6-α-glucosidase that confers isomaltooligosaccharide utilization in the probiotic Lactobacillus acidophilus NCFM. J Bacteriol. 2012;194(16):4249-59. DOI:10.1128/JB.00622-12 |
- Møller MS, Windahl MS, Sim L, Bøjstrup M, Abou Hachem M, Hindsgaul O, Palcic M, Svensson B, and Henriksen A. (2015). Oligosaccharide and substrate binding in the starch debranching enzyme barley limit dextrinase. J Mol Biol. 2015;427(6 Pt B):1263-1277. DOI:10.1016/j.jmb.2014.12.019 |
- Møller MS, Vester-Christensen MB, Jensen JM, Hachem MA, Henriksen A, and 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. J Biol Chem. 2015;290(20):12614-29. DOI:10.1074/jbc.M115.642777 |
- Møller MS, Henriksen A, and Svensson B. (2016). Structure and function of α-glucan debranching enzymes. Cell Mol Life Sci. 2016;73(14):2619-41. DOI:10.1007/s00018-016-2241-y |
- Møller MS and Svensson B. (2016). Structural biology of starch-degrading enzymes and their regulation. Curr Opin Struct Biol. 2016;40:33-42. DOI:10.1016/j.sbi.2016.07.006 |
- Møller MS, Goh YJ, Rasmussen KB, Cypryk W, Celebioglu HU, Klaenhammer TR, Svensson B, and Abou Hachem M. (2017). An Extracellular Cell-Attached Pullulanase Confers Branched α-Glucan Utilization in Human Gut Lactobacillus acidophilus. Appl Environ Microbiol. 2017;83(12). DOI:10.1128/AEM.00402-17 |
- Wilkens C, Svensson B, and Møller MS. (2018). Functional Roles of Starch Binding Domains and Surface Binding Sites in Enzymes Involved in Starch Biosynthesis. Front Plant Sci. 2018;9:1652. DOI:10.3389/fpls.2018.01652 |
- Holck J, Fredslund F, Møller MS, Brask J, Krogh KBRM, Lange L, Welner DH, Svensson B, Meyer AS, and Wilkens C. (2019). A carbohydrate-binding family 48 module enables feruloyl esterase action on polymeric arabinoxylan. J Biol Chem. 2019;294(46):17339-17353. DOI:10.1074/jbc.RA119.009523 |
- Andersen S, Svensson B, and Møller MS. (2020). Roles of the N-terminal domain and remote substrate binding subsites in activity of the debranching barley limit dextrinase. Biochim Biophys Acta Proteins Proteom. 2020;1868(1):140294. DOI:10.1016/j.bbapap.2019.140294 |