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Difference between revisions of "User:Nathalie Juge"
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| − | Nathalie Juge started working on carbohydrate-active enzymes during her PhD she obtained in 1993 in Marseille (France) on the structure-function studies of barley alpha-amylases ([[GH13]]) (see for example <cite>Juge1995</cite>). After two post-doctoral positions in Carlsberg, Copenhagen, Denmark (on EMBO fellowship and EU contract) with Birte Svensson, and a Marie-Curie fellowship at the Institute of Food Research (IFR, Norwich, UK) on glucoamylase ([[GH15]]) <cite>Giardina2001</cite> and starch binding domain (CBM20) <cite>Jugea2006</cite>, she moved back to Marseille as a lecturer in 1997. She then spent several years as visiting scientist at IFR where she coordinated an EU project on glycosidase inhibitors (for a review, see <cite>Jugeb2006</cite>) , her Group focusing on xylanases ([[GH10]] & [[GH11]]) (see for example <cite>AndreLeroux2008</cite>) and xylanase inhibitors ([[GH18]]) <cite>Durand2005 Payan2004</cite> , and supervising a project on human beta-glucosidase ([[GH1]] <cite>Tribolo2007 Berrin2003</cite>. She recently joined the Integrated Biology of the Gastrointestinal Tract programme at IFR to lead a Group focusing on the molecular mechanisms underlying bacteria-mucus interactions and the role of protein-glycan interactions in the control of bacterial adhesion. | + | Nathalie Juge started working on carbohydrate-active enzymes during her PhD she obtained in 1993 in Marseille (France) on the structure-function studies of barley alpha-amylases ([[GH13]]) (see for example <cite>Juge1995</cite>). After two post-doctoral positions in Carlsberg, Copenhagen, Denmark (on EMBO fellowship and EU contract) with Birte Svensson, and a Marie-Curie fellowship at the Institute of Food Research (IFR, Norwich, UK) on glucoamylase ([[GH15]]) <cite>Giardina2001</cite> and starch binding domain (CBM20) <cite>Jugea2006</cite>, she moved back to Marseille as a lecturer in 1997. She then spent several years as visiting scientist at IFR where she coordinated an EU project on glycosidase inhibitors (for a review, see <cite>Jugeb2006</cite>), her Group focusing on xylanases ([[GH10]] & [[GH11]]) (see for example <cite>AndreLeroux2008</cite>) and xylanase inhibitors ([[GH18]]) <cite>Durand2005 Payan2004</cite> , and supervising a project on human beta-glucosidase ([[GH1]]) <cite>Tribolo2007 Berrin2003</cite>. She recently joined the Integrated Biology of the Gastrointestinal Tract programme at IFR to lead a Group focusing on the molecular mechanisms underlying bacteria-mucus interactions and the role of protein-glycan interactions in the control of bacterial adhesion (<cite>MacKenzie2009</cite>). |
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#Tribolo2007 pmid=17555766 | #Tribolo2007 pmid=17555766 | ||
#Jugeb2006 pmid=16774842 | #Jugeb2006 pmid=16774842 | ||
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#Jugea2006 pmid=16403494 | #Jugea2006 pmid=16403494 | ||
#AndreLeroux2008 pmid=18384043 | #AndreLeroux2008 pmid=18384043 | ||
| + | #MacKenzie2009 pmid=19758995 | ||
Latest revision as of 12:09, 8 February 2011
Nathalie Juge started working on carbohydrate-active enzymes during her PhD she obtained in 1993 in Marseille (France) on the structure-function studies of barley alpha-amylases (GH13) (see for example [1]). After two post-doctoral positions in Carlsberg, Copenhagen, Denmark (on EMBO fellowship and EU contract) with Birte Svensson, and a Marie-Curie fellowship at the Institute of Food Research (IFR, Norwich, UK) on glucoamylase (GH15) [2] and starch binding domain (CBM20) [3], she moved back to Marseille as a lecturer in 1997. She then spent several years as visiting scientist at IFR where she coordinated an EU project on glycosidase inhibitors (for a review, see [4]), her Group focusing on xylanases (GH10 & GH11) (see for example [5]) and xylanase inhibitors (GH18) [6, 7] , and supervising a project on human beta-glucosidase (GH1) [8, 9]. She recently joined the Integrated Biology of the Gastrointestinal Tract programme at IFR to lead a Group focusing on the molecular mechanisms underlying bacteria-mucus interactions and the role of protein-glycan interactions in the control of bacterial adhesion ([10]).
<biblio>
- Tribolo2007 pmid=17555766
- Jugeb2006 pmid=16774842
- Durand2005 pmid=15794761
- Payan2004 pmid=15181003
- Berrin2003 pmid=12667141
- Giardina2001 pmid=11700070
- Juge1995 pmid=7737421
- Jugea2006 pmid=16403494
- AndreLeroux2008 pmid=18384043
- MacKenzie2009 pmid=19758995