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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 [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]).


  1. Juge N, Rodenburg KW, Guo XJ, Chaix JC, and Svensson B. Isozyme hybrids within the protruding third loop domain of the barley alpha-amylase (beta/alpha)8-barrel. Implication for BASI sensitivity and substrate affinity. FEBS Lett 1995 Apr 24; 363(3) 299-303. pmid:7737421. PubMed HubMed [Juge1995]
  2. Giardina T, Gunning AP, Juge N, Faulds CB, Furniss CS, Svensson B, Morris VJ, and Williamson G. Both binding sites of the starch-binding domain of Aspergillus niger glucoamylase are essential for inducing a conformational change in amylose. J Mol Biol 2001 Nov 9; 313(5) 1149-59. doi:10.1006/jmbi.2001.5097 pmid:11700070. PubMed HubMed [Giardina2001]
  3. Juge N, Nøhr J, Le Gal-Coëffet MF, Kramhøft B, Furniss CS, Planchot V, Archer DB, Williamson G, and Svensson B. The activity of barley alpha-amylase on starch granules is enhanced by fusion of a starch binding domain from Aspergillus niger glucoamylase. Biochim Biophys Acta 2006 Feb; 1764(2) 275-84. doi:10.1016/j.bbapap.2005.11.008 pmid:16403494. PubMed HubMed [Jugea2006]
  4. Juge N. Plant protein inhibitors of cell wall degrading enzymes. Trends Plant Sci 2006 Jul; 11(7) 359-67. doi:10.1016/j.tplants.2006.05.006 pmid:16774842. PubMed HubMed [Jugeb2006]
  5. André-Leroux G, Berrin JG, Georis J, Arnaut F, and Juge N. Structure-based mutagenesis of Penicillium griseofulvum xylanase using computational design. Proteins 2008 Sep; 72(4) 1298-307. doi:10.1002/prot.22029 pmid:18384043. PubMed HubMed [AndreLeroux2008]
  6. Durand A, Hughes R, Roussel A, Flatman R, Henrissat B, and Juge N. Emergence of a subfamily of xylanase inhibitors within glycoside hydrolase family 18. FEBS J 2005 Apr; 272(7) 1745-55. doi:10.1111/j.1742-4658.2005.04606.x pmid:15794761. PubMed HubMed [Durand2005]
  7. Payan F, Leone P, Porciero S, Furniss C, Tahir T, Williamson G, Durand A, Manzanares P, Gilbert HJ, Juge N, and Roussel A. The dual nature of the wheat xylanase protein inhibitor XIP-I: structural basis for the inhibition of family 10 and family 11 xylanases. J Biol Chem 2004 Aug 20; 279(34) 36029-37. doi:10.1074/jbc.M404225200 pmid:15181003. PubMed HubMed [Payan2004]
  8. Tribolo S, Berrin JG, Kroon PA, Czjzek M, and Juge N. The crystal structure of human cytosolic beta-glucosidase unravels the substrate aglycone specificity of a family 1 glycoside hydrolase. J Mol Biol 2007 Jul 27; 370(5) 964-75. doi:10.1016/j.jmb.2007.05.034 pmid:17555766. PubMed HubMed [Tribolo2007]
  9. Berrin JG, Czjzek M, Kroon PA, McLauchlan WR, Puigserver A, Williamson G, and Juge N. Substrate (aglycone) specificity of human cytosolic beta-glucosidase. Biochem J 2003 Jul 1; 373(Pt 1) 41-8. doi:10.1042/BJ20021876 pmid:12667141. PubMed HubMed [Berrin2003]
  10. MacKenzie DA, Tailford LE, Hemmings AM, and Juge N. Crystal structure of a mucus-binding protein repeat reveals an unexpected functional immunoglobulin binding activity. J Biol Chem 2009 Nov 20; 284(47) 32444-53. doi:10.1074/jbc.M109.040907 pmid:19758995. PubMed HubMed [MacKenzie2009]
All Medline abstracts: PubMed HubMed
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