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Difference between revisions of "User:Mohamed Attia"

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Mohamed Attia obtained his B.Sc. in Pharmacy from Alexandria University, Egypt. He then completed his M.Sc. in the Department of Biological Sciences at University of Calgary where he studied the biosynthetic pathway of the sweet sesquiterpene hernandulcin from ''Lippia dulcis'' leaves  <cite>Attia2012</cite>. He then pursued his Ph.D. in the Department of Chemistry at University of British Columbia under the supervision of ^^^Harry Brumer^^^.  During his Ph.D., Mohamed extensively studied the xyloglucan degradation pathway in the soil saprophyte ''Cellvibrio japonicus'' and he successfully identified and functionally characterized a large suite of glycoside hydrolases from families [[GH3]] <cite>Nelson2017</cite>, [[GH5]] <cite>Attia2018</cite> and [[GH74]] <cite>Attia2016</cite> that are fundamentally involved in the saccharification process.
  
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#Gilbert2008 pmid=18430603
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#Attia2012 pmid=22867794
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#Nelson2017 pmid=29052930
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#Attia2018 pmid=29467823
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#Attia2016 pmid=26929175
  
 
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Revision as of 16:21, 21 March 2018

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Mohamed Attia obtained his B.Sc. in Pharmacy from Alexandria University, Egypt. He then completed his M.Sc. in the Department of Biological Sciences at University of Calgary where he studied the biosynthetic pathway of the sweet sesquiterpene hernandulcin from Lippia dulcis leaves [1]. He then pursued his Ph.D. in the Department of Chemistry at University of British Columbia under the supervision of ^^^Harry Brumer^^^. During his Ph.D., Mohamed extensively studied the xyloglucan degradation pathway in the soil saprophyte Cellvibrio japonicus and he successfully identified and functionally characterized a large suite of glycoside hydrolases from families GH3 [2], GH5 [3] and GH74 [4] that are fundamentally involved in the saccharification process.




  1. Attia M, Kim SU, and Ro DK. (2012). Molecular cloning and characterization of (+)-epi-α-bisabolol synthase, catalyzing the first step in the biosynthesis of the natural sweetener, hernandulcin, in Lippia dulcis. Arch Biochem Biophys. 2012;527(1):37-44. DOI:10.1016/j.abb.2012.07.010 | PubMed ID:22867794 [Attia2012]
  2. Nelson CE, Attia MA, Rogowski A, Morland C, Brumer H, and Gardner JG. (2017). Comprehensive functional characterization of the glycoside hydrolase family 3 enzymes from Cellvibrio japonicus reveals unique metabolic roles in biomass saccharification. Environ Microbiol. 2017;19(12):5025-5039. DOI:10.1111/1462-2920.13959 | PubMed ID:29052930 [Nelson2017]
  3. Attia MA, Nelson CE, Offen WA, Jain N, Davies GJ, Gardner JG, and Brumer H. (2018). In vitro and in vivo characterization of three Cellvibrio japonicus glycoside hydrolase family 5 members reveals potent xyloglucan backbone-cleaving functions. Biotechnol Biofuels. 2018;11:45. DOI:10.1186/s13068-018-1039-6 | PubMed ID:29467823 [Attia2018]
  4. Attia M, Stepper J, Davies GJ, and Brumer H. (2016). Functional and structural characterization of a potent GH74 endo-xyloglucanase from the soil saprophyte Cellvibrio japonicus unravels the first step of xyloglucan degradation. FEBS J. 2016;283(9):1701-19. DOI:10.1111/febs.13696 | PubMed ID:26929175 [Attia2016]

All Medline abstracts: PubMed