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Difference between revisions of "User:Wade Abbott"

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#Abbott2007b pmid=17292916
 
#Abbott2007b pmid=17292916
 
#Abbott2007c pmid=17881361
 
#Abbott2007c pmid=17881361
 
 
#Abbott2008a pmid=18032406
 
#Abbott2008a pmid=18032406
 
 
 
#Finn2008 pmid=18292090
 
#Finn2008 pmid=18292090
 
 
 
#Abbott2009a pmid=19181667
 
#Abbott2009a pmid=19181667
 
 
#Abbott2009b pmid=19181667
 
#Abbott2009b pmid=19181667
+
#Abbott2010a pmid=20851883
 
+
#Correia2010 pmid=20496884
#Abbott2010a pmid=
+
#Abbott2011 pmid=21505233
20851883
+
#Pluvinage2011 pmid=22078560
 
+
#Abbott2012 pmid=22297983
#Correia2010 pmid=
+
#Pluvinage2013 pmid=23154168
20496884
+
#Abbott2013 pmid=24013861
#Abbott2011 pmid=
 
21505233
 
#Pluvinage2011 pmid=
 
22078560
 
 
#Abbott2012 pmid=
 
22297983
 
 
#Pluvinage2013 pmid=
 
23154168
 
#Abbott2013 pmid=
 
24013861
 
 
   
 
   
  
 
[[Category:Contributors|Abbott, Wade]]
 
[[Category:Contributors|Abbott, Wade]]

Revision as of 14:09, 23 September 2013

Wade.jpg

Dr. Abbott received his PhD from the University of Victoria in 2005. He then studied the molecular basis of protein-carbohydrate interactions under Dr. ^^^Alisdair Boraston^^^ at the University of Victoria. In 2008, Dr. Abbott joined Dr. ^^^Harry Gilbert^^^ at the Complex Carbohydrate Research Centre, at the University of Georgia where he investigated the functional genomics of carbohydrate utilization pathways from intestinal bacteria. Currently, Dr. Abbott is a Research Scientist for Agriculture and Agri-Food Canada based at the Lethbridge Research Centre and Adjunct Professor at the University of Lethbridge. His research program investigates the mechanisms of complex carbohydrate modification by intestinal bacteria, and is developing applications for carbohydrates in animal agriculture and human intestinal health.


Glycoside Hydrolases

  • GH20 Streptococcus pneumoniae exo-β-D-N-acetylglucosaminidase (SpnGH20/StrH)[1]. Streptococcus pneumoniae exo-β-D-N-acetylglucosaminidase (SpnGH20/StrH). [2]
  • GH28 Yersinia enterocolitica Exopolygalacturonase (YeGH28)[3]
  • GH85 Streptococcus pneumoniae Endo-beta-D-glucosaminidase D (SpGH85/EndoD)[4]


Polysaccharide Lyases

  • PL2 Yersinia enterocolitica Perplasmic pectate lyase (YePL2A)[5]. Paenibacillus sp. Y412MC10 Cytoplasmic endolytic pectate lyase (PaePL2)[6].
  • PL22 Yersinia enterocolitica Cytoplasmic oligogalacturonate lyase (YePL22/Ogl)[7]

Carbohydrate Binding Modules

  • CBM6 Predicting CBM6 function [8]
  • CBM32 Yersinia enterocolitica Polygalacturonic acid binding protein (YeCBM32)[9]. Predicting CBM32 function [10]. Streptococcus pneumoniae EndoD CBM (SpnCBM32)[11].
  • CBM35 Predicting CBM35 function [12]
  • CBM51 Clostridium perfringens Blood group binding CBMs (GH95CBM51 and GH98CBM51)[9]. Predicting CBM51 function [13]

Carbohydrate Esterases

  • CE8 Yersinia enterocolitica Pectin methylesterase [14]

<biblio>

  1. Abbott2007a pmid=17397864
  2. Abbott2007b pmid=17292916
  3. Abbott2007c pmid=17881361
  4. Abbott2008a pmid=18032406
  5. Finn2008 pmid=18292090
  6. Abbott2009a pmid=19181667
  7. Abbott2009b pmid=19181667
  8. Abbott2010a pmid=20851883
  9. Correia2010 pmid=20496884
  10. Abbott2011 pmid=21505233
  11. Pluvinage2011 pmid=22078560
  12. Abbott2012 pmid=22297983
  13. Pluvinage2013 pmid=23154168
  14. Abbott2013 pmid=24013861