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Difference between revisions of "Template:News"

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* [[File:Alamy 5.jpg|left|x50px|link=http://imb.savba.sk/~janecek/Alamys/Alamy_5/]] [http://imb.savba.sk/~janecek/Alamys/Alamy_5/ Fifth Symposium on the Alpha-Amylase Family - ALAMY_5], October 20-24, Smolenice Castle, Slovakia.
 
* [[File:Alamy 5.jpg|left|x50px|link=http://imb.savba.sk/~janecek/Alamys/Alamy_5/]] [http://imb.savba.sk/~janecek/Alamys/Alamy_5/ Fifth Symposium on the Alpha-Amylase Family - ALAMY_5], October 20-24, Smolenice Castle, Slovakia.
 
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'''28 June 2013'''  ''CAZypedia'' was highlighted in a review article in ''Current Opinion in Structural Biology'' [http://dx.doi.org/10.1016/j.sbi.2013.06.001 available online today].  This review provides a succinct overview of some of the most exciting CAZyme structure-function studies in recent years, and we'd like to thank the authors, '''[[User:Shinya Fushinobu|Shinya Fushinobu]]''', Victor Alves, and '''[[User:Pedro Coutinho|Pedro Coutinho]]''', for showcasing ''CAZypedia'' as well!
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'''19 September 2013:''' ''We are proud to announce the completion of ''CAZypedia's'' first Auxiliary Activity (AA) Family page!''  '''[[User:Paul Harris|Paul Harris]]''', one of the founding fathers of the family previously known as [[GH61]], has composed a lucid summary of the history and state-of-the-art of '''[[Auxiliary Activity Family 9]]'''.  The revelation that these enzymes are actually copper-dependent ''lytic polysaccharide monooxygenases'' (LPMO), and not classic cellulases as originally thought, is one of the most exciting discoveries in enzymatic biomass degradation in recent years.  ''Read more about this fascinating class of enzymes on the '''[[AA9]]''' page, and stay tuned for forthcoming page on the closely related '''[[AA10]]]''' family.
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'''28 June 2013:'''  ''CAZypedia'' was highlighted in a review article in ''Current Opinion in Structural Biology'' [http://dx.doi.org/10.1016/j.sbi.2013.06.001 available online today].  This review provides a succinct overview of some of the most exciting CAZyme structure-function studies in recent years, and we'd like to thank the authors, '''[[User:Shinya Fushinobu|Shinya Fushinobu]]''', Victor Alves, and '''[[User:Pedro Coutinho|Pedro Coutinho]]''', for showcasing ''CAZypedia'' as well!
 
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'''23 June 2013:''' ''Yet another Lexicon page:'' With the help of '''[[User:Motomitsu Kitaoka|Motomitsu Kitaoka]]''', '''[[User:Spencer Williams|Spencer Williams]]''' updated the [[Lexicon]] page on '''[[Phosphorylases]]''' today to [[Curator Approved]] status, bringing the number of completed [[Lexicon]] pages to 20.  '''[[Phosphorylases]]''' catalyze glycosidic bond cleavage through nucleophilic substitution with phosphate (PO<sub>4</sub><sup>--</sup>), and play important roles in, for example, storage polysaccharide breakdown by generating glucose-1-phosphate as a precursor to glycolysis.  Notably, '''[[phosphorylases]]''' based on both [[Glycoside Hydrolase Families|glycoside hydrolase]] and [[Glycosyltransferase Families|glycosyltransferase]] protein folds are known.  ''Read more about this important class of carbohydrate-active enzymes '''[[Phosphorylases|here]]'''.
 
'''23 June 2013:''' ''Yet another Lexicon page:'' With the help of '''[[User:Motomitsu Kitaoka|Motomitsu Kitaoka]]''', '''[[User:Spencer Williams|Spencer Williams]]''' updated the [[Lexicon]] page on '''[[Phosphorylases]]''' today to [[Curator Approved]] status, bringing the number of completed [[Lexicon]] pages to 20.  '''[[Phosphorylases]]''' catalyze glycosidic bond cleavage through nucleophilic substitution with phosphate (PO<sub>4</sub><sup>--</sup>), and play important roles in, for example, storage polysaccharide breakdown by generating glucose-1-phosphate as a precursor to glycolysis.  Notably, '''[[phosphorylases]]''' based on both [[Glycoside Hydrolase Families|glycoside hydrolase]] and [[Glycosyltransferase Families|glycosyltransferase]] protein folds are known.  ''Read more about this important class of carbohydrate-active enzymes '''[[Phosphorylases|here]]'''.
 
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'''22 May 2013:''' ''Our very first CBM page!:'' '''[[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]''' and '''[[User:Al Boraston|Alisdair Boraston]]''' finalized ''CAZypedia's'' first [[Carbohydrate Binding Module Families|Carbohydrate Binding Module Family]] page, '''[[CBM32]]''', today.  This ushers in a new phase in ''CAZypedia's'' development, and we are looking forward to the continued evolution of this group of pages on these [[Carbohydrate-binding_modules|non-catalytic, substrate-binding, CAZyme-associated protein modules]].
 
'''22 May 2013:''' ''Our very first CBM page!:'' '''[[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]''' and '''[[User:Al Boraston|Alisdair Boraston]]''' finalized ''CAZypedia's'' first [[Carbohydrate Binding Module Families|Carbohydrate Binding Module Family]] page, '''[[CBM32]]''', today.  This ushers in a new phase in ''CAZypedia's'' development, and we are looking forward to the continued evolution of this group of pages on these [[Carbohydrate-binding_modules|non-catalytic, substrate-binding, CAZyme-associated protein modules]].
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'''2 May 2013:''' ''Adding on to the Lexicon:'' Today '''[[User:Spencer Williams|Spencer Williams]]''' added the finishing touches to the [[Lexicon]] page on '''[[Transglycosylases]]'''.  Transglycosylation - the ability to ''non-hydrolytically'' rearrange glycosidic bonds between one or more substrates - is a feature of many [[Glycoside hydrolases]], especially those which use the [[retaining]] mechanism.  In such enzymes, the covalent glycosyl-enzyme reaction intermediate can be intercepted by either water (yielding hydrolysis) or a sugar "acceptor" substrate (yielding transglycosylation).  Although transglycosylation is generally a side activity of retaining enzymes, a handful are naturally very predominant '''[[Transglycosylases]]'''.  ''See the [[Lexicon]] page to learn more, including specific examples!''
 
 
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Revision as of 10:38, 20 September 2013

Attention CAZymologists! Upcoming conference:


19 September 2013: We are proud to announce the completion of CAZypedia's first Auxiliary Activity (AA) Family page! Paul Harris, one of the founding fathers of the family previously known as GH61, has composed a lucid summary of the history and state-of-the-art of Auxiliary Activity Family 9. The revelation that these enzymes are actually copper-dependent lytic polysaccharide monooxygenases (LPMO), and not classic cellulases as originally thought, is one of the most exciting discoveries in enzymatic biomass degradation in recent years. Read more about this fascinating class of enzymes on the AA9 page, and stay tuned for forthcoming page on the closely related AA10] family.


28 June 2013: CAZypedia was highlighted in a review article in Current Opinion in Structural Biology available online today. This review provides a succinct overview of some of the most exciting CAZyme structure-function studies in recent years, and we'd like to thank the authors, Shinya Fushinobu, Victor Alves, and Pedro Coutinho, for showcasing CAZypedia as well!


23 June 2013: Yet another Lexicon page: With the help of Motomitsu Kitaoka, Spencer Williams updated the Lexicon page on Phosphorylases today to Curator Approved status, bringing the number of completed Lexicon pages to 20. Phosphorylases catalyze glycosidic bond cleavage through nucleophilic substitution with phosphate (PO4--), and play important roles in, for example, storage polysaccharide breakdown by generating glucose-1-phosphate as a precursor to glycolysis. Notably, phosphorylases based on both glycoside hydrolase and glycosyltransferase protein folds are known. Read more about this important class of carbohydrate-active enzymes here.


22 May 2013: Our very first CBM page!: Elizabeth Ficko-Blean and Alisdair Boraston finalized CAZypedia's first Carbohydrate Binding Module Family page, CBM32, today. This ushers in a new phase in CAZypedia's development, and we are looking forward to the continued evolution of this group of pages on these non-catalytic, substrate-binding, CAZyme-associated protein modules.