CAZypedia needs your help! We have many unassigned GH, PL, CE, AA, GT, and CBM pages in need of Authors and Responsible Curators.
Scientists at all career stages, including students, are welcome to contribute to CAZypedia. Read more here, and in the 10th anniversary article in Glycobiology.
New to the CAZy classification? Read this first.
*
Consider attending the 15th Carbohydrate Bioengineering Meeting in Ghent, 5-8 May 2024.

Difference between revisions of "Template:News"

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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!''
 
'''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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'''16 Jan 2013:''' ''Class I mannosidases &times; Williams<sup>2</sup> = 90<sup>th</sup> CAZypedia GH page.'' '''[[User:Rohan Williams|Rohan Williams]]''' and '''[[User:Spencer Williams|Spencer Williams]]''' completed the '''[[Glycoside Hydrolase Family 47]]''' page today to give CAZypedia its 90<sup>th</sup> [[:Category:Curator approved|Curator Approved]] GH page.  '''[[GH47]]''' is particularly important because it contains alpha-1,2 mannosidases that are responsible for N-glycan processing in eukaryotes.  Delineated by subfamily membership, these eukaryotic mannosidases function either in glycoprotein maturation or endoplasmic reticulum-associated degradation (ERAD).  Very few bacterial '''[[GH47]]''' members are known, in contrast, and their function(s) has not been widely studied.  From a mechanistic perspective, '''[[GH47]]''' members are intriguing because the catalytic residues have not been unambiguously identified, despite high-resolution structure-function studies of these [[inverting]] enzymes.  ''Check out the [[GH47]] page to learn more!''
 
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'''14 Jan 2013:''' ''CAZypedia makes a contribution to MediaWiki community.'' We are proud to announce that [http://www.mediawiki.org/wiki/Extension:BiblioPlus BiblioPlus], an extension that provides automatic reference formatting to CAZypedia, has been officially accepted by the [http://www.mediawiki.org/wiki/Extension:BiblioPlus MediaWiki Extensions repository].  [http://www.mediawiki.org/wiki/Extension:BiblioPlus BiblioPlus] was coded by '''[[User:Karen Eddy|Karen Eddy]]''', a UBC computer science student working with '''[[User:Harry Brumer|Harry Brumer]]''', to resolve formatting issues with non-English characters in PubMed data.  [http://www.mediawiki.org/wiki/Extension:BiblioPlus BiblioPlus] is now available for anyone to use with any MediaWiki-based site to facilitate referencing journals and books. ''Thanks Karen, for all the hard work!''
 
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'''02 Dec 2012:''' ''Spencer does it again, twice.'' '''[[User:Spencer Williams|Spencer Williams]]''' has upgraded another two [[lexicon]] pages to [[:Category:Curator approved|Curator Approved]] status today.  Have no idea what '''[[Oxazolinium ion]]s''' and '''[[Oxocarbenium ion]]s''' are, or why they're important in [[glycosidase]]s?  ''Check out these new pages!''
 
 
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Revision as of 08:59, 17 May 2013

Attention CAZymologists! Upcoming conferences:


2 May 2013: Adding on to the Lexicon: Today 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!