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Difference between revisions of "Template:News"
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'''16 Jan 2013:''' ''Class I mannosidases × 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!'' | '''16 Jan 2013:''' ''Class I mannosidases × 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- | + | '''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!'' | '''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 20:19, 16 January 2013
16 Jan 2013: Class I mannosidases × Williams2 = 90th CAZypedia GH page. Rohan Williams and Spencer Williams completed the Glycoside Hydrolase Family 47 page today to give CAZypedia its 90th 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!
14 Jan 2013: CAZypedia makes a contribution to MediaWiki community. We are proud to announce that BiblioPlus, an extension that provides automatic reference formatting to CAZypedia, has been officially accepted by the MediaWiki Extensions repository. BiblioPlus was coded by Karen Eddy, a UBC computer science student working with Harry Brumer, to resolve formatting issues with non-English characters in PubMed data. 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!
02 Dec 2012: Spencer does it again, twice. Spencer Williams has upgraded another two lexicon pages to Curator Approved status today. Have no idea what Oxazolinium ions and Oxocarbenium ions are, or why they're important in glycosidases? Check out these new pages!