CAZypedia needs your help!
We have many unassigned pages in need of Authors and Responsible Curators. See a page that's out-of-date and just needs a touch-up? - You are also welcome to become a CAZypedian. Here's how.
Scientists at all career stages, including students, are welcome to contribute.
Learn more about CAZypedia's misson here and in this article.
Totally new to the CAZy classification? Read this first.

Difference between revisions of "Template:News"

From CAZypedia
Jump to navigation Jump to search
Line 1: Line 1:
'''19 March 2015:'''  ''Closing-in on 100:'' ''CAZypedia'' is on the way to an important milestone, our 100th [[Curator Approved]] [[Glycoside Hydrolase Families|Glycoside Hydrolase Family]] page.  Thanks go to our colleagues '''[[User:Tomomi Sumida|Tomomi Sumida]]''', who completed the '''[[Glycoside Hydrolase Family 123]]''' page on March 17, and '''[[User:Wataru Saburi|Wataru Saburi]]''' and '''[[User:Haruhide Mori|Haruhide Mori]]''', who completed the '''[[Glycoside Hydrolase Family 130]]''' page on March 18.  Members of these two [[Glycoside Hydrolase Families|GH families]] represent very distinct structures, specificities mechanisms, which you can learn more about on their individual pages.  The high GH family numbers of these two groups reflects their comparatively recent addition to the CAZy Database and highlights the continuing evolution of the field through the discovery of new CAZymes.
+
'''19 March 2015:'''  ''Closing-in on 100:'' ''CAZypedia'' is on the way to an important milestone, our 100th [[Curator Approved]] [[Glycoside Hydrolase Families|Glycoside Hydrolase Family]] page.  Thanks go to our colleagues '''[[User:Tomomi Sumida|Tomomi Sumida]]''', who completed the '''[[Glycoside Hydrolase Family 123]]''' page on March 17, and '''[[User:Wataru Saburi|Wataru Saburi]]''' and '''[[User:Haruhide Mori|Haruhide Mori]]''', who completed the '''[[Glycoside Hydrolase Family 130]]''' page on March 18.  Members of these two [[Glycoside Hydrolase Families|GH families]] represent very distinct structures, specificities mechanisms, which you can learn more about on their individual pages.  The high GH family numbers of these two groups reflect their comparatively recent addition to the CAZy Database and highlight the continuing evolution of the field through the discovery of new CAZymes.
 
----
 
----
 
'''23 February 2015:'''  ''The sites that bind:'' '''[[User:Birte Svensson|Birte Svensson]]''' and '''[[User:Darrell Cockburn|Darrell Cockburn]]''' have completed the '''[[Surface Binding Site]]''' page within the ''CAZypedia'' [[Lexicon]].  Surface binding sites are substrate-binding regions found on the catalytic domain of carbohydrate-active enzymes and appear to play complementary roles to carbohydrate-binding modules in facilitating the action of polysaccharide-degrading glycoside hydrolases. ''Read more about these intriguing features and their distribution among CAZymes [[Surface Binding Site|here]].''
 
'''23 February 2015:'''  ''The sites that bind:'' '''[[User:Birte Svensson|Birte Svensson]]''' and '''[[User:Darrell Cockburn|Darrell Cockburn]]''' have completed the '''[[Surface Binding Site]]''' page within the ''CAZypedia'' [[Lexicon]].  Surface binding sites are substrate-binding regions found on the catalytic domain of carbohydrate-active enzymes and appear to play complementary roles to carbohydrate-binding modules in facilitating the action of polysaccharide-degrading glycoside hydrolases. ''Read more about these intriguing features and their distribution among CAZymes [[Surface Binding Site|here]].''

Revision as of 09:39, 19 March 2015

19 March 2015: Closing-in on 100: CAZypedia is on the way to an important milestone, our 100th Curator Approved Glycoside Hydrolase Family page. Thanks go to our colleagues Tomomi Sumida, who completed the Glycoside Hydrolase Family 123 page on March 17, and Wataru Saburi and Haruhide Mori, who completed the Glycoside Hydrolase Family 130 page on March 18. Members of these two GH families represent very distinct structures, specificities mechanisms, which you can learn more about on their individual pages. The high GH family numbers of these two groups reflect their comparatively recent addition to the CAZy Database and highlight the continuing evolution of the field through the discovery of new CAZymes.


23 February 2015: The sites that bind: Birte Svensson and Darrell Cockburn have completed the Surface Binding Site page within the CAZypedia Lexicon. Surface binding sites are substrate-binding regions found on the catalytic domain of carbohydrate-active enzymes and appear to play complementary roles to carbohydrate-binding modules in facilitating the action of polysaccharide-degrading glycoside hydrolases. Read more about these intriguing features and their distribution among CAZymes here.


20 February 2015: One for the Gals: Harry Gilbert has given the Carbohydrate Binding Module Family 62 page, which was authored by Cedric Montanier, Curator Approved status today. Functional and structural characterization of the archetypal CBM62 member from a Clostridium thermocellum xylanase revealed a strong affinity for galactose residues of either anomeric configuration on plant polysaccharides. Although the precise roles of this and other CBM62 members remains somewhat ambiguous, it is clear that these modules are relevant to the targeting of enzymes to the composite plant cell wall. Read more about the work of the all-star team that put CBM62 on the map (of CAZy families), here.


19 January 2015: Still in the high 70's today: Zui Fujimoto brought the Glycoside Hydrolase Family 78 page up to Curator Approved status today, making it CAZypedia's 97th approved GH page. GH78 is a family of archaeal, bacterial, and fungal alpha-L-rhamnosidases that cleave diverse flavonoid glycosides, polysaccharides, glycoproteins, and glycolipids from plants. Read more on these ecologically relevant enzymes here.


7 January 2015: Love your guts: CAZypedia is ringing in the new year with a new Glycoside Hydrolase Family 76 page by Spencer Williams. GH76 contains endo-acting α-mannanases, including members from the human gut bacterium Bacteroides thetaiotaomicron that enable us to degrade yeast mannans in our diet. A very recent publication in Nature, notably involving CAZypedia contributors Michael Suits, Al Boraston, Spencer Williams, Gideon Davies, Wade Abbott, and Harry Gilbert, has recently shed new light on the structure, mechanism, and biological function of these enzymes. Read more here!