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Difference between revisions of "Template:News"

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'''31 January 2018:''' ''A flurry of CBM activity in the new year:'' Over the past two weeks, ''CAZypedia'' has enjoyed the promotion of no less than ''nine'' [[Carbohydrate-binding modules|Carbohydrate-binding module (CBM)]] family pages to [[Curator Approved]] status, thanks to the tenacity of [[CBM]] vanguard '''[[User:Harry Gilbert|Harry Gilbert]]''' and the keen editorial oversight of '''[[User:Elizabeth Ficko-Blean|Elizabeth Ficko-Blean]]'''. [[CAZypedia:Assigned_pages#Carbohydrate_Binding_Module_Families|In order of appearance]], '''[[CBM2]]''', '''[[CBM10]]''', '''[[CBM15]]''', '''[[CBM29]]''', '''[[CBM66]]''', '''[[CBM60]]''' (co-authored by '''[[User:Cedric Montanier|Cedric Montanier]]'''), '''[[CBM46]]''', and '''[[CBM35]]''' all have completed pages, as does the deleted family '''[[CBM7]]'''. These pages cover many classic [[CBM]] studies and include examples of [[Carbohydrate-binding modules#Types|type A, type B, and type C CBMs]].     ''The CBM legacy runs deep - learn more about each family on [[Carbohydrate Binding Module Families|their respective pages]].''
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'''1 November 2024:''' ''Is this a world record? Six CAZypedia families in one fell swoop!'' The '''[[CBM47]], [[CBM70]], [[CBM96]], [[CBM105]], [[CBM106]] and [[PL44]]''' ''CAZypedia'' pages are now flipped to [[Curator Approved]] status. What do these diverse families from diverse origins with diverse binding specificities have in common?  Astonishingly, at least one characterized member from each family interacts with a charged glycan! '''[[User:Wenwen Tao|Wenwen Tao]]''' authored the [[CBM47]], [[CBM96]] and [[CBM106]] pages, '''[[User:Menghui Sun|Menghui Sun]]''' authored the [[CBM70]] page, '''[[User:Guanchen Liu|Guanchen Liu]]''' authored the [[CBM105]] page and '''[[User:Jinhang Zhou|Jinhang Zhou]]''' authored the [[PL44]] page.  All this under the responsible curatorship of '''[[User:Yaoguang Chang|Yaoguang Chang]]'''. ''Dive into these diverse families on their respective ''CAZypedia'' pages: '''[[CBM47]], [[CBM70]], [[CBM96]], [[CBM105]], [[CBM106]] and [[PL44]]!'''''
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'''25 October 2024:''' ''Laminariawesome!'' Check out two new marine families of CBMs, '''[[CBM102]]''' and '''[[CBM103]]''', now on ''CAZypedia'' which have an ecological role in bacterial degradation of laminarin during phytoplankton blooms.  Some function as surface glycan binding proteins but others have roles in targeting their appended catalytic modules to substrate.  Both pages were [[author]]ed by '''[[User:Marie-Katherin Zuehlke|Marie-Katherin Zühlke]]'''. ''Read up on these environmentally important CBMs on their respective [[CBM102]] and [[CBM103]] pages!''  
 
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'''26 November 2017:''' ''CBM #1:'' Today, [[Carbohydrate-binding modules|CBM]] pioneer '''[[User:Markus Linder|Markus Linder]]''' completed the '''[[Carbohydrate Binding Module Family 1]]''' page.  [[CBM1]] comprises the canonical fungal cellulose-binding modules (originally known as cellulose-binding ''domains''), which were first found as stable cystine-knot-containing protein fragments released by controlled proteolysis of cellulases.  The planar nature of the substrate-binding face, and linear arrangement of key aromatic residues, represent the archetype of [[Carbohydrate-binding modules|CBMs]] that mediate glycosidase targeting to crystalline polysaccharides.  Building on the original discovery of the modules now classified into [[CBM1]] in Sweden, '''[[User:Markus Linder|Markus Linder]]''' (then a Ph.D. student) and Tuula Teeri, working together across the Baltic Sea in Finland, were among the first to undertake structure-function studies and protein engineering of [[CBM1]] using modern molecular techniques in the mid- to late-1990s.  ''We're pleased to finally have this one in CAZYpedia - learn more about this seminal CBM family [[CBM1|here]].''
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'''19 July 2024:''' ''Chalk-up one more for the GTs!'' The '''[[Glycosyltransferase Family 47]]''' page joined the small group of [[Curator Approved]] [[Glycosyltransferase Families]] pages in ''CAZypedia'' today. This entry was [[author]]ed by Ph.D. students '''[[User:Daniel Tehrani|Daniel Tehrani]]''' and '''[[User:Charlie Corulli|Charlie Corulli]]''', and [[Responsible Curator|Curated]] by '''[[User:Breeanna Urbanowicz|Breeanna Urbanowicz]]''' with input from '''[https://ccrc.uga.edu/team/kelley-moremen/ Kelley Moremen]'''.  Widely represented in plants, '''[[GT47]]''' members are anomer-[[inverting]] [[glycosyltransferases]], which are involved in the biosynthesis of several cell wall matrix polysaccharides.  Representatives from mammals are involved in heparin biosynthesis.  Correspondingly, members of [[GH47]] have diverse substrate specificities, including the transfer of both anionic and neutral monosaccharides to polysaccharides.  ''This is a great example where two keen Ph.D. students worked with their supervisors to create a valuable page for the scientific community. We encourage others to follow their lead, on your favorite family!''
 
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'''11 October 2017:''' ''Ten years of CAZypedia!'' We are proud to announce the publication of a [https://academic.oup.com/glycob/article-lookup/doi/10.1093/glycob/cwx089 new article in ''Glycobiology''] in celebration of ''CAZypedia's'' tenth anniversary online. This article was written on behalf of all of present and future '''[[:Category:Contributors|Contributors]]''' by Curators [[User:Harry Brumer|Harry Brumer]] and [[User:Spencer Williams|Spencer Williams]], with input from a number of key individuals involved in the genesis of ''CAZypedia'' (''see the [https://academic.oup.com/glycob/article-lookup/doi/10.1093/glycob/cwx089 Acknowledgements section] for full details''). A [http://hdl.handle.net/2429/63428 post-print version] of the manuscript will be freely available from the UBC Library Open Collections, in addition to the [https://academic.oup.com/glycob/article-lookup/doi/10.1093/glycob/cwx089 final version] on the ''Glycobiology'' website.  ''Thanks to the hard work of a multitude of [[:Category:Contributors|Contributors]], ''CAZypedia'' is a successful example of community-driven, expert-based biocuration. We look forward to the continued development of this resource over the next ten years - and beyond!''
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'''9 July 2024:''' ''Yet another new family of beta-1,2-glucan-active enzymes!'' Today, '''[[User:Masahiro Nakajima|Masahiro Nakajima]]''' [[Curator Approved]] the '''[[Glycoside Hydrolase Family 186]]''' page by '''[[User:Sei Motouchi|Sei Motouchi]]'''. '''[[GH186]]''' is a family of anomer-[[inverting]] enzymes from bacteria, members of which are specific for beta-1,2-glucans.  Intriguingly, although some [[GH186]] members work as classic [[glycoside hydrolases]], others perform transglycosylation by wrapping the sugar chain around in the active-site, to position the 6-OH group of a terminal glucosyl unit for direct attack. Also notable, [[GH186]] members appear to use an extended chain of water molecules to relay acceptor deprotonation by the [[general base]] residue, ''i.e.'' a [https://en.wikipedia.org/wiki/Grotthuss_mechanism Grotthuss mechanism]. ''Check out the '''[[GH186]]''' page to learn more about these interesting enzymes, and make sure to see the [[GH189]], [[GH144]], and [[GH162]] pages from this same group.''
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'''10 September 2017:''' ''Sussing-out starch recognition in CBM58.'' We are excited to report that '''[[User:Nicole Koropatkin|Nicole Koropatkin]]''' has completed the '''[[Carbohydrate Binding Module Family 58]]''' page today.  [[CBM58]] constitutes a comparatively small family of CBMs found in bacteria in the phylum Bacteroidetes, including key members of the human gut microbiota such as ''Bacteroides thetaiotaomicron''.  Within these bacteria, [[CBM58]] modules are found inserted within the [[GH13]] catalytic module of SusG, the essential outer-membrane-bound amylase of the starch utilization system (sus).  [[User:Nicole Koropatkin|Nicole’s]] seminal structural biology has defined the family and provided insight into the recognition of amylose helices by [[CBM58]] members in SusG homologs.  ''Read more about this fascinating system [[Carbohydrate Binding Module Family 58|here]].''    
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'''2 May 2024:''' ''CBDs I to X... A major milestone!'' '''CBM families 1 to 10 are now complete!''' These are the old CBD (cellulose-binding domain) families, which used to have roman numerals as part of their nomenclature. A special thank you to all the authors and responsible curators who have contributed to this major milestone. Go have a peek at each of these old-school families on their respective ''CAZypedia'' pages: '''[[CBM1]], [[CBM2]], [[CBM3]], [[CBM4]], [[CBM5]], [[CBM6]], [[CBM7]], [[CBM8]], [[CBM9]], and [[CBM10]]'''.
 
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Latest revision as of 16:03, 21 November 2024

1 November 2024: Is this a world record? Six CAZypedia families in one fell swoop! The CBM47, CBM70, CBM96, CBM105, CBM106 and PL44 CAZypedia pages are now flipped to Curator Approved status. What do these diverse families from diverse origins with diverse binding specificities have in common? Astonishingly, at least one characterized member from each family interacts with a charged glycan! Wenwen Tao authored the CBM47, CBM96 and CBM106 pages, Menghui Sun authored the CBM70 page, Guanchen Liu authored the CBM105 page and Jinhang Zhou authored the PL44 page. All this under the responsible curatorship of Yaoguang Chang. Dive into these diverse families on their respective CAZypedia pages: CBM47, CBM70, CBM96, CBM105, CBM106 and PL44!

25 October 2024: Laminariawesome! Check out two new marine families of CBMs, CBM102 and CBM103, now on CAZypedia which have an ecological role in bacterial degradation of laminarin during phytoplankton blooms. Some function as surface glycan binding proteins but others have roles in targeting their appended catalytic modules to substrate. Both pages were authored by Marie-Katherin Zühlke. Read up on these environmentally important CBMs on their respective CBM102 and CBM103 pages!

19 July 2024: Chalk-up one more for the GTs! The Glycosyltransferase Family 47 page joined the small group of Curator Approved Glycosyltransferase Families pages in CAZypedia today. This entry was authored by Ph.D. students Daniel Tehrani and Charlie Corulli, and Curated by Breeanna Urbanowicz with input from Kelley Moremen. Widely represented in plants, GT47 members are anomer-inverting glycosyltransferases, which are involved in the biosynthesis of several cell wall matrix polysaccharides. Representatives from mammals are involved in heparin biosynthesis. Correspondingly, members of GH47 have diverse substrate specificities, including the transfer of both anionic and neutral monosaccharides to polysaccharides. This is a great example where two keen Ph.D. students worked with their supervisors to create a valuable page for the scientific community. We encourage others to follow their lead, on your favorite family!

9 July 2024: Yet another new family of beta-1,2-glucan-active enzymes! Today, Masahiro Nakajima Curator Approved the Glycoside Hydrolase Family 186 page by Sei Motouchi. GH186 is a family of anomer-inverting enzymes from bacteria, members of which are specific for beta-1,2-glucans. Intriguingly, although some GH186 members work as classic glycoside hydrolases, others perform transglycosylation by wrapping the sugar chain around in the active-site, to position the 6-OH group of a terminal glucosyl unit for direct attack. Also notable, GH186 members appear to use an extended chain of water molecules to relay acceptor deprotonation by the general base residue, i.e. a Grotthuss mechanism. Check out the GH186 page to learn more about these interesting enzymes, and make sure to see the GH189, GH144, and GH162 pages from this same group.

2 May 2024: CBDs I to X... A major milestone! CBM families 1 to 10 are now complete! These are the old CBD (cellulose-binding domain) families, which used to have roman numerals as part of their nomenclature. A special thank you to all the authors and responsible curators who have contributed to this major milestone. Go have a peek at each of these old-school families on their respective CAZypedia pages: CBM1, CBM2, CBM3, CBM4, CBM5, CBM6, CBM7, CBM8, CBM9, and CBM10.

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