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 See a page that's out-of-date and just needs a touch-up?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 "User:Ana Luis"
Harry Brumer (talk | contribs) (Created page with "200px|right '''This is an empty template to help you get started with composing your User page.''' You should begin by opening this page for ed...") |
Harry Brumer (talk | contribs) m (Text replacement - "\^\^\^(.*)\^\^\^" to "$1") |
||
| (9 intermediate revisions by 2 users not shown) | |||
| Line 1: | Line 1: | ||
| − | [[Image: | + | [[Image:ALfoto.jpg|200px|right]] |
| − | + | I obtained a M.Sc in Pharmaceutical Sciences at [http://http://www.ulisboa.pt/en/ Universtiy of Lisbon] in 2009. After I worked with Dr. Carlos Fontes at [http://www.fmv.ulisboa.pt/_ingles/ Technical University of Lisbon], studying the mechanisms of protein-carbohydrate interactions. Between 2013 and 2017 I moved to [http://www.ncl.ac.uk/ Newcastle University] (UK) to do my PhD under the supervision of Prof. [[User:Harry Gilbert|Harry Gilbert]]. During this time I studied the mechanisms behind pectin degradation and utilization by the gut bacterium ''Bacteroides thetaiotaomicron''. I’m currently a PostDoc mentored by Prof. [http://www.medkem.gu.se/mucinbiology/biblio2015.html Gunnar C. Hansson] ([https://www.gu.se/English University of Gothenburg], Sweden) and [http://microbe.med.umich.edu/people/eric-martens-phd Eric C. Martens] ([http://umich.edu/ University of Michigan], USA). My research is focused on functional and structural characterization of enzymes and carbohydrate-binding modules. I'm currently interested in understanding the mechanisms behind mucin degradation by gut bacteria and its implications in inflammatory bowel disease. | |
| − | |||
| − | |||
| − | |||
| − | |||
| − | |||
| − | |||
| − | |||
| − | ' | ||
| − | |||
| + | I contributed to structural-functional characterization of: | ||
| + | * [[CBM65]] from ''Eubacterium cellulosolvens'' ('''Family First''' structure and description of substrate recognition) <cite>Luis2013</cite> | ||
| + | * [[CBM77]] from ''Ruminococcus flavefaciens'' ('''Family First''') <cite>Venditto2016</cite> | ||
| + | * [[GH106]] BT0986 and BT4145 from ''Bacteorides thetaiotaomicron'' ('''Family First''' structure and mechanism of catalysis description) <cite>Ndeh2017, Luis2018 </cite> | ||
| + | * [[GH103]] BT1003 from ''Bacteorides thetaiotaomicron'' (first report of an aceric acidase enzyme) <cite>Ndeh2017</cite>; | ||
| + | * [[PL9]] BT4170 ''Bacteroides thetaiotaomicron'' (first rhamnogalacturonan lyase inside PL9 family) <cite>Luis2018</cite>; | ||
---- | ---- | ||
<biblio> | <biblio> | ||
| − | # | + | #Luis2013 pmid=23229556 |
| + | #Venditto2016 pmid=27298375 | ||
| + | #Ndeh2017 pmid=28329766 | ||
| + | #Luis2018 pmid=29255254 | ||
</biblio> | </biblio> | ||
Latest revision as of 13:35, 18 December 2021
I obtained a M.Sc in Pharmaceutical Sciences at Universtiy of Lisbon in 2009. After I worked with Dr. Carlos Fontes at Technical University of Lisbon, studying the mechanisms of protein-carbohydrate interactions. Between 2013 and 2017 I moved to Newcastle University (UK) to do my PhD under the supervision of Prof. Harry Gilbert. During this time I studied the mechanisms behind pectin degradation and utilization by the gut bacterium Bacteroides thetaiotaomicron. I’m currently a PostDoc mentored by Prof. Gunnar C. Hansson (University of Gothenburg, Sweden) and Eric C. Martens (University of Michigan, USA). My research is focused on functional and structural characterization of enzymes and carbohydrate-binding modules. I'm currently interested in understanding the mechanisms behind mucin degradation by gut bacteria and its implications in inflammatory bowel disease.
I contributed to structural-functional characterization of:
- CBM65 from Eubacterium cellulosolvens (Family First structure and description of substrate recognition) [1]
- CBM77 from Ruminococcus flavefaciens (Family First) [2]
- GH106 BT0986 and BT4145 from Bacteorides thetaiotaomicron (Family First structure and mechanism of catalysis description) [3, 4]
- GH103 BT1003 from Bacteorides thetaiotaomicron (first report of an aceric acidase enzyme) [3];
- PL9 BT4170 Bacteroides thetaiotaomicron (first rhamnogalacturonan lyase inside PL9 family) [4];
- Luís AS, Venditto I, Temple MJ, Rogowski A, Baslé A, Xue J, Knox JP, Prates JA, Ferreira LM, Fontes CM, Najmudin S, and Gilbert HJ. (2013). Understanding how noncatalytic carbohydrate binding modules can display specificity for xyloglucan. J Biol Chem. 2013;288(7):4799-809. DOI:10.1074/jbc.M112.432781 |
- Venditto I, Luis AS, Rydahl M, Schückel J, Fernandes VO, Vidal-Melgosa S, Bule P, Goyal A, Pires VM, Dourado CG, Ferreira LM, Coutinho PM, Henrissat B, Knox JP, Baslé A, Najmudin S, Gilbert HJ, Willats WG, and Fontes CM. (2016). Complexity of the Ruminococcus flavefaciens cellulosome reflects an expansion in glycan recognition. Proc Natl Acad Sci U S A. 2016;113(26):7136-41. DOI:10.1073/pnas.1601558113 |
- Ndeh D, Rogowski A, Cartmell A, Luis AS, Baslé A, Gray J, Venditto I, Briggs J, Zhang X, Labourel A, Terrapon N, Buffetto F, Nepogodiev S, Xiao Y, Field RA, Zhu Y, O'Neil MA, Urbanowicz BR, York WS, Davies GJ, Abbott DW, Ralet MC, Martens EC, Henrissat B, and Gilbert HJ. (2017). Complex pectin metabolism by gut bacteria reveals novel catalytic functions. Nature. 2017;544(7648):65-70. DOI:10.1038/nature21725 |
- Luis AS, Briggs J, Zhang X, Farnell B, Ndeh D, Labourel A, Baslé A, Cartmell A, Terrapon N, Stott K, Lowe EC, McLean R, Shearer K, Schückel J, Venditto I, Ralet MC, Henrissat B, Martens EC, Mosimann SC, Abbott DW, and Gilbert HJ. (2018). Dietary pectic glycans are degraded by coordinated enzyme pathways in human colonic Bacteroides. Nat Microbiol. 2018;3(2):210-219. DOI:10.1038/s41564-017-0079-1 |