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Difference between revisions of "User:Plinio Vieira"
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Plinio Vieira obtained his B.Sc. Lic. in Chemistry from the University of São Paulo (2010) and his Ph.D. (2016) at the University of Campinas under the supervision of [[User:Mario Murakami|Mario Murakami]]. The work focused on the crystallographic studies of NEK kinases from Trypanosomatids, aiming for structural-based drug design. During his post-doc at [https://cnpem.br/ Brazilian National Center for Research in Energy and Materials] under the supervision of Dr. Murakami, he studied Glycoside Hydrolases from ''Xanthomonas'' that act on Xyloglucan depolymerization. He also developed a post-doc project under the supervision of [https://miguelalcaldelab.eu/contact/ Miguel Alcalde] at [https://icp.csic.es/ Institute of Catalysis and Petrochemistry], focusing on the random and semi-rational evolution of a GH35 β-galactosidase. He currently works as Researcher Specialist at [https://lnbr.cnpem.br Brazilian Biorenewables Laboratory], focusing on the discovery and the structure-function-mechanism relationship from CAZymes. He has contributed for the tridimensional structure determination of: | Plinio Vieira obtained his B.Sc. Lic. in Chemistry from the University of São Paulo (2010) and his Ph.D. (2016) at the University of Campinas under the supervision of [[User:Mario Murakami|Mario Murakami]]. The work focused on the crystallographic studies of NEK kinases from Trypanosomatids, aiming for structural-based drug design. During his post-doc at [https://cnpem.br/ Brazilian National Center for Research in Energy and Materials] under the supervision of Dr. Murakami, he studied Glycoside Hydrolases from ''Xanthomonas'' that act on Xyloglucan depolymerization. He also developed a post-doc project under the supervision of [https://miguelalcaldelab.eu/contact/ Miguel Alcalde] at [https://icp.csic.es/ Institute of Catalysis and Petrochemistry], focusing on the random and semi-rational evolution of a GH35 β-galactosidase. He currently works as Researcher Specialist at [https://lnbr.cnpem.br Brazilian Biorenewables Laboratory], focusing on the discovery and the structure-function-mechanism relationship from CAZymes. He has contributed for the tridimensional structure determination of: | ||
− | *[[CE20]] '''Family first''' ''Xanthomonas citri'' pv. ''citri'' xyloglucan acetylesterase [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] <cite>Vieira2021</cite> | + | *[[CE20]] '''Family first''' ''Xanthomonas citri'' pv. ''citri'' xyloglucan acetylesterase (''Xac''XaeA) [https://www.rcsb.org/structure/7KMM PDB ID 7KMM] <cite>Vieira2021</cite> |
− | *[[GH2]] ''Xanthomonas citri'' pv. ''citri'' exo-β-mannanase [https://www.rcsb.org/structure/6BYC PDB ID 6BYC] <cite>Domingues2018</cite> | + | *[[GH2]] ''Xanthomonas citri'' pv. ''citri'' exo-β-mannanase (''Xac''Man2A) [https://www.rcsb.org/structure/6BYC PDB ID 6BYC] <cite>Domingues2018</cite> |
− | *[[GH2]] ''Xanthomonas citri'' pv. ''citri'' exo-β-mannanase, in complex with mannose [https://www.rcsb.org/structure/6BYE PDB ID 6BYE] <cite>Domingues2018</cite> | + | *[[GH2]] ''Xanthomonas citri'' pv. ''citri'' exo-β-mannanase, in complex with mannose (''Xac''Man2A) [https://www.rcsb.org/structure/6BYE PDB ID 6BYE] <cite>Domingues2018</cite> |
− | *[[GH2]] ''Xanthomonas citri'' pv. ''citri'' exo-β-mannanase mutant E477A [https://www.rcsb.org/structure/6BYI PDB ID 6BYI] <cite>Domingues2018</cite> | + | *[[GH2]] ''Xanthomonas citri'' pv. ''citri'' exo-β-mannanase mutant E477A (''Xac''Man2A) [https://www.rcsb.org/structure/6BYI PDB ID 6BYI] <cite>Domingues2018</cite> |
− | *[[GH2]] ''Xanthomonas citri'' pv. ''citri'' exo-β-mannanase mutant E575A [https://www.rcsb.org/structure/6BYG PDB ID 6BYG] <cite>Domingues2018</cite> | + | *[[GH2]] ''Xanthomonas citri'' pv. ''citri'' exo-β-mannanase mutant E575A (''Xac''Man2A) [https://www.rcsb.org/structure/6BYG PDB ID 6BYG] <cite>Domingues2018</cite> |
− | *[[GH31]] ''Xanthomonas citri'' pv. ''citri'' exo-α-xylosidase [https://www.rcsb.org/structure/7KMP PDB ID 7KMP] <cite>Vieira2021</cite> | + | *[[GH31]] ''Xanthomonas citri'' pv. ''citri'' exo-α-xylosidase (''Xac''Xyl31) [https://www.rcsb.org/structure/7KMP PDB ID 7KMP] <cite>Vieira2021</cite> |
− | *[[GH31]] ''Xanthomonas citri'' pv. ''citri'' exo-α-xylosidase, in complex with xylose [https://www.rcsb.org/structure/7KNC PDB ID 7KNC] <cite>Vieira2021</cite> | + | *[[GH31]] ''Xanthomonas citri'' pv. ''citri'' exo-α-xylosidase, in complex with xylose (''Xac''Xyl31) [https://www.rcsb.org/structure/7KNC PDB ID 7KNC] <cite>Vieira2021</cite> |
− | *[[GH35]] ''Xanthomonas citri'' pv. ''citri'' exo-β-galactosidase [https://www.rcsb.org/structure/7KMN PDB ID 7KMN] <cite>Vieira2021</cite> | + | *[[GH35]] ''Xanthomonas citri'' pv. ''citri'' exo-β-galactosidase (''Xac''GalD) [https://www.rcsb.org/structure/7KMN PDB ID 7KMN] <cite>Vieira2021</cite> |
− | *[[GH35]] ''Xanthomonas citri'' pv. ''citri'' exo-β-galactosidase, in complex with galactose [https://www.rcsb.org/structure/7KMO PDB ID 7KMO] <cite>Vieira2021</cite> | + | *[[GH35]] ''Xanthomonas citri'' pv. ''citri'' exo-β-galactosidase, in complex with galactose (''Xac''GalD) [https://www.rcsb.org/structure/7KMO PDB ID 7KMO] <cite>Vieira2021</cite> |
− | *[[GH74]] ''Xanthomonas campestris'' pv. ''campestris'' endo-xyloglucanase, in complex with XG oligosaccharide [https://www.rcsb.org/structure/7KN8 PDB ID 7KN8] <cite>Vieira2021</cite> | + | *[[GH74]] ''Xanthomonas campestris'' pv. ''campestris'' endo-xyloglucanase, in complex with XG oligosaccharide (''Xcc''Xeg74) [https://www.rcsb.org/structure/7KN8 PDB ID 7KN8] <cite>Vieira2021</cite> |
− | *[[GH95]] ''Xanthomonas citri'' pv. ''citri'' α-L-1,2-fucosidase [https://www.rcsb.org/structure/7KMQ PDB ID 7KMQ] <cite>Vieira2021</cite> | + | *[[GH95]] ''Xanthomonas citri'' pv. ''citri'' α-L-1,2-fucosidase (''Xac''Afc95) [https://www.rcsb.org/structure/7KMQ PDB ID 7KMQ] <cite>Vieira2021</cite> |
− | *[[GH128]] ''Amycolatopsis mediterranei'' endo-β-1,3-glucanase E102A mutant, in complex with laminaritriose and laminaribiose [https://www.rcsb.org/structure/6UAU PDB ID 6UAU] <cite>Santos2020</cite> | + | *[[GH128]] ''Amycolatopsis mediterranei'' endo-β-1,3-glucanase E102A mutant, in complex with laminaritriose and laminaribiose (AmGH128_I) [https://www.rcsb.org/structure/6UAU PDB ID 6UAU] <cite>Santos2020</cite> |
− | *[[GH128]] ''Amycolatopsis mediterranei'' endo-β-1,3-glucanase E102A mutant, in complex with laminaripentaose [https://www.rcsb.org/structure/6UAT PDB ID 6UAT] <cite>Santos2020</cite> | + | *[[GH128]] ''Amycolatopsis mediterranei'' endo-β-1,3-glucanase E102A mutant, in complex with laminaripentaose (AmGH128_I) [https://www.rcsb.org/structure/6UAT PDB ID 6UAT] <cite>Santos2020</cite> |
− | *[[GH128]] ''Amycolatopsis mediterranei'' endo-β-1,3-glucanase E199Q mutant [https://www.rcsb.org/structure/6UFZ PDB ID 6UBFZ] <cite>Santos2020</cite> | + | *[[GH128]] ''Amycolatopsis mediterranei'' endo-β-1,3-glucanase E199Q mutant (AmGH128_I) [https://www.rcsb.org/structure/6UFZ PDB ID 6UBFZ] <cite>Santos2020</cite> |
− | *[[GH128]] ''Amycolatopsis mediterranei'' endo-β-1,3-glucanase E199A mutant, in complex with laminaripentaose [https://www.rcsb.org/structure/6UAS/ PDB ID 6UAS] <cite>Santos2020</cite> | + | *[[GH128]] ''Amycolatopsis mediterranei'' endo-β-1,3-glucanase E199A mutant, in complex with laminaripentaose (AmGH128_I) [https://www.rcsb.org/structure/6UAS/ PDB ID 6UAS] <cite>Santos2020</cite> |
− | *[[GH128]] ''Amycolatopsis mediterranei'' endo-β-1,3-glucanase E199A mutant, in complex with laminarihexaose [https://www.rcsb.org/structure/6UFL PDB ID 6UFL] <cite>Santos2020</cite> | + | *[[GH128]] ''Amycolatopsis mediterranei'' endo-β-1,3-glucanase E199A mutant, in complex with laminarihexaose (AmGH128_I) [https://www.rcsb.org/structure/6UFL PDB ID 6UFL] <cite>Santos2020</cite> |
− | *[[GH128]] ''Sorangium cellulosum'' endo-β-1,3-glucanase [https://www.rcsb.org/structure/6UAX/ PDB ID 6UAX] <cite>Santos2020</cite> | + | *[[GH128]] ''Sorangium cellulosum'' endo-β-1,3-glucanase (ScGH128_II) [https://www.rcsb.org/structure/6UAX/ PDB ID 6UAX] <cite>Santos2020</cite> |
− | *[[GH128]] ''Lentinula edodes'' endo-β-1,3-glucanase [https://www.rcsb.org/structure/6UB2 PDB ID 6UB2] <cite>Santos2020</cite> | + | *[[GH128]] ''Lentinula edodes'' endo-β-1,3-glucanase (LeGH128_IV) [https://www.rcsb.org/structure/6UB2 PDB ID 6UB2] <cite>Santos2020</cite> |
− | *[[GH128]] ''Aureobasidium namibiae'' exo-β-1,3-glucanase [https://www.rcsb.org/structure/6UB8 PDB ID 6UB8] <cite>Santos2020</cite> | + | *[[GH128]] ''Aureobasidium namibiae'' exo-β-1,3-glucanase (AnGH128_VI) [https://www.rcsb.org/structure/6UB8 PDB ID 6UB8] <cite>Santos2020</cite> |
− | *[[GH128]] ''Aureobasidium namibiae'' exo-β-1,3-glucanase, in complex with laminaritriose [https://www.rcsb.org/structure/6UBA PDB ID 6UAB] <cite>Santos2020</cite> | + | *[[GH128]] ''Aureobasidium namibiae'' exo-β-1,3-glucanase, in complex with laminaritriose (AnGH128_VI) [https://www.rcsb.org/structure/6UBA PDB ID 6UAB] <cite>Santos2020</cite> |
− | *[[GH128]] ''Aureobasidium namibiae'' exo-β-1,3-glucanase, with laminaribiose at the surface-binding site [https://www.rcsb.org/structure/6UBB PDB ID 6UBB] <cite>Santos2020</cite> | + | *[[GH128]] ''Aureobasidium namibiae'' exo-β-1,3-glucanase, with laminaribiose at the surface-binding site (AnGH128_VI) [https://www.rcsb.org/structure/6UBB PDB ID 6UBB] <cite>Santos2020</cite> |
− | *[[GH128]] ''Cryptococcus neoformans'' oligosaccharide-binding protein [https://www.rcsb.org/structure/6UBC PDB ID 6UBC] <cite>Santos2020</cite | + | *[[GH128]] ''Cryptococcus neoformans'' oligosaccharide-binding protein (CnGH128_VII) [https://www.rcsb.org/structure/6UBC PDB ID 6UBC] <cite>Santos2020</cite> |
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#Vieira2021 pmid=34193873 | #Vieira2021 pmid=34193873 | ||
− | |||
#Santos2020 pmid=32451508 | #Santos2020 pmid=32451508 | ||
#Domingues2018 pmid=29997257 | #Domingues2018 pmid=29997257 | ||
+ | |||
</biblio> | </biblio> | ||
Revision as of 12:16, 24 January 2023
Plinio Vieira obtained his B.Sc. Lic. in Chemistry from the University of São Paulo (2010) and his Ph.D. (2016) at the University of Campinas under the supervision of Mario Murakami. The work focused on the crystallographic studies of NEK kinases from Trypanosomatids, aiming for structural-based drug design. During his post-doc at Brazilian National Center for Research in Energy and Materials under the supervision of Dr. Murakami, he studied Glycoside Hydrolases from Xanthomonas that act on Xyloglucan depolymerization. He also developed a post-doc project under the supervision of Miguel Alcalde at Institute of Catalysis and Petrochemistry, focusing on the random and semi-rational evolution of a GH35 β-galactosidase. He currently works as Researcher Specialist at Brazilian Biorenewables Laboratory, focusing on the discovery and the structure-function-mechanism relationship from CAZymes. He has contributed for the tridimensional structure determination of:
- CE20 Family first Xanthomonas citri pv. citri xyloglucan acetylesterase (XacXaeA) PDB ID 7KMM [1]
- GH2 Xanthomonas citri pv. citri exo-β-mannanase (XacMan2A) PDB ID 6BYC [2]
- GH2 Xanthomonas citri pv. citri exo-β-mannanase, in complex with mannose (XacMan2A) PDB ID 6BYE [2]
- GH2 Xanthomonas citri pv. citri exo-β-mannanase mutant E477A (XacMan2A) PDB ID 6BYI [2]
- GH2 Xanthomonas citri pv. citri exo-β-mannanase mutant E575A (XacMan2A) PDB ID 6BYG [2]
- GH31 Xanthomonas citri pv. citri exo-α-xylosidase (XacXyl31) PDB ID 7KMP [1]
- GH31 Xanthomonas citri pv. citri exo-α-xylosidase, in complex with xylose (XacXyl31) PDB ID 7KNC [1]
- GH35 Xanthomonas citri pv. citri exo-β-galactosidase (XacGalD) PDB ID 7KMN [1]
- GH35 Xanthomonas citri pv. citri exo-β-galactosidase, in complex with galactose (XacGalD) PDB ID 7KMO [1]
- GH74 Xanthomonas campestris pv. campestris endo-xyloglucanase, in complex with XG oligosaccharide (XccXeg74) PDB ID 7KN8 [1]
- GH95 Xanthomonas citri pv. citri α-L-1,2-fucosidase (XacAfc95) PDB ID 7KMQ [1]
- GH128 Amycolatopsis mediterranei endo-β-1,3-glucanase E102A mutant, in complex with laminaritriose and laminaribiose (AmGH128_I) PDB ID 6UAU [3]
- GH128 Amycolatopsis mediterranei endo-β-1,3-glucanase E102A mutant, in complex with laminaripentaose (AmGH128_I) PDB ID 6UAT [3]
- GH128 Amycolatopsis mediterranei endo-β-1,3-glucanase E199Q mutant (AmGH128_I) PDB ID 6UBFZ [3]
- GH128 Amycolatopsis mediterranei endo-β-1,3-glucanase E199A mutant, in complex with laminaripentaose (AmGH128_I) PDB ID 6UAS [3]
- GH128 Amycolatopsis mediterranei endo-β-1,3-glucanase E199A mutant, in complex with laminarihexaose (AmGH128_I) PDB ID 6UFL [3]
- GH128 Sorangium cellulosum endo-β-1,3-glucanase (ScGH128_II) PDB ID 6UAX [3]
- GH128 Lentinula edodes endo-β-1,3-glucanase (LeGH128_IV) PDB ID 6UB2 [3]
- GH128 Aureobasidium namibiae exo-β-1,3-glucanase (AnGH128_VI) PDB ID 6UB8 [3]
- GH128 Aureobasidium namibiae exo-β-1,3-glucanase, in complex with laminaritriose (AnGH128_VI) PDB ID 6UAB [3]
- GH128 Aureobasidium namibiae exo-β-1,3-glucanase, with laminaribiose at the surface-binding site (AnGH128_VI) PDB ID 6UBB [3]
- GH128 Cryptococcus neoformans oligosaccharide-binding protein (CnGH128_VII) PDB ID 6UBC [3]
- Vieira PS, Bonfim IM, Araujo EA, Melo RR, Lima AR, Fessel MR, Paixão DAA, Persinoti GF, Rocco SA, Lima TB, Pirolla RAS, Morais MAB, Correa JBL, Zanphorlin LM, Diogo JA, Lima EA, Grandis A, Buckeridge MS, Gozzo FC, Benedetti CE, Polikarpov I, Giuseppe PO, and Murakami MT. (2021). Xyloglucan processing machinery in Xanthomonas pathogens and its role in the transcriptional activation of virulence factors. Nat Commun. 2021;12(1):4049. DOI:10.1038/s41467-021-24277-4 |
- Domingues MN, Souza FHM, Vieira PS, de Morais MAB, Zanphorlin LM, Dos Santos CR, Pirolla RAS, Honorato RV, de Oliveira PSL, Gozzo FC, and Murakami MT. (2018). Structural basis of exo-β-mannanase activity in the GH2 family. J Biol Chem. 2018;293(35):13636-13649. DOI:10.1074/jbc.RA118.002374 |
- Santos CR, Costa PACR, Vieira PS, Gonzalez SET, Correa TLR, Lima EA, Mandelli F, Pirolla RAS, Domingues MN, Cabral L, Martins MP, Cordeiro RL, Junior AT, Souza BP, Prates ÉT, Gozzo FC, Persinoti GF, Skaf MS, and Murakami MT. (2020). Structural insights into β-1,3-glucan cleavage by a glycoside hydrolase family. Nat Chem Biol. 2020;16(8):920-929. DOI:10.1038/s41589-020-0554-5 |