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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:
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Plinio Salmazo 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]] and [[User:Priscila Giuseppe|Priscila Oliveira de Giuseppe]]. 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 worked on 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 engineering and 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 and biochemical characterization of:
*[[CE20]] '''Family first''' ''Xanthomonas citri'' pv. ''citri'' xyloglucan acetylesterase [https://www.rcsb.org/structure/7KMM PDB ID 7KMM]
 
  
*[[GH2]] ''Xanthomonas citri'' pv. ''citri'' exo-β-mannanase [https://www.rcsb.org/structure/6BYC PDB ID 6BYC]
+
*[[CE20]] '''Family first''' ''Xac''XaeA [https://www.rcsb.org/structure/7KMM 7KMM] <cite>Vieira2021</cite>
 
+
*[[GH1]] ''Em''Bgl <cite>Sousa2020</cite>
*[[GH2]] ''Xanthomonas citri'' pv. ''citri'' exo-&beta;-mannanase, in complex with mannose [https://www.rcsb.org/structure/6BYE PDB ID 6BYE]
+
*[[GH2]] ''Xac''Man2A [https://www.rcsb.org/structure/6BYC 6BYC] [https://www.rcsb.org/structure/6BYE 6BYE] [https://www.rcsb.org/structure/6BYI ID 6BYI][https://www.rcsb.org/structure/6BYG 6BYG] <cite>Domingues2018</cite>
 
+
*[[GH3]]  ''Xac''Xyl3A, ''Xac''Xyl3B, ''Xac''Bgl3A, ''Xac''Bgl3B, ''Xac''Bgl3C  <cite>Vieira2021</cite>
*[[GH2]] ''Xanthomonas citri'' pv. ''citri'' exo-&beta;-mannanase mutant E477A [https://www.rcsb.org/structure/6BYI PDB ID 6BYI]
+
*[[GH8]] ''Xac''Cel8A <cite>Melo2021</cite>
 
+
*[[GH31]] ''Xac''Xyl31 [https://www.rcsb.org/structure/7KMP 7KMP] [https://www.rcsb.org/structure/7KNC 7KNC] <cite>Vieira2021</cite>
*[[GH2]] ''Xanthomonas citri'' pv. ''citri'' exo-&beta;-mannanase mutant E575A [https://www.rcsb.org/structure/6BYG PDB ID 6BYG]
+
*[[GH35]] ''Xac''GalD [https://www.rcsb.org/structure/7KMN 7KMN] [https://www.rcsb.org/structure/7KMO 7KMO] <cite>Vieira2021</cite>
 
+
*[[GH74]] ''Xcc''Xeg74 [https://www.rcsb.org/structure/7KN8 7KN8] <cite>Vieira2021</cite>
*[[GH31]] ''Xanthomonas citri'' pv. ''citri'' exo-&alpha;-xylosidase [https://www.rcsb.org/structure/7KMP PDB ID 7KMP]
+
*[[GH95]] ''Xac''Afc95 [https://www.rcsb.org/structure/7KMQ 7KMQ] <cite>Vieira2021</cite>
 
+
*[[GH128]] AmGH128_I [https://www.rcsb.org/structure/6UAU 6UAU] [https://www.rcsb.org/structure/6UAT 6UAT] [https://www.rcsb.org/structure/6UFZ 6UBFZ] [https://www.rcsb.org/structure/6UAS/ 6UAS] [https://www.rcsb.org/structure/6UFL 6UFL] <cite>Santos2020</cite>
*[[GH31]] ''Xanthomonas citri'' pv. ''citri'' exo-&alpha;-xylosidase, in complex with xylose [https://www.rcsb.org/structure/7KNC PDB ID 7KNC]
+
*[[GH128]] ScGH128_II [https://www.rcsb.org/structure/6UAX/ 6UAX] <cite>Santos2020</cite>
 
+
*[[GH128]] LeGH128_IV [https://www.rcsb.org/structure/6UB2 6UB2] <cite>Santos2020</cite>
*[[GH35]] ''Xanthomonas citri'' pv. ''citri'' exo-&beta;-galactosidase [https://www.rcsb.org/structure/7KMN PDB ID 7KMN]
+
*[[GH128]] AnGH128_VI [https://www.rcsb.org/structure/6UB8 6UB8] [https://www.rcsb.org/structure/6UBA 6UAB] [https://www.rcsb.org/structure/6UBB 6UBB] <cite>Santos2020</cite>
 
+
*[[GH128]] CnGH128_VII [https://www.rcsb.org/structure/6UBC 6UBC] <cite>Santos2020</cite>
*[[GH35]] ''Xanthomonas citri'' pv. ''citri'' exo-&beta;-galactosidase, in complex with galactose [https://www.rcsb.org/structure/7KMO PDB ID 7KMO]
 
 
 
*[[GH74]] ''Xanthomonas campestris'' pv. ''campestris'' endo-xyloglucanase, in complex with XG oligosaccharide [https://www.rcsb.org/structure/7KN8 PDB ID 7KN8]
 
 
 
*[[GH35]] ''Xanthomonas citri'' pv. ''citri'' &alpha;-L-1,2-fucosidase [https://www.rcsb.org/structure/7KMQ PDB ID 7KMQ]
 
 
 
*[[GH128]] ''Amycolatopsis mediterranei'' endo-&beta;-1,3-glucanase E102A mutant, in complex with laminaritriose and laminaribiose [https://www.rcsb.org/structure/6UAU PDB ID 6UAU]
 
 
 
*[[GH128]] ''Amycolatopsis mediterranei'' endo-&beta;-1,3-glucanase E102A mutant, in complex with laminaripentaose [https://www.rcsb.org/structure/6UAT PDB ID 6UAT]
 
*[[GH128]] ''Amycolatopsis mediterranei'' endo-&beta;-1,3-glucanase E199Q mutant [https://www.rcsb.org/structure/6UFZ PDB ID 6UBFZ]
 
*[[GH128]] ''Amycolatopsis mediterranei'' endo-&beta;-1,3-glucanase E199A mutant, in complex with laminaripentaose [https://www.rcsb.org/structure/6UAS/ PDB ID 6UAS]
 
*[[GH128]] ''Amycolatopsis mediterranei'' endo-&beta;-1,3-glucanase E199A mutant, in complex with laminarihexaose [https://www.rcsb.org/structure/6UFL PDB ID 6UFL]
 
*[[GH128]] ''Sorangium cellulosum'' endo-&beta;-1,3-glucanase [https://www.rcsb.org/structure/6UAX/ PDB ID 6UAX]
 
*[[GH128]] ''Lentinula edodes'' endo-&beta;-1,3-glucanase [https://www.rcsb.org/structure/6UB2 PDB ID 6UB2]
 
*[[GH128]] ''Aureobasidium namibiae'' exo-&beta;-1,3-glucanase [https://www.rcsb.org/structure/6UB8 PDB ID 6UB8]
 
*[[GH128]] ''Aureobasidium namibiae'' exo-&beta;-1,3-glucanase, in complex with laminaritriose [https://www.rcsb.org/structure/6UBA PDB ID 6UAB]
 
*[[GH128]] ''Aureobasidium namibiae'' exo-&beta;-1,3-glucanase, with laminaribiose at the surface-binding site [https://www.rcsb.org/structure/6UBB PDB ID 6UBB]
 
*[[GH128]] ''Cryptococcus neoformans'' oligosaccharide-binding protein [https://www.rcsb.org/structure/6UBC PDB ID 6UBC]
 
 
 
 
 
 
 
</div><div>
 
</div><div>
 
</div>
 
  
 
----
 
----
  
 
<biblio>
 
<biblio>
 +
#Sousa2020 de Sousa, A.S., de Melo, R.R., Miyamoto, R.Y., Morais, M.A.B., Andrade, L.P., Milan, N., de Avila, M.C., de Souza, C.M., Adão, R.C., Scarpassa, J.A., Vieira, P.S., dos Santos, L.V., Ramos, C.H.I., Murakami, M.T. and Zanphorlin, L.M. (2020). ''A rationally identified marine GH1 β-glucosidase has distinguishing functional features for simultaneous saccharification and fermentation''. ''Biofuels, Bioprod. Bioref.'' 2020;'''14'''(6):1163-1179. [https://dx.doi.org/10.1002/bbb.2136 DOI: 10.1002/bbb.2136]
 +
 +
#Melo2021 pmid=33164774
  
# Gilbert2008 pmid=18430603
+
#Vieira2021 pmid=34193873
 +
#Santos2020 pmid=32451508
 +
#Domingues2018 pmid=29997257
  
 
</biblio>
 
</biblio>

Latest revision as of 06:33, 24 March 2023

Psvieira.jpg

Plinio Salmazo 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 and Priscila Oliveira de Giuseppe. 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 worked on a post-doc project under the supervision of Miguel Alcalde at Institute of Catalysis and Petrochemistry, focusing on the engineering and 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 and biochemical characterization of:


  1. 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 | PubMed ID:34193873 [Vieira2021]
  2. de Sousa, A.S., de Melo, R.R., Miyamoto, R.Y., Morais, M.A.B., Andrade, L.P., Milan, N., de Avila, M.C., de Souza, C.M., Adão, R.C., Scarpassa, J.A., Vieira, P.S., dos Santos, L.V., Ramos, C.H.I., Murakami, M.T. and Zanphorlin, L.M. (2020). A rationally identified marine GH1 β-glucosidase has distinguishing functional features for simultaneous saccharification and fermentation. Biofuels, Bioprod. Bioref. 2020;14(6):1163-1179. DOI: 10.1002/bbb.2136

    [Sousa2020]
  3. 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 | PubMed ID:29997257 [Domingues2018]
  4. de Melo RR, de Lima EA, Persinoti GF, Vieira PS, de Sousa AS, Zanphorlin LM, de Giuseppe PO, Ruller R, and Murakami MT. (2021). Identification of a cold-adapted and metal-stimulated β-1,4-glucanase with potential use in the extraction of bioactive compounds from plants. Int J Biol Macromol. 2021;166:190-199. DOI:10.1016/j.ijbiomac.2020.10.137 | PubMed ID:33164774 [Melo2021]
  5. 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 | PubMed ID:32451508 [Santos2020]

All Medline abstracts: PubMed