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SILVA, Catharina dos Santos e DIAS, Marcio Vinicius Bertacine. The multiple roles of the NlpC_P60 peptidase family in mycobacteria: an underexplored target for antimicrobial drug discovery. FEBS Letters, v. 599, p. 1203-1221, 2025Tradução . . Disponível em: https://doi.org/10.1002/1873-3468.70021. Acesso em: 26 nov. 2025.
APA
Silva, C. dos S., & Dias, M. V. B. (2025). The multiple roles of the NlpC_P60 peptidase family in mycobacteria: an underexplored target for antimicrobial drug discovery. FEBS Letters, 599, 1203-1221. doi:10.1002/1873-3468.70021
NLM
Silva C dos S, Dias MVB. The multiple roles of the NlpC_P60 peptidase family in mycobacteria: an underexplored target for antimicrobial drug discovery [Internet]. FEBS Letters. 2025 ; 599 1203-1221.[citado 2025 nov. 26 ] Available from: https://doi.org/10.1002/1873-3468.70021
Vancouver
Silva C dos S, Dias MVB. The multiple roles of the NlpC_P60 peptidase family in mycobacteria: an underexplored target for antimicrobial drug discovery [Internet]. FEBS Letters. 2025 ; 599 1203-1221.[citado 2025 nov. 26 ] Available from: https://doi.org/10.1002/1873-3468.70021
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GOMES, Brisa Moreira et al. Structural and functional characterization of a bifunctional GH43 α-L-arabinofuranosidase/β-xylosidase from the metagenome of Pseudacanthotermes militaris gut. International Journal of Biological Macromolecules: structure, function and interactions, v. No 2025, p. 01-13, 2025Tradução . . Disponível em: http://dx.doi.org/10.1016/j.ijbiomac.2025.147909. Acesso em: 26 nov. 2025.
APA
Gomes, B. M., Oliveira, G. S. de, Melo, V. S. de, Rossini, N. de O., Adriani, P. P., Dias, M. V. B., & Chambergo Alcalde, F. S. (2025). Structural and functional characterization of a bifunctional GH43 α-L-arabinofuranosidase/β-xylosidase from the metagenome of Pseudacanthotermes militaris gut. International Journal of Biological Macromolecules: structure, function and interactions, No 2025, 01-13. doi:10.1016/j.ijbiomac.2025.147909
NLM
Gomes BM, Oliveira GS de, Melo VS de, Rossini N de O, Adriani PP, Dias MVB, Chambergo Alcalde FS. Structural and functional characterization of a bifunctional GH43 α-L-arabinofuranosidase/β-xylosidase from the metagenome of Pseudacanthotermes militaris gut [Internet]. International Journal of Biological Macromolecules: structure, function and interactions. 2025 ; No 2025 01-13.[citado 2025 nov. 26 ] Available from: http://dx.doi.org/10.1016/j.ijbiomac.2025.147909
Vancouver
Gomes BM, Oliveira GS de, Melo VS de, Rossini N de O, Adriani PP, Dias MVB, Chambergo Alcalde FS. Structural and functional characterization of a bifunctional GH43 α-L-arabinofuranosidase/β-xylosidase from the metagenome of Pseudacanthotermes militaris gut [Internet]. International Journal of Biological Macromolecules: structure, function and interactions. 2025 ; No 2025 01-13.[citado 2025 nov. 26 ] Available from: http://dx.doi.org/10.1016/j.ijbiomac.2025.147909
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ADRIANI, Patricia Pereira et al. PEP-1 fused to glutathione peroxidase from Trichoderma reesei: a safe and effective antioxidant active ingredient for cutaneous applications. Journal of Drug Delivery Science and Technology, v. 110, p. 01-11 art. 107054, 2025Tradução . . Disponível em: http://dx.doi.org/10.1016/j.jddst.2025.107054. Acesso em: 26 nov. 2025.
APA
Adriani, P. P., Lopes, L. B., Oliveira, G. S. de, Nunes, J. R., Salata, G. C., Fernandes, M. T. P., et al. (2025). PEP-1 fused to glutathione peroxidase from Trichoderma reesei: a safe and effective antioxidant active ingredient for cutaneous applications. Journal of Drug Delivery Science and Technology, 110, 01-11 art. 107054. doi:10.1016/j.jddst.2025.107054
NLM
Adriani PP, Lopes LB, Oliveira GS de, Nunes JR, Salata GC, Fernandes MTP, Reigado GR, Camarena DEM, Maria-Engler SS, Dias MVB, Dantas VANC, Chambergo Alcalde FS. PEP-1 fused to glutathione peroxidase from Trichoderma reesei: a safe and effective antioxidant active ingredient for cutaneous applications [Internet]. Journal of Drug Delivery Science and Technology. 2025 ; 110 01-11 art. 107054.[citado 2025 nov. 26 ] Available from: http://dx.doi.org/10.1016/j.jddst.2025.107054
Vancouver
Adriani PP, Lopes LB, Oliveira GS de, Nunes JR, Salata GC, Fernandes MTP, Reigado GR, Camarena DEM, Maria-Engler SS, Dias MVB, Dantas VANC, Chambergo Alcalde FS. PEP-1 fused to glutathione peroxidase from Trichoderma reesei: a safe and effective antioxidant active ingredient for cutaneous applications [Internet]. Journal of Drug Delivery Science and Technology. 2025 ; 110 01-11 art. 107054.[citado 2025 nov. 26 ] Available from: http://dx.doi.org/10.1016/j.jddst.2025.107054
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ROSSINI, Nicolas de Oliveira et al. Using cryo-electron microscopy to understand the mechanisms of antimicrobial resistance to DNA gyrase in Mycobacterium tuberculosis. FEBS Open Bio, v. 15, 2025Tradução . . Disponível em: https://doi.org/10.1002/2211-5463.70071. Acesso em: 26 nov. 2025.
APA
Rossini, N. de O., Shiroma, S. T., Rosa, L. T., Coureaux, P., Souza, P. C. T. de, & Dias, M. V. B. (2025). Using cryo-electron microscopy to understand the mechanisms of antimicrobial resistance to DNA gyrase in Mycobacterium tuberculosis. FEBS Open Bio, 15. doi:10.1002/2211-5463.70071
NLM
Rossini N de O, Shiroma ST, Rosa LT, Coureaux P, Souza PCT de, Dias MVB. Using cryo-electron microscopy to understand the mechanisms of antimicrobial resistance to DNA gyrase in Mycobacterium tuberculosis [Internet]. FEBS Open Bio. 2025 ; 15[citado 2025 nov. 26 ] Available from: https://doi.org/10.1002/2211-5463.70071
Vancouver
Rossini N de O, Shiroma ST, Rosa LT, Coureaux P, Souza PCT de, Dias MVB. Using cryo-electron microscopy to understand the mechanisms of antimicrobial resistance to DNA gyrase in Mycobacterium tuberculosis [Internet]. FEBS Open Bio. 2025 ; 15[citado 2025 nov. 26 ] Available from: https://doi.org/10.1002/2211-5463.70071
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SILVA, Catharina dos Santos et al. Using a fragment-based approach against a potential novel drug target in Mycobacterium tuberculosis. 2025, Anais.. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular - SBBq, 2025. Disponível em: https://www2.sbbq.org.br/reuniao/2025/images/resumos.pdf. Acesso em: 26 nov. 2025.
APA
Silva, C. dos S., Rodrigues, V. L. T., Libreros-Zunigã, G. A., Rossini, N. de O., Guterrez, K., Barroso, V. de M., et al. (2025). Using a fragment-based approach against a potential novel drug target in Mycobacterium tuberculosis. In Livro de Resumos. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular - SBBq. Recuperado de https://www2.sbbq.org.br/reuniao/2025/images/resumos.pdf
NLM
Silva C dos S, Rodrigues VLT, Libreros-Zunigã GA, Rossini N de O, Guterrez K, Barroso V de M, Mesquita NC de MR, Tinoco L, Sforça ML, Guimarães AM de S, Ishida K, Emery F da S, Dias MVB. Using a fragment-based approach against a potential novel drug target in Mycobacterium tuberculosis [Internet]. Livro de Resumos. 2025 ;[citado 2025 nov. 26 ] Available from: https://www2.sbbq.org.br/reuniao/2025/images/resumos.pdf
Vancouver
Silva C dos S, Rodrigues VLT, Libreros-Zunigã GA, Rossini N de O, Guterrez K, Barroso V de M, Mesquita NC de MR, Tinoco L, Sforça ML, Guimarães AM de S, Ishida K, Emery F da S, Dias MVB. Using a fragment-based approach against a potential novel drug target in Mycobacterium tuberculosis [Internet]. Livro de Resumos. 2025 ;[citado 2025 nov. 26 ] Available from: https://www2.sbbq.org.br/reuniao/2025/images/resumos.pdf
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OLIVEIRA, Gabriel Stephani de et al. Structural and functional basis of GenB2 isomerase activity from Gentamicin biosynthesis. ACS Chemical Biology, v. 19, n. 9, p. 2002-2011, 2024Tradução . . Disponível em: https://doi.org/10.1021/acschembio.4c00334. Acesso em: 26 nov. 2025.
APA
Oliveira, G. S. de, Bury, P. dos S., Huang, F., Li, Y., Araújo, N. C. de, Zhou, J., et al. (2024). Structural and functional basis of GenB2 isomerase activity from Gentamicin biosynthesis. ACS Chemical Biology, 19( 9), 2002-2011. doi:10.1021/acschembio.4c00334
NLM
Oliveira GS de, Bury P dos S, Huang F, Li Y, Araújo NC de, Zhou J, Sun Y, Leeper FJ, Leadlay PF, Dias MVB. Structural and functional basis of GenB2 isomerase activity from Gentamicin biosynthesis [Internet]. ACS Chemical Biology. 2024 ; 19( 9): 2002-2011.[citado 2025 nov. 26 ] Available from: https://doi.org/10.1021/acschembio.4c00334
Vancouver
Oliveira GS de, Bury P dos S, Huang F, Li Y, Araújo NC de, Zhou J, Sun Y, Leeper FJ, Leadlay PF, Dias MVB. Structural and functional basis of GenB2 isomerase activity from Gentamicin biosynthesis [Internet]. ACS Chemical Biology. 2024 ; 19( 9): 2002-2011.[citado 2025 nov. 26 ] Available from: https://doi.org/10.1021/acschembio.4c00334
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VICARI, Hugo Passos et al. Cyclopenta [b] indoles as novel antimicrotubule agents with antileukemia activity. Toxicology in Vitro, v. 99, p. 11 , 2024Tradução . . Disponível em: https://doi.org/10.1016/j.tiv.2024.105856. Acesso em: 26 nov. 2025.
APA
Vicari, H. P., Gomes, R. da C., Lima, K., Rossini, N. de O., Rodrigues Junior, M. T., Miranda, L. B. L. D., et al. (2024). Cyclopenta [b] indoles as novel antimicrotubule agents with antileukemia activity. Toxicology in Vitro, 99, 11 . doi:10.1016/j.tiv.2024.105856
NLM
Vicari HP, Gomes R da C, Lima K, Rossini N de O, Rodrigues Junior MT, Miranda LBLD, Coelho FAS, Dias MVB, Costa-Lotufo LV, Machado Neto JA. Cyclopenta [b] indoles as novel antimicrotubule agents with antileukemia activity [Internet]. Toxicology in Vitro. 2024 ; 99 11 .[citado 2025 nov. 26 ] Available from: https://doi.org/10.1016/j.tiv.2024.105856
Vancouver
Vicari HP, Gomes R da C, Lima K, Rossini N de O, Rodrigues Junior MT, Miranda LBLD, Coelho FAS, Dias MVB, Costa-Lotufo LV, Machado Neto JA. Cyclopenta [b] indoles as novel antimicrotubule agents with antileukemia activity [Internet]. Toxicology in Vitro. 2024 ; 99 11 .[citado 2025 nov. 26 ] Available from: https://doi.org/10.1016/j.tiv.2024.105856
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SILVA, Adriana Sanches da et al. Biochemical characterization of an esterase from Thermobifida fusca YX with acetyl xylan esterase activity. Molecular Biology Reports, v. 51, n. 1, p. art. 767 ( 1-11), 2024Tradução . . Disponível em: https://doi.org/10.1007/s11033-024-09601-7. Acesso em: 26 nov. 2025.
APA
Silva, A. S. da, Adriani, P. P., Oliveira, G. S. de, Rocha, A. R. L., Perpetuo, E. A., Chambergo Alcalde, F. S., & Dias, M. V. B. (2024). Biochemical characterization of an esterase from Thermobifida fusca YX with acetyl xylan esterase activity. Molecular Biology Reports, 51( 1), art. 767 ( 1-11). doi:10.1007/s11033-024-09601-7
NLM
Silva AS da, Adriani PP, Oliveira GS de, Rocha ARL, Perpetuo EA, Chambergo Alcalde FS, Dias MVB. Biochemical characterization of an esterase from Thermobifida fusca YX with acetyl xylan esterase activity [Internet]. Molecular Biology Reports. 2024 ; 51( 1): art. 767 ( 1-11).[citado 2025 nov. 26 ] Available from: https://doi.org/10.1007/s11033-024-09601-7
Vancouver
Silva AS da, Adriani PP, Oliveira GS de, Rocha ARL, Perpetuo EA, Chambergo Alcalde FS, Dias MVB. Biochemical characterization of an esterase from Thermobifida fusca YX with acetyl xylan esterase activity [Internet]. Molecular Biology Reports. 2024 ; 51( 1): art. 767 ( 1-11).[citado 2025 nov. 26 ] Available from: https://doi.org/10.1007/s11033-024-09601-7
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ZÚÑIGA, Gerardo Andrés Libreros et al. Integration of biophysical and biological approaches to validate fragment-like compounds targeting l,d-transpeptidases from Mycobacterium tuberculosis. Bioorganic Chemistry, v. 142, n. Ja 2024, p. 106960-1-106960-11, 2024Tradução . . Disponível em: https://doi.org/10.1016/j.bioorg.2023.106960. Acesso em: 26 nov. 2025.
APA
Zúñiga, G. A. L., Pavão, D. P. e, Barroso, V. de M., Mesquita, N. C. de M. R., Braga, S. F. P., Oliva, G., et al. (2024). Integration of biophysical and biological approaches to validate fragment-like compounds targeting l,d-transpeptidases from Mycobacterium tuberculosis. Bioorganic Chemistry, 142( Ja 2024), 106960-1-106960-11. doi:10.1016/j.bioorg.2023.106960
NLM
Zúñiga GAL, Pavão DP e, Barroso V de M, Mesquita NC de MR, Braga SFP, Oliva G, Ferreira RS, Ishida K, Dias MVB. Integration of biophysical and biological approaches to validate fragment-like compounds targeting l,d-transpeptidases from Mycobacterium tuberculosis [Internet]. Bioorganic Chemistry. 2024 ; 142( Ja 2024): 106960-1-106960-11.[citado 2025 nov. 26 ] Available from: https://doi.org/10.1016/j.bioorg.2023.106960
Vancouver
Zúñiga GAL, Pavão DP e, Barroso V de M, Mesquita NC de MR, Braga SFP, Oliva G, Ferreira RS, Ishida K, Dias MVB. Integration of biophysical and biological approaches to validate fragment-like compounds targeting l,d-transpeptidases from Mycobacterium tuberculosis [Internet]. Bioorganic Chemistry. 2024 ; 142( Ja 2024): 106960-1-106960-11.[citado 2025 nov. 26 ] Available from: https://doi.org/10.1016/j.bioorg.2023.106960
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KIRKMAN, Tim et al. How to find a fragment: methods for screening and validation in fragment-based drug discovery. ChemMedChem: chemistry enabling drug, v. 19, n. 24, p. 14 , 2024Tradução . . Disponível em: https://doi.org/10.1002/cmdc.202400342. Acesso em: 26 nov. 2025.
APA
Kirkman, T., Silva, C. dos S., Tosin, M., & Dias, M. V. B. (2024). How to find a fragment: methods for screening and validation in fragment-based drug discovery. ChemMedChem: chemistry enabling drug, 19( 24), 14 . doi:10.1002/cmdc.202400342
NLM
Kirkman T, Silva C dos S, Tosin M, Dias MVB. How to find a fragment: methods for screening and validation in fragment-based drug discovery [Internet]. ChemMedChem: chemistry enabling drug. 2024 ; 19( 24): 14 .[citado 2025 nov. 26 ] Available from: https://doi.org/10.1002/cmdc.202400342
Vancouver
Kirkman T, Silva C dos S, Tosin M, Dias MVB. How to find a fragment: methods for screening and validation in fragment-based drug discovery [Internet]. ChemMedChem: chemistry enabling drug. 2024 ; 19( 24): 14 .[citado 2025 nov. 26 ] Available from: https://doi.org/10.1002/cmdc.202400342
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ROSSINI, Nicolas de Oliveira e DIAS, Marcio Vinicius Bertacine. Mutations and insights into the molecular mechanisms of resistance of Mycobacterium tuberculosis to first-line. Genetics and Molecular Biology, v. 46, n. 1(suppl 2), p. 1-17, 2023Tradução . . Disponível em: https://doi.org/10.1590/1678-4685-GMB-2022-0261. Acesso em: 26 nov. 2025.
APA
Rossini, N. de O., & Dias, M. V. B. (2023). Mutations and insights into the molecular mechanisms of resistance of Mycobacterium tuberculosis to first-line. Genetics and Molecular Biology, 46( 1(suppl 2), 1-17. doi:10.1590/1678-4685-GMB-2022-0261
NLM
Rossini N de O, Dias MVB. Mutations and insights into the molecular mechanisms of resistance of Mycobacterium tuberculosis to first-line [Internet]. Genetics and Molecular Biology. 2023 ; 46( 1(suppl 2): 1-17.[citado 2025 nov. 26 ] Available from: https://doi.org/10.1590/1678-4685-GMB-2022-0261
Vancouver
Rossini N de O, Dias MVB. Mutations and insights into the molecular mechanisms of resistance of Mycobacterium tuberculosis to first-line [Internet]. Genetics and Molecular Biology. 2023 ; 46( 1(suppl 2): 1-17.[citado 2025 nov. 26 ] Available from: https://doi.org/10.1590/1678-4685-GMB-2022-0261
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KIRKMAN, Tim et al. Fragment-Merging strategies with known pyrimidine scaffolds targeting dihydrofolate reductase from mycobacterium tuberculosis. ChemMedChem, 2023Tradução . . Disponível em: https://doi.org/10.1002/cmdc.202300240. Acesso em: 26 nov. 2025.
APA
Kirkman, T., Tan, S. F., Chavez-Pacheco, S. M., Hammer, A., Abell, C., Tosin, M., et al. (2023). Fragment-Merging strategies with known pyrimidine scaffolds targeting dihydrofolate reductase from mycobacterium tuberculosis. ChemMedChem. doi:10.1002/cmdc.202300240
NLM
Kirkman T, Tan SF, Chavez-Pacheco SM, Hammer A, Abell C, Tosin M, Anthony G. Coyne, Dias MVB. Fragment-Merging strategies with known pyrimidine scaffolds targeting dihydrofolate reductase from mycobacterium tuberculosis [Internet]. ChemMedChem. 2023 ;[citado 2025 nov. 26 ] Available from: https://doi.org/10.1002/cmdc.202300240
Vancouver
Kirkman T, Tan SF, Chavez-Pacheco SM, Hammer A, Abell C, Tosin M, Anthony G. Coyne, Dias MVB. Fragment-Merging strategies with known pyrimidine scaffolds targeting dihydrofolate reductase from mycobacterium tuberculosis [Internet]. ChemMedChem. 2023 ;[citado 2025 nov. 26 ] Available from: https://doi.org/10.1002/cmdc.202300240
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KIRKMAN, Tim et al. Crystal structure of dihydrofolate reductase from the emerging pathogenic fungus Candida auris. Acta Crystallographica. Section D: Structural Biology, v. 79, p. 735-745, 2023Tradução . . Disponível em: https://doi.org/10.1107/s2059798323004709. Acesso em: 26 nov. 2025.
APA
Kirkman, T., Barroso, M. V. de M., Tosin, M., Dias, V. B., & Ishida, K. (2023). Crystal structure of dihydrofolate reductase from the emerging pathogenic fungus Candida auris. Acta Crystallographica. Section D: Structural Biology, 79, 735-745. doi:10.1107/s2059798323004709
NLM
Kirkman T, Barroso MV de M, Tosin M, Dias VB, Ishida K. Crystal structure of dihydrofolate reductase from the emerging pathogenic fungus Candida auris [Internet]. Acta Crystallographica. Section D: Structural Biology. 2023 ; 79 735-745.[citado 2025 nov. 26 ] Available from: https://doi.org/10.1107/s2059798323004709
Vancouver
Kirkman T, Barroso MV de M, Tosin M, Dias VB, Ishida K. Crystal structure of dihydrofolate reductase from the emerging pathogenic fungus Candida auris [Internet]. Acta Crystallographica. Section D: Structural Biology. 2023 ; 79 735-745.[citado 2025 nov. 26 ] Available from: https://doi.org/10.1107/s2059798323004709
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Brazilian Symposium on Medicinal Chemistry - BrazMedChem, 11. . Salvador: Universidade Federal da Bahia - UFBA. . Acesso em: 26 nov. 2025. , 2023
APA
Brazilian Symposium on Medicinal Chemistry - BrazMedChem, 11. (2023). Brazilian Symposium on Medicinal Chemistry - BrazMedChem, 11. Salvador: Universidade Federal da Bahia - UFBA.
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ROSSINI, Nicolas de Oliveira e SILVA, Catharina e DIAS, Marcio Vinicius Bertacine. The crystal structure of Mycobacterium thermoresistibile MurE ligase reveals the binding mode of the substrate m-diaminopimelate. Journal of Structural Biology, v. 215, n. 2, p. 1-10, 2023Tradução . . Disponível em: https://doi.org/10.1016/j.jsb.2023.107957. Acesso em: 26 nov. 2025.
APA
Rossini, N. de O., Silva, C., & Dias, M. V. B. (2023). The crystal structure of Mycobacterium thermoresistibile MurE ligase reveals the binding mode of the substrate m-diaminopimelate. Journal of Structural Biology, 215( 2), 1-10. doi:10.1016/j.jsb.2023.107957
NLM
Rossini N de O, Silva C, Dias MVB. The crystal structure of Mycobacterium thermoresistibile MurE ligase reveals the binding mode of the substrate m-diaminopimelate [Internet]. Journal of Structural Biology. 2023 ; 215( 2): 1-10.[citado 2025 nov. 26 ] Available from: https://doi.org/10.1016/j.jsb.2023.107957
Vancouver
Rossini N de O, Silva C, Dias MVB. The crystal structure of Mycobacterium thermoresistibile MurE ligase reveals the binding mode of the substrate m-diaminopimelate [Internet]. Journal of Structural Biology. 2023 ; 215( 2): 1-10.[citado 2025 nov. 26 ] Available from: https://doi.org/10.1016/j.jsb.2023.107957
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VASSILIADES, Sandra Valeria et al. Mycobacterium tuberculosis dihydrofolate reductase inhibitors: State of Art Past 20 Years. Biointerface Research in Applied Chemistry, v. 13, n. 1 p. 1-20 art. 79, 2023Tradução . . Disponível em: https://doi.org/10.33263/BRIAC131.079. Acesso em: 26 nov. 2025.
APA
Vassiliades, S. V., Navarausckas, V. B., Dias, M. V. B., & Parise Filho, R. (2023). Mycobacterium tuberculosis dihydrofolate reductase inhibitors: State of Art Past 20 Years. Biointerface Research in Applied Chemistry, 13( 1 p. 1-20 art. 79). doi:10.33263/BRIAC131.079
NLM
Vassiliades SV, Navarausckas VB, Dias MVB, Parise Filho R. Mycobacterium tuberculosis dihydrofolate reductase inhibitors: State of Art Past 20 Years [Internet]. Biointerface Research in Applied Chemistry. 2023 ; 13( 1 p. 1-20 art. 79):[citado 2025 nov. 26 ] Available from: https://doi.org/10.33263/BRIAC131.079
Vancouver
Vassiliades SV, Navarausckas VB, Dias MVB, Parise Filho R. Mycobacterium tuberculosis dihydrofolate reductase inhibitors: State of Art Past 20 Years [Internet]. Biointerface Research in Applied Chemistry. 2023 ; 13( 1 p. 1-20 art. 79):[citado 2025 nov. 26 ] Available from: https://doi.org/10.33263/BRIAC131.079
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ARENAS, Laura Alejandra Rivas et al. Crystal structure of BtrK, a decarboxylase involved in the (S)-4-amino-2-hydroxybutyrate (AHBA) formation during butirosin biosynthesis. Journal of Molecular Structure, v. 1267, p. 1-10, 2022Tradução . . Disponível em: https://doi.org/10.1016/j.molstruc.2022.133576. Acesso em: 26 nov. 2025.
APA
Arenas, L. A. R., Paiva, F. C. R. de, Rossini, N. de O. \F. F. 0E., Li, Y., Spencer, J., Leadlay, P., & Dias, M. V. B. (2022). Crystal structure of BtrK, a decarboxylase involved in the (S)-4-amino-2-hydroxybutyrate (AHBA) formation during butirosin biosynthesis. Journal of Molecular Structure, 1267, 1-10. doi:10.1016/j.molstruc.2022.133576
NLM
Arenas LAR, Paiva FCR de, Rossini N de O\FF0E, Li Y, Spencer J, Leadlay P, Dias MVB. Crystal structure of BtrK, a decarboxylase involved in the (S)-4-amino-2-hydroxybutyrate (AHBA) formation during butirosin biosynthesis [Internet]. Journal of Molecular Structure. 2022 ; 1267 1-10.[citado 2025 nov. 26 ] Available from: https://doi.org/10.1016/j.molstruc.2022.133576
Vancouver
Arenas LAR, Paiva FCR de, Rossini N de O\FF0E, Li Y, Spencer J, Leadlay P, Dias MVB. Crystal structure of BtrK, a decarboxylase involved in the (S)-4-amino-2-hydroxybutyrate (AHBA) formation during butirosin biosynthesis [Internet]. Journal of Molecular Structure. 2022 ; 1267 1-10.[citado 2025 nov. 26 ] Available from: https://doi.org/10.1016/j.molstruc.2022.133576
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DIAS, Marcio Vinicius Bertacine et al. Da física à biologia, luz síncrotron ajuda cientistas a elucidar a estrutura das moléculas [Depoimento]. Jornal da USP. São Paulo: Instituto de Ciências Biomédicas, Universidade de São Paulo. Disponível em: https://jornal.usp.br/ciencias/da-fisica-a-biologia-luz-sincrotron-ajuda-cientistas-a-elucidar-a-estrutura-das-moleculas/. Acesso em: 26 nov. 2025. , 2022
APA
Dias, M. V. B., Garcia, F. A., Netto, L. E. S., & Guzzo, C. R. (2022). Da física à biologia, luz síncrotron ajuda cientistas a elucidar a estrutura das moléculas [Depoimento]. Jornal da USP. São Paulo: Instituto de Ciências Biomédicas, Universidade de São Paulo. Recuperado de https://jornal.usp.br/ciencias/da-fisica-a-biologia-luz-sincrotron-ajuda-cientistas-a-elucidar-a-estrutura-das-moleculas/
NLM
Dias MVB, Garcia FA, Netto LES, Guzzo CR. Da física à biologia, luz síncrotron ajuda cientistas a elucidar a estrutura das moléculas [Depoimento] [Internet]. Jornal da USP. 2022 ; 17 No 2022[citado 2025 nov. 26 ] Available from: https://jornal.usp.br/ciencias/da-fisica-a-biologia-luz-sincrotron-ajuda-cientistas-a-elucidar-a-estrutura-das-moleculas/
Vancouver
Dias MVB, Garcia FA, Netto LES, Guzzo CR. Da física à biologia, luz síncrotron ajuda cientistas a elucidar a estrutura das moléculas [Depoimento] [Internet]. Jornal da USP. 2022 ; 17 No 2022[citado 2025 nov. 26 ] Available from: https://jornal.usp.br/ciencias/da-fisica-a-biologia-luz-sincrotron-ajuda-cientistas-a-elucidar-a-estrutura-das-moleculas/
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
BILYK, Oksana et al. Enzyme-catalyzed spiroacetal formation in polyketide antibiotic biosynthesis. Journal of American Chemical Society, v. 144, n. 32, p. 14555–14563, 2022Tradução . . Disponível em: https://doi.org/10.1021/jacs.2c03313. Acesso em: 26 nov. 2025.
APA
Bilyk, O., Oliveira, G. S. de, Angelo, R. M. de, Almeida, M. de O., Honorio, K. M., Leeper, F. J., et al. (2022). Enzyme-catalyzed spiroacetal formation in polyketide antibiotic biosynthesis. Journal of American Chemical Society, 144( 32), 14555–14563. doi:10.1021/jacs.2c03313
NLM
Bilyk O, Oliveira GS de, Angelo RM de, Almeida M de O, Honorio KM, Leeper FJ, Dias MVB, Leadlay PF. Enzyme-catalyzed spiroacetal formation in polyketide antibiotic biosynthesis [Internet]. Journal of American Chemical Society. 2022 ; 144( 32): 14555–14563.[citado 2025 nov. 26 ] Available from: https://doi.org/10.1021/jacs.2c03313
Vancouver
Bilyk O, Oliveira GS de, Angelo RM de, Almeida M de O, Honorio KM, Leeper FJ, Dias MVB, Leadlay PF. Enzyme-catalyzed spiroacetal formation in polyketide antibiotic biosynthesis [Internet]. Journal of American Chemical Society. 2022 ; 144( 32): 14555–14563.[citado 2025 nov. 26 ] Available from: https://doi.org/10.1021/jacs.2c03313
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
LI, Sicong et al. Mechanistic insights into dideoxygenation in gentamicin biosynthesis. ACS Catalysis, v. 11, n. 19, p. 12274–12283, 2021Tradução . . Disponível em: https://doi.org/10.1021/acscatal.1c03508. Acesso em: 26 nov. 2025.
APA
Li, S., Bury, P. D. S., Huang, F., Guo, J., Sun, G., Reva, A., et al. (2021). Mechanistic insights into dideoxygenation in gentamicin biosynthesis. ACS Catalysis, 11( 19), 12274–12283. doi:10.1021/acscatal.1c03508
NLM
Li S, Bury PDS, Huang F, Guo J, Sun G, Reva A, Huang C, Jian X, Li Y, Zhou J, Deng Z, Leeper FJ, Leadlay PF, Dias MVB, Sun Y. Mechanistic insights into dideoxygenation in gentamicin biosynthesis [Internet]. ACS Catalysis. 2021 ; 11( 19): 12274–12283.[citado 2025 nov. 26 ] Available from: https://doi.org/10.1021/acscatal.1c03508
Vancouver
Li S, Bury PDS, Huang F, Guo J, Sun G, Reva A, Huang C, Jian X, Li Y, Zhou J, Deng Z, Leeper FJ, Leadlay PF, Dias MVB, Sun Y. Mechanistic insights into dideoxygenation in gentamicin biosynthesis [Internet]. ACS Catalysis. 2021 ; 11( 19): 12274–12283.[citado 2025 nov. 26 ] Available from: https://doi.org/10.1021/acscatal.1c03508