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SANTOS, Daisy Woellner et al. Schistosoma mansoni vaccine candidates identified by unbiased phage display screening in self-cured rhesus macaques. NPJ Vaccines, v. 09, n. Ja 2024, p. 5-1-5-19, 2024Tradução . . Disponível em: https://doi.org/10.1038/s41541-023-00803-x. Acesso em: 16 nov. 2024.
APA
Santos, D. W., Tahira, A. C., Malvezzi, J. V. de M., Mesel, V., Morales-Vicente, D. A., Trentini, M. M., et al. (2024). Schistosoma mansoni vaccine candidates identified by unbiased phage display screening in self-cured rhesus macaques. NPJ Vaccines, 09( Ja 2024), 5-1-5-19. doi:10.1038/s41541-023-00803-x
NLM
Santos DW, Tahira AC, Malvezzi JV de M, Mesel V, Morales-Vicente DA, Trentini MM, Marques Neto LM, Matos I de A, Kanno AI, Pereira A da SA, Teixeira AAR, Giordano RJ, Leite LC de C, Pereira CA de B, Marco RD, Amaral MS, Verjovski-Almeida S. Schistosoma mansoni vaccine candidates identified by unbiased phage display screening in self-cured rhesus macaques [Internet]. NPJ Vaccines. 2024 ; 09( Ja 2024): 5-1-5-19.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1038/s41541-023-00803-x
Vancouver
Santos DW, Tahira AC, Malvezzi JV de M, Mesel V, Morales-Vicente DA, Trentini MM, Marques Neto LM, Matos I de A, Kanno AI, Pereira A da SA, Teixeira AAR, Giordano RJ, Leite LC de C, Pereira CA de B, Marco RD, Amaral MS, Verjovski-Almeida S. Schistosoma mansoni vaccine candidates identified by unbiased phage display screening in self-cured rhesus macaques [Internet]. NPJ Vaccines. 2024 ; 09( Ja 2024): 5-1-5-19.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1038/s41541-023-00803-x
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CORREIA, Camila Rolemberg Santana Travaglini Berti de et al. Functional characterization of cullin-1-RING ubiquitin ligase (CRL1) complex in Leishmania infantum. PLOS Pathogens, v. 20, n. 7, p. e1012336-1-e1012336-34 + supporting information, 2024Tradução . . Disponível em: https://doi.org/10.1371/journal.ppat.1012336. Acesso em: 16 nov. 2024.
APA
Correia, C. R. S. T. B. de, Torres, C., Gomes, E., Rodriguez, G. M., Regatieri, W. K. P., Takamiya, N. T., et al. (2024). Functional characterization of cullin-1-RING ubiquitin ligase (CRL1) complex in Leishmania infantum. PLOS Pathogens, 20( 7), e1012336-1-e1012336-34 + supporting information. doi:10.1371/journal.ppat.1012336
NLM
Correia CRSTB de, Torres C, Gomes E, Rodriguez GM, Regatieri WKP, Takamiya NT, Rogerio LA, Malavazi I, Gomes MD, Damasceno JD, Silva VL da, Oliveira MAF de, Silva MS da, Nascimento AS, Coelho AC, Maruyama SRC, Teixeira FR. Functional characterization of cullin-1-RING ubiquitin ligase (CRL1) complex in Leishmania infantum [Internet]. PLOS Pathogens. 2024 ; 20( 7): e1012336-1-e1012336-34 + supporting information.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1371/journal.ppat.1012336
Vancouver
Correia CRSTB de, Torres C, Gomes E, Rodriguez GM, Regatieri WKP, Takamiya NT, Rogerio LA, Malavazi I, Gomes MD, Damasceno JD, Silva VL da, Oliveira MAF de, Silva MS da, Nascimento AS, Coelho AC, Maruyama SRC, Teixeira FR. Functional characterization of cullin-1-RING ubiquitin ligase (CRL1) complex in Leishmania infantum [Internet]. PLOS Pathogens. 2024 ; 20( 7): e1012336-1-e1012336-34 + supporting information.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1371/journal.ppat.1012336
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FERREIRA, Millena Pereira et al. Biomimetic catalysis of nitrite reductase enzyme using copper complexes in chemical and electrochemical reduction of nitrite. Dalton Transactions, v. 52, n. 32, p. 11254-11264, 2023Tradução . . Disponível em: https://doi.org/10.1039/D3DT01091K. Acesso em: 16 nov. 2024.
APA
Ferreira, M. P., Castro, C. B. de, Honorato, J., He, S., Guimarães Júnior, W. G., Esmieu, C., et al. (2023). Biomimetic catalysis of nitrite reductase enzyme using copper complexes in chemical and electrochemical reduction of nitrite. Dalton Transactions, 52( 32), 11254-11264. doi:10.1039/D3DT01091K
NLM
Ferreira MP, Castro CB de, Honorato J, He S, Guimarães Júnior WG, Esmieu C, Castellano EE, Moura AF de, Truzzi DR, Nascimento OR, Simonneau A, Marques Netto CGC. Biomimetic catalysis of nitrite reductase enzyme using copper complexes in chemical and electrochemical reduction of nitrite [Internet]. Dalton Transactions. 2023 ; 52( 32): 11254-11264.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1039/D3DT01091K
Vancouver
Ferreira MP, Castro CB de, Honorato J, He S, Guimarães Júnior WG, Esmieu C, Castellano EE, Moura AF de, Truzzi DR, Nascimento OR, Simonneau A, Marques Netto CGC. Biomimetic catalysis of nitrite reductase enzyme using copper complexes in chemical and electrochemical reduction of nitrite [Internet]. Dalton Transactions. 2023 ; 52( 32): 11254-11264.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1039/D3DT01091K
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MARQUIONI, Vinícius et al. Isolation and characterization of vB_XciM_LucasX, a new jumbo phage that infects Xanthomonas citri and Xanthomonas fuscans. PLOS One, v. 17, n. 4, p. e0266891-1-e0266891-19 + supporting information, 2022Tradução . . Disponível em: https://doi.org/10.1371/journal.pone.0266891. Acesso em: 16 nov. 2024.
APA
Marquioni, V., Rossi, F. P. N., Mendonça, D. C., Martins, L. F., Behlau, F., Setubal, J. C., et al. (2022). Isolation and characterization of vB_XciM_LucasX, a new jumbo phage that infects Xanthomonas citri and Xanthomonas fuscans. PLOS One, 17( 4), e0266891-1-e0266891-19 + supporting information. doi:10.1371/journal.pone.0266891
NLM
Marquioni V, Rossi FPN, Mendonça DC, Martins LF, Behlau F, Setubal JC, Da Silva AM, Novo-Mansur MTM. Isolation and characterization of vB_XciM_LucasX, a new jumbo phage that infects Xanthomonas citri and Xanthomonas fuscans [Internet]. PLOS One. 2022 ; 17( 4): e0266891-1-e0266891-19 + supporting information.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1371/journal.pone.0266891
Vancouver
Marquioni V, Rossi FPN, Mendonça DC, Martins LF, Behlau F, Setubal JC, Da Silva AM, Novo-Mansur MTM. Isolation and characterization of vB_XciM_LucasX, a new jumbo phage that infects Xanthomonas citri and Xanthomonas fuscans [Internet]. PLOS One. 2022 ; 17( 4): e0266891-1-e0266891-19 + supporting information.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1371/journal.pone.0266891
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OLIVEIRA, Valeria Maia de et al. Microorganisms: the secret agents of the biosphere, and their key roles in biotechnology. Biota Neotropica, v. 22 Nesp, p. 1-10, 2022Tradução . . Disponível em: https://doi.org/10.1590/1676-0611-BN-2022-1343. Acesso em: 16 nov. 2024.
APA
Oliveira, V. M. de, Andreote, F. D., Cortelo, P. C., Castro-Gamboa, I., Costa-Lotufo, L. V., Polizeli, M. de L. T. D. M., et al. (2022). Microorganisms: the secret agents of the biosphere, and their key roles in biotechnology. Biota Neotropica, 22 Nesp, 1-10. doi:10.1590/1676-0611-BN-2022-1343
NLM
Oliveira VM de, Andreote FD, Cortelo PC, Castro-Gamboa I, Costa-Lotufo LV, Polizeli M de LTDM, Thiemann OH, Setubal JC. Microorganisms: the secret agents of the biosphere, and their key roles in biotechnology [Internet]. Biota Neotropica. 2022 ; 22 Nesp 1-10.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1590/1676-0611-BN-2022-1343
Vancouver
Oliveira VM de, Andreote FD, Cortelo PC, Castro-Gamboa I, Costa-Lotufo LV, Polizeli M de LTDM, Thiemann OH, Setubal JC. Microorganisms: the secret agents of the biosphere, and their key roles in biotechnology [Internet]. Biota Neotropica. 2022 ; 22 Nesp 1-10.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1590/1676-0611-BN-2022-1343
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FERREIRA, Julio Cesar Batista e MUNHOZ, Carolina Demarchi. Scientific Reports. Scientific Reports. London: Nature. Disponível em: https://repositorio.usp.br/directbitstream/64c69769-bbef-4859-b13c-f3fa23cef373/P19207.pdf. Acesso em: 16 nov. 2024. , 2021
APA
Ferreira, J. C. B., & Munhoz, C. D. (2021). Scientific Reports. Scientific Reports. London: Nature. Recuperado de https://repositorio.usp.br/directbitstream/64c69769-bbef-4859-b13c-f3fa23cef373/P19207.pdf
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VELDMAN, Wayde et al. Differences in gluco and galacto substrate-binding interactions in a dual 6Pβ-Glucosidase/6Pβ-Galactosidase glycoside hydrolase 1 enzyme from Bacillus licheniformis. Journal of Chemical Information and Modeling, v. 61, n. 9, p. 4554-4570, 2021Tradução . . Disponível em: https://doi.org/10.1021/acs.jcim.1c00413. Acesso em: 16 nov. 2024.
APA
Veldman, W., Liberato, M. V., Souza, V. P., Almeida, V. M., Marana, S. R., Bishop, O. T., & Polikarpov, I. (2021). Differences in gluco and galacto substrate-binding interactions in a dual 6Pβ-Glucosidase/6Pβ-Galactosidase glycoside hydrolase 1 enzyme from Bacillus licheniformis. Journal of Chemical Information and Modeling, 61( 9), 4554-4570. doi:10.1021/acs.jcim.1c00413
NLM
Veldman W, Liberato MV, Souza VP, Almeida VM, Marana SR, Bishop OT, Polikarpov I. Differences in gluco and galacto substrate-binding interactions in a dual 6Pβ-Glucosidase/6Pβ-Galactosidase glycoside hydrolase 1 enzyme from Bacillus licheniformis [Internet]. Journal of Chemical Information and Modeling. 2021 ; 61( 9): 4554-4570.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1021/acs.jcim.1c00413
Vancouver
Veldman W, Liberato MV, Souza VP, Almeida VM, Marana SR, Bishop OT, Polikarpov I. Differences in gluco and galacto substrate-binding interactions in a dual 6Pβ-Glucosidase/6Pβ-Galactosidase glycoside hydrolase 1 enzyme from Bacillus licheniformis [Internet]. Journal of Chemical Information and Modeling. 2021 ; 61( 9): 4554-4570.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1021/acs.jcim.1c00413
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VIGNONI, Alejandro et al. Alkylation of a hydrophilic photosensitizer enhances the contact-dependent photo-induced oxidation of phospholipid membranes. Dyes and Pigments, v. 187, 2021Tradução . . Disponível em: https://doi.org/10.1016/j.dyepig.2020.109131. Acesso em: 16 nov. 2024.
APA
Vignoni, A., Layana, C., Junqueira, H. C., Thomas, A. H., Itri, R., Baptista, M. da S., & Vignoni, M. (2021). Alkylation of a hydrophilic photosensitizer enhances the contact-dependent photo-induced oxidation of phospholipid membranes. Dyes and Pigments, 187. doi:10.1016/j.dyepig.2020.109131
NLM
Vignoni A, Layana C, Junqueira HC, Thomas AH, Itri R, Baptista M da S, Vignoni M. Alkylation of a hydrophilic photosensitizer enhances the contact-dependent photo-induced oxidation of phospholipid membranes [Internet]. Dyes and Pigments. 2021 ; 187[citado 2024 nov. 16 ] Available from: https://doi.org/10.1016/j.dyepig.2020.109131
Vancouver
Vignoni A, Layana C, Junqueira HC, Thomas AH, Itri R, Baptista M da S, Vignoni M. Alkylation of a hydrophilic photosensitizer enhances the contact-dependent photo-induced oxidation of phospholipid membranes [Internet]. Dyes and Pigments. 2021 ; 187[citado 2024 nov. 16 ] Available from: https://doi.org/10.1016/j.dyepig.2020.109131
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VELDMAN, Wayde et al. X-ray structure, bioinformatics analysis, and substrate specificity of a 6-phospho-β-glucosidase glycoside hydrolase 1 enzyme from Bacillus licheniformis. Journal of Chemical Information and Modeling, v. 60, n. 12, p. 6392-6407, 2020Tradução . . Disponível em: https://doi.org/10.1021/acs.jcim.0c00759. Acesso em: 16 nov. 2024.
APA
Veldman, W., Liberato, M. V., Almeida, V. M., Souza, V. P., Frutuoso, M. A., Marana, S. R., et al. (2020). X-ray structure, bioinformatics analysis, and substrate specificity of a 6-phospho-β-glucosidase glycoside hydrolase 1 enzyme from Bacillus licheniformis. Journal of Chemical Information and Modeling, 60( 12), 6392-6407. doi:10.1021/acs.jcim.0c00759
NLM
Veldman W, Liberato MV, Almeida VM, Souza VP, Frutuoso MA, Marana SR, Moses V, Bishop OT, Polikarpov I. X-ray structure, bioinformatics analysis, and substrate specificity of a 6-phospho-β-glucosidase glycoside hydrolase 1 enzyme from Bacillus licheniformis [Internet]. Journal of Chemical Information and Modeling. 2020 ; 60( 12): 6392-6407.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1021/acs.jcim.0c00759
Vancouver
Veldman W, Liberato MV, Almeida VM, Souza VP, Frutuoso MA, Marana SR, Moses V, Bishop OT, Polikarpov I. X-ray structure, bioinformatics analysis, and substrate specificity of a 6-phospho-β-glucosidase glycoside hydrolase 1 enzyme from Bacillus licheniformis [Internet]. Journal of Chemical Information and Modeling. 2020 ; 60( 12): 6392-6407.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1021/acs.jcim.0c00759
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GARCIA, Pâmela Soto et al. Nanoimmunosensor based on atomic force spectroscopy to detect anti-myelin basic protein related to early-stage multiple sclerosis. Ultramicroscopy, v. 211, p. 112946-1-112946-8, 2020Tradução . . Disponível em: https://doi.org/10.1016/j.ultramic.2020.112946. Acesso em: 16 nov. 2024.
APA
Garcia, P. S., Brum, D. G., Oliveira Junior, O. N. de, Higa, A. M., Ierich, J. C. M., Moraes, A. de S., et al. (2020). Nanoimmunosensor based on atomic force spectroscopy to detect anti-myelin basic protein related to early-stage multiple sclerosis. Ultramicroscopy, 211, 112946-1-112946-8. doi:10.1016/j.ultramic.2020.112946
NLM
Garcia PS, Brum DG, Oliveira Junior ON de, Higa AM, Ierich JCM, Moraes A de S, Shimizu FM, Okuda-Shinagawa NM, Peroni LA, Gama PD da, Machini MT, Leite FL. Nanoimmunosensor based on atomic force spectroscopy to detect anti-myelin basic protein related to early-stage multiple sclerosis [Internet]. Ultramicroscopy. 2020 ; 211 112946-1-112946-8.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1016/j.ultramic.2020.112946
Vancouver
Garcia PS, Brum DG, Oliveira Junior ON de, Higa AM, Ierich JCM, Moraes A de S, Shimizu FM, Okuda-Shinagawa NM, Peroni LA, Gama PD da, Machini MT, Leite FL. Nanoimmunosensor based on atomic force spectroscopy to detect anti-myelin basic protein related to early-stage multiple sclerosis [Internet]. Ultramicroscopy. 2020 ; 211 112946-1-112946-8.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1016/j.ultramic.2020.112946
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GARCIA, Bruna M. et al. Mice born to females with oocytespecific deletion of mitofusin 2 have increased weight gain and impaired glucose homeostasis. Molecular Human Reproduction, v. 26, n. 12, p. 938-952 + supplementary data, 2020Tradução . . Disponível em: https://doi.org/10.1093/molehr/gaaa071. Acesso em: 16 nov. 2024.
APA
Garcia, B. M., Machado, T. S., Carvalho, K. F., Nolasco, P., Nociti, R. P., Del Collado, M. B., et al. (2020). Mice born to females with oocytespecific deletion of mitofusin 2 have increased weight gain and impaired glucose homeostasis. Molecular Human Reproduction, 26( 12), 938-952 + supplementary data. doi:10.1093/molehr/gaaa071
NLM
Garcia BM, Machado TS, Carvalho KF, Nolasco P, Nociti RP, Del Collado MB, Bianco MJDC, Grejo MP, Augustro Neto JDA, Sugiyama FHC, Tostes K, Pandey AK, Gonçalves LM, Perecin F, Meirelles FV, Ferraz JBS, Vanzela EC, Boschero AC, Guimarães FEG, Abdulkader FR de M, Laurindo FRM, Kowaltowski AJ, Chiaratti MR. Mice born to females with oocytespecific deletion of mitofusin 2 have increased weight gain and impaired glucose homeostasis [Internet]. Molecular Human Reproduction. 2020 ; 26( 12): 938-952 + supplementary data.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1093/molehr/gaaa071
Vancouver
Garcia BM, Machado TS, Carvalho KF, Nolasco P, Nociti RP, Del Collado MB, Bianco MJDC, Grejo MP, Augustro Neto JDA, Sugiyama FHC, Tostes K, Pandey AK, Gonçalves LM, Perecin F, Meirelles FV, Ferraz JBS, Vanzela EC, Boschero AC, Guimarães FEG, Abdulkader FR de M, Laurindo FRM, Kowaltowski AJ, Chiaratti MR. Mice born to females with oocytespecific deletion of mitofusin 2 have increased weight gain and impaired glucose homeostasis [Internet]. Molecular Human Reproduction. 2020 ; 26( 12): 938-952 + supplementary data.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1093/molehr/gaaa071
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SASTRE, Diego Emiliano et al. The phosphatidic acid pathway enzyme PlsX plays both catalytic and channeling roles in bacterial phospholipid synthesis. Journal of Biological Chemistry, v. 295, n. 7, p. 2148-2159 + Supplementary materials Figs. S1-S5 and Tables S1 and S2, 2020Tradução . . Disponível em: https://doi.org/10.1074/jbc.RA119.011147. Acesso em: 16 nov. 2024.
APA
Sastre, D. E., Pulschen, A. A., Basso, L. G. M., Pariente, J. S. B., Marques Netto, C. G. C., Machinandiarena, F., et al. (2020). The phosphatidic acid pathway enzyme PlsX plays both catalytic and channeling roles in bacterial phospholipid synthesis. Journal of Biological Chemistry, 295( 7), 2148-2159 + Supplementary materials Figs. S1-S5 and Tables S1 and S2. doi:10.1074/jbc.RA119.011147
NLM
Sastre DE, Pulschen AA, Basso LGM, Pariente JSB, Marques Netto CGC, Machinandiarena F, Albanesi D, Navarro MV de AS, Mendoza D de, Gueiros Filho FJ. The phosphatidic acid pathway enzyme PlsX plays both catalytic and channeling roles in bacterial phospholipid synthesis [Internet]. Journal of Biological Chemistry. 2020 ; 295( 7): 2148-2159 + Supplementary materials Figs. S1-S5 and Tables S1 and S2.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1074/jbc.RA119.011147
Vancouver
Sastre DE, Pulschen AA, Basso LGM, Pariente JSB, Marques Netto CGC, Machinandiarena F, Albanesi D, Navarro MV de AS, Mendoza D de, Gueiros Filho FJ. The phosphatidic acid pathway enzyme PlsX plays both catalytic and channeling roles in bacterial phospholipid synthesis [Internet]. Journal of Biological Chemistry. 2020 ; 295( 7): 2148-2159 + Supplementary materials Figs. S1-S5 and Tables S1 and S2.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1074/jbc.RA119.011147
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COSTA, Fernanda Rodrigues et al. Merulinic acid C overcomes gentamicin resistance in Enterococcus faecium. Bioorganic Chemistry, v. 100, p. 1-8 art. 103921, 2020Tradução . . Disponível em: https://doi.org/10.1016/j.bioorg.2020.103921. Acesso em: 16 nov. 2024.
APA
Costa, F. R., Slivinski, J., Ióca, L. P., Bertonha, A. F., Felício, R. de, Cunha, M. G. da, et al. (2020). Merulinic acid C overcomes gentamicin resistance in Enterococcus faecium. Bioorganic Chemistry, 100, 1-8 art. 103921. doi:10.1016/j.bioorg.2020.103921
NLM
Costa FR, Slivinski J, Ióca LP, Bertonha AF, Felício R de, Cunha MG da, Madeira PV da M, Cauz ACG, Trindade DM, Freire VF, Ropke CD, Gales A, Brocchi M, Ferreira AG, Gueiros Filho FJ, Trivella DBB, Berlinck RG de S, Dessen A. Merulinic acid C overcomes gentamicin resistance in Enterococcus faecium [Internet]. Bioorganic Chemistry. 2020 ; 100 1-8 art. 103921.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1016/j.bioorg.2020.103921
Vancouver
Costa FR, Slivinski J, Ióca LP, Bertonha AF, Felício R de, Cunha MG da, Madeira PV da M, Cauz ACG, Trindade DM, Freire VF, Ropke CD, Gales A, Brocchi M, Ferreira AG, Gueiros Filho FJ, Trivella DBB, Berlinck RG de S, Dessen A. Merulinic acid C overcomes gentamicin resistance in Enterococcus faecium [Internet]. Bioorganic Chemistry. 2020 ; 100 1-8 art. 103921.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1016/j.bioorg.2020.103921
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SASTRE, Diego Emiliano et al. Membrane fluidity adjusts the insertion of the transacylase PlsX to regulate phospholipid biosynthesis in Gram-positive bacteria. Journal of Biological Chemistry, v. 295, n. 7, p. 2136-2147 + Supplementary materials Figs. S1-S9, 2020Tradução . . Disponível em: https://doi.org/10.1074/jbc.RA119.011122. Acesso em: 16 nov. 2024.
APA
Sastre, D. E., Basso, L. G. M., Trastoy, B., Cifuente, J. O., Contreras, X., Gueiros Filho, F. J., et al. (2020). Membrane fluidity adjusts the insertion of the transacylase PlsX to regulate phospholipid biosynthesis in Gram-positive bacteria. Journal of Biological Chemistry, 295( 7), 2136-2147 + Supplementary materials Figs. S1-S9. doi:10.1074/jbc.RA119.011122
NLM
Sastre DE, Basso LGM, Trastoy B, Cifuente JO, Contreras X, Gueiros Filho FJ, Mendoza D de, Navarro MV de AS, Guerin ME. Membrane fluidity adjusts the insertion of the transacylase PlsX to regulate phospholipid biosynthesis in Gram-positive bacteria [Internet]. Journal of Biological Chemistry. 2020 ; 295( 7): 2136-2147 + Supplementary materials Figs. S1-S9.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1074/jbc.RA119.011122
Vancouver
Sastre DE, Basso LGM, Trastoy B, Cifuente JO, Contreras X, Gueiros Filho FJ, Mendoza D de, Navarro MV de AS, Guerin ME. Membrane fluidity adjusts the insertion of the transacylase PlsX to regulate phospholipid biosynthesis in Gram-positive bacteria [Internet]. Journal of Biological Chemistry. 2020 ; 295( 7): 2136-2147 + Supplementary materials Figs. S1-S9.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1074/jbc.RA119.011122