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Artigo de periodico
Cryo-EM structure of 1-deoxy-D-xylulose 5-phosphate synthase DXPS from plasmodium falciparum reveals a distinct N-terminal domain (2024)
Gawriljuk, Victor Oliveira; Godoy, Andre Schutzer de ; Oerlemans, Rick; Welker, Luise A. T.; Hirsch, Anna Katharina Herta ; Groves, Matthew R.
Source: Nature Communications. Unidade: IFSC
Subjects: MALÁRIA, PLASMODIUM FALCIPARUM, ENZIMAS
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ABNT
GAWRILJUK, Victor Oliveira et al. Cryo-EM structure of 1-deoxy-D-xylulose 5-phosphate synthase DXPS from plasmodium falciparum reveals a distinct N-terminal domain. Nature Communications, v. 15, p. 6642-1-6642-10 + supplementary information, 2024Tradução . . Disponível em: https://doi.org/10.1038/s41467-024-50671-9. Acesso em: 07 nov. 2024.
APA
Gawriljuk, V. O., Godoy, A. S. de, Oerlemans, R., Welker, L. A. T., Hirsch, A. K. H., & Groves, M. R. (2024). Cryo-EM structure of 1-deoxy-D-xylulose 5-phosphate synthase DXPS from plasmodium falciparum reveals a distinct N-terminal domain. Nature Communications, 15, 6642-1-6642-10 + supplementary information. doi:10.1038/s41467-024-50671-9
NLM
Gawriljuk VO, Godoy AS de, Oerlemans R, Welker LAT, Hirsch AKH, Groves MR. Cryo-EM structure of 1-deoxy-D-xylulose 5-phosphate synthase DXPS from plasmodium falciparum reveals a distinct N-terminal domain [Internet]. Nature Communications. 2024 ; 15 6642-1-6642-10 + supplementary information.[citado 2024 nov. 07 ] Available from: https://doi.org/10.1038/s41467-024-50671-9
Vancouver
Gawriljuk VO, Godoy AS de, Oerlemans R, Welker LAT, Hirsch AKH, Groves MR. Cryo-EM structure of 1-deoxy-D-xylulose 5-phosphate synthase DXPS from plasmodium falciparum reveals a distinct N-terminal domain [Internet]. Nature Communications. 2024 ; 15 6642-1-6642-10 + supplementary information.[citado 2024 nov. 07 ] Available from: https://doi.org/10.1038/s41467-024-50671-9
Artigo de periodico
Hematologically important mutations: X-linked chronic granulomatous disease (fourth update) (2021)
Roos, Dirk; Leeuwen, Karin van; Hsu, Amy P.; Priel, Debra Long ; Begtrup, Amber ; Brandon, Rhonda; Stasia, Marie José ; Bakri, Faris Ghalib ; Köker, Nezihe ; Köker, Mustafa Yavuz ; Madkaika, Manisha; Boer, Martin de ; Morato, Maria Bravo Garcia ; Shephard, Juan Luis Valdivieso; Roesler, Joachim ; Kanegane, Hirokazu ; Kawai, Toshinao ; Matteo, Gigliola Di ; Shahrooei, Mohammad ; Bustamante, Jacinta ; Rawat, Amit ; Vignesh, Pandiarajan ; Mortaz, Esmaeil ; Fayezi, Abbas; Cagdas, Deniz ; Tezcan, Ilhan ; Kitcharoensakkul, Maleewan ; Dinauer, Mary C. ; Meyts, Isabelle; Wolach, Baruch; Condino Neto, Antonio ; Zerbe, Christa S. ; Holland, Steven M.; Malech, Harry L. ; Gallin, John I.; Kuhns, Douglas B.
Source: Blood Cells, Molecules and Diseases. Unidade: ICB
Subjects: IMUNOLOGIA, IMUNODEFICIÊNCIA DE VARIÁVEL COMUM, MUTAÇÃO GENÉTICA, DOENÇAS SANGUÍNEAS E LINFÁTICAS, SUPERÓXIDO DISMUTASE, ATIVAÇÃO ENZIMÁTICA, IMUNOGENÉTICA, ENZIMAS
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ROOS, Dirk et al. Hematologically important mutations: X-linked chronic granulomatous disease (fourth update). Blood Cells, Molecules and Diseases, v. 90, p. 1-36, 2021Tradução . . Disponível em: https://doi.org/10.1016/j.bcmd.2021.102587. Acesso em: 07 nov. 2024.
APA
Roos, D., Leeuwen, K. van, Hsu, A. P., Priel, D. L., Begtrup, A., Brandon, R., et al. (2021). Hematologically important mutations: X-linked chronic granulomatous disease (fourth update). Blood Cells, Molecules and Diseases, 90, 1-36. doi:10.1016/j.bcmd.2021.102587
NLM
Roos D, Leeuwen K van, Hsu AP, Priel DL, Begtrup A, Brandon R, Stasia MJ, Bakri FG, Köker N, Köker MY, Madkaika M, Boer M de, Morato MBG, Shephard JLV, Roesler J, Kanegane H, Kawai T, Matteo GD, Shahrooei M, Bustamante J, Rawat A, Vignesh P, Mortaz E, Fayezi A, Cagdas D, Tezcan I, Kitcharoensakkul M, Dinauer MC, Meyts I, Wolach B, Condino Neto A, Zerbe CS, Holland SM, Malech HL, Gallin JI, Kuhns DB. Hematologically important mutations: X-linked chronic granulomatous disease (fourth update) [Internet]. Blood Cells, Molecules and Diseases. 2021 ; 90 1-36.[citado 2024 nov. 07 ] Available from: https://doi.org/10.1016/j.bcmd.2021.102587
Vancouver
Roos D, Leeuwen K van, Hsu AP, Priel DL, Begtrup A, Brandon R, Stasia MJ, Bakri FG, Köker N, Köker MY, Madkaika M, Boer M de, Morato MBG, Shephard JLV, Roesler J, Kanegane H, Kawai T, Matteo GD, Shahrooei M, Bustamante J, Rawat A, Vignesh P, Mortaz E, Fayezi A, Cagdas D, Tezcan I, Kitcharoensakkul M, Dinauer MC, Meyts I, Wolach B, Condino Neto A, Zerbe CS, Holland SM, Malech HL, Gallin JI, Kuhns DB. Hematologically important mutations: X-linked chronic granulomatous disease (fourth update) [Internet]. Blood Cells, Molecules and Diseases. 2021 ; 90 1-36.[citado 2024 nov. 07 ] Available from: https://doi.org/10.1016/j.bcmd.2021.102587
Artigo de periodico
Mangrove soil as a source for novel xylanase and amylase as determined by cultivation-dependent and cultivation-independent methods (2020)
Alves, Kelly Jaqueline ; Silva, Mylenne Calciolari Pinheiro da; Cotta, Simone Raposo ; Ottoni, Júlia Ronzella; van Elsas, Jan Dirk; Oliveira, Valeria Maia de; Andreote, Fernando Dini
Source: Brazilian Journal of Microbiology. Unidades: ESALQ, CENA
Subjects: AMILASES, BACTÉRIAS, BIODEGRADAÇÃO, BIOTECNOLOGIA, ECOSSISTEMAS DE MANGUE, ENZIMAS, MICROBIOLOGIA DO SOLO
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ABNT
ALVES, Kelly Jaqueline et al. Mangrove soil as a source for novel xylanase and amylase as determined by cultivation-dependent and cultivation-independent methods. Brazilian Journal of Microbiology, v. 51, p. 217-228, 2020Tradução . . Disponível em: https://doi.org/10.1007/s42770-019-00162-7. Acesso em: 07 nov. 2024.
APA
Alves, K. J., Silva, M. C. P. da, Cotta, S. R., Ottoni, J. R., van Elsas, J. D., Oliveira, V. M. de, & Andreote, F. D. (2020). Mangrove soil as a source for novel xylanase and amylase as determined by cultivation-dependent and cultivation-independent methods. Brazilian Journal of Microbiology, 51, 217-228. doi:10.1007/s42770-019-00162-7
NLM
Alves KJ, Silva MCP da, Cotta SR, Ottoni JR, van Elsas JD, Oliveira VM de, Andreote FD. Mangrove soil as a source for novel xylanase and amylase as determined by cultivation-dependent and cultivation-independent methods [Internet]. Brazilian Journal of Microbiology. 2020 ; 51 217-228.[citado 2024 nov. 07 ] Available from: https://doi.org/10.1007/s42770-019-00162-7
Vancouver
Alves KJ, Silva MCP da, Cotta SR, Ottoni JR, van Elsas JD, Oliveira VM de, Andreote FD. Mangrove soil as a source for novel xylanase and amylase as determined by cultivation-dependent and cultivation-independent methods [Internet]. Brazilian Journal of Microbiology. 2020 ; 51 217-228.[citado 2024 nov. 07 ] Available from: https://doi.org/10.1007/s42770-019-00162-7
Artigo de periodico
Development of a generic high-throughput screening assay for profiling snake venom protease activity after high-resolution chromatographic fractionation (2020)
Neumann, Coleen; Slagboom, Julien; Somsen, Govert W.; Vonk, Freek; Casewell, Nicholas R.; Cardoso, Carmen Lucia ; Kool, Jeroen
Source: Toxicon. Unidade: FFCLRP
Subjects: VENENOS DE ORIGEM ANIMAL, TOXINAS EM ANIMAL, ENVENENAMENTO POR ANIMAIS PEÇONHENTOS, COBRAS, ENZIMAS
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ABNT
NEUMANN, Coleen et al. Development of a generic high-throughput screening assay for profiling snake venom protease activity after high-resolution chromatographic fractionation. Toxicon, v. 178, p. 61-68, 2020Tradução . . Disponível em: https://doi.org/10.1016/j.toxicon.2020.02.015. Acesso em: 07 nov. 2024.
APA
Neumann, C., Slagboom, J., Somsen, G. W., Vonk, F., Casewell, N. R., Cardoso, C. L., & Kool, J. (2020). Development of a generic high-throughput screening assay for profiling snake venom protease activity after high-resolution chromatographic fractionation. Toxicon, 178, 61-68. doi:10.1016/j.toxicon.2020.02.015
NLM
Neumann C, Slagboom J, Somsen GW, Vonk F, Casewell NR, Cardoso CL, Kool J. Development of a generic high-throughput screening assay for profiling snake venom protease activity after high-resolution chromatographic fractionation [Internet]. Toxicon. 2020 ; 178 61-68.[citado 2024 nov. 07 ] Available from: https://doi.org/10.1016/j.toxicon.2020.02.015
Vancouver
Neumann C, Slagboom J, Somsen GW, Vonk F, Casewell NR, Cardoso CL, Kool J. Development of a generic high-throughput screening assay for profiling snake venom protease activity after high-resolution chromatographic fractionation [Internet]. Toxicon. 2020 ; 178 61-68.[citado 2024 nov. 07 ] Available from: https://doi.org/10.1016/j.toxicon.2020.02.015
Artigo de periodico
Porphyrin-nanodiamond hybrid materials-active, stable and reusable cyclohexene oxidation catalysts (2020)
Dias, Lucas Danilo ; Rodrigues, Fábio M. S. ; Calvete, Mário J. F. ; Carabineiro, Sónia A. C. ; Scherer, Marisa D.; Caires, Anderson R. L. ; Buijnsters, Josephus G. ; Figueiredo, José L. ; Bagnato, Vanderlei Salvador ; Pereira, Mariette M.
Source: Catalysts. Unidade: IFSC
Subjects: ENZIMAS, FUNGOS TERMÓFILOS, RESSONÂNCIA PARAMAGNÉTICA ELETRÔNICA
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ABNT
DIAS, Lucas Danilo et al. Porphyrin-nanodiamond hybrid materials-active, stable and reusable cyclohexene oxidation catalysts. Catalysts, v. 10, n. 2, p. 1402-1-1402-13, 2020Tradução . . Disponível em: https://doi.org/10.3390/catal10121402. Acesso em: 07 nov. 2024.
APA
Dias, L. D., Rodrigues, F. M. S., Calvete, M. J. F., Carabineiro, S. A. C., Scherer, M. D., Caires, A. R. L., et al. (2020). Porphyrin-nanodiamond hybrid materials-active, stable and reusable cyclohexene oxidation catalysts. Catalysts, 10( 2), 1402-1-1402-13. doi:10.3390/catal10121402
NLM
Dias LD, Rodrigues FMS, Calvete MJF, Carabineiro SAC, Scherer MD, Caires ARL, Buijnsters JG, Figueiredo JL, Bagnato VS, Pereira MM. Porphyrin-nanodiamond hybrid materials-active, stable and reusable cyclohexene oxidation catalysts [Internet]. Catalysts. 2020 ; 10( 2): 1402-1-1402-13.[citado 2024 nov. 07 ] Available from: https://doi.org/10.3390/catal10121402
Vancouver
Dias LD, Rodrigues FMS, Calvete MJF, Carabineiro SAC, Scherer MD, Caires ARL, Buijnsters JG, Figueiredo JL, Bagnato VS, Pereira MM. Porphyrin-nanodiamond hybrid materials-active, stable and reusable cyclohexene oxidation catalysts [Internet]. Catalysts. 2020 ; 10( 2): 1402-1-1402-13.[citado 2024 nov. 07 ] Available from: https://doi.org/10.3390/catal10121402
Artigo de periodico
Oligomeric protein interference validates druggability of aspartate interconversion in Plasmodium falciparum (2019)
Batista, Fernando A. ; Bosch, Soraya Soledad ; Butzloff, Sabine; Lunev, Sergey; Müller, Ingrid B.; Dömling, Alexander S. S. ; Groves, Matthew R. ; Wrenger, Carsten
Source: Microbiology Open. Unidade: ICB
Subjects: PARASITOLOGIA, PLASMODIUM FALCIPARUM, MALÁRIA, PROTEÍNAS, ENZIMAS, ANTIMALÁRICOS
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ABNT
BATISTA, Fernando A. et al. Oligomeric protein interference validates druggability of aspartate interconversion in Plasmodium falciparum. Microbiology Open, p. 1-14, 2019Tradução . . Disponível em: https://doi.org/10.1002/mbo3.779. Acesso em: 07 nov. 2024.
APA
Batista, F. A., Bosch, S. S., Butzloff, S., Lunev, S., Müller, I. B., Dömling, A. S. S., et al. (2019). Oligomeric protein interference validates druggability of aspartate interconversion in Plasmodium falciparum. Microbiology Open, 1-14. doi:10.1002/mbo3.779
NLM
Batista FA, Bosch SS, Butzloff S, Lunev S, Müller IB, Dömling ASS, Groves MR, Wrenger C. Oligomeric protein interference validates druggability of aspartate interconversion in Plasmodium falciparum [Internet]. Microbiology Open. 2019 ; 1-14.[citado 2024 nov. 07 ] Available from: https://doi.org/10.1002/mbo3.779
Vancouver
Batista FA, Bosch SS, Butzloff S, Lunev S, Müller IB, Dömling ASS, Groves MR, Wrenger C. Oligomeric protein interference validates druggability of aspartate interconversion in Plasmodium falciparum [Internet]. Microbiology Open. 2019 ; 1-14.[citado 2024 nov. 07 ] Available from: https://doi.org/10.1002/mbo3.779
Artigo de periodico
Membrane-anchored serine protease matriptase is a trigger of pulmonary fibrogenesis (2016)
Bardou, Olivier; Menou, Awen; François, Charlène; Duitman, Jan Willem; Thüsen, Jan H. von der; Borie, Raphaël; Sales, Katiuchia Uzzun; Mutze, Kathrin; Castier, Yves; Sage, Edouard; Liu, Ligong; Bugge, Thomas H.; Fairlie, David P.; Königshoff, Mélanie; Crestani, Bruno; Borensztajn, Keren S.
Source: American Journal of Respiratory and Critical Care Medicine. Unidade: FMRP
Subjects: FIBROSE PULMONAR, FIBROBLASTOS, TERAPÊUTICA MÉDICA, ENZIMAS
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ABNT
BARDOU, Olivier et al. Membrane-anchored serine protease matriptase is a trigger of pulmonary fibrogenesis. American Journal of Respiratory and Critical Care Medicine, v. 193, n. 8, p. 847-860, 2016Tradução . . Disponível em: https://doi.org/10.1164/rccm.201502-0299OC. Acesso em: 07 nov. 2024.
APA
Bardou, O., Menou, A., François, C., Duitman, J. W., Thüsen, J. H. von der, Borie, R., et al. (2016). Membrane-anchored serine protease matriptase is a trigger of pulmonary fibrogenesis. American Journal of Respiratory and Critical Care Medicine, 193( 8), 847-860. doi:10.1164/rccm.201502-0299OC
NLM
Bardou O, Menou A, François C, Duitman JW, Thüsen JH von der, Borie R, Sales KU, Mutze K, Castier Y, Sage E, Liu L, Bugge TH, Fairlie DP, Königshoff M, Crestani B, Borensztajn KS. Membrane-anchored serine protease matriptase is a trigger of pulmonary fibrogenesis [Internet]. American Journal of Respiratory and Critical Care Medicine. 2016 ; 193( 8): 847-860.[citado 2024 nov. 07 ] Available from: https://doi.org/10.1164/rccm.201502-0299OC
Vancouver
Bardou O, Menou A, François C, Duitman JW, Thüsen JH von der, Borie R, Sales KU, Mutze K, Castier Y, Sage E, Liu L, Bugge TH, Fairlie DP, Königshoff M, Crestani B, Borensztajn KS. Membrane-anchored serine protease matriptase is a trigger of pulmonary fibrogenesis [Internet]. American Journal of Respiratory and Critical Care Medicine. 2016 ; 193( 8): 847-860.[citado 2024 nov. 07 ] Available from: https://doi.org/10.1164/rccm.201502-0299OC

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