Crystallographic structure and substrate-binding interactions of the molybdate-binding protein of the phytopathogen Xanthomonas axonopodis pv. citri (2008)
- Authors:
- Autor USP: FERREIRA, LUIS CARLOS DE SOUZA - ICB
- Unidade: ICB
- DOI: 10.1016/j.bbapap.2007.11.013
- Assunto: MICROBIOLOGIA
- Language: Inglês
- Imprenta:
- Source:
- Título: Biochimica et Biophysica Acta
- ISSN: 1570-9639
- Volume/Número/Paginação/Ano: v. 1784, n. 2, p. 393-399, 2008
- Status:
- Nenhuma versão em acesso aberto identificada
-
ABNT
BALAN, Andrea et al. Crystallographic structure and substrate-binding interactions of the molybdate-binding protein of the phytopathogen Xanthomonas axonopodis pv. citri. Biochimica et Biophysica Acta, v. 1784, n. 2, p. 393-399, 2008Tradução . . Disponível em: https://doi.org/10.1016/j.bbapap.2007.11.013. Acesso em: 10 abr. 2026. -
APA
Balan, A., Santacruz-Pérez, C., Moutran, A., Ferreira, L. C. de S., Neshich, G., & Barbosa, J. A. R. G. (2008). Crystallographic structure and substrate-binding interactions of the molybdate-binding protein of the phytopathogen Xanthomonas axonopodis pv. citri. Biochimica et Biophysica Acta, 1784( 2), 393-399. doi:10.1016/j.bbapap.2007.11.013 -
NLM
Balan A, Santacruz-Pérez C, Moutran A, Ferreira LC de S, Neshich G, Barbosa JARG. Crystallographic structure and substrate-binding interactions of the molybdate-binding protein of the phytopathogen Xanthomonas axonopodis pv. citri [Internet]. Biochimica et Biophysica Acta. 2008 ; 1784( 2): 393-399.[citado 2026 abr. 10 ] Available from: https://doi.org/10.1016/j.bbapap.2007.11.013 -
Vancouver
Balan A, Santacruz-Pérez C, Moutran A, Ferreira LC de S, Neshich G, Barbosa JARG. Crystallographic structure and substrate-binding interactions of the molybdate-binding protein of the phytopathogen Xanthomonas axonopodis pv. citri [Internet]. Biochimica et Biophysica Acta. 2008 ; 1784( 2): 393-399.[citado 2026 abr. 10 ] Available from: https://doi.org/10.1016/j.bbapap.2007.11.013 - Evaluation of experimental conditions for quantification of LT produced by human derived enterotoxigenic Escherichia coli strains
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