Functional study of the division-associated protein FtsA in Bacillus subtilis (2006)
- Authors:
- Autor USP: GUEIROS FILHO, FREDERICO JOSÉ - IQ
- Unidade: IQ
- Subjects: DIVISÃO CELULAR; BIOQUÍMICA
- Language: Inglês
- Imprenta:
- Source:
- Título do periódico: Programas e Resumos
- Conference titles: Reunião Anual da Sociedade Brasileira de Bioquímica e Biologia Molecular
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ABNT
PANCETTI, Alessandra Roque; GUEIROS FILHO, Frederico José. Functional study of the division-associated protein FtsA in Bacillus subtilis. Anais.. São Paulo: SBBq, 2006. -
APA
Pancetti, A. R., & Gueiros Filho, F. J. (2006). Functional study of the division-associated protein FtsA in Bacillus subtilis. In Programas e Resumos. São Paulo: SBBq. -
NLM
Pancetti AR, Gueiros Filho FJ. Functional study of the division-associated protein FtsA in Bacillus subtilis. Programas e Resumos. 2006 ; -
Vancouver
Pancetti AR, Gueiros Filho FJ. Functional study of the division-associated protein FtsA in Bacillus subtilis. Programas e Resumos. 2006 ; - Using dual color GFP microscopy to study the assembly of the cell division complex of Bacillus subtilis
- Genetic study of the interaction between the tubulin-like protein FTSZ and division modulators in Bacillus subtilis
- Cytological characterization of YpsB, a novel component of the Bacillus subtilis divisome
- Vectorial signalling mechanism required for cell-cell communication during sporulation in Bacillus subtilis
- Antibiosis and dark-pigments secretion by the phytopathogenic and environmental fungal species after interaction in vitro with a Bacillus subtilis isolate
- In-silico characterization of a novel domain of the cell division protein amic
- Study of the interaction of two division proteins, FtsZ and ZapA, in Bacillus subtilis
- The use of GFP microscopy to understand the asymmetric division in Bacillus subtilis
- The role of the proteins FtsA and ZapA during division ring formation in bacillus subtilis
- The use of fluorescence microscopy to study the dynamics of divisome assembly in Bacillus subtilis
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