Characterization of the interaction sites of bacterial division proteins (2010)
- Authors:
- Autor USP: GUEIROS FILHO, FREDERICO JOSÉ - IQ
- Unidade: IQ
- Subjects: DIVISÃO CELULAR; PROTEÍNAS (INTERAÇÃO)
- Language: Inglês
- Imprenta:
- Source:
- Título: Abstracts
- Conference titles: Annual Meeting of Brazilian Biochemistry and Molecular Biology (SBBq)
-
ABNT
BLASIOS JUNIOR, Valdir e BISSON FILHO, Alexandre Wilson e GUEIROS FILHO, Frederico José. Characterization of the interaction sites of bacterial division proteins. 2010, Anais.. São Paulo: SBBq, 2010. . Acesso em: 21 jan. 2026. -
APA
Blasios Junior, V., Bisson Filho, A. W., & Gueiros Filho, F. J. (2010). Characterization of the interaction sites of bacterial division proteins. In Abstracts. São Paulo: SBBq. -
NLM
Blasios Junior V, Bisson Filho AW, Gueiros Filho FJ. Characterization of the interaction sites of bacterial division proteins. Abstracts. 2010 ;[citado 2026 jan. 21 ] -
Vancouver
Blasios Junior V, Bisson Filho AW, Gueiros Filho FJ. Characterization of the interaction sites of bacterial division proteins. Abstracts. 2010 ;[citado 2026 jan. 21 ] - The use of GFP microscopy to understand the asymmetric division in Bacillus subtilis
- Vectorial signalling mechanism required for cell-cell communication during sporulation in Bacillus subtilis
- FtsZ filament capping by MciZ, a developmental regulator of bacterial division
- Backbone and side chain NMR assignments for the N-terminal domain of the cell division regulator MinC from Bacillus subtilis
- The role of the proteins FtsA and ZapA during division ring formation in bacillus subtilis
- YrzD: a novel cell division protein of Bacillus subtilis
- Estudo molecular do controle de crescimento em Bacillus subtilis
- Study of the interaction of two division proteins, FtsZ and ZapA, in Bacillus subtilis
- Functional study of the division-associated protein FtsA in Bacillus subtilis
- Unmasking sites of interaction between bacterial division proteins
How to cite
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
